ID 3BHS1_MOUSE Reviewed; 373 AA. AC P24815; Q7TQ00; DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 19-MAR-2014, entry version 117. DE RecName: Full=3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 1; DE AltName: Full=3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type I; DE Short=3-beta-HSD I; DE Includes: DE RecName: Full=3-beta-hydroxy-Delta(5)-steroid dehydrogenase; DE EC=1.1.1.145; DE AltName: Full=3-beta-hydroxy-5-ene steroid dehydrogenase; DE AltName: Full=Progesterone reductase; DE Includes: DE RecName: Full=Steroid Delta-isomerase; DE EC=5.3.3.1; DE AltName: Full=Delta-5-3-ketosteroid isomerase; GN Name=Hsd3b1; Synonyms=Hsd3b; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=CD-1; RX PubMed=1924345; DOI=10.1073/pnas.88.20.8870; RA Bain P.A., Yoo M., Clarke T., Hammond S.H., Payne A.H.; RT "Multiple forms of mouse 3 beta-hydroxysteroid dehydrogenase/delta 5- RT delta 4 isomerase and differential expression in gonads, adrenal RT glands, liver, and kidneys of both sexes."; RL Proc. Natl. Acad. Sci. U.S.A. 88:8870-8874(1991). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Egg; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: 3-beta-HSD is a bifunctional enzyme, that catalyzes the CC oxidative conversion of Delta(5)-ene-3-beta-hydroxy steroid, and CC the oxidative conversion of ketosteroids. The 3-beta-HSD enzymatic CC system plays a crucial role in the biosynthesis of all classes of CC hormonal steroids. CC -!- CATALYTIC ACTIVITY: A 3-beta-hydroxy-Delta(5)-steroid + NAD(+) = a CC 3-oxo-Delta(5)-steroid + NADH. CC -!- CATALYTIC ACTIVITY: A 3-oxo-Delta(5)-steroid = a 3-oxo-Delta(4)- CC steroid. CC -!- PATHWAY: Lipid metabolism; steroid biosynthesis. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass CC membrane protein. Mitochondrion membrane; Single-pass membrane CC protein. CC -!- TISSUE SPECIFICITY: Steroidogenic tissues (includes testes, CC ovaries and adrenal glands). CC -!- SIMILARITY: Belongs to the 3-beta-HSD family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M58567; AAA37860.1; -; mRNA. DR EMBL; BC052659; AAH52659.1; -; mRNA. DR PIR; I49762; I49762. DR RefSeq; NP_032319.1; NM_008293.3. DR RefSeq; XP_006501098.1; XM_006501035.1. DR RefSeq; XP_006501099.1; XM_006501036.1. DR RefSeq; XP_006501100.1; XM_006501037.1. DR UniGene; Mm.140811; -. DR ProteinModelPortal; P24815; -. DR SMR; P24815; 5-360. DR STRING; 10090.ENSMUSP00000102630; -. DR PhosphoSite; P24815; -. DR PaxDb; P24815; -. DR PRIDE; P24815; -. DR Ensembl; ENSMUST00000107016; ENSMUSP00000102630; ENSMUSG00000027871. DR GeneID; 15492; -. DR KEGG; mmu:15492; -. DR UCSC; uc008qqh.1; mouse. DR CTD; 3283; -. DR MGI; MGI:96233; Hsd3b1. DR eggNOG; COG0451; -. DR HOVERGEN; HBG000014; -. DR InParanoid; P24815; -. DR KO; K00070; -. DR OMA; MAGWSCL; -. DR TreeFam; TF343138; -. DR SABIO-RK; P24815; -. DR UniPathway; UPA00062; -. DR NextBio; 288366; -. DR PRO; PR:P24815; -. DR ArrayExpress; P24815; -. DR Bgee; P24815; -. DR Genevestigator; P24815; -. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR GO; GO:0003854; F:3-beta-hydroxy-delta5-steroid dehydrogenase activity; IEA:UniProtKB-EC. DR GO; GO:0004769; F:steroid delta-isomerase activity; IEA:UniProtKB-EC. DR GO; GO:0006694; P:steroid biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR002225; 3Beta_OHSteriod_DH/Estase. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Pfam; PF01073; 3Beta_HSD; 1. PE 2: Evidence at transcript level; KW Complete proteome; Endoplasmic reticulum; Isomerase; Membrane; KW Mitochondrion; Multifunctional enzyme; NAD; Oxidoreductase; KW Reference proteome; Steroidogenesis; Transmembrane; KW Transmembrane helix. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 373 3 beta-hydroxysteroid dehydrogenase/Delta FT 5-->4-isomerase type 1. FT /FTId=PRO_0000087780. FT TRANSMEM 288 308 Helical; (Potential). FT ACT_SITE 155 155 Proton acceptor (By similarity). FT BINDING 159 159 NAD (By similarity). FT CONFLICT 128 128 V -> A (in Ref. 2; AAH52659). FT CONFLICT 319 319 L -> S (in Ref. 2; AAH52659). SQ SEQUENCE 373 AA; 42062 MW; 395F9D786C7BA010 CRC64; MAGWSCLVTG AGGFVGQRII KMLVQEKELQ EVRALDKVFR PETKEEFSKL QTKTKVTVLE GDILDAQCLR RACQGISVVI HTAAVIDVTG VIPRQTILDV NLKGTQNLLE ACVQASVPAF IFCSSVDVAG PNSYKKIVLN GHEEQNHEST WSDPYPYSKK MAEKAVLAAN GSMLKNGGTL NTCALRPMYI YGERSPFIFN AIIRALKNKG ILCVTGKFSI ANPVYVENVA WAHILAARGL RDPKKSTSIQ GQFYYISDDT PHQSYDDLNY TLSKEWGLRP NASWSLPLPL LYWLAFLLET VSFLLRPVYR YRPLFNRHLI TLSNSTFTFS YKKAQRDLGY EPLVNWEEAK QKTSEWIGTI VEQHREILDT KCQ // ID 3BHS2_MOUSE Reviewed; 373 AA. AC P26149; B1ARN7; Q8R0J6; DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot. DT 28-JUN-2011, sequence version 4. DT 19-MAR-2014, entry version 120. DE RecName: Full=3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 2; DE AltName: Full=3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type II; DE Short=3-beta-HSD II; DE Includes: DE RecName: Full=3-beta-hydroxy-Delta(5)-steroid dehydrogenase; DE EC=1.1.1.145; DE AltName: Full=3-beta-hydroxy-5-ene steroid dehydrogenase; DE AltName: Full=Progesterone reductase; DE Includes: DE RecName: Full=Steroid Delta-isomerase; DE EC=5.3.3.1; DE AltName: Full=Delta-5-3-ketosteroid isomerase; GN Name=Hsd3b2; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Kidney, and Liver; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] OF 109-373. RC STRAIN=BALB/c; RX PubMed=1924345; DOI=10.1073/pnas.88.20.8870; RA Bain P.A., Yoo M., Clarke T., Hammond S.H., Payne A.H.; RT "Multiple forms of mouse 3 beta-hydroxysteroid dehydrogenase/delta 5- RT delta 4 isomerase and differential expression in gonads, adrenal RT glands, liver, and kidneys of both sexes."; RL Proc. Natl. Acad. Sci. U.S.A. 88:8870-8874(1991). CC -!- FUNCTION: 3-beta-HSD is a bifunctional enzyme, that catalyzes the CC oxidative conversion of Delta(5)-ene-3-beta-hydroxy steroid, and CC the oxidative conversion of ketosteroids. The 3-beta-HSD enzymatic CC system plays a crucial role in the biosynthesis of all classes of CC hormonal steroids. CC -!- CATALYTIC ACTIVITY: A 3-beta-hydroxy-Delta(5)-steroid + NAD(+) = a CC 3-oxo-Delta(5)-steroid + NADH. CC -!- CATALYTIC ACTIVITY: A 3-oxo-Delta(5)-steroid = a 3-oxo-Delta(4)- CC steroid. CC -!- PATHWAY: Lipid metabolism; steroid biosynthesis. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass CC membrane protein. Mitochondrion membrane; Single-pass membrane CC protein. CC -!- TISSUE SPECIFICITY: Liver and kidney. CC -!- SIMILARITY: Belongs to the 3-beta-HSD family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AL606755; CAM13688.1; -; Genomic_DNA. DR EMBL; BC026757; AAH26757.1; -; mRNA. DR EMBL; BC040397; AAH40397.1; -; mRNA. DR EMBL; M75886; -; NOT_ANNOTATED_CDS; mRNA. DR RefSeq; NP_694873.2; NM_153193.3. DR RefSeq; XP_006501101.1; XM_006501038.1. DR UniGene; Mm.482364; -. DR ProteinModelPortal; P26149; -. DR SMR; P26149; 5-360. DR STRING; 10090.ENSMUSP00000102635; -. DR PhosphoSite; P26149; -. DR PaxDb; P26149; -. DR PRIDE; P26149; -. DR Ensembl; ENSMUST00000107021; ENSMUSP00000102635; ENSMUSG00000063730. DR Ensembl; ENSMUST00000107022; ENSMUSP00000102636; ENSMUSG00000063730. DR Ensembl; ENSMUST00000177651; ENSMUSP00000136533; ENSMUSG00000063730. DR GeneID; 15493; -. DR KEGG; mmu:15493; -. DR UCSC; uc008qqc.2; mouse. DR CTD; 3284; -. DR MGI; MGI:96234; Hsd3b2. DR eggNOG; COG0451; -. DR GeneTree; ENSGT00550000074557; -. DR HOGENOM; HOG000167989; -. DR HOVERGEN; HBG000014; -. DR InParanoid; B1ARN7; -. DR KO; K00070; -. DR OMA; HEEECHE; -. DR OrthoDB; EOG74J985; -. DR TreeFam; TF343138; -. DR BRENDA; 1.1.1.145; 244. DR BRENDA; 5.3.3.1; 244. DR UniPathway; UPA00062; -. DR NextBio; 288370; -. DR PRO; PR:P26149; -. DR Bgee; P26149; -. DR Genevestigator; P26149; -. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell. DR GO; GO:0003854; F:3-beta-hydroxy-delta5-steroid dehydrogenase activity; IEA:UniProtKB-EC. DR GO; GO:0004769; F:steroid delta-isomerase activity; IEA:UniProtKB-EC. DR GO; GO:0006694; P:steroid biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.720; -; 2. DR InterPro; IPR002225; 3Beta_OHSteriod_DH/Estase. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Pfam; PF01073; 3Beta_HSD; 1. PE 2: Evidence at transcript level; KW Complete proteome; Endoplasmic reticulum; Isomerase; Membrane; KW Mitochondrion; Multifunctional enzyme; NAD; Oxidoreductase; KW Reference proteome; Steroidogenesis; Transmembrane; KW Transmembrane helix. FT CHAIN 1 373 3 beta-hydroxysteroid dehydrogenase/Delta FT 5-->4-isomerase type 2. FT /FTId=PRO_0000087781. FT TRANSMEM 288 308 Helical; (Potential). FT ACT_SITE 155 155 Proton acceptor (By similarity). FT BINDING 159 159 NAD (By similarity). FT CONFLICT 12 12 G -> K (in Ref. 2; AAH26757/AAH40397). FT CONFLICT 54 54 I -> N (in Ref. 2; AAH26757/AAH40397). SQ SEQUENCE 373 AA; 41923 MW; 2500AF16F38C081B CRC64; MPGWSCLVTG AGGFLGQRII QLLVQEEDLE EIRVLDKVFR PETRKEFFNL ETSIKVTVLE GDILDTQYLR RACQGISVVI HTAAIIDVTG VIPRQTILDV NLKGTQNLLE ACIQASVPAF IFSSSVDVAG PNSYKEIVLN GHEEECHEST WSDPYPYSKK MAEKAVLAAN GSMLKNGGTL QTCALRPMCI YGERSPLISN IIIMALKHKG ILRSFGKFNT ANPVYVGNVA WAHILAARGL RDPKKSPNIQ GEFYYISDDT PHQSFDDISY TLSKEWGFCL DSSWSLPVPL LYWLAFLLET VSFLLSPIYR YIPPFNRHLV TLSGSTFTFS YKKAQRDLGY EPLVSWEEAK QKTSEWIGTL VEQHRETLDT KSQ // ID 3BHS3_MOUSE Reviewed; 373 AA. AC P26150; DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 19-MAR-2014, entry version 110. DE RecName: Full=3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 3; DE AltName: Full=3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type III; DE Short=3-beta-HSD III; DE Includes: DE RecName: Full=3-beta-hydroxy-Delta(5)-steroid dehydrogenase; DE EC=1.1.1.145; DE AltName: Full=3-beta-hydroxy-5-ene steroid dehydrogenase; DE AltName: Full=Progesterone reductase; DE Includes: DE RecName: Full=Steroid Delta-isomerase; DE EC=5.3.3.1; DE AltName: Full=Delta-5-3-ketosteroid isomerase; GN Name=Hsd3b3; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=BALB/c; RX PubMed=1924345; DOI=10.1073/pnas.88.20.8870; RA Bain P.A., Yoo M., Clarke T., Hammond S.H., Payne A.H.; RT "Multiple forms of mouse 3 beta-hydroxysteroid dehydrogenase/delta 5- RT delta 4 isomerase and differential expression in gonads, adrenal RT glands, liver, and kidneys of both sexes."; RL Proc. Natl. Acad. Sci. U.S.A. 88:8870-8874(1991). CC -!- FUNCTION: 3-beta-HSD is a bifunctional enzyme, that catalyzes the CC oxidative conversion of Delta(5)-ene-3-beta-hydroxy steroid, and CC the oxidative conversion of ketosteroids. The 3-beta-HSD enzymatic CC system plays a crucial role in the biosynthesis of all classes of CC hormonal steroids. CC -!- CATALYTIC ACTIVITY: A 3-beta-hydroxy-Delta(5)-steroid + NAD(+) = a CC 3-oxo-Delta(5)-steroid + NADH. CC -!- CATALYTIC ACTIVITY: A 3-oxo-Delta(5)-steroid = a 3-oxo-Delta(4)- CC steroid. CC -!- PATHWAY: Lipid metabolism; steroid biosynthesis. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass CC membrane protein. Mitochondrion membrane; Single-pass membrane CC protein. CC -!- TISSUE SPECIFICITY: Liver and kidney. Greater expression in liver. CC -!- SIMILARITY: Belongs to the 3-beta-HSD family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M77015; -; NOT_ANNOTATED_CDS; mRNA. DR RefSeq; NP_001155214.1; NM_001161742.1. DR RefSeq; NP_001155215.1; NM_001161743.1. DR RefSeq; NP_001155216.1; NM_001161744.1. DR RefSeq; NP_001155217.1; NM_001161745.1. DR RefSeq; XP_006501104.1; XM_006501041.1. DR RefSeq; XP_006501105.1; XM_006501042.1. DR UniGene; Mm.158717; -. DR ProteinModelPortal; P26150; -. DR SMR; P26150; 5-360. DR MINT; MINT-1857437; -. DR PaxDb; P26150; -. DR PRIDE; P26150; -. DR Ensembl; ENSMUST00000090743; ENSMUSP00000088246; ENSMUSG00000062410. DR Ensembl; ENSMUST00000107018; ENSMUSP00000102632; ENSMUSG00000062410. DR Ensembl; ENSMUST00000107019; ENSMUSP00000102633; ENSMUSG00000062410. DR GeneID; 15494; -. DR KEGG; mmu:15494; -. DR UCSC; uc008qqf.2; mouse. DR CTD; 15494; -. DR MGI; MGI:96235; Hsd3b3. DR eggNOG; COG0451; -. DR GeneTree; ENSGT00550000074557; -. DR HOGENOM; HOG000167989; -. DR HOVERGEN; HBG000014; -. DR InParanoid; P26150; -. DR OMA; HEDEHRE; -. DR OrthoDB; EOG74J985; -. DR TreeFam; TF343138; -. DR SABIO-RK; P26150; -. DR UniPathway; UPA00062; -. DR NextBio; 288374; -. DR PRO; PR:P26150; -. DR ArrayExpress; P26150; -. DR Bgee; P26150; -. DR Genevestigator; P26150; -. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:MGI. DR GO; GO:0003854; F:3-beta-hydroxy-delta5-steroid dehydrogenase activity; IEA:UniProtKB-EC. DR GO; GO:0004769; F:steroid delta-isomerase activity; IEA:UniProtKB-EC. DR GO; GO:0006694; P:steroid biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.720; -; 2. DR InterPro; IPR002225; 3Beta_OHSteriod_DH/Estase. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Pfam; PF01073; 3Beta_HSD; 1. PE 2: Evidence at transcript level; KW Complete proteome; Endoplasmic reticulum; Isomerase; Membrane; KW Mitochondrion; Multifunctional enzyme; NAD; Oxidoreductase; KW Reference proteome; Steroidogenesis; Transmembrane; KW Transmembrane helix. FT CHAIN 1 373 3 beta-hydroxysteroid dehydrogenase/Delta FT 5-->4-isomerase type 3. FT /FTId=PRO_0000087782. FT TRANSMEM 288 308 Helical; (Potential). FT ACT_SITE 155 155 Proton acceptor (By similarity). FT BINDING 159 159 NAD (By similarity). SQ SEQUENCE 373 AA; 42031 MW; 6F320FF1707974A6 CRC64; MPGWSCLVTG AGGFLGQRII QLLVQEKDLE EIRVLDKVFK PETREQFFNL GTSIKVTVLE GDILDTQYLR RACQGISVVI HTAAIIDVTG VIPRQTILDV NLKGTQNLLE ACIQASVPAF IFSSSVDVAG PNSYKDIVLN GHEDEHREST WSDPYPYSKK MAEKAVLAAN GSMLKNGGTL QTCALRPMCI YGERSQFLSN TIIKALKNKF ILRGGGKFST ANPVYVGNVA WAHILAARGL RNPKKSPNIQ GEFYYISDDT PHQSYDDLNY TLSKEWGFCL NSRWYLPVPI LYWLAFLLET VSFLLSPIYR YIPPFNRHLV TLTASTFTFS YKKAQRDLGY EPLVSWEEAK QKTSEWIGTL VEQHRETLDT KSQ // ID 3BHS4_MOUSE Reviewed; 373 AA. AC Q61767; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 19-MAR-2014, entry version 127. DE RecName: Full=3 beta-hydroxysteroid dehydrogenase type 4; DE AltName: Full=3 beta-hydroxysteroid dehydrogenase type IV; DE Short=3-beta-HSD IV; DE AltName: Full=3-beta-hydroxy-5-ene steroid dehydrogenase; DE AltName: Full=NADPH-dependent 3-beta-hydroxy-Delta(5)-steroid dehydrogenase; DE EC=1.1.1.-; DE AltName: Full=Progesterone reductase; GN Name=Hsd3b4; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=ICR (CD-1); TISSUE=Kidney; RX PubMed=8145763; DOI=10.1210/me.7.12.1569; RA Clarke T.R., Bain P.A., Greco T.L., Payne A.H.; RT "A novel mouse kidney 3 beta-hydroxysteroid dehydrogenase RT complementary DNA encodes a 3-ketosteroid reductase instead of a 3 RT beta-hydroxysteroid dehydrogenase/delta 5-delta 4-isomerase."; RL Mol. Endocrinol. 7:1569-1578(1993). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Kidney; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: The 3-beta-HSD enzymatic system plays a crucial role in CC the biosynthesis of all classes of hormonal steroids. HSD IV can CC only catalyze the conversion of dihydrotestosterone to 5 alpha- CC androstanediol in the presence of the cofactor NADPH. Does not CC function as a isomerase. CC -!- CATALYTIC ACTIVITY: 3-beta-hydroxy-Delta(5)-steroid + NADP(+) = 3- CC oxo-Delta(5)-steroid + NADPH. CC -!- PATHWAY: Lipid metabolism; steroid biosynthesis. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass CC membrane protein. Mitochondrion membrane; Single-pass membrane CC protein. CC -!- TISSUE SPECIFICITY: Kidney; found only in the cortex, appears to CC be associated with the proximal tubules; and a minor expression in CC testis. CC -!- DEVELOPMENTAL STAGE: Expression between 15-20 days post- CC implantation occurs only in the kidney of the male fetus and not CC in the female, whereas a similar expression is found in adult male CC and female kidneys. CC -!- SIMILARITY: Belongs to the 3-beta-HSD family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L16919; AAA39374.1; -; mRNA. DR EMBL; BC013449; AAH13449.1; -; mRNA. DR PIR; A49573; A49573. DR RefSeq; NP_001104806.1; NM_001111336.1. DR RefSeq; NP_001257358.1; NM_001270429.1. DR RefSeq; NP_032320.1; NM_008294.2. DR UniGene; Mm.14309; -. DR UniGene; Mm.475664; -. DR ProteinModelPortal; Q61767; -. DR SMR; Q61767; 7-243. DR IntAct; Q61767; 731. DR MINT; MINT-1837112; -. DR PhosphoSite; Q61767; -. DR PaxDb; Q61767; -. DR PRIDE; Q61767; -. DR Ensembl; ENSMUST00000058728; ENSMUSP00000055886; ENSMUSG00000095388. DR Ensembl; ENSMUST00000178221; ENSMUSP00000136749; ENSMUSG00000095388. DR Ensembl; ENSMUST00000179429; ENSMUSP00000136588; ENSMUSG00000095143. DR GeneID; 100043456; -. DR GeneID; 15495; -. DR KEGG; mmu:100043456; -. DR KEGG; mmu:15495; -. DR UCSC; uc008qpw.2; mouse. DR CTD; 15495; -. DR MGI; MGI:96236; Hsd3b4. DR eggNOG; COG0451; -. DR GeneTree; ENSGT00550000074557; -. DR HOGENOM; HOG000167989; -. DR HOVERGEN; HBG000014; -. DR InParanoid; Q61767; -. DR KO; K00070; -. DR OMA; ISCSTIR; -. DR OrthoDB; EOG7W41CS; -. DR TreeFam; TF343138; -. DR UniPathway; UPA00062; -. DR NextBio; 288378; -. DR PRO; PR:Q61767; -. DR ArrayExpress; Q61767; -. DR Bgee; Q61767; -. DR Genevestigator; Q61767; -. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell. DR GO; GO:0003854; F:3-beta-hydroxy-delta5-steroid dehydrogenase activity; IEA:InterPro. DR GO; GO:0035634; P:response to stilbenoid; IEP:UniProtKB. DR GO; GO:0006694; P:steroid biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR002225; 3Beta_OHSteriod_DH/Estase. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Pfam; PF01073; 3Beta_HSD; 1. PE 2: Evidence at transcript level; KW Acetylation; Complete proteome; Endoplasmic reticulum; Membrane; KW Mitochondrion; NADP; Oxidoreductase; Reference proteome; KW Steroidogenesis; Transmembrane; Transmembrane helix. FT CHAIN 1 373 3 beta-hydroxysteroid dehydrogenase type FT 4. FT /FTId=PRO_0000087783. FT TRANSMEM 288 308 Helical; (Potential). FT ACT_SITE 155 155 Proton acceptor (By similarity). FT BINDING 159 159 NAD (By similarity). FT MOD_RES 350 350 N6-acetyllysine (By similarity). SQ SEQUENCE 373 AA; 41766 MW; 303E56BF9A8FAF1A CRC64; MPGWSCLVTG AGGFLGQRIV RMLVQEEELQ EIRALFRTFG RKQEEELSKL QTKTKVTVLK GDILDAQCLK RACQGMSAVI HTAAAIDPLG AASRQTILDV NLKGTQLLLD ACVEANVPTF IYSSSVLVAG PNSYKEIILN AHEEEHHEST WSNPYPYSKK MAEKAVLAAN GSILKNGGTL HTCALRLSFI YGEECQVTST TVKTALKNNS IIKKNATFSI ANPVYVGNAA WAHILAARSL QDPKKSPSIQ GQFYYITDDT PHQSYDDLKC TLSKEWGLRL DTSWSLPLPL LYWLAFLLET VSFLLRPVYN YRPPFNRLLI TVLNSVFTFS YKKAQRDLGY EPLVSWEEAK QKTSEWIGTL VMQHREIGNK KSQ // ID 3BHS6_MOUSE Reviewed; 373 AA. AC O35469; Q3UQN7; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 28-JUN-2011, sequence version 4. DT 19-MAR-2014, entry version 106. DE RecName: Full=3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 6; DE EC=1.1.1.-; DE AltName: Full=3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type VI; DE Short=3-beta-HSD VI; DE Includes: DE RecName: Full=3-beta-hydroxy-Delta(5)-steroid dehydrogenase; DE EC=1.1.1.145; DE AltName: Full=3-beta-hydroxy-5-ene steroid dehydrogenase; DE AltName: Full=Progesterone reductase; DE Includes: DE RecName: Full=Steroid Delta-isomerase; DE EC=5.3.3.1; DE AltName: Full=Delta-5-3-ketosteroid isomerase; GN Name=Hsd3b6; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=C57BL/6J; RX PubMed=9075693; DOI=10.1210/en.138.4.1392; RA Abbaszade I.G., Arensburg J., Park C.-H.J., Kasa-Vubu J.Z., Orly J., RA Payne A.H.; RT "Isolation of a new mouse 3beta-hydroxysteroid dehydrogenase isoform, RT 3beta-HSD VI, expressed during early pregnancy."; RL Endocrinology 138:1392-1399(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Heart; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: 3-beta-HSD is a bifunctional enzyme, that catalyzes the CC oxidative conversion of Delta(5)-ene-3-beta-hydroxy steroid, and CC the oxidative conversion of ketosteroids. The 3-beta-HSD enzymatic CC system plays a crucial role in the biosynthesis of all classes of CC hormonal steroids. May be involved in local production of CC progesterone. CC -!- CATALYTIC ACTIVITY: A 3-beta-hydroxy-Delta(5)-steroid + NAD(+) = a CC 3-oxo-Delta(5)-steroid + NADH. CC -!- CATALYTIC ACTIVITY: A 3-oxo-Delta(5)-steroid = a 3-oxo-Delta(4)- CC steroid. CC -!- PATHWAY: Lipid metabolism; steroid biosynthesis. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass CC membrane protein. Mitochondrion membrane; Single-pass membrane CC protein. CC -!- TISSUE SPECIFICITY: Expressed in skin and testis. CC -!- DEVELOPMENTAL STAGE: Earliest isoform to be expressed during CC embryogenesis in cells of embryonic origin at 7 and 9.5 dpc, and CC is the major isoform expressed in uterine tissue at the time of CC implantation (4.5 dpc) and continues to be expressed in uterine CC tissue at 6.5, 7.5 and 9.5 dpc. It is expressed in giant CC trophoblasts at 9.5 dpc and is expressed in the placenta through CC 15.5 dpc. CC -!- SIMILARITY: Belongs to the 3-beta-HSD family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF031170; AAB84299.1; -; mRNA. DR EMBL; AK142267; BAE25002.1; -; mRNA. DR EMBL; AL606755; CAM13693.1; -; Genomic_DNA. DR EMBL; CH466620; EDL38971.1; -; Genomic_DNA. DR RefSeq; NP_038849.2; NM_013821.3. DR UniGene; Mm.14435; -. DR ProteinModelPortal; O35469; -. DR SMR; O35469; 5-360. DR PRIDE; O35469; -. DR Ensembl; ENSMUST00000029463; ENSMUSP00000029463; ENSMUSG00000027869. DR Ensembl; ENSMUST00000170847; ENSMUSP00000129911; ENSMUSG00000027869. DR GeneID; 15497; -. DR KEGG; mmu:15497; -. DR UCSC; uc012cuq.1; mouse. DR CTD; 15497; -. DR MGI; MGI:109598; Hsd3b6. DR GeneTree; ENSGT00550000074557; -. DR HOGENOM; HOG000167989; -. DR HOVERGEN; HBG000014; -. DR InParanoid; Q3UQN7; -. DR KO; K00070; -. DR OMA; TTEWLAS; -. DR OrthoDB; EOG74J985; -. DR TreeFam; TF343138; -. DR BRENDA; 1.1.1.145; 244. DR BRENDA; 5.3.3.1; 244. DR UniPathway; UPA00062; -. DR NextBio; 288386; -. DR PRO; PR:O35469; -. DR Bgee; O35469; -. DR Genevestigator; O35469; -. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell. DR GO; GO:0003854; F:3-beta-hydroxy-delta5-steroid dehydrogenase activity; IEA:UniProtKB-EC. DR GO; GO:0004769; F:steroid delta-isomerase activity; IEA:UniProtKB-EC. DR GO; GO:0006694; P:steroid biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.720; -; 2. DR InterPro; IPR002225; 3Beta_OHSteriod_DH/Estase. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Pfam; PF01073; 3Beta_HSD; 1. PE 2: Evidence at transcript level; KW Complete proteome; Endoplasmic reticulum; Isomerase; Membrane; KW Mitochondrion; Multifunctional enzyme; NAD; Oxidoreductase; KW Reference proteome; Steroidogenesis; Transmembrane; KW Transmembrane helix. FT CHAIN 1 373 3 beta-hydroxysteroid dehydrogenase/Delta FT 5-->4-isomerase type 6. FT /FTId=PRO_0000087785. FT TRANSMEM 288 308 Helical; (Potential). FT ACT_SITE 155 155 Proton acceptor (By similarity). FT BINDING 159 159 NAD (By similarity). FT CONFLICT 189 189 Y -> F (in Ref. 1; AAB84299). FT CONFLICT 366 366 E -> A (in Ref. 1; AAB84299). FT CONFLICT 371 371 K -> T (in Ref. 1; AAB84299). SQ SEQUENCE 373 AA; 41977 MW; 10FE9278C5BDC534 CRC64; MPGWSCLVTG AGGFLGQRIV QLLMQEKDLE EIRVLDKFFR PETREQFFNL DTNIKVTVLE GDILDTQYLR KACQGISVVI HTAAVIDVTG VIPRQTILDV NLKGTQNLLE ACIQASVPAF IFSSSVDVAG PNSYKEIILN GNEEEHHESI WSDPYPYSKK MAEKAVLAAN GSMLKIGGTL HTCALRPMYI YGERSPFISN TIITALKNKN ILGCTGKFST ANPVYVGNVA WAHILAARGL RDPKKSPNIQ GEFYYISDDT PHQSYDDLNY TLSKEWGFCP DSSWSLPVPL LYWLAFMLET VSFLLSPIYR FIPPFNRHLV TLTGSTFTFS YKKAQRDLGY EPLVSWEEAK QKTSEWIGTL VEQHRETLDT KSQ // ID 3BHS5_MOUSE Reviewed; 373 AA. AC Q61694; Q91X27; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 4. DT 19-MAR-2014, entry version 115. DE RecName: Full=3 beta-hydroxysteroid dehydrogenase type 5; DE AltName: Full=3 beta-hydroxysteroid dehydrogenase type V; DE Short=3-beta-HSD V; DE AltName: Full=3-beta-hydroxy-5-ene steroid dehydrogenase; DE AltName: Full=NADPH-dependent 3-beta-hydroxy-Delta(5)-steroid dehydrogenase; DE EC=1.1.1.-; DE AltName: Full=Progesterone reductase; GN Name=Hsd3b5; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=BALB/c; TISSUE=Liver; RX PubMed=7491113; DOI=10.1210/me.9.9.1214; RA Abbaszade I.G., Clarke T.R., Park C.-H.J., Payne A.H.; RT "The mouse 3 beta-hydroxysteroid dehydrogenase multigene family RT includes two functionally distinct groups of proteins."; RL Mol. Endocrinol. 9:1214-1222(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Salivary gland; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-350, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23576753; DOI=10.1073/pnas.1302961110; RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., RA Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.; RT "Label-free quantitative proteomics of the lysine acetylome in RT mitochondria identifies substrates of SIRT3 in metabolic pathways."; RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013). CC -!- FUNCTION: The 3-beta-HSD enzymatic system plays a crucial role in CC the biosynthesis of all classes of hormonal steroids. HSD V can CC only catalyze the conversion of dihydrotestosterone to 5 alpha- CC androstanediol in the presence of the cofactor NADPH. Does not CC function as a isomerase. CC -!- CATALYTIC ACTIVITY: 3-beta-hydroxy-Delta(5)-steroid + NADP(+) = 3- CC oxo-Delta(5)-steroid + NADPH. CC -!- PATHWAY: Lipid metabolism; steroid biosynthesis. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass CC membrane protein. Mitochondrion membrane; Single-pass membrane CC protein. CC -!- TISSUE SPECIFICITY: Expressed in the male liver, starting in late CC puberty. CC -!- SIMILARITY: Belongs to the 3-beta-HSD family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L41519; AAB81242.1; -; mRNA. DR EMBL; BC012715; AAH12715.1; -; mRNA. DR PIR; A57559; A57559. DR RefSeq; NP_032321.2; NM_008295.2. DR UniGene; Mm.17910; -. DR ProteinModelPortal; Q61694; -. DR SMR; Q61694; 7-243. DR STRING; 10090.ENSMUSP00000041442; -. DR PhosphoSite; Q61694; -. DR PaxDb; Q61694; -. DR PRIDE; Q61694; -. DR Ensembl; ENSMUST00000044094; ENSMUSP00000041442; ENSMUSG00000038092. DR GeneID; 15496; -. DR KEGG; mmu:15496; -. DR UCSC; uc008qqb.1; mouse. DR CTD; 15496; -. DR MGI; MGI:104645; Hsd3b5. DR eggNOG; COG0451; -. DR GeneTree; ENSGT00550000074557; -. DR HOGENOM; HOG000167989; -. DR HOVERGEN; HBG000014; -. DR InParanoid; Q61694; -. DR KO; K00070; -. DR OMA; DACVEAS; -. DR OrthoDB; EOG74J985; -. DR TreeFam; TF343138; -. DR UniPathway; UPA00062; -. DR NextBio; 288382; -. DR PRO; PR:Q61694; -. DR Bgee; Q61694; -. DR Genevestigator; Q61694; -. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:MGI. DR GO; GO:0003854; F:3-beta-hydroxy-delta5-steroid dehydrogenase activity; IEA:InterPro. DR GO; GO:0035634; P:response to stilbenoid; IEP:UniProtKB. DR GO; GO:0006694; P:steroid biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.720; -; 2. DR InterPro; IPR002225; 3Beta_OHSteriod_DH/Estase. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Pfam; PF01073; 3Beta_HSD; 1. PE 1: Evidence at protein level; KW Acetylation; Complete proteome; Endoplasmic reticulum; Membrane; KW Mitochondrion; NADP; Oxidoreductase; Reference proteome; KW Steroidogenesis; Transmembrane; Transmembrane helix. FT CHAIN 1 373 3 beta-hydroxysteroid dehydrogenase type FT 5. FT /FTId=PRO_0000087784. FT TRANSMEM 288 308 Helical; (Potential). FT ACT_SITE 155 155 Proton acceptor (By similarity). FT BINDING 159 159 NAD (By similarity). FT MOD_RES 350 350 N6-acetyllysine. FT CONFLICT 89 89 L -> R (in Ref. 1; AAB81242). FT CONFLICT 147 147 R -> H (in Ref. 1; AAB81242). FT CONFLICT 285 285 S -> R (in Ref. 1; AAB81242). FT CONFLICT 316 316 N -> T (in Ref. 1; AAB81242). SQ SEQUENCE 373 AA; 41892 MW; EE35DE19075390A5 CRC64; MPGWSCLVTG AGGFLGQRIV RMLVQEEELQ EIRALFRTFG RKHEEELSKL QTKAKVRVLK GDILDAQCLK RACQGMSAVI HTAAAIDPLG AASRQTILDV NLKGTQLLLD ACVEASVPTF IYSSSVLVAG PNSYKEIILN AHEEEHREST WPNPYPYSKR MAEKAVLATN GRLLKNGGTL HTCALRLPFI YGEECQVTST TVKTALKNNS IIKKNATFSI ANPVYVGNAA WAHILAARSL QDPKKSPSIQ GQFYYISDNT PHQSYDDLNY TLSKEWGLCL DSGWSLPLSL LYWLAFLLET VSFLLRPVYN YRPPFNRLLI TVLNSVFTIS YKKAQRDLGY QPLVSWEEAK QKTSEWIGTL VKQHRETLHK KSQ // ID 3BHS7_MOUSE Reviewed; 369 AA. AC Q9EQC1; A2RTR5; DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2001, sequence version 1. DT 19-FEB-2014, entry version 97. DE RecName: Full=3 beta-hydroxysteroid dehydrogenase type 7; DE AltName: Full=3 beta-hydroxysteroid dehydrogenase type VII; DE Short=3-beta-HSD VII; DE AltName: Full=3-beta-hydroxy-Delta(5)-C27 steroid oxidoreductase; DE Short=C(27) 3-beta-HSD; DE EC=1.1.1.-; DE AltName: Full=Cholest-5-ene-3-beta,7-alpha-diol 3-beta-dehydrogenase; DE EC=1.1.1.181; GN Name=Hsd3b7; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY. RC STRAIN=C57BL/6J X 129/SvEv; RX PubMed=11067870; DOI=10.1172/JCI10902; RA Schwarz M., Wright A.C., Davis D.L., Nazer H., Bjorkhem I., RA Russell D.W.; RT "The bile acid synthetic gene 3beta-hydroxy-delta(5)-C(27)-steroid RT oxidoreductase is mutated in progressive intrahepatic cholestasis."; RL J. Clin. Invest. 106:1175-1184(2000). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: The 3-beta-HSD enzymatic system plays a crucial role in CC the biosynthesis of all classes of hormonal steroids. HSD VII is CC active against four 7-alpha-hydroxylated sterols. Does not CC metabolize several different C(19/21) steroids as substrates. CC Involved in bile acid synthesis. CC -!- CATALYTIC ACTIVITY: 3-beta-hydroxy-Delta(5)-steroid + NAD(+) = 3- CC oxo-Delta(5)-steroid + NADH. CC -!- CATALYTIC ACTIVITY: Cholest-5-ene-3-beta,7-alpha-diol + NAD(+) = CC 7-alpha-hydroxycholest-4-en-3-one + NADH. CC -!- PATHWAY: Lipid metabolism; steroid biosynthesis. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass CC membrane protein. CC -!- TISSUE SPECIFICITY: Predominantly expressed in liver. CC -!- SIMILARITY: Belongs to the 3-beta-HSD family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF277718; AAG37823.1; -; mRNA. DR EMBL; BC132605; AAI32606.1; -; mRNA. DR EMBL; BC138589; AAI38590.1; -; mRNA. DR RefSeq; NP_598704.2; NM_133943.2. DR UniGene; Mm.157103; -. DR ProteinModelPortal; Q9EQC1; -. DR SMR; Q9EQC1; 13-170. DR IntAct; Q9EQC1; 542. DR MINT; MINT-1845620; -. DR PhosphoSite; Q9EQC1; -. DR PaxDb; Q9EQC1; -. DR PRIDE; Q9EQC1; -. DR Ensembl; ENSMUST00000046863; ENSMUSP00000036245; ENSMUSG00000042289. DR GeneID; 101502; -. DR KEGG; mmu:101502; -. DR UCSC; uc009jwu.1; mouse. DR CTD; 80270; -. DR MGI; MGI:2141879; Hsd3b7. DR eggNOG; COG0451; -. DR GeneTree; ENSGT00550000074557; -. DR HOGENOM; HOG000167989; -. DR HOVERGEN; HBG000014; -. DR InParanoid; A2RTR5; -. DR KO; K12408; -. DR OMA; PCGLRLV; -. DR OrthoDB; EOG74J985; -. DR TreeFam; TF354279; -. DR UniPathway; UPA00062; -. DR ChiTaRS; HSD3B7; mouse. DR NextBio; 354976; -. DR PRO; PR:Q9EQC1; -. DR ArrayExpress; Q9EQC1; -. DR Bgee; Q9EQC1; -. DR Genevestigator; Q9EQC1; -. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0003854; F:3-beta-hydroxy-delta5-steroid dehydrogenase activity; IEA:InterPro. DR GO; GO:0047016; F:cholest-5-ene-3-beta,7-alpha-diol 3-beta-dehydrogenase activity; IEA:UniProtKB-EC. DR GO; GO:0006694; P:steroid biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.720; -; 2. DR InterPro; IPR002225; 3Beta_OHSteriod_DH/Estase. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Pfam; PF01073; 3Beta_HSD; 1. PE 2: Evidence at transcript level; KW Complete proteome; Endoplasmic reticulum; Membrane; NAD; KW Oxidoreductase; Reference proteome; Steroidogenesis; Transmembrane; KW Transmembrane helix. FT CHAIN 1 369 3 beta-hydroxysteroid dehydrogenase type FT 7. FT /FTId=PRO_0000087792. FT TRANSMEM 289 309 Helical; (Potential). FT TRANSMEM 312 334 Helical; (Potential). FT ACT_SITE 159 159 Proton acceptor (By similarity). FT BINDING 163 163 NAD (By similarity). SQ SEQUENCE 369 AA; 41135 MW; 5857A690E0600F13 CRC64; MADSAQVPTL VYLVTGGCGF LGEHIVRMLL EREPRLRELR VFDLHLSSWL EELKAGPVQV TAIQGDVTQA HEVAAAMSGS HVVIHTAGLV DVFGKASPKT IHKVNVQGTQ NVIDACVQTG TQYLVYTSSM EVVGPNIKGH PFYRGNEDTP YEAVHSHPYP CSKALAEQLV LEANGRKVNG GLPLVTCALR PTGIYGEGHQ VMRDFYYQGL RFGGRLFRAV PASVEHGRVY VGNVAWMHIL VARELEQRAA LMGGQVYFCY DKSPYKSYED FNMEFLSPCG LRLIGAHPLL PYWLLVLLAT LNALLQWLLR PLVLYTPLLN PYTLAMANTT FTVSTNKAQR HFGYKPLFSW EESRTRTIQW VQAMEGSAR // ID 3HAO_MOUSE Reviewed; 286 AA. AC Q78JT3; Q52L88; DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 19-MAR-2014, entry version 93. DE RecName: Full=3-hydroxyanthranilate 3,4-dioxygenase; DE EC=1.13.11.6; DE AltName: Full=3-hydroxyanthranilate oxygenase; DE Short=3-HAO; DE AltName: Full=3-hydroxyanthranilic acid dioxygenase; DE Short=HAD; GN Name=Haao; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Liver; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=18630941; DOI=10.1021/pr800223m; RA Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.; RT "Specific phosphopeptide enrichment with immobilized titanium ion RT affinity chromatography adsorbent for phosphoproteome analysis."; RL J. Proteome Res. 7:3957-3967(2008). CC -!- FUNCTION: Catalyzes the oxidative ring opening of 3- CC hydroxyanthranilate to 2-amino-3-carboxymuconate semialdehyde, CC which spontaneously cyclizes to quinolinate (By similarity). CC -!- CATALYTIC ACTIVITY: 3-hydroxyanthranilate + O(2) = 2-amino-3- CC carboxymuconate semialdehyde. CC -!- COFACTOR: Fe(2+) ion (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate CC from L-kynurenine: step 3/3. CC -!- SUBUNIT: Monomer (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the 3-HAO family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BC012872; AAH12872.1; -; mRNA. DR EMBL; BC094021; AAH94021.1; -; mRNA. DR RefSeq; NP_079601.1; NM_025325.2. DR RefSeq; XP_006523526.1; XM_006523463.1. DR RefSeq; XP_006523527.1; XM_006523464.1. DR UniGene; Mm.30100; -. DR ProteinModelPortal; Q78JT3; -. DR SMR; Q78JT3; 2-284. DR MINT; MINT-1868896; -. DR PhosphoSite; Q78JT3; -. DR PaxDb; Q78JT3; -. DR PRIDE; Q78JT3; -. DR DNASU; 107766; -. DR Ensembl; ENSMUST00000000687; ENSMUSP00000000687; ENSMUSG00000000673. DR GeneID; 107766; -. DR KEGG; mmu:107766; -. DR UCSC; uc008dsk.1; mouse. DR CTD; 23498; -. DR MGI; MGI:1349444; Haao. DR eggNOG; NOG77058; -. DR GeneTree; ENSGT00390000013008; -. DR HOGENOM; HOG000218448; -. DR HOVERGEN; HBG000018; -. DR InParanoid; Q78JT3; -. DR KO; K00452; -. DR OMA; DMCLKVI; -. DR OrthoDB; EOG7FFMS4; -. DR TreeFam; TF300246; -. DR UniPathway; UPA00253; UER00330. DR NextBio; 359412; -. DR PRO; PR:Q78JT3; -. DR Bgee; Q78JT3; -. DR CleanEx; MM_HAAO; -. DR Genevestigator; Q78JT3; -. DR GO; GO:0005829; C:cytosol; IEA:Ensembl. DR GO; GO:0031966; C:mitochondrial membrane; IEA:Ensembl. DR GO; GO:0000334; F:3-hydroxyanthranilate 3,4-dioxygenase activity; IDA:MGI. DR GO; GO:0008198; F:ferrous iron binding; IEA:Ensembl. DR GO; GO:0019825; F:oxygen binding; IEA:Ensembl. DR GO; GO:0009435; P:NAD biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0070050; P:neuron cellular homeostasis; IEA:Ensembl. DR GO; GO:0046874; P:quinolinate metabolic process; IEA:Ensembl. DR GO; GO:0046686; P:response to cadmium ion; IEA:Ensembl. DR GO; GO:0010043; P:response to zinc ion; IEA:Ensembl. DR Gene3D; 2.60.120.10; -; 2. DR HAMAP; MF_00825; 3_HAO; 1. DR InterPro; IPR010329; 3hydroanth_dOase. DR InterPro; IPR016700; 3hydroanth_dOase_met. DR InterPro; IPR014710; RmlC-like_jellyroll. DR InterPro; IPR011051; RmlC_Cupin. DR Pfam; PF06052; 3-HAO; 1. DR PIRSF; PIRSF017681; 3hydroanth_dOase_animal; 1. DR SUPFAM; SSF51182; SSF51182; 2. DR TIGRFAMs; TIGR03037; anthran_nbaC; 1. PE 1: Evidence at protein level; KW Complete proteome; Cytoplasm; Dioxygenase; Iron; Metal-binding; KW Oxidoreductase; Pyridine nucleotide biosynthesis; Reference proteome. FT CHAIN 1 286 3-hydroxyanthranilate 3,4-dioxygenase. FT /FTId=PRO_0000064373. FT REGION 1 160 Domain A (catalytic) (By similarity). FT REGION 161 177 Linker (By similarity). FT REGION 178 286 Domain B (By similarity). FT METAL 47 47 Iron; catalytic (By similarity). FT METAL 53 53 Iron; catalytic (By similarity). FT METAL 91 91 Iron; catalytic (By similarity). FT BINDING 43 43 Dioxygen (By similarity). FT BINDING 53 53 Substrate (By similarity). FT BINDING 95 95 Substrate (By similarity). FT BINDING 105 105 Substrate (By similarity). SQ SEQUENCE 286 AA; 32804 MW; CD8A706EE264B4CD CRC64; MERRVRVKSW VEENRASFQP PVCNKLMHQE QLKIMFVGGP NTRKDYHIEE GEEVFYQLEG DMILRVLEQG QHRDVPIRQG EIFLLPARVP HSPQRFANTM GLVIERRRLE SELDGLRYYV GDTEDVLFEK WFHCKDLGTQ LAPIIQEFFH SEQYRTGKPN PDQLLKELPF PLNTRSIMKP MSLKAWLDGH SRELQAGTSL SLFGDSYETQ VIAHGQGSSK GPRQDVDVWL WQQEGSSKVT MGGQCIALAP DDSLLVPAGT SYVWERAQGS VALSVTQDPA RKKPWW // ID 3HIDH_MOUSE Reviewed; 335 AA. AC Q99L13; Q8BJY2; DT 27-JUN-2003, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 19-MAR-2014, entry version 108. DE RecName: Full=3-hydroxyisobutyrate dehydrogenase, mitochondrial; DE Short=HIBADH; DE EC=1.1.1.31; DE Flags: Precursor; GN Name=Hibadh; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Olfactory bulb; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-59; LYS-75; LYS-78; RP LYS-94; LYS-140; LYS-148; LYS-237; LYS-241; LYS-296 AND LYS-320, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., RA Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). RN [4] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-59; LYS-75; LYS-78; LYS-120; RP LYS-144; LYS-148; LYS-237; LYS-241 AND LYS-320, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23576753; DOI=10.1073/pnas.1302961110; RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., RA Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.; RT "Label-free quantitative proteomics of the lysine acetylome in RT mitochondria identifies substrates of SIRT3 in metabolic pathways."; RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013). CC -!- CATALYTIC ACTIVITY: 3-hydroxy-2-methylpropanoate + NAD(+) = 2- CC methyl-3-oxopropanoate + NADH. CC -!- PATHWAY: Amino-acid degradation; L-valine degradation. CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SUBCELLULAR LOCATION: Mitochondrion (By similarity). CC -!- SIMILARITY: Belongs to the 3-hydroxyisobutyrate dehydrogenase CC family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BC003914; AAH03914.1; -; mRNA. DR EMBL; AK078175; BAC37162.1; -; mRNA. DR RefSeq; NP_663542.1; NM_145567.1. DR UniGene; Mm.286458; -. DR ProteinModelPortal; Q99L13; -. DR SMR; Q99L13; 40-333. DR IntAct; Q99L13; 2. DR MINT; MINT-1841750; -. DR PhosphoSite; Q99L13; -. DR REPRODUCTION-2DPAGE; Q99L13; -. DR PaxDb; Q99L13; -. DR PRIDE; Q99L13; -. DR Ensembl; ENSMUST00000031788; ENSMUSP00000031788; ENSMUSG00000029776. DR GeneID; 58875; -. DR KEGG; mmu:58875; -. DR UCSC; uc009byw.1; mouse. DR CTD; 11112; -. DR MGI; MGI:1889802; Hibadh. DR eggNOG; COG2084; -. DR GeneTree; ENSGT00530000063270; -. DR HOGENOM; HOG000219610; -. DR HOVERGEN; HBG050424; -. DR InParanoid; Q99L13; -. DR KO; K00020; -. DR OMA; NIVHCGE; -. DR OrthoDB; EOG7NSB31; -. DR TreeFam; TF314043; -. DR UniPathway; UPA00362; -. DR ChiTaRS; HIBADH; mouse. DR NextBio; 314442; -. DR PRO; PR:Q99L13; -. DR Bgee; Q99L13; -. DR CleanEx; MM_HIBADH; -. DR Genevestigator; Q99L13; -. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR GO; GO:0008442; F:3-hydroxyisobutyrate dehydrogenase activity; ISS:UniProtKB. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR GO; GO:0004616; F:phosphogluconate dehydrogenase (decarboxylating) activity; IEA:InterPro. DR GO; GO:0006098; P:pentose-phosphate shunt; IEA:InterPro. DR GO; GO:0006574; P:valine catabolic process; ISS:UniProtKB. DR Gene3D; 1.10.1040.10; -; 1. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR002204; 3-OH-isobutyrate_DH-rel_CS. DR InterPro; IPR008927; 6-PGluconate_DH_C-like. DR InterPro; IPR006115; 6PGDH_NADP-bd. DR InterPro; IPR013328; DH_multihelical. DR InterPro; IPR015815; HIBADH-type. DR InterPro; IPR011548; IsoBut3OH_DH. DR InterPro; IPR016040; NAD(P)-bd_dom. DR PANTHER; PTHR22981; PTHR22981; 1. DR Pfam; PF03446; NAD_binding_2; 1. DR PIRSF; PIRSF000103; HIBADH; 1. DR SUPFAM; SSF48179; SSF48179; 1. DR TIGRFAMs; TIGR01692; HIBADH; 1. DR PROSITE; PS00895; 3_HYDROXYISOBUT_DH; 1. PE 1: Evidence at protein level; KW Acetylation; Branched-chain amino acid catabolism; Complete proteome; KW Mitochondrion; NAD; Oxidoreductase; Reference proteome; KW Transit peptide. FT TRANSIT 1 35 Mitochondrion (By similarity). FT CHAIN 36 335 3-hydroxyisobutyrate dehydrogenase, FT mitochondrial. FT /FTId=PRO_0000007159. FT NP_BIND 39 68 NAD (By similarity). FT NP_BIND 102 103 NAD (By similarity). FT ACT_SITE 208 208 By similarity. FT BINDING 107 107 NAD (By similarity). FT BINDING 133 133 NAD; via amide nitrogen (By similarity). FT BINDING 283 283 NAD (By similarity). FT MOD_RES 59 59 N6-acetyllysine; alternate. FT MOD_RES 59 59 N6-succinyllysine; alternate. FT MOD_RES 75 75 N6-acetyllysine; alternate. FT MOD_RES 75 75 N6-succinyllysine; alternate. FT MOD_RES 78 78 N6-acetyllysine; alternate. FT MOD_RES 78 78 N6-succinyllysine; alternate. FT MOD_RES 94 94 N6-succinyllysine. FT MOD_RES 120 120 N6-acetyllysine. FT MOD_RES 140 140 N6-succinyllysine. FT MOD_RES 144 144 N6-acetyllysine. FT MOD_RES 148 148 N6-acetyllysine; alternate. FT MOD_RES 148 148 N6-succinyllysine; alternate. FT MOD_RES 237 237 N6-acetyllysine; alternate. FT MOD_RES 237 237 N6-succinyllysine; alternate. FT MOD_RES 241 241 N6-acetyllysine; alternate. FT MOD_RES 241 241 N6-succinyllysine; alternate. FT MOD_RES 296 296 N6-succinyllysine. FT MOD_RES 320 320 N6-acetyllysine; alternate. FT MOD_RES 320 320 N6-succinyllysine; alternate. FT CONFLICT 2 2 A -> S (in Ref. 1; BAC37162). SQ SEQUENCE 335 AA; 35440 MW; 5E9ECB03997DB110 CRC64; MAASLGFRGA ASGLWYWSGR RRPVGSLAAV CSRSMASKTP VGFIGLGNMG NPMAKNLMKH GYPLILYDVF PDVCKEFKEA GEQVASSPAE VAEKADRIIT MLPSSMNAVE VYSGANGILK KVKKGSLLID SSTIDPSVSK ELAKEVEKMG AVFMDAPVSG GVGAARSGNL TFMVGGVEDE FAAAQELLEC MGSNVVYCGA VGTGQSAKIC NNMLLAISMI GTAEAMNLGI RSGLDPKLLA KILNMSSGRC WSSDTYNPVP GVMHGVPSSN NYQGGFGTTL MAKDLGLAQD SATSTKTPIL LGSLAHQIYR MMCSKGYSKK DFSSVFQYLR EEEPF // ID 6PGD_MOUSE Reviewed; 483 AA. AC Q9DCD0; Q3UD80; DT 15-MAY-2002, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 19-MAR-2014, entry version 110. DE RecName: Full=6-phosphogluconate dehydrogenase, decarboxylating; DE EC=1.1.1.44; GN Name=Pgd; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=BALB/c, and C57BL/6J; TISSUE=Bone marrow, and Kidney; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-38, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic fibroblast; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., RA Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). CC -!- FUNCTION: Catalyzes the oxidative decarboxylation of 6- CC phosphogluconate to ribulose 5-phosphate and CO(2), with CC concomitant reduction of NADP to NADPH (By similarity). CC -!- CATALYTIC ACTIVITY: 6-phospho-D-gluconate + NADP(+) = D-ribulose CC 5-phosphate + CO(2) + NADPH. CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D- CC ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): CC step 3/3. CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the 6-phosphogluconate dehydrogenase CC family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK002894; BAB22439.1; -; mRNA. DR EMBL; AK145602; BAE26535.1; -; mRNA. DR EMBL; AK150210; BAE29381.1; -; mRNA. DR EMBL; AK153409; BAE31969.1; -; mRNA. DR EMBL; AK155027; BAE32999.1; -; mRNA. DR EMBL; AK166733; BAE38978.1; -; mRNA. DR EMBL; AK166947; BAE39134.1; -; mRNA. DR EMBL; AK167215; BAE39341.1; -; mRNA. DR EMBL; AK168251; BAE40201.1; -; mRNA. DR RefSeq; NP_001074743.1; NM_001081274.1. DR UniGene; Mm.252080; -. DR ProteinModelPortal; Q9DCD0; -. DR SMR; Q9DCD0; 2-470. DR MINT; MINT-1868998; -. DR PhosphoSite; Q9DCD0; -. DR PaxDb; Q9DCD0; -. DR PRIDE; Q9DCD0; -. DR Ensembl; ENSMUST00000084124; ENSMUSP00000081141; ENSMUSG00000028961. DR GeneID; 110208; -. DR KEGG; mmu:110208; -. DR UCSC; uc008vvv.1; mouse. DR CTD; 5226; -. DR MGI; MGI:97553; Pgd. DR eggNOG; COG0362; -. DR GeneTree; ENSGT00390000009023; -. DR HOGENOM; HOG000255147; -. DR HOVERGEN; HBG000029; -. DR InParanoid; Q9DCD0; -. DR KO; K00033; -. DR OMA; PEHANEN; -. DR OrthoDB; EOG7K3TKV; -. DR TreeFam; TF300386; -. DR UniPathway; UPA00115; UER00410. DR ChiTaRS; PGD; mouse. DR NextBio; 363535; -. DR PRO; PR:Q9DCD0; -. DR Bgee; Q9DCD0; -. DR CleanEx; MM_PGD; -. DR Genevestigator; Q9DCD0; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0050661; F:NADP binding; IEA:InterPro. DR GO; GO:0004616; F:phosphogluconate dehydrogenase (decarboxylating) activity; ISS:UniProtKB. DR GO; GO:0019521; P:D-gluconate metabolic process; IEA:UniProtKB-KW. DR GO; GO:0019322; P:pentose biosynthetic process; IDA:MGI. DR GO; GO:0006098; P:pentose-phosphate shunt; ISS:UniProtKB. DR GO; GO:0009051; P:pentose-phosphate shunt, oxidative branch; IEA:Ensembl. DR Gene3D; 1.10.1040.10; -; 1. DR Gene3D; 1.20.5.320; -; 1. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR008927; 6-PGluconate_DH_C-like. DR InterPro; IPR006114; 6PGDH_C. DR InterPro; IPR006113; 6PGDH_decarbox. DR InterPro; IPR006115; 6PGDH_NADP-bd. DR InterPro; IPR006184; 6PGdom_BS. DR InterPro; IPR013328; DH_multihelical. DR InterPro; IPR012284; Fibritin/6PGD_C-extension. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Pfam; PF00393; 6PGD; 1. DR Pfam; PF03446; NAD_binding_2; 1. DR PIRSF; PIRSF000109; 6PGD; 1. DR SUPFAM; SSF48179; SSF48179; 1. DR TIGRFAMs; TIGR00873; gnd; 1. DR PROSITE; PS00461; 6PGD; 1. PE 1: Evidence at protein level; KW Acetylation; Complete proteome; Cytoplasm; Gluconate utilization; KW NADP; Oxidoreductase; Pentose shunt; Phosphoprotein; KW Reference proteome. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 483 6-phosphogluconate dehydrogenase, FT decarboxylating. FT /FTId=PRO_0000090064. FT NP_BIND 10 15 NADP (By similarity). FT NP_BIND 33 35 NADP (By similarity). FT NP_BIND 75 77 NADP (By similarity). FT NP_BIND 478 481 NADP; shared with dimeric partner (By FT similarity). FT REGION 129 131 Substrate binding (By similarity). FT REGION 187 188 Substrate binding (By similarity). FT ACT_SITE 184 184 Proton acceptor (By similarity). FT ACT_SITE 191 191 Proton donor (By similarity). FT BINDING 103 103 NADP (By similarity). FT BINDING 103 103 Substrate (By similarity). FT BINDING 192 192 Substrate (By similarity). FT BINDING 261 261 Substrate; via amide nitrogen (By FT similarity). FT BINDING 288 288 Substrate (By similarity). FT BINDING 447 447 Substrate; shared with dimeric partner FT (By similarity). FT BINDING 453 453 Substrate; shared with dimeric partner FT (By similarity). FT MOD_RES 38 38 N6-acetyllysine. FT MOD_RES 59 59 N6-acetyllysine (By similarity). FT MOD_RES 257 257 Phosphoserine (By similarity). FT MOD_RES 263 263 Phosphothreonine (By similarity). FT MOD_RES 267 267 Phosphothreonine (By similarity). FT MOD_RES 270 270 Phosphoserine (By similarity). SQ SEQUENCE 483 AA; 53247 MW; CD0A3F72EEC2831E CRC64; MAQADIALIG LAVMGQNLIL NMNDHGFVVC AFNRTVSKVD DFLANEAKGT KVVGAQSLKD MVSKLKKPRR VILLVKAGQA VDDFIEKLVP LLDTGDIIID GGNSEYRDTT RRCRDLKAKG ILFVGSGVSG GEEGARYGPS LMPGGNKEAW PHIKAIFQAI AAKVGTGEPC CDWVGDEGAG HFVKMVHNGI EYGDMQLICE AYHLMKDVLG MRHEEMAQAF EEWNKTELDS FLIEITANIL KYRDTDGKEL LPKIRDSAGQ KGTGKWTAIS ALEYGMPVTL IGEAVFARCL SSLKEERVQA SQKLKGPKVV QLEGSKKSFL EDIRKALYAS KIISYAQGFM LLRQAATEFG WTLNYGGIAL MWRGGCIIRS VFLGKIKDAF ERNPELQNLL LDDFFKSAVD NCQDSWRRVI STGVQAGIPM PCFTTALSFY DGYRHEMLPA NLIQAQRDYF GAHTYELLTK PGEFIHTNWT GHGGSVSSSS YNA // ID AASS_MOUSE Reviewed; 926 AA. AC Q99K67; Q9Z1I9; DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 19-MAR-2014, entry version 102. DE RecName: Full=Alpha-aminoadipic semialdehyde synthase, mitochondrial; DE AltName: Full=LKR/SDH; DE Includes: DE RecName: Full=Lysine ketoglutarate reductase; DE Short=LKR; DE Short=LOR; DE EC=1.5.1.8; DE Includes: DE RecName: Full=Saccharopine dehydrogenase; DE Short=SDH; DE EC=1.5.1.9; DE Flags: Precursor; GN Name=Aass; Synonyms=Lorsdh; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=C57BL/6J X CBA/J; TISSUE=Liver; RX PubMed=10567240; DOI=10.1042/0264-6021:3440555; RA Papes F., Kemper E.L., Cord-Neto G., Langone F., Arruda P.; RT "Lysine degradation through the saccharopine pathway in mammals: RT involvement of both bifunctional and monofunctional lysine-degrading RT enzymes in mouse."; RL Biochem. J. 344:555-563(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Mammary tumor; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-93; LYS-138; LYS-274; RP LYS-286; LYS-333; LYS-458; LYS-523; LYS-535; LYS-584; LYS-732 AND RP LYS-761, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Liver; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., RA Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). RN [4] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-48; LYS-52; LYS-56; LYS-93; RP LYS-128; LYS-138; LYS-286; LYS-458; LYS-523; LYS-535; LYS-584; RP LYS-707; LYS-739; LYS-761; LYS-778 AND LYS-780, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23576753; DOI=10.1073/pnas.1302961110; RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., RA Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.; RT "Label-free quantitative proteomics of the lysine acetylome in RT mitochondria identifies substrates of SIRT3 in metabolic pathways."; RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013). CC -!- FUNCTION: Bifunctional enzyme that catalyzes the first two steps CC in lysine degradation. The N-terminal and the C-terminal contain CC lysine-oxoglutarate reductase and saccharopine dehydrogenase CC activity, respectively. CC -!- CATALYTIC ACTIVITY: N(6)-(L-1,3-dicarboxypropyl)-L-lysine + CC NADP(+) + H(2)O = L-lysine + 2-oxoglutarate + NADPH. CC -!- CATALYTIC ACTIVITY: N(6)-(L-1,3-dicarboxypropyl)-L-lysine + NAD(+) CC + H(2)O = L-glutamate + (S)-2-amino-6-oxohexanoate + NADH. CC -!- PATHWAY: Amino-acid degradation; L-lysine degradation via CC saccharopine pathway; glutaryl-CoA from L-lysine: step 1/6. CC -!- PATHWAY: Amino-acid degradation; L-lysine degradation via CC saccharopine pathway; glutaryl-CoA from L-lysine: step 2/6. CC -!- SUBUNIT: Homodimer. CC -!- SUBCELLULAR LOCATION: Mitochondrion. CC -!- TISSUE SPECIFICITY: Both enzymes are highly expressed in kidney CC and liver, very low expression is seen in heart, brain, spleen, CC lung, skeletal muscle and testis. SDH was detected only in CC cortical regions of the kidney. CC -!- INDUCTION: Induced by starvation. CC -!- SIMILARITY: In the N-terminal section; belongs to the AlaDH/PNT CC family. CC -!- SIMILARITY: In the C-terminal section; belongs to the saccharopine CC dehydrogenase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJ224761; CAA12114.1; -; mRNA. DR EMBL; BC005420; AAH05420.1; -; mRNA. DR RefSeq; NP_038958.2; NM_013930.4. DR UniGene; Mm.18651; -. DR ProteinModelPortal; Q99K67; -. DR SMR; Q99K67; 30-424, 481-912. DR IntAct; Q99K67; 2. DR MINT; MINT-1840773; -. DR PhosphoSite; Q99K67; -. DR REPRODUCTION-2DPAGE; Q99K67; -. DR PaxDb; Q99K67; -. DR PRIDE; Q99K67; -. DR Ensembl; ENSMUST00000031707; ENSMUSP00000031707; ENSMUSG00000029695. DR GeneID; 30956; -. DR KEGG; mmu:30956; -. DR UCSC; uc009bbc.2; mouse. DR CTD; 10157; -. DR MGI; MGI:1353573; Aass. DR eggNOG; COG1748; -. DR GeneTree; ENSGT00390000013249; -. DR HOGENOM; HOG000252920; -. DR HOVERGEN; HBG048688; -. DR InParanoid; Q99K67; -. DR KO; K14157; -. DR OMA; ILKQEIR; -. DR OrthoDB; EOG7F7W7Z; -. DR TreeFam; TF105728; -. DR UniPathway; UPA00868; UER00835. DR UniPathway; UPA00868; UER00836. DR NextBio; 307440; -. DR PRO; PR:Q99K67; -. DR ArrayExpress; Q99K67; -. DR Bgee; Q99K67; -. DR CleanEx; MM_AASS; -. DR Genevestigator; Q99K67; -. DR GO; GO:0005739; C:mitochondrion; TAS:UniProtKB. DR GO; GO:0047131; F:saccharopine dehydrogenase (NAD+, L-glutamate-forming) activity; IDA:UniProtKB. DR GO; GO:0047130; F:saccharopine dehydrogenase (NADP+, L-lysine-forming) activity; IEA:UniProtKB-EC. DR GO; GO:0006091; P:generation of precursor metabolites and energy; TAS:UniProtKB. DR GO; GO:0019477; P:L-lysine catabolic process; IDA:MGI. DR GO; GO:0033512; P:L-lysine catabolic process to acetyl-CoA via saccharopine; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR007886; AlaDH/PNT_N. DR InterPro; IPR007698; AlaDH/PNT_NAD(H)-bd. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR005097; Saccharopine_DH/HSpermid_syn. DR Pfam; PF01262; AlaDh_PNT_C; 1. DR Pfam; PF05222; AlaDh_PNT_N; 1. DR Pfam; PF03435; Saccharop_dh; 1. DR SMART; SM01002; AlaDh_PNT_C; 1. DR SMART; SM01003; AlaDh_PNT_N; 1. PE 1: Evidence at protein level; KW Acetylation; Complete proteome; Mitochondrion; Multifunctional enzyme; KW NAD; NADP; Oxidoreductase; Reference proteome; Transit peptide. FT TRANSIT 1 32 Mitochondrion. FT CHAIN 33 926 Alpha-aminoadipic semialdehyde synthase, FT mitochondrial. FT /FTId=PRO_0000001053. FT REGION 33 455 Lysine-ketoglutarate reductase. FT REGION 477 926 Saccharopine dehydrogenase. FT MOD_RES 48 48 N6-acetyllysine. FT MOD_RES 52 52 N6-acetyllysine. FT MOD_RES 56 56 N6-acetyllysine. FT MOD_RES 93 93 N6-acetyllysine; alternate. FT MOD_RES 93 93 N6-succinyllysine; alternate. FT MOD_RES 128 128 N6-acetyllysine. FT MOD_RES 138 138 N6-acetyllysine; alternate. FT MOD_RES 138 138 N6-succinyllysine; alternate. FT MOD_RES 274 274 N6-succinyllysine. FT MOD_RES 286 286 N6-acetyllysine; alternate. FT MOD_RES 286 286 N6-succinyllysine; alternate. FT MOD_RES 333 333 N6-succinyllysine. FT MOD_RES 458 458 N6-acetyllysine; alternate. FT MOD_RES 458 458 N6-succinyllysine; alternate. FT MOD_RES 523 523 N6-acetyllysine; alternate. FT MOD_RES 523 523 N6-succinyllysine; alternate. FT MOD_RES 535 535 N6-acetyllysine; alternate. FT MOD_RES 535 535 N6-succinyllysine; alternate. FT MOD_RES 584 584 N6-acetyllysine; alternate. FT MOD_RES 584 584 N6-succinyllysine; alternate. FT MOD_RES 707 707 N6-acetyllysine. FT MOD_RES 732 732 N6-succinyllysine. FT MOD_RES 739 739 N6-acetyllysine. FT MOD_RES 761 761 N6-acetyllysine; alternate. FT MOD_RES 761 761 N6-succinyllysine; alternate. FT MOD_RES 778 778 N6-acetyllysine. FT MOD_RES 780 780 N6-acetyllysine. FT CONFLICT 198 198 V -> I (in Ref. 1; CAA12114). FT CONFLICT 851 851 L -> A (in Ref. 1; CAA12114). SQ SEQUENCE 926 AA; 102975 MW; 5B4369C51F7D1D53 CRC64; MLRAQRPRLA RLRACLSRGL HHKPVMALRR EDVNAWERRA PLAPKHIKGI TKLGYKVLIQ PSNRRAIHDK EYVRAGGILQ EDITEACLIL GVKRPPEEKL MSKKTYAFFS HTIKAQEANM NLLDEVLKQE IRLIDYEKMV DHRGSRIVAF GQWAGVAGMI NILHGMGLRL LALGHHTPFM HLGMAHNYRN SSQAVQAVRD AGYEISLGLM PKSIGPLTFV FTGTGNVSKG AQEVFNELPC EYVEPHELRE VSKTGDLRKV YGTVLSRHHH LVRKTDGVYD PVEYEKYPER YTSRFNTDIA PYTTCLINGI YWEQNTPRLL TRQDAQSLLV PVKSSVVPVE GCPELPHKLV AICDISADTG GSIDFMTECT TIERPFCMYD ADQQIIHDSV EGSGILMCSI DNLPAQLPIE ATEYFGDMLY PYVEEMLLSD ASQPLESQNF SPVVRDAVIT SNGLLTDKYK YIQKLRESRE RIQFLSMSTK KKVLVLGSGY VSGPVLEYLS RDNNIEITLG SDMTNQMQQL SKKYNINPVS LTVGKQEAKL QSLVESQDLV ISLLPYVLHP VVAKACIESR VNMVTASYIT PAMKELEKSV DDAGITVIGE LGLDPGLDHM LAMETIDTAK ELGATVESYV SYCGGLPAPE HSDNPLRYKF SWSPVGVLMN IMQPASYLLN GKVVNVTGGV SFLNSVTPMD YFPGLNLEGY PNRDSIKYAE IYGISSAHTL LRGTLRYKGY SKALNGFVKL GLINREAYPA LRPEANPLTW KQLLCDLVGI SRSSPCEKLK EVVFTKLGGD NTQLEAAEWL GLLGDEQVPQ AESIVDAFSK HLVSKLSYGP EEKDMIVMRD SFGIRHPSGH LENKTIDLVV YGDFNGFSAM AKTVGLPTAM AAKMLLDGEI EAKGLMGPFT KEIYGPILER IKAEGIVFNT QSTIKL // ID ACAD9_MOUSE Reviewed; 625 AA. AC Q8JZN5; Q3ULL9; Q8BK76; Q8C0B5; DT 03-JUL-2003, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 2. DT 19-MAR-2014, entry version 101. DE RecName: Full=Acyl-CoA dehydrogenase family member 9, mitochondrial; DE Short=ACAD-9; DE EC=1.3.99.-; DE Flags: Precursor; GN Name=Acad9; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Medulla oblongata; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Kidney; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-96; LYS-242 AND LYS-525, RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., RA Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). RN [4] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-525, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23576753; DOI=10.1073/pnas.1302961110; RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., RA Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.; RT "Label-free quantitative proteomics of the lysine acetylome in RT mitochondria identifies substrates of SIRT3 in metabolic pathways."; RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013). CC -!- FUNCTION: Has a dehydrogenase activity on palmitoyl-CoA (C16:0) CC and stearoyl-CoA (C18:0). It is three times more active on CC palmitoyl-CoA then on stearoyl-CoA. Has little activity on CC octanoyl-CoA (C8:0), butyryl-CoA (C4:0) or isovaleryl-CoA (5:0) CC (By similarity). CC -!- COFACTOR: FAD (By similarity). CC -!- SUBUNIT: Part of the mitochondrial complex I assembly (MCIA) CC complex. The complex comprises at least TMEM126B, NDUFAF1, ECSIT, CC and ACAD9 (By similarity). CC -!- SUBCELLULAR LOCATION: Mitochondrion (By similarity). CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK031820; BAC27565.1; -; mRNA. DR EMBL; AK075984; BAC36096.1; -; mRNA. DR EMBL; AK145423; BAE26429.1; -; mRNA. DR EMBL; BC031137; AAH31137.1; -; mRNA. DR EMBL; BC032213; AAH32213.1; -; mRNA. DR EMBL; BC033277; AAH33277.1; -; mRNA. DR RefSeq; NP_766266.3; NM_172678.3. DR UniGene; Mm.260997; -. DR ProteinModelPortal; Q8JZN5; -. DR SMR; Q8JZN5; 39-621. DR DIP; DIP-59192N; -. DR IntAct; Q8JZN5; 2. DR MINT; MINT-4086603; -. DR PhosphoSite; Q8JZN5; -. DR PaxDb; Q8JZN5; -. DR PRIDE; Q8JZN5; -. DR Ensembl; ENSMUST00000011492; ENSMUSP00000011492; ENSMUSG00000027710. DR GeneID; 229211; -. DR KEGG; mmu:229211; -. DR UCSC; uc008oze.1; mouse. DR CTD; 28976; -. DR MGI; MGI:1914272; Acad9. DR eggNOG; COG1960; -. DR GeneTree; ENSGT00740000114853; -. DR HOGENOM; HOG000131665; -. DR HOVERGEN; HBG050448; -. DR InParanoid; Q3ULL9; -. DR KO; K15980; -. DR OMA; GTTRGNK; -. DR OrthoDB; EOG712TVX; -. DR TreeFam; TF105053; -. DR NextBio; 379350; -. DR PRO; PR:Q8JZN5; -. DR ArrayExpress; Q8JZN5; -. DR Bgee; Q8JZN5; -. DR CleanEx; MM_ACAD9; -. DR Genevestigator; Q8JZN5; -. DR GO; GO:0030425; C:dendrite; IEA:Ensembl. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR GO; GO:0005634; C:nucleus; IEA:Ensembl. DR GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IEA:InterPro. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. DR Gene3D; 1.10.540.10; -; 1. DR Gene3D; 2.40.110.10; -; 1. DR InterPro; IPR006089; Acyl-CoA_DH_CS. DR InterPro; IPR006091; Acyl-CoA_Oxase/DH_cen-dom. DR InterPro; IPR009075; AcylCo_DH/oxidase_C. DR InterPro; IPR013786; AcylCoA_DH/ox_N. DR InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom. DR Pfam; PF00441; Acyl-CoA_dh_1; 1. DR Pfam; PF02770; Acyl-CoA_dh_M; 1. DR Pfam; PF02771; Acyl-CoA_dh_N; 1. DR SUPFAM; SSF47203; SSF47203; 2. DR SUPFAM; SSF56645; SSF56645; 1. DR PROSITE; PS00072; ACYL_COA_DH_1; 1. DR PROSITE; PS00073; ACYL_COA_DH_2; 1. PE 1: Evidence at protein level; KW Acetylation; Complete proteome; FAD; Flavoprotein; Mitochondrion; KW Oxidoreductase; Reference proteome; Transit peptide. FT TRANSIT 1 ? Mitochondrion (Potential). FT CHAIN ? 625 Acyl-CoA dehydrogenase family member 9, FT mitochondrial. FT /FTId=PRO_0000000525. FT ACT_SITE 430 430 Proton acceptor (By similarity). FT MOD_RES 45 45 N6-acetyllysine (By similarity). FT MOD_RES 96 96 N6-succinyllysine. FT MOD_RES 242 242 N6-succinyllysine. FT MOD_RES 525 525 N6-acetyllysine; alternate. FT MOD_RES 525 525 N6-succinyllysine; alternate. FT CONFLICT 15 15 A -> G (in Ref. 1; BAC27565). FT CONFLICT 53 53 E -> K (in Ref. 2; AAH31137/AAH32213/ FT AAH33277). FT CONFLICT 163 163 E -> D (in Ref. 2; AAH31137/AAH32213/ FT AAH33277). FT CONFLICT 540 540 I -> V (in Ref. 1; BAC27565). SQ SEQUENCE 625 AA; 68722 MW; 29567F60B52E6FEA CRC64; MSGCVLLSRG ATAAAAAARA SRVLREFTAR RRPLHTSLQS CSFAKELFLG NIEQKGVFPF PEVSQHELSE INQFVGPLEK FFTEEVDSRK IDQEGKIPVD TLEKLKSLGL FGIQVPEEYG GLGLSNTMYA RLGEIISLDA SITVTLAAHQ AIGLKGIILV GNEEQKAKYL PKLSSGEHIA AFCLTEPASG SDAASIQTRA TLSEDKKYFI LNGSKVWITN GGLANIFTVF AKTEVVDSDG SKTDKMTAFI VERDFGGITN GKPEDKLGIR GSNTCEVHFE NTRVPVENVL GEVGGGFKVA MNILNSGRFS MGSAVAGMLK KLIELTAEYA CTRKQFNRNL SEFGLIQEKF ALMAQKAYVM ESMAYLTSGM LDQPGFPDCS IEAAMVKVFS SEAAWQCVSE ALQILGGSGY MKDYPYERML RDARILLIFE GTNEILRLFI ALTGLQHAGR ILTSRIKELK SGNVTTVMET IGRKLRDSLG RTVDLGLTGD LGVVHPSLGD SANKLEENVH YFGRTVETLL LRFGKNIVEE QLVLKRVANI LINLYGMTAV LSRASRSIRI GLRNHDHEVL LANMFCVEAY FQNLFSLSQL DKNAPENLDE QIKKVSRQIL EKRAYICAHP LDRAS // ID ACAD8_MOUSE Reviewed; 413 AA. AC Q9D7B6; Q8BK36; Q8BKQ8; Q8CFY9; Q9D2L8; DT 28-NOV-2002, integrated into UniProtKB/Swiss-Prot. DT 16-MAY-2003, sequence version 2. DT 19-MAR-2014, entry version 106. DE RecName: Full=Isobutyryl-CoA dehydrogenase, mitochondrial; DE EC=1.3.99.-; DE AltName: Full=Acyl-CoA dehydrogenase family member 8; DE Short=ACAD-8; DE Flags: Precursor; GN Name=Acad8; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Embryo, Pituitary, Skin, Testis, and Tongue; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Liver; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-48; LYS-211 AND LYS-269, RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., RA Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). RN [4] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-48 AND LYS-229, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23576753; DOI=10.1073/pnas.1302961110; RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., RA Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.; RT "Label-free quantitative proteomics of the lysine acetylome in RT mitochondria identifies substrates of SIRT3 in metabolic pathways."; RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013). CC -!- FUNCTION: Has very high activity toward isobutyryl-CoA. Is an CC isobutyryl-CoA dehydrogenase that functions in valine catabolism CC (By similarity). CC -!- CATALYTIC ACTIVITY: Isobutyryl-CoA + ETF = methylacrylyl-CoA + CC reduced ETF. CC -!- COFACTOR: FAD (By similarity). CC -!- PATHWAY: Amino-acid degradation; L-valine degradation. CC -!- SUBUNIT: Homotetramer, formed by a dimer of dimers. Subunit of the CC large multiprotein complex ARC/DRIP (By similarity). CC -!- SUBCELLULAR LOCATION: Mitochondrion (By similarity). CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family. CC -!- SEQUENCE CAUTION: CC Sequence=BAC26664.1; Type=Erroneous initiation; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK009379; BAB26255.2; -; mRNA. DR EMBL; AK019502; BAB31764.1; -; mRNA. DR EMBL; AK029897; BAC26664.1; ALT_INIT; mRNA. DR EMBL; AK051091; BAC34521.1; -; mRNA. DR EMBL; AK077335; BAC36757.1; -; mRNA. DR EMBL; BC037644; AAH37644.1; -; mRNA. DR RefSeq; NP_080138.2; NM_025862.2. DR UniGene; Mm.289244; -. DR ProteinModelPortal; Q9D7B6; -. DR SMR; Q9D7B6; 30-413. DR IntAct; Q9D7B6; 2. DR MINT; MINT-1861259; -. DR STRING; 10090.ENSMUSP00000054370; -. DR PhosphoSite; Q9D7B6; -. DR PaxDb; Q9D7B6; -. DR PRIDE; Q9D7B6; -. DR Ensembl; ENSMUST00000060513; ENSMUSP00000054370; ENSMUSG00000031969. DR GeneID; 66948; -. DR KEGG; mmu:66948; -. DR UCSC; uc009opy.2; mouse. DR CTD; 27034; -. DR MGI; MGI:1914198; Acad8. DR eggNOG; COG1960; -. DR GeneTree; ENSGT00740000115026; -. DR HOGENOM; HOG000131659; -. DR HOVERGEN; HBG000224; -. DR KO; K11538; -. DR UniPathway; UPA00362; -. DR NextBio; 323096; -. DR PRO; PR:Q9D7B6; -. DR ArrayExpress; Q9D7B6; -. DR Bgee; Q9D7B6; -. DR CleanEx; MM_ACAD8; -. DR Genevestigator; Q9D7B6; -. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IEA:Ensembl. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. DR GO; GO:0006574; P:valine catabolic process; IEA:UniProtKB-UniPathway. DR Gene3D; 1.10.540.10; -; 1. DR Gene3D; 2.40.110.10; -; 1. DR InterPro; IPR006089; Acyl-CoA_DH_CS. DR InterPro; IPR006091; Acyl-CoA_Oxase/DH_cen-dom. DR InterPro; IPR009075; AcylCo_DH/oxidase_C. DR InterPro; IPR013786; AcylCoA_DH/ox_N. DR InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom. DR Pfam; PF00441; Acyl-CoA_dh_1; 1. DR Pfam; PF02770; Acyl-CoA_dh_M; 1. DR Pfam; PF02771; Acyl-CoA_dh_N; 1. DR SUPFAM; SSF47203; SSF47203; 1. DR SUPFAM; SSF56645; SSF56645; 1. DR PROSITE; PS00072; ACYL_COA_DH_1; 1. PE 1: Evidence at protein level; KW Acetylation; Branched-chain amino acid catabolism; Complete proteome; KW FAD; Flavoprotein; Mitochondrion; Oxidoreductase; Reference proteome; KW Transit peptide. FT TRANSIT 1 20 Mitochondrion (Potential). FT CHAIN 21 413 Isobutyryl-CoA dehydrogenase, FT mitochondrial. FT /FTId=PRO_0000000523. FT NP_BIND 155 165 FAD (By similarity). FT NP_BIND 156 165 FAD (By similarity). FT NP_BIND 189 191 FAD (By similarity). FT NP_BIND 310 311 FAD; shared with dimeric partner (By FT similarity). FT NP_BIND 369 375 FAD (By similarity). FT NP_BIND 398 400 FAD (By similarity). FT REGION 272 275 Substrate binding (By similarity). FT ACT_SITE 396 396 Proton acceptor (By similarity). FT BINDING 165 165 Substrate; via carbonyl oxygen (By FT similarity). FT BINDING 300 300 FAD (By similarity). FT BINDING 300 300 FAD; shared with dimeric partner (By FT similarity). FT BINDING 397 397 Substrate; via amide nitrogen (By FT similarity). FT BINDING 408 408 Substrate (By similarity). FT MOD_RES 48 48 N6-acetyllysine; alternate. FT MOD_RES 48 48 N6-succinyllysine; alternate. FT MOD_RES 211 211 N6-succinyllysine. FT MOD_RES 229 229 N6-acetyllysine. FT MOD_RES 269 269 N6-succinyllysine. FT CONFLICT 207 207 G -> E (in Ref. 1; BAB26255/BAB31764/ FT BAC26664/BAC34521/BAC36757). FT CONFLICT 254 254 A -> P (in Ref. 1; BAC34521). FT CONFLICT 413 413 D -> RLAPKLESLAWSLCAAGISLDAPMGCSVQVNHEVDQ FT RAELF (in Ref. 1; BAB31764). SQ SEQUENCE 413 AA; 45020 MW; 13DED42D4BD51231 CRC64; MAMLRSGYRR FGCLRAALKS LAQTHHRSIT FCIDPSLGLN EEQKGFQKVA FDFAAREMAP NMAEWDQKEL FPVDVMRKAA QLGFGGVYVR TDVGGSGLSR LDTSVIFEAL ATGCTSTTAY ISIHNMCAWM IDSFGNEEQR HKFCPPLCTM EKFASYCLTE PGSGSDAASL LTSAKQQGDH YILNGSKAFI SGGGESDIYV VMCRTGGSGA KGISCIVVEK GTPGLSFGKK EKKVGWNSQP TRAVIFEDCA VPVANRIGTE GQGFLIAMKG LNGGRINVAS CSLGAAHASV ILTQEHLKVR KQFGAPLARS QYLQFQLADM ATKLVASRLM IRTAAVALQE EREDAVALCS MAKLFATEEC FAICNQALQM HGGYGYLKDY AVQQYMRDSR VHQILEGSNE VMRMLISRNL LQD // ID ACADL_MOUSE Reviewed; 430 AA. AC P51174; B2KGC6; O35302; Q8QZR6; Q9CU29; Q9DB83; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 16-JUN-2003, sequence version 2. DT 19-MAR-2014, entry version 126. DE RecName: Full=Long-chain specific acyl-CoA dehydrogenase, mitochondrial; DE Short=LCAD; DE EC=1.3.8.8; DE Flags: Precursor; GN Name=Acadl; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=BALB/c; TISSUE=Liver; RX PubMed=8530022; DOI=10.1006/geno.1995.1127; RA Hinsdale M.E., Farmer S.C., Johnson K.R., Davisson M.T., Hamm D.A., RA Tolwani R.J., Wood P.A.; RT "RNA expression and chromosomal location of the mouse long-chain acyl- RT CoA dehydrogenase gene."; RL Genomics 28:163-170(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Cerebellum; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Kidney; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-201. RC STRAIN=129/Sv; RX PubMed=9545492; DOI=10.1007/s003359900770; RA Kurtz D.M., Tolwani R.J., Wood P.A.; RT "Structural characterization of the mouse long-chain acyl-CoA RT dehydrogenase gene and 5' regulatory region."; RL Mamm. Genome 9:361-365(1998). RN [6] RP ACETYLATION AT LYS-42; LYS-318 AND LYS-322, DEACETYLATION BY SIRT3, RP AND MUTAGENESIS OF LYS-42; LYS-318 AND LYS-322. RX PubMed=24121500; DOI=10.1074/jbc.M113.510354; RA Bharathi S.S., Zhang Y., Mohsen A.W., Uppala R., Balasubramani M., RA Schreiber E., Uechi G., Beck M.E., Rardin M.J., Vockley J., Verdin E., RA Gibson B.W., Hirschey M.D., Goetzman E.S.; RT "SIRT3 regulates long-chain acyl-coA dehydrogenase by deacetylating RT conserved lysines near the active site."; RL J. Biol. Chem. 288:33837-33847(2013). RN [7] RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-66; LYS-81; LYS-165; RP LYS-240; LYS-254; LYS-279 AND LYS-322, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., RA Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). RN [8] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-42; LYS-66; LYS-81; LYS-92; RP LYS-95; LYS-254; LYS-279; LYS-322 AND LYS-358, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23576753; DOI=10.1073/pnas.1302961110; RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., RA Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.; RT "Label-free quantitative proteomics of the lysine acetylome in RT mitochondria identifies substrates of SIRT3 in metabolic pathways."; RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013). CC -!- CATALYTIC ACTIVITY: Long-chain-acyl-CoA + electron-transfer CC flavoprotein = long-chain-2,3-dehydroacyl-CoA + reduced electron- CC transfer flavoprotein. CC -!- COFACTOR: FAD. CC -!- PATHWAY: Lipid metabolism; mitochondrial fatty acid beta- CC oxidation. CC -!- SUBUNIT: Homotetramer. CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix. CC -!- PTM: Acetylation at Lys-318 and Lys-322 in proximity of the CC cofactor-binding sites strongly reduces catalytic activity. These CC sites are deacetylated by SIRT3. CC -!- MISCELLANEOUS: A number of straight-chain acyl-CoA dehydrogenases CC of different substrate specificities are present in mammalian CC tissues. CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U21489; AAC52329.1; -; mRNA. DR EMBL; AK005140; BAB23838.1; -; mRNA. DR EMBL; AK018319; BAB31161.1; -; mRNA. DR EMBL; CU302198; CAQ52312.1; -; Genomic_DNA. DR EMBL; BC027412; AAH27412.1; -; mRNA. DR EMBL; AH006178; AAC23587.1; -; Genomic_DNA. DR RefSeq; NP_031407.2; NM_007381.4. DR UniGene; Mm.2445; -. DR ProteinModelPortal; P51174; -. DR SMR; P51174; 51-426. DR IntAct; P51174; 2. DR MINT; MINT-1861818; -. DR PhosphoSite; P51174; -. DR PaxDb; P51174; -. DR PRIDE; P51174; -. DR Ensembl; ENSMUST00000027153; ENSMUSP00000027153; ENSMUSG00000026003. DR GeneID; 11363; -. DR KEGG; mmu:11363; -. DR UCSC; uc007bir.1; mouse. DR CTD; 33; -. DR MGI; MGI:87866; Acadl. DR eggNOG; COG1960; -. DR GeneTree; ENSGT00740000114853; -. DR HOGENOM; HOG000131659; -. DR HOVERGEN; HBG104903; -. DR InParanoid; B2KGC6; -. DR KO; K00255; -. DR OrthoDB; EOG77126W; -. DR TreeFam; TF105054; -. DR BRENDA; 1.3.99.13; 3474. DR UniPathway; UPA00660; -. DR ChiTaRS; ACADL; mouse. DR NextBio; 278636; -. DR PRO; PR:P51174; -. DR Bgee; P51174; -. DR CleanEx; MM_ACADL; -. DR Genevestigator; P51174; -. DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell. DR GO; GO:0031966; C:mitochondrial membrane; IEA:Ensembl. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR GO; GO:0000062; F:fatty-acyl-CoA binding; IEA:Ensembl. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:Ensembl. DR GO; GO:0004466; F:long-chain-acyl-CoA dehydrogenase activity; IMP:BHF-UCL. DR GO; GO:0016401; F:palmitoyl-CoA oxidase activity; IMP:BHF-UCL. DR GO; GO:0042413; P:carnitine catabolic process; IMP:BHF-UCL. DR GO; GO:0019254; P:carnitine metabolic process, CoA-linked; IMP:BHF-UCL. DR GO; GO:0033539; P:fatty acid beta-oxidation using acyl-CoA dehydrogenase; IMP:BHF-UCL. DR GO; GO:0042758; P:long-chain fatty acid catabolic process; IEA:Ensembl. DR GO; GO:0045717; P:negative regulation of fatty acid biosynthetic process; IMP:BHF-UCL. DR GO; GO:0046322; P:negative regulation of fatty acid oxidation; IMP:BHF-UCL. DR GO; GO:0051289; P:protein homotetramerization; IEA:Ensembl. DR GO; GO:0090181; P:regulation of cholesterol metabolic process; IMP:BHF-UCL. DR GO; GO:0001659; P:temperature homeostasis; IMP:BHF-UCL. DR Gene3D; 1.10.540.10; -; 1. DR Gene3D; 2.40.110.10; -; 1. DR InterPro; IPR006089; Acyl-CoA_DH_CS. DR InterPro; IPR006091; Acyl-CoA_Oxase/DH_cen-dom. DR InterPro; IPR009075; AcylCo_DH/oxidase_C. DR InterPro; IPR013786; AcylCoA_DH/ox_N. DR InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom. DR Pfam; PF00441; Acyl-CoA_dh_1; 1. DR Pfam; PF02770; Acyl-CoA_dh_M; 1. DR Pfam; PF02771; Acyl-CoA_dh_N; 1. DR SUPFAM; SSF47203; SSF47203; 1. DR SUPFAM; SSF56645; SSF56645; 1. DR PROSITE; PS00072; ACYL_COA_DH_1; 1. DR PROSITE; PS00073; ACYL_COA_DH_2; 1. PE 1: Evidence at protein level; KW Acetylation; Complete proteome; FAD; Fatty acid metabolism; KW Flavoprotein; Lipid metabolism; Mitochondrion; Oxidoreductase; KW Reference proteome; Transit peptide. FT TRANSIT 1 30 Mitochondrion (By similarity). FT CHAIN 31 430 Long-chain specific acyl-CoA FT dehydrogenase, mitochondrial. FT /FTId=PRO_0000000511. FT MOD_RES 42 42 N6-acetyllysine. FT MOD_RES 66 66 N6-acetyllysine; alternate. FT MOD_RES 66 66 N6-succinyllysine; alternate. FT MOD_RES 81 81 N6-acetyllysine; alternate. FT MOD_RES 81 81 N6-succinyllysine; alternate. FT MOD_RES 92 92 N6-acetyllysine. FT MOD_RES 95 95 N6-acetyllysine. FT MOD_RES 165 165 N6-succinyllysine. FT MOD_RES 240 240 N6-succinyllysine. FT MOD_RES 254 254 N6-acetyllysine; alternate. FT MOD_RES 254 254 N6-succinyllysine; alternate. FT MOD_RES 279 279 N6-acetyllysine; alternate. FT MOD_RES 279 279 N6-succinyllysine; alternate. FT MOD_RES 318 318 N6-acetyllysine. FT MOD_RES 322 322 N6-acetyllysine; alternate. FT MOD_RES 322 322 N6-succinyllysine; alternate. FT MOD_RES 358 358 N6-acetyllysine. FT MUTAGEN 42 42 K->R: Reduces activity by 90% when FT associated with R-318 and R-322. FT MUTAGEN 318 318 K->R: Reduces activity by 37%; reduces FT activity by 80% when associated with R- FT 322. FT MUTAGEN 322 322 K->R: Reduces activity by 23%; reduces FT activity by 80% when associated with R- FT 318. FT CONFLICT 14 15 KA -> RP (in Ref. 1; AAC52329 and 5; FT AAC23587). FT CONFLICT 14 14 K -> S (in Ref. 2; BAB23838). FT CONFLICT 19 20 PR -> TL (in Ref. 1; AAC52329). FT CONFLICT 22 22 P -> L (in Ref. 1; AAC52329 and 2; FT BAB23838). FT CONFLICT 25 25 A -> S (in Ref. 1; AAC52329). FT CONFLICT 32 32 A -> P (in Ref. 1; AAC52329). FT CONFLICT 35 35 R -> G (in Ref. 1; AAC52329). FT CONFLICT 47 47 V -> I (in Ref. 1; AAC52329 and 2; FT BAB23838). FT CONFLICT 58 58 D -> E (in Ref. 2; BAB31161). FT CONFLICT 131 132 GP -> RA (in Ref. 1; AAC52329). FT CONFLICT 135 135 S -> T (in Ref. 1; AAC52329). FT CONFLICT 225 225 S -> W (in Ref. 1; AAC52329). SQ SEQUENCE 430 AA; 47908 MW; 45CFED51640EAFFB CRC64; MAARLLLRSL RVLKARSAPR PPPSARCSHS GAEARLETPS AKKLTDVGIR RIFSSEHDIF RESVRKFFQE EVIPHHTEWE KAGEVSREVW EKAGKQGLLG INIAEKHGGI GGDLLSTAVT WEEQAYSNCT GPGFSLHSDI VMPYIANYGT KEQIEKFIPQ MTAGKCIGAI AMTEPGAGSD LQGVRTNAKR SGSDWILNGS KVFITNGWLS DLVIVVAVTN REARSPAHGI SLFLVENGMK GFIKGRKLHK MGMKAQDTAE LFFEDVRLPA NALLGEENKG FYYLMQELPQ ERLLIAELAI SACEFMFEET RNYVKQRKAF GKTVAHIQTV QHKLAELKTH ICVTRAFVDS CLQLHETKRL DSGSASMAKY WASELQNSVA YECVQLHGGW GYMWEYPIAK AYVDARVQPI YGGTNEIMKE LIARQIVSDS // ID ACADS_MOUSE Reviewed; 412 AA. AC Q07417; Q91W85; DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 2. DT 19-MAR-2014, entry version 125. DE RecName: Full=Short-chain specific acyl-CoA dehydrogenase, mitochondrial; DE Short=SCAD; DE EC=1.3.8.1; DE AltName: Full=Butyryl-CoA dehydrogenase; DE Flags: Precursor; GN Name=Acads; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=8276399; DOI=10.1006/geno.1993.1438; RA Kelly C.L., Hinsdale M.E., Wood P.A.; RT "Cloning and characterization of the mouse short-chain acyl-CoA RT dehydrogenase cDNA."; RL Genomics 18:137-140(1993). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J, and NOD; TISSUE=Heart; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Salivary gland; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-51; LYS-129; LYS-262 AND RP LYS-306, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Liver; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., RA Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). RN [6] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-51; LYS-72; LYS-129; RP LYS-208; LYS-262; LYS-292 AND LYS-306, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23576753; DOI=10.1073/pnas.1302961110; RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., RA Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.; RT "Label-free quantitative proteomics of the lysine acetylome in RT mitochondria identifies substrates of SIRT3 in metabolic pathways."; RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013). CC -!- CATALYTIC ACTIVITY: Butanoyl-CoA + electron-transfer flavoprotein CC = 2-butenoyl-CoA + reduced electron-transfer flavoprotein. CC -!- COFACTOR: FAD. CC -!- PATHWAY: Lipid metabolism; mitochondrial fatty acid beta- CC oxidation. CC -!- SUBUNIT: Homotetramer. CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix. CC -!- MISCELLANEOUS: A number of straight-chain acyl-CoA dehydrogenases CC of different substrate specificities are present in mammalian CC tissues. CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L11163; AAA16714.1; -; mRNA. DR EMBL; AK155361; BAE33217.1; -; mRNA. DR EMBL; AK169428; BAE41170.1; -; mRNA. DR EMBL; CH466529; EDL19883.1; -; Genomic_DNA. DR EMBL; BC016259; AAH16259.1; -; mRNA. DR PIR; I49605; I49605. DR RefSeq; NP_031409.2; NM_007383.3. DR UniGene; Mm.18759; -. DR ProteinModelPortal; Q07417; -. DR SMR; Q07417; 28-411. DR IntAct; Q07417; 5. DR MINT; MINT-4086625; -. DR STRING; 10090.ENSMUSP00000031524; -. DR PhosphoSite; Q07417; -. DR REPRODUCTION-2DPAGE; Q07417; -. DR PaxDb; Q07417; -. DR PRIDE; Q07417; -. DR Ensembl; ENSMUST00000031524; ENSMUSP00000031524; ENSMUSG00000029545. DR GeneID; 11409; -. DR KEGG; mmu:11409; -. DR UCSC; uc008zdb.1; mouse. DR CTD; 35; -. DR MGI; MGI:87868; Acads. DR eggNOG; COG1960; -. DR GeneTree; ENSGT00740000115026; -. DR HOGENOM; HOG000131659; -. DR HOVERGEN; HBG000224; -. DR InParanoid; Q91W85; -. DR KO; K00248; -. DR OMA; AMRCRAV; -. DR OrthoDB; EOG74FF0S; -. DR TreeFam; TF105019; -. DR UniPathway; UPA00660; -. DR NextBio; 278650; -. DR PRO; PR:Q07417; -. DR Bgee; Q07417; -. DR CleanEx; MM_ACADS; -. DR Genevestigator; Q07417; -. DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell. DR GO; GO:0031966; C:mitochondrial membrane; IEA:Ensembl. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IEA:InterPro. DR GO; GO:0004085; F:butyryl-CoA dehydrogenase activity; IEA:UniProtKB-EC. DR GO; GO:0000062; F:fatty-acyl-CoA binding; IEA:Ensembl. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. DR GO; GO:0046359; P:butyrate catabolic process; IEA:Ensembl. DR GO; GO:0033539; P:fatty acid beta-oxidation using acyl-CoA dehydrogenase; IEA:Ensembl. DR GO; GO:0051289; P:protein homotetramerization; IEA:Ensembl. DR GO; GO:0051384; P:response to glucocorticoid; IEA:Ensembl. DR GO; GO:0042594; P:response to starvation; IEA:Ensembl. DR Gene3D; 1.10.540.10; -; 1. DR Gene3D; 2.40.110.10; -; 1. DR InterPro; IPR006089; Acyl-CoA_DH_CS. DR InterPro; IPR006091; Acyl-CoA_Oxase/DH_cen-dom. DR InterPro; IPR009075; AcylCo_DH/oxidase_C. DR InterPro; IPR013786; AcylCoA_DH/ox_N. DR InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom. DR Pfam; PF00441; Acyl-CoA_dh_1; 1. DR Pfam; PF02770; Acyl-CoA_dh_M; 1. DR Pfam; PF02771; Acyl-CoA_dh_N; 1. DR SUPFAM; SSF47203; SSF47203; 1. DR SUPFAM; SSF56645; SSF56645; 1. DR PROSITE; PS00072; ACYL_COA_DH_1; 1. DR PROSITE; PS00073; ACYL_COA_DH_2; 1. PE 1: Evidence at protein level; KW Acetylation; Complete proteome; FAD; Fatty acid metabolism; KW Flavoprotein; Lipid metabolism; Mitochondrion; Oxidoreductase; KW Reference proteome; Transit peptide. FT TRANSIT 1 24 Mitochondrion (By similarity). FT CHAIN 25 412 Short-chain specific acyl-CoA FT dehydrogenase, mitochondrial. FT /FTId=PRO_0000000499. FT NP_BIND 152 161 FAD (By similarity). FT NP_BIND 185 187 FAD (By similarity). FT NP_BIND 365 369 FAD (By similarity). FT NP_BIND 365 369 FAD; shared with dimeric partner (By FT similarity). FT NP_BIND 394 396 FAD (By similarity). FT REGION 269 272 Substrate binding (By similarity). FT ACT_SITE 392 392 Proton acceptor (By similarity). FT BINDING 161 161 Substrate; via carbonyl oxygen (By FT similarity). FT BINDING 297 297 FAD (By similarity). FT BINDING 297 297 FAD; shared with dimeric partner (By FT similarity). FT BINDING 308 308 FAD (By similarity). FT BINDING 393 393 Substrate; via amide nitrogen (By FT similarity). FT MOD_RES 51 51 N6-acetyllysine; alternate. FT MOD_RES 51 51 N6-succinyllysine; alternate. FT MOD_RES 72 72 N6-acetyllysine. FT MOD_RES 129 129 N6-acetyllysine; alternate. FT MOD_RES 129 129 N6-succinyllysine; alternate. FT MOD_RES 208 208 N6-acetyllysine. FT MOD_RES 262 262 N6-acetyllysine; alternate. FT MOD_RES 262 262 N6-succinyllysine; alternate. FT MOD_RES 292 292 N6-acetyllysine. FT MOD_RES 306 306 N6-acetyllysine; alternate. FT MOD_RES 306 306 N6-succinyllysine; alternate. FT CONFLICT 94 94 D -> G (in Ref. 1; AAA16714). FT CONFLICT 348 348 A -> R (in Ref. 1; AAA16714). FT CONFLICT 369 369 G -> S (in Ref. 1; AAA16714). SQ SEQUENCE 412 AA; 44890 MW; 53DDE98661DF6333 CRC64; MAAALLARAR GPLRRALGVR DWRRLHTVYQ SVELPETHQM LRQTCRDFAE KELVPIAAQL DREHLFPTAQ VKKMGELGLL AMDVPEELSG AGLDYLAYSI ALEEISRACA STGVIMSVNN SLYLGPILKF GSAQQKQQWI TPFTNGDKIG CFALSEPGNG SDAGAASTTA REEGDSWVLN GTKAWITNSW EASATVVFAS TDRSRQNKGI SAFLVPMPTP GLTLGKKEDK LGIRASSTAN LIFEDCRIPK ENLLGEPGMG FKIAMQTLDM GRIGIASQAL GIAQASLDCA VKYAENRNAF GAPLTKLQNI QFKLADMALA LESARLLTWR AAMLKDNKKP FTKESAMAKL AASEAATAIS HQAIQILGGM GYVTEMPAER YYRDARITEI YEGTSEIQRL VIAGHLLRSY RS // ID ACADM_MOUSE Reviewed; 421 AA. AC P45952; Q64235; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 19-MAR-2014, entry version 132. DE RecName: Full=Medium-chain specific acyl-CoA dehydrogenase, mitochondrial; DE Short=MCAD; DE EC=1.3.8.7; DE Flags: Precursor; GN Name=Acadm; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=BALB/c; TISSUE=Liver; RX PubMed=7829081; DOI=10.1006/geno.1994.1486; RA Tolwani R.J., Farmer S.C., Wood P.A.; RT "Molecular cloning and characterization of the mouse medium-chain RT acyl-CoA dehydrogenase cDNA."; RL Genomics 23:247-249(1994). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 134-193. RX PubMed=1438358; RA Wood P.A., Farmer S.C., Tolwani R.J., Warren J.R., Steinkampf M.P., RA Johnson L.W., Mountz J.D., Kelly D.P.; RT "Molecular studies of mouse medium and long-chain acyl-CoA RT dehydrogenase genes for site-directed mutagenesis of embryonic stem RT cells."; RL Prog. Clin. Biol. Res. 375:151-160(1992). RN [3] RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-30; LYS-69; LYS-179; RP LYS-212; LYS-217; LYS-235; LYS-259 AND LYS-271, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., RA Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). RN [4] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-30; LYS-69; LYS-79; LYS-212; RP LYS-217; LYS-235; LYS-259; LYS-271 AND LYS-301, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23576753; DOI=10.1073/pnas.1302961110; RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., RA Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.; RT "Label-free quantitative proteomics of the lysine acetylome in RT mitochondria identifies substrates of SIRT3 in metabolic pathways."; RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013). CC -!- FUNCTION: This enzyme is specific for acyl chain lengths of 4 to CC 16. CC -!- CATALYTIC ACTIVITY: A medium-chain acyl-CoA + electron-transfer CC flavoprotein = a medium-chain trans-2,3-dehydroacyl-CoA + reduced CC electron-transfer flavoprotein. CC -!- COFACTOR: FAD (By similarity). CC -!- PATHWAY: Lipid metabolism; mitochondrial fatty acid beta- CC oxidation. CC -!- SUBUNIT: Homotetramer (By similarity). CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix (By similarity). CC -!- PTM: Acetylation at Lys-307 and Lys-311 in proximity of the CC cofactor-binding sites reduces catalytic activity. These sites are CC deacetylated by SIRT3 (By similarity). CC -!- MISCELLANEOUS: A number of straight-chain acyl-CoA dehydrogenases CC of different substrate specificities are present in mammalian CC tissues. CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U07159; AAA76733.1; -; mRNA. DR EMBL; S48761; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; S48759; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR PIR; A55724; A55724. DR RefSeq; NP_031408.1; NM_007382.5. DR UniGene; Mm.10530; -. DR ProteinModelPortal; P45952; -. DR SMR; P45952; 35-421. DR IntAct; P45952; 2. DR MINT; MINT-1860219; -. DR PhosphoSite; P45952; -. DR SWISS-2DPAGE; P45952; -. DR PaxDb; P45952; -. DR PRIDE; P45952; -. DR Ensembl; ENSMUST00000072697; ENSMUSP00000072483; ENSMUSG00000062908. DR GeneID; 11364; -. DR KEGG; mmu:11364; -. DR UCSC; uc008ruj.1; mouse. DR CTD; 34; -. DR MGI; MGI:87867; Acadm. DR eggNOG; COG1960; -. DR GeneTree; ENSGT00740000115026; -. DR HOGENOM; HOG000131659; -. DR HOVERGEN; HBG000224; -. DR InParanoid; P45952; -. DR KO; K00249; -. DR OMA; IAMGTFD; -. DR OrthoDB; EOG74FF0S; -. DR TreeFam; TF105020; -. DR UniPathway; UPA00660; -. DR NextBio; 278640; -. DR PRO; PR:P45952; -. DR ArrayExpress; P45952; -. DR Bgee; P45952; -. DR CleanEx; MM_ACADM; -. DR Genevestigator; P45952; -. DR GO; GO:0030424; C:axon; IEA:Ensembl. DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. DR GO; GO:0070991; F:medium-chain-acyl-CoA dehydrogenase activity; IMP:BHF-UCL. DR GO; GO:0055007; P:cardiac muscle cell differentiation; IMP:MGI. DR GO; GO:0045329; P:carnitine biosynthetic process; IEA:Ensembl. DR GO; GO:0019254; P:carnitine metabolic process, CoA-linked; IMP:BHF-UCL. DR GO; GO:0033539; P:fatty acid beta-oxidation using acyl-CoA dehydrogenase; IMP:BHF-UCL. DR GO; GO:0005978; P:glycogen biosynthetic process; IMP:BHF-UCL. DR GO; GO:0001889; P:liver development; IMP:MGI. DR GO; GO:0051793; P:medium-chain fatty acid catabolic process; IEA:Ensembl. DR GO; GO:0051791; P:medium-chain fatty acid metabolic process; IMP:BHF-UCL. DR GO; GO:0009791; P:post-embryonic development; IMP:MGI. DR GO; GO:0006111; P:regulation of gluconeogenesis; IMP:BHF-UCL. DR GO; GO:0009409; P:response to cold; IMP:MGI. DR GO; GO:0042594; P:response to starvation; IMP:MGI. DR Gene3D; 1.10.540.10; -; 1. DR Gene3D; 2.40.110.10; -; 1. DR InterPro; IPR006089; Acyl-CoA_DH_CS. DR InterPro; IPR006091; Acyl-CoA_Oxase/DH_cen-dom. DR InterPro; IPR009075; AcylCo_DH/oxidase_C. DR InterPro; IPR013786; AcylCoA_DH/ox_N. DR InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom. DR Pfam; PF00441; Acyl-CoA_dh_1; 1. DR Pfam; PF02770; Acyl-CoA_dh_M; 1. DR Pfam; PF02771; Acyl-CoA_dh_N; 1. DR SUPFAM; SSF47203; SSF47203; 1. DR SUPFAM; SSF56645; SSF56645; 1. DR PROSITE; PS00072; ACYL_COA_DH_1; 1. DR PROSITE; PS00073; ACYL_COA_DH_2; 1. PE 1: Evidence at protein level; KW Acetylation; Complete proteome; FAD; Fatty acid metabolism; KW Flavoprotein; Lipid metabolism; Mitochondrion; Oxidoreductase; KW Reference proteome; Transit peptide. FT TRANSIT 1 25 Mitochondrion (By similarity). FT CHAIN 26 421 Medium-chain specific acyl-CoA FT dehydrogenase, mitochondrial. FT /FTId=PRO_0000000504. FT NP_BIND 158 167 FAD (By similarity). FT NP_BIND 191 193 FAD (By similarity). FT NP_BIND 306 308 FAD (By similarity). FT NP_BIND 316 317 FAD (By similarity). FT NP_BIND 374 378 FAD (By similarity). FT NP_BIND 403 405 FAD (By similarity). FT REGION 278 281 Substrate binding (By similarity). FT ACT_SITE 401 401 Proton acceptor (By similarity). FT BINDING 167 167 Substrate; via carbonyl oxygen (By FT similarity). FT BINDING 402 402 Substrate; via amide nitrogen (By FT similarity). FT BINDING 413 413 Substrate (By similarity). FT MOD_RES 30 30 N6-acetyllysine; alternate. FT MOD_RES 30 30 N6-succinyllysine; alternate. FT MOD_RES 69 69 N6-acetyllysine; alternate. FT MOD_RES 69 69 N6-succinyllysine; alternate. FT MOD_RES 79 79 N6-acetyllysine. FT MOD_RES 179 179 N6-succinyllysine. FT MOD_RES 212 212 N6-acetyllysine; alternate. FT MOD_RES 212 212 N6-succinyllysine; alternate. FT MOD_RES 217 217 N6-acetyllysine; alternate. FT MOD_RES 217 217 N6-succinyllysine; alternate. FT MOD_RES 235 235 N6-acetyllysine; alternate. FT MOD_RES 235 235 N6-succinyllysine; alternate. FT MOD_RES 259 259 N6-acetyllysine; alternate. FT MOD_RES 259 259 N6-succinyllysine; alternate. FT MOD_RES 271 271 N6-acetyllysine; alternate. FT MOD_RES 271 271 N6-succinyllysine; alternate. FT MOD_RES 301 301 N6-acetyllysine. FT CONFLICT 135 135 L -> I (in Ref. 2; S48759). FT CONFLICT 184 184 V -> A (in Ref. 2; S48761). SQ SEQUENCE 421 AA; 46481 MW; 36976704E3E48CBB CRC64; MAAAFRRGCR VLRSVSHFEC RTQHSKAAHK QEPGLGFSFE LTEQQKEFQA TARKFAREEI IPVAPEYDKS GEYPFPLIKR AWELGLINAH IPESCGGLGL GTFDACLITE ELAYGCTGVQ TAIEANSLGQ MPVILAGNDQ QKKKYLGRMT EQPMMCAYCV TEPSAGSDVA AIKTKAEKKG DEYVINGQKM WITNGGKANW YFLLARSNPD PKVPASKAFT GFIVEADTPG IHIGKKELNM GQRCSDTRGI AFEDVRVPKE NVLIGEGAGF KIAMGAFDRT RPTVAAGAVG LAQRALDEAT KYALDRKTFG KLLVEHQGVS FLLAEMAMKV ELARLSYQRA AWEVDSGRRN TYYASIAKAF AGDIANQLAT DAVQIFGGYG FNTEYPVEKL MRDAKIYQIY EGTAQIQRLI IAREHIEKYK N // ID ACADV_MOUSE Reviewed; 656 AA. AC P50544; O35289; O55133; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2000, sequence version 3. DT 19-MAR-2014, entry version 126. DE RecName: Full=Very long-chain specific acyl-CoA dehydrogenase, mitochondrial; DE EC=1.3.8.9; DE AltName: Full=MVLCAD; DE Short=VLCAD; DE Flags: Precursor; GN Name=Acadvl; Synonyms=Vlcad; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=129/SvJ; TISSUE=Blood; RA Andresen B.S., Lund H., Bross P., Gregersen N.; RT "Mouse very-long-chain acyl-CoA dehydrogenase (VLCAD) gene."; RL Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=BALB/c; TISSUE=Heart; RA Andresen B., Lund H., Bross P., Corydon M., Gregersen N.; RT "Cloning and characterization of mouse very-long-chain acyl-CoA RT dehydrogenase."; RL Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Czech II; TISSUE=Mammary gland; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] OF 84-656. RC STRAIN=ICR; TISSUE=Liver; RX PubMed=9680378; DOI=10.1007/s003359900830; RA Cox K.B., Johnson K.R., Wood P.A.; RT "Chromosomal locations of the mouse fatty acid oxidation genes Cpt1a, RT Cpt1b, Cpt2, Acadvl, and metabolically related Crat gene."; RL Mamm. Genome 9:608-610(1998). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 339-656. RA Rao G., Krimer D., Krasikov T., Austin C., Skoultchi A.I.; RL Submitted (NOV-1995) to the EMBL/GenBank/DDBJ databases. RN [6] RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-332. RC TISSUE=Heart; RX PubMed=17451654; DOI=10.1016/j.bbrc.2007.04.015; RA Jeon H.B., Choi E.S., Yoon J.H., Hwang J.H., Chang J.W., Lee E.K., RA Choi H.W., Park Z.-Y., Yoo Y.J.; RT "A proteomics approach to identify the ubiquitinated proteins in mouse RT heart."; RL Biochem. Biophys. Res. Commun. 357:731-736(2007). RN [7] RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-72; LYS-128; LYS-196; RP LYS-240; LYS-269; LYS-277; LYS-279; LYS-332; LYS-373; LYS-483; LYS-557 RP AND LYS-640, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Embryonic fibroblast, and Liver; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., RA Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). RN [8] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-52; LYS-72; LYS-128; RP LYS-240; LYS-277; LYS-279; LYS-299; LYS-317; LYS-332; LYS-483; LYS-551 RP AND LYS-557, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Liver; RX PubMed=23576753; DOI=10.1073/pnas.1302961110; RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., RA Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.; RT "Label-free quantitative proteomics of the lysine acetylome in RT mitochondria identifies substrates of SIRT3 in metabolic pathways."; RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013). RN [9] RP S-NITROSYLATION AT CYS-238. RX PubMed=23281369; DOI=10.1126/scisignal.2003252; RA Doulias P.T., Tenopoulou M., Greene J.L., Raju K., Ischiropoulos H.; RT "Nitric oxide regulates mitochondrial Fatty Acid metabolism through RT reversible protein s-nitrosylation."; RL Sci. Signal. 6:RS1-RS1(2013). CC -!- FUNCTION: Active toward esters of long-chain and very long chain CC fatty acids such as palmitoyl-CoA, mysritoyl-CoA and stearoyl-CoA. CC Can accommodate substrate acyl chain lengths as long as 24 CC carbons, but shows little activity for substrates of less than 12 CC carbons (By similarity). CC -!- CATALYTIC ACTIVITY: A very-long-chain acyl-CoA + electron-transfer CC flavoprotein = a very-long-chain trans-2,3-dehydroacyl-CoA + CC reduced electron-transfer flavoprotein. CC -!- COFACTOR: FAD. CC -!- PATHWAY: Lipid metabolism; mitochondrial fatty acid beta- CC oxidation. CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane. CC -!- PTM: S-nitrosylation at Cys-238 in liver improves catalytic CC efficiency. CC -!- MISCELLANEOUS: A number of straight-chain acyl-CoA dehydrogenases CC of different substrate specificities are present in mammalian CC tissues. CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; Y11770; CAA72435.1; -; Genomic_DNA. DR EMBL; Z71189; CAA94919.2; -; mRNA. DR EMBL; BC026559; AAH26559.1; -; mRNA. DR EMBL; AF017176; AAC31642.1; -; mRNA. DR EMBL; U41497; AAA85185.1; -; mRNA. DR RefSeq; NP_059062.1; NM_017366.3. DR UniGene; Mm.18630; -. DR ProteinModelPortal; P50544; -. DR SMR; P50544; 70-655. DR BioGrid; 197914; 1. DR IntAct; P50544; 2. DR MINT; MINT-1860557; -. DR PhosphoSite; P50544; -. DR SWISS-2DPAGE; P50544; -. DR PaxDb; P50544; -. DR PRIDE; P50544; -. DR Ensembl; ENSMUST00000102574; ENSMUSP00000099634; ENSMUSG00000018574. DR GeneID; 11370; -. DR KEGG; mmu:11370; -. DR UCSC; uc007jto.1; mouse. DR CTD; 37; -. DR MGI; MGI:895149; Acadvl. DR eggNOG; COG1960; -. DR GeneTree; ENSGT00740000114853; -. DR HOGENOM; HOG000131665; -. DR HOVERGEN; HBG050448; -. DR InParanoid; P50544; -. DR KO; K09479; -. DR OMA; RNFRSIS; -. DR OrthoDB; EOG712TVX; -. DR TreeFam; TF105053; -. DR UniPathway; UPA00660; -. DR NextBio; 278646; -. DR PRO; PR:P50544; -. DR ArrayExpress; P50544; -. DR Bgee; P50544; -. DR CleanEx; MM_ACADVL; -. DR Genevestigator; P50544; -. DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell. DR GO; GO:0042645; C:mitochondrial nucleoid; IEA:Ensembl. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IEA:InterPro. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. DR GO; GO:0033539; P:fatty acid beta-oxidation using acyl-CoA dehydrogenase; IMP:BHF-UCL. DR GO; GO:0045717; P:negative regulation of fatty acid biosynthetic process; IMP:BHF-UCL. DR GO; GO:0046322; P:negative regulation of fatty acid oxidation; IMP:BHF-UCL. DR GO; GO:0090181; P:regulation of cholesterol metabolic process; IMP:BHF-UCL. DR GO; GO:0001659; P:temperature homeostasis; IMP:BHF-UCL. DR Gene3D; 1.10.540.10; -; 1. DR Gene3D; 2.40.110.10; -; 1. DR InterPro; IPR006089; Acyl-CoA_DH_CS. DR InterPro; IPR006091; Acyl-CoA_Oxase/DH_cen-dom. DR InterPro; IPR009075; AcylCo_DH/oxidase_C. DR InterPro; IPR013786; AcylCoA_DH/ox_N. DR InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom. DR Pfam; PF00441; Acyl-CoA_dh_1; 1. DR Pfam; PF02770; Acyl-CoA_dh_M; 1. DR Pfam; PF02771; Acyl-CoA_dh_N; 1. DR SUPFAM; SSF47203; SSF47203; 1. DR SUPFAM; SSF56645; SSF56645; 1. DR PROSITE; PS00072; ACYL_COA_DH_1; 1. DR PROSITE; PS00073; ACYL_COA_DH_2; 1. PE 1: Evidence at protein level; KW Acetylation; Complete proteome; FAD; Fatty acid metabolism; KW Flavoprotein; Isopeptide bond; Lipid metabolism; Membrane; KW Mitochondrion; Mitochondrion inner membrane; Oxidoreductase; KW Reference proteome; S-nitrosylation; Transit peptide; Ubl conjugation. FT TRANSIT 1 41 Mitochondrion (By similarity). FT CHAIN 42 656 Very long-chain specific acyl-CoA FT dehydrogenase, mitochondrial. FT /FTId=PRO_0000000517. FT NP_BIND 215 224 FAD (By similarity). FT NP_BIND 250 252 FAD (By similarity). FT NP_BIND 436 440 FAD (By similarity). FT NP_BIND 465 467 FAD (By similarity). FT REGION 42 483 Catalytic. FT REGION 339 342 Substrate binding (By similarity). FT REGION 463 464 Substrate binding (By similarity). FT REGION 484 517 Membrane-anchoring (Probable). FT ACT_SITE 463 463 Proton acceptor (By similarity). FT BINDING 224 224 Substrate; via carbonyl oxygen (By FT similarity). FT BINDING 367 367 FAD (By similarity). FT BINDING 464 464 Substrate; via amide nitrogen (By FT similarity). FT MOD_RES 52 52 N6-acetyllysine. FT MOD_RES 72 72 N6-acetyllysine; alternate. FT MOD_RES 72 72 N6-succinyllysine; alternate. FT MOD_RES 128 128 N6-acetyllysine; alternate. FT MOD_RES 128 128 N6-succinyllysine; alternate. FT MOD_RES 196 196 N6-succinyllysine. FT MOD_RES 238 238 S-nitrosocysteine. FT MOD_RES 240 240 N6-acetyllysine; alternate. FT MOD_RES 240 240 N6-succinyllysine; alternate. FT MOD_RES 269 269 N6-succinyllysine. FT MOD_RES 277 277 N6-acetyllysine; alternate. FT MOD_RES 277 277 N6-succinyllysine; alternate. FT MOD_RES 279 279 N6-acetyllysine; alternate. FT MOD_RES 279 279 N6-succinyllysine; alternate. FT MOD_RES 299 299 N6-acetyllysine. FT MOD_RES 317 317 N6-acetyllysine. FT MOD_RES 332 332 N6-acetyllysine; alternate. FT MOD_RES 332 332 N6-succinyllysine; alternate. FT MOD_RES 373 373 N6-succinyllysine. FT MOD_RES 483 483 N6-acetyllysine; alternate. FT MOD_RES 483 483 N6-succinyllysine; alternate. FT MOD_RES 551 551 N6-acetyllysine. FT MOD_RES 557 557 N6-acetyllysine; alternate. FT MOD_RES 557 557 N6-succinyllysine; alternate. FT MOD_RES 640 640 N6-succinyllysine. FT CROSSLNK 332 332 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in ubiquitin); FT alternate. FT CONFLICT 339 341 NNG -> GTR (in Ref. 5; AAA85185). FT CONFLICT 423 423 C -> W (in Ref. 5; AAA85185). FT CONFLICT 427 427 A -> G (in Ref. 5; AAA85185). FT CONFLICT 441 441 M -> I (in Ref. 5; AAA85185). FT CONFLICT 507 507 G -> A (in Ref. 5; AAA85185). FT CONFLICT 532 532 R -> P (in Ref. 5; AAA85185). FT CONFLICT 567 567 Q -> K (in Ref. 5; AAA85185). FT CONFLICT 570 571 AD -> GG (in Ref. 5; AAA85185). FT CONFLICT 573 573 A -> P (in Ref. 5; AAA85185). FT CONFLICT 593 593 G -> A (in Ref. 5; AAA85185). FT CONFLICT 596 596 T -> A (in Ref. 5; AAA85185). FT CONFLICT 612 612 A -> P (in Ref. 5; AAA85185). FT CONFLICT 628 628 H -> Q (in Ref. 4; AAC31642). SQ SEQUENCE 656 AA; 70875 MW; A0110CA5C6CF4F89 CRC64; MQSARMTPSV GRQLLRLGAR SSRSTTVLQG QPRPISAQRL YAREATQAVL DKPETLSSDA STREKPARAE SKSFAVGMFK GQLTIDQVFP YPSVLSEEQA QFLKELVGPV ARFFEEVNDP AKNDALEKVE DDTLQGLKEL GAFGLQVPSE LGGLGLSNTQ YARLAEIVGM HDLGVSVTLG AHQSIGFKGI LLYGTKAQRE KYLPRVASGQ ALAAFCLTEP SSGSDVASIR SSAIPSPCGK YYTLNGSKIW ISNGGLADIF TVFAKTPIKD AATGAVKEKI TAFVVERSFG GVTHGLPEKK MGIKASNTSE VYFDGVKVPS ENVLGEVGDG FKVAVNILNN GRFGMAATLA GTMKSLIAKA VDHATNRTQF GDKIHNFGVI QEKLARMAIL QYVTESMAYM LSANMDQGFK DFQIEAAISK IFCSEAAWKV ADECIQIMGG MGFMKEPGVE RVLRDIRIFR IFEGANDILR LFVALQGCMD KGKELTGLGN ALKNPFGNVG LLMGEAGKQL RRRTGIGSGL SLSGIVHPEL SRSGELAVQA LDQFATVVEA KLVKHKKGIV NEQFLLQRLA DGAIDLYAMV VVLSRASRSL SEGYPTAQHE KMLCDSWCIE AATRIRENMA SLQSSPQHQE LFRNFRSISK AMVENGGLVT GNPLGI // ID ACD10_MOUSE Reviewed; 1069 AA. AC Q8K370; Q8BWQ0; Q8K313; DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2002, sequence version 1. DT 19-MAR-2014, entry version 102. DE RecName: Full=Acyl-CoA dehydrogenase family member 10; DE Short=ACAD-10; DE EC=1.3.99.-; GN Name=Acad10; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Liver; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Mammary tumor; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-413; LYS-427 AND LYS-1052, RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., RA Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). RN [4] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-427 AND LYS-1052, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23576753; DOI=10.1073/pnas.1302961110; RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., RA Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.; RT "Label-free quantitative proteomics of the lysine acetylome in RT mitochondria identifies substrates of SIRT3 in metabolic pathways."; RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013). CC -!- FUNCTION: Acyl-CoA dehydrogenase only active with R- and S-2- CC methyl-C15-CoA (By similarity). CC -!- CATALYTIC ACTIVITY: Acyl-CoA + acceptor = 2,3-dehydroacyl-CoA + CC reduced acceptor. CC -!- COFACTOR: FAD (By similarity). CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family. CC -!- SEQUENCE CAUTION: CC Sequence=AAH29047.1; Type=Erroneous initiation; CC Sequence=BAC34193.1; Type=Frameshift; Positions=59; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK050332; BAC34193.1; ALT_FRAME; mRNA. DR EMBL; BC027825; AAH27825.1; -; mRNA. DR EMBL; BC029047; AAH29047.1; ALT_INIT; mRNA. DR RefSeq; NP_082313.2; NM_028037.4. DR RefSeq; XP_006530521.1; XM_006530458.1. DR RefSeq; XP_006530523.1; XM_006530460.1. DR RefSeq; XP_006530524.1; XM_006530461.1. DR UniGene; Mm.45423; -. DR ProteinModelPortal; Q8K370; -. DR SMR; Q8K370; 41-599, 659-1055. DR IntAct; Q8K370; 2. DR MINT; MINT-1839952; -. DR STRING; 10090.ENSMUSP00000107400; -. DR PaxDb; Q8K370; -. DR PRIDE; Q8K370; -. DR Ensembl; ENSMUST00000031412; ENSMUSP00000031412; ENSMUSG00000029456. DR Ensembl; ENSMUST00000111770; ENSMUSP00000107400; ENSMUSG00000029456. DR GeneID; 71985; -. DR KEGG; mmu:71985; -. DR UCSC; uc008zjy.1; mouse. DR CTD; 80724; -. DR MGI; MGI:1919235; Acad10. DR eggNOG; COG1011; -. DR GeneTree; ENSGT00740000115026; -. DR HOGENOM; HOG000131666; -. DR HOVERGEN; HBG057142; -. DR InParanoid; Q8K370; -. DR KO; K11729; -. DR OMA; CMRLIGF; -. DR OrthoDB; EOG7JDQWS; -. DR TreeFam; TF333953; -. DR NextBio; 335134; -. DR Bgee; Q8K370; -. DR CleanEx; MM_ACAD10; -. DR Genevestigator; Q8K370; -. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IEA:InterPro. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. DR GO; GO:0016787; F:hydrolase activity; IEA:InterPro. DR GO; GO:0016772; F:transferase activity, transferring phosphorus-containing groups; IEA:InterPro. DR Gene3D; 1.10.150.240; -; 1. DR Gene3D; 1.10.540.10; -; 1. DR Gene3D; 2.40.110.10; -; 1. DR Gene3D; 3.40.50.1000; -; 1. DR InterPro; IPR006091; Acyl-CoA_Oxase/DH_cen-dom. DR InterPro; IPR009075; AcylCo_DH/oxidase_C. DR InterPro; IPR013786; AcylCoA_DH/ox_N. DR InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom. DR InterPro; IPR002575; Aminoglycoside_PTrfase. DR InterPro; IPR023214; HAD-like_dom. DR InterPro; IPR006439; HAD-SF_hydro_IA. DR InterPro; IPR011945; HAD-SF_ppase_IA/epoxid_hydro_N. DR InterPro; IPR011009; Kinase-like_dom. DR InterPro; IPR023198; PGP_dom2. DR Pfam; PF00441; Acyl-CoA_dh_1; 1. DR Pfam; PF02770; Acyl-CoA_dh_M; 1. DR Pfam; PF02771; Acyl-CoA_dh_N; 1. DR Pfam; PF01636; APH; 1. DR Pfam; PF13419; HAD_2; 1. DR PRINTS; PR00413; HADHALOGNASE. DR SUPFAM; SSF47203; SSF47203; 1. DR SUPFAM; SSF56112; SSF56112; 1. DR SUPFAM; SSF56645; SSF56645; 1. DR SUPFAM; SSF56784; SSF56784; 1. DR TIGRFAMs; TIGR02247; HAD-1A3-hyp; 1. DR TIGRFAMs; TIGR01509; HAD-SF-IA-v3; 1. PE 1: Evidence at protein level; KW Acetylation; Complete proteome; FAD; Flavoprotein; Oxidoreductase; KW Reference proteome. FT CHAIN 1 1069 Acyl-CoA dehydrogenase family member 10. FT /FTId=PRO_0000284771. FT NP_BIND 792 802 FAD (By similarity). FT BINDING 828 828 FAD (By similarity). FT BINDING 943 943 FAD (By similarity). FT BINDING 1013 1013 FAD (By similarity). FT BINDING 1044 1044 FAD (By similarity). FT MOD_RES 413 413 N6-succinyllysine. FT MOD_RES 427 427 N6-acetyllysine; alternate. FT MOD_RES 427 427 N6-succinyllysine; alternate. FT MOD_RES 1052 1052 N6-acetyllysine; alternate. FT MOD_RES 1052 1052 N6-succinyllysine; alternate. FT CONFLICT 511 512 IL -> MM (in Ref. 2; AAH29047). SQ SEQUENCE 1069 AA; 118979 MW; 27A4D0823FDAA3D5 CRC64; MLVRRLFQPS TLHWAWRTTA LNHPLGRHQG GLRWTHSGGR SYRAVIFDTG GVLVPSPGTV AVGWEVQNHV PSGTIVKAFI RGGDSGPWIR FIKGEITTEH FLEEFGRLCS EIAKTSVPVS SYFSLLTSEQ VTKQFPVMTQ AISQIRAKGL QTAVLTNNFH LSSGESFLPL DRKQFDVVVE SCLEGICKPD PRIFQLCLQR LSLQPSEAIF LDDLGSNLKV AASLGIHTIK VDRPETAVKE LEALLGFPLH LGVPNTRPVR KTMAIPQDAL EKYLKGLLGT HSTGPMELLQ FDHGQSNPTY YIRLADRQLV LRKKPSGTLL PSAHAIEREF RIMKALANAG VPVPTVLDLC EDSSIIGTPF YLMEYCPGII YKDPSLPGLE PSRREAIYTA MNQVLCRIHS VDLQATSLDS FGKQGDYIPR QVQTWTKQYR AAETSSIPAM ERLIQWLPLH LPRQQRTTLV HGDFRLDNLI FHPEKAEVLA VLDWELSTLG DPFADVAYSC LAYYLPSSFP ILRGFRDQDV TKLGIPTVEE YFRMYCLNMG IPPIDNWNFY MAFSFFRVAA ILQGVYKRSL TGQASSATAQ QSGKLTESMA ELAWDFATKE GFRVFKEMPA TKTLSRSYHA WAGPRSPRTP KGVRGHSTVA AASPSHEAKG GLVISPEGLS PAVRKLYEQL VQFIEQKVYP LEPELQRHQA SADRWSPSPL IEDLKEKAKA EGLWNLFLPL ETDPEKKYGA GLTNVEYAHL CEVMGMSLYA SEIFNCSAPD TGNMEILVRY GTEEQKARWL VPLLEGRIRS CFAMTEPQVA SSDASNIEAS IKEEDGCYVI NGHKWWTSGI LDPRCKLCVF MGKTDPQAPR HQQQSMLLVP MDSPGITVIR PLSVFGLEDP PGGHGEVRFK DVRVPKENIL LGPGRGFEIA QGRLGPGRIH HCMRLIGYSE RALALMKTRV MSRTAFGKPL VEQGTILADI ARSRVEIEQA RLLVLKAAHL MDVAGNKTAA LDIAMIKMVV PSMAYHVIDR AIQAFGAAGL SSDYPLAQFF GWARALRFAD GPDEVHQLTV AKMELKNQSR MQEPAVPRV // ID ACD11_MOUSE Reviewed; 779 AA. AC Q80XL6; Q8BK19; DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot. DT 31-OCT-2006, sequence version 2. DT 19-MAR-2014, entry version 98. DE RecName: Full=Acyl-CoA dehydrogenase family member 11; DE Short=ACAD-11; DE EC=1.3.99.-; GN Name=Acad11; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Embryo, and Placenta; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Liver; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP SUBCELLULAR LOCATION. RC TISSUE=Kidney; RX PubMed=17768142; DOI=10.1074/mcp.M700169-MCP200; RA Wiese S., Gronemeyer T., Ofman R., Kunze M., Grou C.P., Almeida J.A., RA Eisenacher M., Stephan C., Hayen H., Schollenberger L., Korosec T., RA Waterham H.R., Schliebs W., Erdmann R., Berger J., Meyer H.E., RA Just W., Azevedo J.E., Wanders R.J., Warscheid B.; RT "Proteomics characterization of mouse kidney peroxisomes by tandem RT mass spectrometry and protein correlation profiling."; RL Mol. Cell. Proteomics 6:2045-2057(2007). RN [4] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-210 AND TYR-323, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=17242355; DOI=10.1073/pnas.0609836104; RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; RT "Large-scale phosphorylation analysis of mouse liver."; RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). RN [5] RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-368 AND LYS-390, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., RA Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). RN [6] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-163; LYS-166; LYS-175 AND RP LYS-765, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Liver; RX PubMed=23576753; DOI=10.1073/pnas.1302961110; RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., RA Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.; RT "Label-free quantitative proteomics of the lysine acetylome in RT mitochondria identifies substrates of SIRT3 in metabolic pathways."; RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013). CC -!- FUNCTION: Acyl-CoA dehydrogenase, that exhibits maximal activity CC towards saturated C22-CoA (By similarity). CC -!- CATALYTIC ACTIVITY: Acyl-CoA + acceptor = 2,3-dehydroacyl-CoA + CC reduced acceptor. CC -!- COFACTOR: FAD (By similarity). CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SUBCELLULAR LOCATION: Peroxisome. Mitochondrion (By similarity). CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK077531; BAC36849.2; -; mRNA. DR EMBL; AK145561; BAE26511.1; -; mRNA. DR EMBL; AK145834; BAE26684.1; -; mRNA. DR EMBL; BC045199; AAH45199.1; -; mRNA. DR RefSeq; NP_780533.2; NM_175324.3. DR UniGene; Mm.269254; -. DR UniGene; Mm.41274; -. DR ProteinModelPortal; Q80XL6; -. DR SMR; Q80XL6; 17-356, 374-775. DR IntAct; Q80XL6; 2. DR MINT; MINT-4111042; -. DR PhosphoSite; Q80XL6; -. DR PaxDb; Q80XL6; -. DR PRIDE; Q80XL6; -. DR Ensembl; ENSMUST00000047799; ENSMUSP00000043424; ENSMUSG00000090150. DR GeneID; 102632; -. DR KEGG; mmu:102632; -. DR UCSC; uc009rhg.1; mouse. DR CTD; 84129; -. DR MGI; MGI:2143169; Acad11. DR eggNOG; COG0457; -. DR GeneTree; ENSGT00740000115026; -. DR HOGENOM; HOG000131666; -. DR HOVERGEN; HBG057142; -. DR KO; K11730; -. DR TreeFam; TF333953; -. DR ChiTaRS; ACAD11; mouse. DR NextBio; 355574; -. DR PRO; PR:Q80XL6; -. DR ArrayExpress; Q80XL6; -. DR Bgee; Q80XL6; -. DR Genevestigator; Q80XL6; -. DR GO; GO:0031966; C:mitochondrial membrane; IEA:Ensembl. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR GO; GO:0005634; C:nucleus; IEA:Ensembl. DR GO; GO:0005777; C:peroxisome; ISS:HGNC. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. DR GO; GO:0070991; F:medium-chain-acyl-CoA dehydrogenase activity; IEA:Ensembl. DR GO; GO:0016772; F:transferase activity, transferring phosphorus-containing groups; IEA:InterPro. DR GO; GO:0017099; F:very-long-chain-acyl-CoA dehydrogenase activity; IEA:Ensembl. DR GO; GO:0033539; P:fatty acid beta-oxidation using acyl-CoA dehydrogenase; IEA:Ensembl. DR Gene3D; 1.10.540.10; -; 1. DR Gene3D; 2.40.110.10; -; 1. DR InterPro; IPR006091; Acyl-CoA_Oxase/DH_cen-dom. DR InterPro; IPR009075; AcylCo_DH/oxidase_C. DR InterPro; IPR013786; AcylCoA_DH/ox_N. DR InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom. DR InterPro; IPR002575; Aminoglycoside_PTrfase. DR InterPro; IPR011009; Kinase-like_dom. DR Pfam; PF00441; Acyl-CoA_dh_1; 1. DR Pfam; PF02770; Acyl-CoA_dh_M; 1. DR Pfam; PF02771; Acyl-CoA_dh_N; 1. DR Pfam; PF01636; APH; 1. DR SUPFAM; SSF47203; SSF47203; 1. DR SUPFAM; SSF56112; SSF56112; 1. DR SUPFAM; SSF56645; SSF56645; 1. PE 1: Evidence at protein level; KW Acetylation; Complete proteome; FAD; Flavoprotein; Mitochondrion; KW Oxidoreductase; Peroxisome; Phosphoprotein; Reference proteome. FT CHAIN 1 779 Acyl-CoA dehydrogenase family member 11. FT /FTId=PRO_0000254146. FT NP_BIND 503 513 FAD (By similarity). FT NP_BIND 503 506 FAD (By similarity). FT NP_BIND 511 513 FAD (By similarity). FT NP_BIND 537 539 FAD (By similarity). FT NP_BIND 726 730 FAD; shared with dimeric partner (By FT similarity). FT NP_BIND 755 757 FAD (By similarity). FT REGION 628 631 Substrate binding (By similarity). FT BINDING 513 513 Substrate; via carbonyl oxygen (By FT similarity). FT BINDING 539 539 FAD (By similarity). FT BINDING 656 656 FAD (By similarity). FT BINDING 656 656 FAD; shared with dimeric partner (By FT similarity). FT BINDING 726 726 FAD (By similarity). FT BINDING 754 754 Substrate; via amide nitrogen (By FT similarity). FT BINDING 757 757 FAD (By similarity). FT MOD_RES 163 163 N6-acetyllysine. FT MOD_RES 166 166 N6-acetyllysine. FT MOD_RES 175 175 N6-acetyllysine. FT MOD_RES 210 210 Phosphoserine. FT MOD_RES 323 323 Phosphotyrosine. FT MOD_RES 368 368 N6-succinyllysine. FT MOD_RES 390 390 N6-succinyllysine. FT MOD_RES 765 765 N6-acetyllysine. FT CONFLICT 426 426 M -> I (in Ref. 1; BAC36849/BAE26511/ FT BAE26684). FT CONFLICT 555 555 T -> M (in Ref. 2; AAH45199). SQ SEQUENCE 779 AA; 87366 MW; ABE9D1919D23426E CRC64; METDVTSDTV EVLPQHKFDL RSLEAYLNQH LPGFGSDSRA VLTVTQYRSG QSNPTFFLQK GSQAYVLRKK PPGSLLPKAH KIDREFKIQK ALFSIGFPVA KPLLYCRDAS VIGTEFYVME HVQGRIFRDF SIPGVSSAER AAIYVSVAET LAWLHSLDIR SLKLDKYGTG VGYCKRQVST WTKQYQASAH QSIPAMDQLS TWLMKNLPDS DSEECLVHGD FKLDNIVFHP KECRVIAVLD WELSTFGHPL TDLAHLSLFY YWPRTLPMIN RGSHIPENTG IPLMEELISI YCHRRGIDPN LPNWNFFMAL SFFKLAGISQ GVYRRYLMGN NSSEDSFLTA NTVQPLAETG LQLSKRTLRT TPPQADAKSQ LFAQSRRGQE VLTRVKQFMK QHVFPAEKEV AEYYAQSGNS AEKWGHPLVI EKLKEMAKAE GLWNLFLPAV SGLSQVDYAL IAEETGKCFF APDVFNCQAP DTGNMEVLHL YGSEQQKKQW LEPLLRGDIT SVFCMTEPNV SSSDATNIEC TIQRDGGGYI VNGKKWWSSG AGNPKCKIAI VLGRTESPSA SRHRQHSMIL VPMDTPGVEL IRPLSVFGYM DNMHGGHWEV HFNHVRVPAS NLILGEGRGF EISQGRLGPG RIHHCMRTVG LAERILQIMC DRAVQREAFK KKLYEHEVVA HWIAKSRIAI EEIRLLTLKA AHSIDTLGSA SARKEIAMIK VAAPKAVCKI ADWAIQVHGG AGVSQDYPLA NMYAIIRTLR LADGPDEVHL SAIAKMELQD QARRLTARM // ID ACDSB_MOUSE Reviewed; 432 AA. AC Q9DBL1; DT 28-NOV-2002, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 19-MAR-2014, entry version 106. DE RecName: Full=Short/branched chain specific acyl-CoA dehydrogenase, mitochondrial; DE Short=SBCAD; DE EC=1.3.8.5; DE AltName: Full=2-methyl branched chain acyl-CoA dehydrogenase; DE Short=2-MEBCAD; DE AltName: Full=2-methylbutyryl-coenzyme A dehydrogenase; DE Short=2-methylbutyryl-CoA dehydrogenase; DE Flags: Precursor; GN Name=Acadsb; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Liver; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP PROTEIN SEQUENCE OF 348-355, AND MASS SPECTROMETRY. RC STRAIN=C57BL/6; TISSUE=Brain; RA Lubec G., Kang S.U.; RL Submitted (APR-2007) to UniProtKB. RN [3] RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-70; LYS-278 AND LYS-284, RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., RA Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). RN [4] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-70; LYS-284 AND LYS-426, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23576753; DOI=10.1073/pnas.1302961110; RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., RA Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.; RT "Label-free quantitative proteomics of the lysine acetylome in RT mitochondria identifies substrates of SIRT3 in metabolic pathways."; RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013). CC -!- FUNCTION: Has greatest activity toward short branched chain acyl- CC CoA derivative such as (s)-2-methylbutyryl-CoA, isobutyryl-CoA, CC and 2-methylhexanoyl-CoA as well as toward short straight chain CC acyl-CoAs such as butyryl-CoA and hexanoyl-CoA. Can use valproyl- CC CoA as substrate and may play a role in controlling the metabolic CC flux of valproic acid in the development of toxicity of this agent CC (By similarity). CC -!- CATALYTIC ACTIVITY: Acyl-CoA + acceptor = 2,3-dehydroacyl-CoA + CC reduced acceptor. CC -!- CATALYTIC ACTIVITY: 2-methylbutanoyl-CoA + electron-transfer CC flavoprotein = (E)-2-methylbut-2-enoyl-CoA + reduced electron- CC transfer flavoprotein + H(+). CC -!- COFACTOR: FAD (By similarity). CC -!- PATHWAY: Lipid metabolism; mitochondrial fatty acid beta- CC oxidation. CC -!- SUBUNIT: Homotetramer (By similarity). CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix (Probable). CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK004889; BAB23646.1; -; mRNA. DR RefSeq; NP_080102.1; NM_025826.4. DR UniGene; Mm.334274; -. DR UniGene; Mm.487956; -. DR ProteinModelPortal; Q9DBL1; -. DR SMR; Q9DBL1; 24-432. DR IntAct; Q9DBL1; 2. DR MINT; MINT-1861281; -. DR PhosphoSite; Q9DBL1; -. DR PaxDb; Q9DBL1; -. DR PRIDE; Q9DBL1; -. DR Ensembl; ENSMUST00000015829; ENSMUSP00000015829; ENSMUSG00000030861. DR GeneID; 66885; -. DR KEGG; mmu:66885; -. DR UCSC; uc009kbm.2; mouse. DR CTD; 36; -. DR MGI; MGI:1914135; Acadsb. DR eggNOG; COG1960; -. DR GeneTree; ENSGT00740000114853; -. DR HOGENOM; HOG000131659; -. DR HOVERGEN; HBG000224; -. DR KO; K09478; -. DR OrthoDB; EOG74FF0S; -. DR TreeFam; TF105055; -. DR UniPathway; UPA00660; -. DR NextBio; 322929; -. DR PRO; PR:Q9DBL1; -. DR ArrayExpress; Q9DBL1; -. DR Bgee; Q9DBL1; -. DR Genevestigator; Q9DBL1; -. DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IEA:InterPro. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. DR GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-KW. DR Gene3D; 1.10.540.10; -; 1. DR Gene3D; 2.40.110.10; -; 1. DR InterPro; IPR006089; Acyl-CoA_DH_CS. DR InterPro; IPR006091; Acyl-CoA_Oxase/DH_cen-dom. DR InterPro; IPR009075; AcylCo_DH/oxidase_C. DR InterPro; IPR013786; AcylCoA_DH/ox_N. DR InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom. DR Pfam; PF00441; Acyl-CoA_dh_1; 1. DR Pfam; PF02770; Acyl-CoA_dh_M; 1. DR Pfam; PF02771; Acyl-CoA_dh_N; 1. DR SUPFAM; SSF47203; SSF47203; 1. DR SUPFAM; SSF56645; SSF56645; 1. DR PROSITE; PS00072; ACYL_COA_DH_1; 1. DR PROSITE; PS00073; ACYL_COA_DH_2; 1. PE 1: Evidence at protein level; KW Acetylation; Complete proteome; Direct protein sequencing; FAD; KW Fatty acid metabolism; Flavoprotein; Lipid metabolism; Mitochondrion; KW Oxidoreductase; Reference proteome; Transit peptide. FT TRANSIT 1 33 Mitochondrion (By similarity). FT CHAIN 34 432 Short/branched chain specific acyl-CoA FT dehydrogenase, mitochondrial. FT /FTId=PRO_0000000520. FT NP_BIND 174 183 FAD (By similarity). FT NP_BIND 207 209 FAD (By similarity). FT NP_BIND 387 391 FAD; shared with dimeric partner (By FT similarity). FT NP_BIND 416 418 FAD (By similarity). FT REGION 229 230 Substrate binding (By similarity). FT REGION 291 294 Substrate binding (By similarity). FT ACT_SITE 414 414 Proton acceptor (By similarity). FT BINDING 183 183 Substrate; via carbonyl oxygen (By FT similarity). FT BINDING 283 283 Substrate (By similarity). FT BINDING 319 319 FAD; shared with dimeric partner (By FT similarity). FT BINDING 330 330 FAD; shared with dimeric partner (By FT similarity). FT BINDING 415 415 Substrate; via amide nitrogen (By FT similarity). FT MOD_RES 70 70 N6-acetyllysine; alternate. FT MOD_RES 70 70 N6-succinyllysine; alternate. FT MOD_RES 278 278 N6-succinyllysine. FT MOD_RES 284 284 N6-acetyllysine; alternate. FT MOD_RES 284 284 N6-succinyllysine; alternate. FT MOD_RES 426 426 N6-acetyllysine. SQ SEQUENCE 432 AA; 47874 MW; 0272723CE36BCC46 CRC64; MAVSALQLWR MGGLLRRRFP TCLSPWKIPP RVLKSSQPEA LVSLTNNAVA FAPLQTLTDE EIMMKQTVKK FAQEHVAPLV SSMDENSKME KSVIQGLFQQ GLMGIEVEAQ YGGTEASFFC SVLVIEELAK VDASVALLCD IQNTIINNLF RKHASEEQKA TYLPKLVTEK LGSFCLSEAG AGSDSFAMKT RADKSGNYYV LNGSKMWISH AEHAELFLVF ANVDPSSGYR GITCFLVDRD TEGFQIGKRE NKMGIRASST CQLTFENVKV PETNILGKIG HGYKYAIGSL NEGRIGIAAQ MLGLAQGCFD YTIPYIKERM QFGKRIFDFQ GLQHQVAQVA TQLEATRLLT YNAARLVEAG RPFIKEASMA KYYASEVAGL TTSKCIEWMG GVGYTKDYPV EKFFRDAKIG TIYEGASNIQ LNTIAKHIDA EY // ID ACOD1_MOUSE Reviewed; 355 AA. AC P13516; Q922I6; DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot. DT 06-JUN-2002, sequence version 2. DT 19-FEB-2014, entry version 135. DE RecName: Full=Acyl-CoA desaturase 1; DE EC=1.14.19.1; DE AltName: Full=Delta(9)-desaturase 1; DE Short=Delta-9 desaturase 1; DE AltName: Full=Fatty acid desaturase 1; DE AltName: Full=Stearoyl-CoA desaturase 1; GN Name=Scd1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC TISSUE=Adipocyte; RX PubMed=2903162; RA Ntambi J.M., Buhrow S.A., Kaestner K.H., Christy R.J., Sibley E., RA Kelly T.J. Jr., Lane M.D.; RT "Differentiation-induced gene expression in 3T3-L1 preadipocytes. RT Characterization of a differentially expressed gene encoding stearoyl- RT CoA desaturase."; RL J. Biol. Chem. 263:17291-17300(1988). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Mammary gland; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP SUBCELLULAR LOCATION, AND MEMBRANE TOPOLOGY. RX PubMed=16275639; DOI=10.1074/jbc.M508733200; RA Man W.C., Miyazaki M., Chu K., Ntambi J.M.; RT "Membrane topology of mouse stearoyl-CoA desaturase 1."; RL J. Biol. Chem. 281:1251-1260(2006). CC -!- FUNCTION: Terminal component of the liver microsomal stearyl-CoA CC desaturase system, that utilizes O(2) and electrons from reduced CC cytochrome b5 to catalyze the insertion of a double bond into a CC spectrum of fatty acyl-CoA substrates including palmitoyl-CoA and CC stearoyl-CoA. CC -!- CATALYTIC ACTIVITY: Stearoyl-CoA + 2 ferrocytochrome b5 + O(2) + 2 CC H(+) = oleoyl-CoA + 2 ferricytochrome b5 + 2 H(2)O. CC -!- COFACTOR: Iron. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass CC membrane protein. CC -!- DOMAIN: The histidine box domains may contain the active site CC and/or be involved in metal ion binding. CC -!- SIMILARITY: Belongs to the fatty acid desaturase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M21285; AAA40103.1; -; Genomic_DNA. DR EMBL; M21280; AAA40103.1; JOINED; Genomic_DNA. DR EMBL; M21281; AAA40103.1; JOINED; Genomic_DNA. DR EMBL; M21282; AAA40103.1; JOINED; Genomic_DNA. DR EMBL; M21283; AAA40103.1; JOINED; Genomic_DNA. DR EMBL; M21284; AAA40103.1; JOINED; Genomic_DNA. DR EMBL; BC007474; AAH07474.1; -; mRNA. DR EMBL; BC055453; AAH55453.1; -; mRNA. DR PIR; A32115; A32115. DR RefSeq; NP_033153.2; NM_009127.4. DR UniGene; Mm.267377; -. DR ProteinModelPortal; P13516; -. DR MINT; MINT-4996454; -. DR BindingDB; P13516; -. DR ChEMBL; CHEMBL5353; -. DR PhosphoSite; P13516; -. DR PaxDb; P13516; -. DR PRIDE; P13516; -. DR Ensembl; ENSMUST00000041331; ENSMUSP00000036936; ENSMUSG00000037071. DR GeneID; 20249; -. DR KEGG; mmu:20249; -. DR UCSC; uc008hpr.2; mouse. DR CTD; 20249; -. DR MGI; MGI:98239; Scd1. DR eggNOG; COG1398; -. DR HOGENOM; HOG000270352; -. DR HOVERGEN; HBG003367; -. DR InParanoid; P13516; -. DR KO; K00507; -. DR OMA; WNETWTN; -. DR OrthoDB; EOG7ZPNKS; -. DR TreeFam; TF313251; -. DR ChiTaRS; Scd1; mouse. DR NextBio; 297897; -. DR PRO; PR:P13516; -. DR ArrayExpress; P13516; -. DR Bgee; P13516; -. DR CleanEx; MM_SCD1; -. DR Genevestigator; P13516; -. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0004768; F:stearoyl-CoA 9-desaturase activity; IEA:UniProtKB-EC. DR GO; GO:0050873; P:brown fat cell differentiation; IDA:MGI. DR GO; GO:0034435; P:cholesterol esterification; IMP:MGI. DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IMP:MGI. DR GO; GO:0006633; P:fatty acid biosynthetic process; IMP:MGI. DR GO; GO:0044130; P:negative regulation of growth of symbiont in host; IMP:MGI. DR GO; GO:0010873; P:positive regulation of cholesterol esterification; TAS:BHF-UCL. DR GO; GO:0050872; P:white fat cell differentiation; IDA:MGI. DR InterPro; IPR005804; Fatty_acid_desaturase-1. DR InterPro; IPR001522; Fatty_acid_desaturase-1_C. DR InterPro; IPR015876; Fatty_acid_desaturase-1_core. DR Pfam; PF00487; FA_desaturase; 1. DR PRINTS; PR00075; FACDDSATRASE. DR PROSITE; PS00476; FATTY_ACID_DESATUR_1; 1. PE 1: Evidence at protein level; KW Complete proteome; Endoplasmic reticulum; Fatty acid biosynthesis; KW Fatty acid metabolism; Iron; Lipid biosynthesis; Lipid metabolism; KW Membrane; Oxidoreductase; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 355 Acyl-CoA desaturase 1. FT /FTId=PRO_0000185397. FT TOPO_DOM 1 67 Cytoplasmic (Potential). FT TRANSMEM 68 89 Helical; (Potential). FT TOPO_DOM 90 98 Lumenal (Potential). FT TRANSMEM 99 115 Helical; (Potential). FT TOPO_DOM 116 212 Cytoplasmic (Potential). FT TRANSMEM 213 231 Helical; (Potential). FT TOPO_DOM 232 246 Lumenal (Potential). FT TRANSMEM 247 269 Helical; (Potential). FT TOPO_DOM 270 355 Cytoplasmic (Potential). FT MOTIF 116 121 Histidine box-1. FT MOTIF 153 157 Histidine box-2. FT MOTIF 294 298 Histidine box-3. FT CONFLICT 97 97 C -> A (in Ref. 1; AAA40103). FT CONFLICT 148 148 E -> D (in Ref. 1; AAA40103). SQ SEQUENCE 355 AA; 41046 MW; 00E2348C1898FE75 CRC64; MPAHMLQEIS SSYTTTTTIT APPSGNEREK VKTVPLHLEE DIRPEMKEDI HDPTYQDEEG PPPKLEYVWR NIILMVLLHL GGLYGIILVP SCKLYTCLFG IFYYMTSALG ITAGAHRLWS HRTYKARLPL RIFLIIANTM AFQNDVYEWA RDHRAHHKFS ETHADPHNSR RGFFFSHVGW LLVRKHPAVK EKGGKLDMSD LKAEKLVMFQ RRYYKPGLLL MCFILPTLVP WYCWGETFVN SLFVSTFLRY TLVLNATWLV NSAAHLYGYR PYDKNIQSRE NILVSLGAVG EGFHNYHHTF PFDYSASEYR WHINFTTFFI DCMAALGLAY DRKKVSKATV LARIKRTGDG SHKSS // ID ACOD2_MOUSE Reviewed; 358 AA. AC P13011; Q8BH96; DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 2. DT 19-FEB-2014, entry version 122. DE RecName: Full=Acyl-CoA desaturase 2; DE EC=1.14.19.1; DE AltName: Full=Delta(9)-desaturase 2; DE Short=Delta-9 desaturase 2; DE AltName: Full=Fatty acid desaturase 2; DE AltName: Full=Stearoyl-CoA desaturase 2; GN Name=Scd2; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Adipocyte; RX PubMed=2570068; RA Kaestner K.H., Ntambi J.M., Kelly T.J. Jr., Lane M.D.; RT "Differentiation-induced gene expression in 3T3-L1 preadipocytes. A RT second differentially expressed gene encoding stearoyl-CoA RT desaturase."; RL J. Biol. Chem. 264:14755-14761(1989). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6, and C57BL/6J; TISSUE=Brain, and Spinal ganglion; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=129; TISSUE=Mammary tumor; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: Terminal component of the liver microsomal stearyl-CoA CC desaturase system, that utilizes O(2) and electrons from reduced CC cytochrome b5 to catalyze the insertion of a double bond into a CC spectrum of fatty acyl-CoA substrates including palmitoyl-CoA and CC stearoyl-CoA. CC -!- CATALYTIC ACTIVITY: Stearoyl-CoA + 2 ferrocytochrome b5 + O(2) + 2 CC H(+) = oleoyl-CoA + 2 ferricytochrome b5 + 2 H(2)O. CC -!- COFACTOR: Iron. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass CC membrane protein (Probable). CC -!- DOMAIN: The histidine box domains may contain the active site CC and/or be involved in metal ion binding. CC -!- SIMILARITY: Belongs to the fatty acid desaturase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M26270; AAA40094.1; -; mRNA. DR EMBL; AK083922; BAC39066.1; -; mRNA. DR EMBL; AK147406; BAE27893.1; -; mRNA. DR EMBL; CH466534; EDL41928.1; -; Genomic_DNA. DR EMBL; BC040384; AAH40384.1; -; mRNA. DR PIR; A36507; A36507. DR RefSeq; NP_033154.2; NM_009128.2. DR UniGene; Mm.487021; -. DR ProteinModelPortal; P13011; -. DR STRING; 10090.ENSMUSP00000026221; -. DR PhosphoSite; P13011; -. DR PaxDb; P13011; -. DR PRIDE; P13011; -. DR Ensembl; ENSMUST00000026221; ENSMUSP00000026221; ENSMUSG00000025203. DR GeneID; 20250; -. DR KEGG; mmu:20250; -. DR UCSC; uc008hpp.2; mouse. DR CTD; 20250; -. DR MGI; MGI:98240; Scd2. DR eggNOG; COG1398; -. DR GeneTree; ENSGT00530000063158; -. DR HOGENOM; HOG000270352; -. DR HOVERGEN; HBG003367; -. DR InParanoid; Q8BH96; -. DR KO; K00507; -. DR OMA; LTWEHIK; -. DR OrthoDB; EOG7ZPNKS; -. DR TreeFam; TF313251; -. DR BRENDA; 1.14.19.1; 3474. DR ChiTaRS; Scd2; mouse. DR NextBio; 297901; -. DR PRO; PR:P13011; -. DR Bgee; P13011; -. DR CleanEx; MM_SCD2; -. DR Genevestigator; P13011; -. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0004768; F:stearoyl-CoA 9-desaturase activity; IEA:UniProtKB-EC. DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW. DR InterPro; IPR005804; Fatty_acid_desaturase-1. DR InterPro; IPR001522; Fatty_acid_desaturase-1_C. DR InterPro; IPR015876; Fatty_acid_desaturase-1_core. DR Pfam; PF00487; FA_desaturase; 1. DR PRINTS; PR00075; FACDDSATRASE. DR PROSITE; PS00476; FATTY_ACID_DESATUR_1; 1. PE 2: Evidence at transcript level; KW Complete proteome; Endoplasmic reticulum; Fatty acid biosynthesis; KW Fatty acid metabolism; Iron; Lipid biosynthesis; Lipid metabolism; KW Membrane; Oxidoreductase; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 358 Acyl-CoA desaturase 2. FT /FTId=PRO_0000185398. FT TOPO_DOM 2 70 Cytoplasmic (Potential). FT TRANSMEM 71 92 Helical; (Potential). FT TOPO_DOM 93 101 Lumenal (Potential). FT TRANSMEM 102 118 Helical; (Potential). FT TOPO_DOM 119 215 Cytoplasmic (Potential). FT TRANSMEM 216 234 Helical; (Potential). FT TOPO_DOM 235 249 Lumenal (Potential). FT TRANSMEM 250 272 Helical; (Potential). FT TOPO_DOM 273 358 Cytoplasmic (Potential). FT MOTIF 119 124 Histidine box-1. FT MOTIF 156 160 Histidine box-2. FT MOTIF 297 301 Histidine box-3. FT CONFLICT 220 220 G -> D (in Ref. 1; AAA40094). FT CONFLICT 295 295 G -> R (in Ref. 1; AAA40094). SQ SEQUENCE 358 AA; 40916 MW; 3E04893F12E92A9A CRC64; MPAHILQEIS GAYSATTTIT APPSGGQQNG GEKFEKSSHH WGADVRPELK DDLYDPTYQD DEGPPPKLEY VWRNIILMAL LHLGALYGIT LVPSCKLYTC LFAYLYYVIS ALGITAGAHR LWSHRTYKAR LPLRLFLIIA NTMAFQNDVY EWARDHRAHH KFSETHADPH NSRRGFFFSH VGWLLVRKHP AVKEKGGKLD MSDLKAEKLV MFQRRYYKPG LLLMCFVLPT LVPWYCWGET FVNSLCVSTF LRYAVVLNAT WLVNSAAHLY GYRPYDKNIS SRENILVSMG AVGEGFHNYH HAFPYDYSAS EYRWHINFTT FFIDCMALLG LAYDRKRVSR AAVLARIKRT GDGSCKSG // ID ACOX1_MOUSE Reviewed; 661 AA. AC Q9R0H0; A2A850; O35616; Q3TDG0; Q8BYC3; DT 02-NOV-2001, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 5. DT 19-MAR-2014, entry version 117. DE RecName: Full=Peroxisomal acyl-coenzyme A oxidase 1; DE Short=AOX; DE EC=1.3.3.6; DE AltName: Full=Palmitoyl-CoA oxidase; GN Name=Acox1; Synonyms=Acox, Paox; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=10672038; DOI=10.1046/j.1432-1327.2000.01128.x; RA Nohammer C., El-Shabrawi Y., Schauer S., Hiden M., Berger J., RA Forss-Petter S., Winter E., Eferl R., Zechner R., Hoefler G.; RT "cDNA cloning and analysis of tissue-specific expression of mouse RT peroxisomal straight-chain acyl-CoA oxidase."; RL Eur. J. Biochem. 267:1254-1260(2000). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC STRAIN=C57BL/6; TISSUE=Liver; RA Saibara T., Adachi K.; RL Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC STRAIN=C57BL/6J, and NOD; TISSUE=Dendritic cell, and Thymus; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC STRAIN=C57BL/6; TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [7] RP TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE. RX PubMed=20195242; DOI=10.1038/labinvest.2010.46; RA Vluggens A., Andreoletti P., Viswakarma N., Jia Y., Matsumoto K., RA Kulik W., Khan M., Huang J., Guo D., Yu S., Sarkar J., Singh I., RA Rao M.S., Wanders R.J., Reddy J.K., Cherkaoui-Malki M.; RT "Reversal of mouse Acyl-CoA oxidase 1 (ACOX1) null phenotype by human RT ACOX1b isoform."; RL Lab. Invest. 90:696-708(2010). RN [8] RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-89; LYS-90; LYS-159; RP LYS-241; LYS-349; LYS-437; LYS-446; LYS-512; LYS-542; LYS-637; LYS-643 RP AND LYS-655, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Liver; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., RA Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). RN [9] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-65; LYS-216; LYS-267; RP LYS-272; LYS-437; LYS-446; LYS-512; LYS-637 AND LYS-652, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23576753; DOI=10.1073/pnas.1302961110; RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., RA Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.; RT "Label-free quantitative proteomics of the lysine acetylome in RT mitochondria identifies substrates of SIRT3 in metabolic pathways."; RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013). CC -!- FUNCTION: Catalyzes the desaturation of acyl-CoAs to 2-trans- CC enoyl-CoAs. Isoform 1 shows highest activity against medium-chain CC fatty acyl-CoAs and activity decreases with increasing chain CC length. Isoform 2 is active against a much broader range of CC substrates and shows activity towards very long-chain acyl-CoAs CC (By similarity). CC -!- CATALYTIC ACTIVITY: Acyl-CoA + O(2) = trans-2,3-dehydroacyl-CoA + CC H(2)O(2). CC -!- COFACTOR: FAD (By similarity). CC -!- PATHWAY: Lipid metabolism; peroxisomal fatty acid beta-oxidation. CC -!- SUBCELLULAR LOCATION: Peroxisome (By similarity). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9R0H0-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9R0H0-2; Sequence=VSP_042477; CC -!- TISSUE SPECIFICITY: Highest levels of isoform 1 are found in liver CC and kidney while highest levels of isoform 2 are found in white CC adipose tissue. Isoform 1 is expressed at higher levels than CC isoform 2 in liver and kidney while isoform 2 is expressed at CC higher levels in brain, heart, lung, muscle, white adipose tissue CC and testis. CC -!- DISRUPTION PHENOTYPE: Severe microvesicular hepatic steatosis, CC sustained activation of Ppara, spontaneous massive peroxisome CC proliferation and eventual development of hepatocellular CC carcinomas. CC -!- SIMILARITY: Belongs to the acyl-CoA oxidase family. CC -!- SEQUENCE CAUTION: CC Sequence=BAE41642.1; Type=Erroneous initiation; Note=Translation N-terminally extended; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF006688; AAB62926.1; -; mRNA. DR EMBL; AB034914; BAA86870.1; -; mRNA. DR EMBL; AK040566; BAC30628.1; -; mRNA. DR EMBL; AK170217; BAE41642.1; ALT_INIT; mRNA. DR EMBL; AL669925; CAM16380.1; -; Genomic_DNA. DR EMBL; AL607108; CAM16380.1; JOINED; Genomic_DNA. DR EMBL; AL669925; CAM16381.1; -; Genomic_DNA. DR EMBL; AL607108; CAM16381.1; JOINED; Genomic_DNA. DR EMBL; AL607108; CAM24036.1; -; Genomic_DNA. DR EMBL; AL669925; CAM24036.1; JOINED; Genomic_DNA. DR EMBL; AL607108; CAM24037.1; -; Genomic_DNA. DR EMBL; AL669925; CAM24037.1; JOINED; Genomic_DNA. DR EMBL; CH466558; EDL34562.1; -; Genomic_DNA. DR EMBL; CH466558; EDL34563.1; -; Genomic_DNA. DR EMBL; BC056448; AAH56448.1; -; mRNA. DR RefSeq; NP_001258827.1; NM_001271898.1. DR RefSeq; NP_056544.2; NM_015729.3. DR UniGene; Mm.356689; -. DR ProteinModelPortal; Q9R0H0; -. DR SMR; Q9R0H0; 1-655. DR IntAct; Q9R0H0; 4. DR MINT; MINT-1861412; -. DR PhosphoSite; Q9R0H0; -. DR PaxDb; Q9R0H0; -. DR PRIDE; Q9R0H0; -. DR Ensembl; ENSMUST00000066587; ENSMUSP00000063325; ENSMUSG00000020777. [Q9R0H0-2] DR Ensembl; ENSMUST00000072948; ENSMUSP00000072717; ENSMUSG00000020777. [Q9R0H0-1] DR GeneID; 11430; -. DR KEGG; mmu:11430; -. DR UCSC; uc007mkj.1; mouse. [Q9R0H0-1] DR UCSC; uc007mkl.1; mouse. [Q9R0H0-2] DR CTD; 51; -. DR MGI; MGI:1330812; Acox1. DR eggNOG; COG1960; -. DR GeneTree; ENSGT00530000062919; -. DR HOGENOM; HOG000181256; -. DR HOVERGEN; HBG050451; -. DR InParanoid; A2A850; -. DR KO; K00232; -. DR OMA; VHESYKH; -. DR OrthoDB; EOG7D59MV; -. DR TreeFam; TF300672; -. DR UniPathway; UPA00661; -. DR ChiTaRS; ACOX1; mouse. DR NextBio; 278708; -. DR PRO; PR:Q9R0H0; -. DR ArrayExpress; Q9R0H0; -. DR Bgee; Q9R0H0; -. DR CleanEx; MM_ACOX1; -. DR CleanEx; MM_PAOX; -. DR Genevestigator; Q9R0H0; -. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR GO; GO:0005778; C:peroxisomal membrane; IDA:MGI. DR GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IEA:InterPro. DR GO; GO:0003997; F:acyl-CoA oxidase activity; TAS:MGI. DR GO; GO:0071949; F:FAD binding; IEA:Ensembl. DR GO; GO:0005504; F:fatty acid binding; IEA:Ensembl. DR GO; GO:0016401; F:palmitoyl-CoA oxidase activity; IEA:Ensembl. DR GO; GO:0030165; F:PDZ domain binding; ISO:MGI. DR GO; GO:0006635; P:fatty acid beta-oxidation; TAS:MGI. DR GO; GO:0033540; P:fatty acid beta-oxidation using acyl-CoA oxidase; IEA:UniProtKB-UniPathway. DR GO; GO:0006091; P:generation of precursor metabolites and energy; IEA:Ensembl. DR GO; GO:0055088; P:lipid homeostasis; IEA:Ensembl. DR GO; GO:0016559; P:peroxisome fission; IEA:Ensembl. DR GO; GO:2000189; P:positive regulation of cholesterol homeostasis; IEA:Ensembl. DR GO; GO:0006693; P:prostaglandin metabolic process; IEA:Ensembl. DR GO; GO:0007283; P:spermatogenesis; IMP:MGI. DR GO; GO:0000038; P:very long-chain fatty acid metabolic process; IEA:Ensembl. DR Gene3D; 1.10.540.10; -; 1. DR Gene3D; 2.40.110.10; -; 1. DR InterPro; IPR006091; Acyl-CoA_Oxase/DH_cen-dom. DR InterPro; IPR012258; Acyl-CoA_oxidase. DR InterPro; IPR002655; Acyl-CoA_oxidase_C. DR InterPro; IPR009075; AcylCo_DH/oxidase_C. DR InterPro; IPR013786; AcylCoA_DH/ox_N. DR InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom. DR PANTHER; PTHR10909:SF11; PTHR10909:SF11; 1. DR Pfam; PF01756; ACOX; 1. DR Pfam; PF02770; Acyl-CoA_dh_M; 1. DR PIRSF; PIRSF000168; Acyl-CoA_oxidase; 1. DR SUPFAM; SSF47203; SSF47203; 2. DR SUPFAM; SSF56645; SSF56645; 1. PE 1: Evidence at protein level; KW Acetylation; Alternative splicing; Complete proteome; FAD; KW Fatty acid metabolism; Flavoprotein; Lipid metabolism; Oxidoreductase; KW Peroxisome; Phosphoprotein; Reference proteome. FT CHAIN 1 661 Peroxisomal acyl-coenzyme A oxidase 1. FT /FTId=PRO_0000204678. FT MOTIF 659 661 Microbody targeting signal. FT ACT_SITE 421 421 Proton acceptor (By similarity). FT BINDING 139 139 FAD (By similarity). FT BINDING 178 178 FAD; via amide nitrogen (By similarity). FT MOD_RES 26 26 Phosphoserine (By similarity). FT MOD_RES 65 65 N6-acetyllysine. FT MOD_RES 89 89 N6-succinyllysine. FT MOD_RES 90 90 N6-succinyllysine. FT MOD_RES 159 159 N6-succinyllysine. FT MOD_RES 216 216 N6-acetyllysine. FT MOD_RES 241 241 N6-succinyllysine. FT MOD_RES 255 255 N6-acetyllysine (By similarity). FT MOD_RES 267 267 N6-acetyllysine. FT MOD_RES 272 272 N6-acetyllysine. FT MOD_RES 349 349 N6-succinyllysine. FT MOD_RES 437 437 N6-acetyllysine; alternate. FT MOD_RES 437 437 N6-succinyllysine; alternate. FT MOD_RES 446 446 N6-acetyllysine; alternate. FT MOD_RES 446 446 N6-succinyllysine; alternate. FT MOD_RES 500 500 N6-acetyllysine (By similarity). FT MOD_RES 512 512 N6-acetyllysine; alternate. FT MOD_RES 512 512 N6-succinyllysine; alternate. FT MOD_RES 542 542 N6-succinyllysine. FT MOD_RES 637 637 N6-acetyllysine; alternate. FT MOD_RES 637 637 N6-succinyllysine; alternate. FT MOD_RES 643 643 N6-succinyllysine. FT MOD_RES 652 652 N6-acetyllysine. FT MOD_RES 655 655 N6-succinyllysine. FT VAR_SEQ 90 133 KLHMVNFVEPVGLNYSMFIPTLLNQGTTAQQEKWMHPSQEL FT QII -> NSVHRGHPEPLDLHLGMFLPTLLHQATEEQQERF FT FMPAWNLEIT (in isoform 2). FT /FTId=VSP_042477. FT CONFLICT 22 22 I -> V (in Ref. 1; AAB62926). FT CONFLICT 263 263 G -> D (in Ref. 3; BAE41642). FT CONFLICT 516 516 W -> R (in Ref. 3; BAE41642). FT CONFLICT 523 523 L -> I (in Ref. 3; BAE41642). FT CONFLICT 648 648 E -> Q (in Ref. 1; AAB62926). SQ SEQUENCE 661 AA; 74649 MW; 4140DB77A4CE7BE6 CRC64; MNPDLRKERA AATFNPELIT HILDGSPENT RRRREIENLI LNDPDFQHED YNFLTRSQRY EVAVKKSATM VKKMREFGIA DPEEIMWFKK LHMVNFVEPV GLNYSMFIPT LLNQGTTAQQ EKWMHPSQEL QIIGTYAQTE MGHGTHLRGL ETTATYDPKT QEFILNSPTV TSIKWWPGGL GKTSNHAIVL AQLITRGECY GLHAFVVPIR EIGTHKPLPG ITVGDIGPKF GYEEMDNGYL KMDNYRIPRE NMLMKYAQVK PDGTYVKPLS NKLTYGTMVF VRSFLVGSAA QSLSKACTIA IRYSAVRRQS EIKRSEPEPQ ILDFQTQQYK LFPLLATAYA FHFLGRYIKE TYMRINESIG QGDLSELPEL HALTAGLKAF TTWTANAGIE ECRMACGGHG YSHSSGIPNI YVTFTPACTF EGENTVMMLQ TARFLMKIYD QVQSGKLVGG MVSYLNDLPS QRIQPQQVAV WPTLVDINSL DSLTEAYKLR AARLVEIAAK NLQAQVSHRK SKEVAWNLTS VDLVRASEAH CHYVTVKVFA DKLPKIQDRA VQAVLRNLCL LYSLYGISQK GGDFLEGNII TGAQMSQVNS RILELLTVTR PNAVALVDAF DFKDVTLGSV LGRYDGNVYE NLFEWAKKSP LNKTEVHESY YKHLKPLQSK L // ID ACOX3_MOUSE Reviewed; 700 AA. AC Q9EPL9; Q7TPP6; Q80UQ0; DT 02-NOV-2001, integrated into UniProtKB/Swiss-Prot. DT 20-FEB-2007, sequence version 2. DT 19-MAR-2014, entry version 99. DE RecName: Full=Peroxisomal acyl-coenzyme A oxidase 3; DE EC=1.3.3.6; DE AltName: Full=Branched-chain acyl-CoA oxidase; DE Short=BRCACox; DE AltName: Full=Pristanoyl-CoA oxidase; GN Name=Acox3; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Van Veldhoven P.P., Ghys K.; RT "Cloning of the mouse pristanoyl-CoA oxidase."; RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N, and FVB/N-3; TISSUE=Liver, and Mammary tumor; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-505, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., RA Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). CC -!- FUNCTION: Oxidizes the CoA-esters of 2-methyl-branched fatty acids CC (By similarity). CC -!- CATALYTIC ACTIVITY: Acyl-CoA + O(2) = trans-2,3-dehydroacyl-CoA + CC H(2)O(2). CC -!- COFACTOR: FAD (By similarity). CC -!- PATHWAY: Lipid metabolism; peroxisomal fatty acid beta-oxidation. CC -!- SUBCELLULAR LOCATION: Peroxisome (Potential). CC -!- SIMILARITY: Belongs to the acyl-CoA oxidase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJ278430; CAC20692.1; -; mRNA. DR EMBL; BC044725; AAH44725.1; -; mRNA. DR EMBL; BC055019; AAH55019.1; -; mRNA. DR RefSeq; NP_109646.2; NM_030721.2. DR RefSeq; XP_006504261.1; XM_006504198.1. DR UniGene; Mm.291503; -. DR ProteinModelPortal; Q9EPL9; -. DR SMR; Q9EPL9; 21-668. DR STRING; 10090.ENSMUSP00000109876; -. DR PhosphoSite; Q9EPL9; -. DR PaxDb; Q9EPL9; -. DR PRIDE; Q9EPL9; -. DR Ensembl; ENSMUST00000068947; ENSMUSP00000063412; ENSMUSG00000029098. DR Ensembl; ENSMUST00000114237; ENSMUSP00000109875; ENSMUSG00000029098. DR GeneID; 80911; -. DR KEGG; mmu:80911; -. DR UCSC; uc008xdx.1; mouse. DR CTD; 8310; -. DR MGI; MGI:1933156; Acox3. DR eggNOG; COG1960; -. DR GeneTree; ENSGT00530000062919; -. DR HOGENOM; HOG000245077; -. DR HOVERGEN; HBG101107; -. DR KO; K00232; -. DR OrthoDB; EOG744T8F; -. DR TreeFam; TF314226; -. DR UniPathway; UPA00661; -. DR NextBio; 350282; -. DR PRO; PR:Q9EPL9; -. DR ArrayExpress; Q9EPL9; -. DR Bgee; Q9EPL9; -. DR CleanEx; MM_ACOX3; -. DR Genevestigator; Q9EPL9; -. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR GO; GO:0005782; C:peroxisomal matrix; TAS:MGI. DR GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IEA:InterPro. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. DR GO; GO:0016402; F:pristanoyl-CoA oxidase activity; TAS:MGI. DR GO; GO:0006635; P:fatty acid beta-oxidation; TAS:MGI. DR GO; GO:0033540; P:fatty acid beta-oxidation using acyl-CoA oxidase; IEA:UniProtKB-UniPathway. DR Gene3D; 2.40.110.10; -; 1. DR InterPro; IPR006091; Acyl-CoA_Oxase/DH_cen-dom. DR InterPro; IPR012258; Acyl-CoA_oxidase. DR InterPro; IPR002655; Acyl-CoA_oxidase_C. DR InterPro; IPR009075; AcylCo_DH/oxidase_C. DR InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom. DR PANTHER; PTHR10909:SF11; PTHR10909:SF11; 1. DR Pfam; PF01756; ACOX; 1. DR Pfam; PF00441; Acyl-CoA_dh_1; 1. DR Pfam; PF02770; Acyl-CoA_dh_M; 1. DR PIRSF; PIRSF000168; Acyl-CoA_oxidase; 1. DR SUPFAM; SSF47203; SSF47203; 2. DR SUPFAM; SSF56645; SSF56645; 1. PE 1: Evidence at protein level; KW Complete proteome; FAD; Fatty acid metabolism; Flavoprotein; KW Lipid metabolism; Oxidoreductase; Peroxisome; Phosphoprotein; KW Reference proteome. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 700 Peroxisomal acyl-coenzyme A oxidase 3. FT /FTId=PRO_0000204686. FT MOTIF 698 700 Microbody targeting signal (By FT similarity). FT MOD_RES 281 281 Phosphothreonine (By similarity). FT MOD_RES 505 505 N6-succinyllysine. FT CONFLICT 177 178 DP -> ES (in Ref. 1; CAC20692). FT CONFLICT 364 364 Y -> H (in Ref. 1; CAC20692). FT CONFLICT 408 409 KP -> NR (in Ref. 1; CAC20692). FT CONFLICT 555 555 C -> V (in Ref. 1; CAC20692). FT CONFLICT 576 576 H -> Y (in Ref. 2; AAH44725). FT CONFLICT 593 594 TL -> SV (in Ref. 1; CAC20692). FT CONFLICT 607 607 L -> S (in Ref. 1; CAC20692). FT CONFLICT 669 669 A -> R (in Ref. 1; CAC20692). FT CONFLICT 681 681 A -> R (in Ref. 1; CAC20692). SQ SEQUENCE 700 AA; 78404 MW; 85C448E38A4A0C67 CRC64; MGSLPEEKDS ALWSDTPKGP LSAYRARASF NSGELLLFWD GQDVIHFKKT IFSTLENDPL FARSYGADLP LEKLRELNFL RCKRVFEYGF FKVEELLKNP LKILVLINCL GMYDWSLANK CVLHMLVFGT TVFVSGSEKH FKYLEKIYSL EIFGCFALTE LSHGSNTKAM RTTAHYDPDT QEFILHSPDF EAAKFWVGNL GKTATHAVVF AQLYMPDGQC HGLHSFLVQI RDTKTLLPMT GVMVGDIGKK LGQNGLDNGF AMFNKVRIPR QNLLDRTGNI TSEGTYNSPF KDVRQRLGAS LGSLSSGRIS IISMSVVNLK LAVSIAIRFS ATRCQFGPTD KEEIPVLEYP LQQWRILPYL AAAYALDHFS KTIFMDLIEV QSARLRGDHS DQQAELGREI HALASAGKPL ASWTAQRGIQ ECREACGGHG YLAMNRFGDL RNDNDPNCTY EGDNNVLLQQ TSNYLLSLLE PPLQDGAHFT SPLKTVDFLE AYPGILGQKF LGSSKADWMD SAAPLAAYRW LVCYLLQESH RRYCQEKKSR GSDFEARNNS QVYGCRPLAL AFMELTVMQR FHEHIHSSGL SPSLRTVLGR LSTLYGLWCL SQHMALLYRG GYISGEQTGR AMEDAILTLC EQLKDDAVAL VDVIAPSDFV LNSPIAKADG ELYKNLWAAV LQQNGVLERA AWWPEFSANK SVADRLKSQL // ID ACOXL_MOUSE Reviewed; 632 AA. AC Q9DBS4; Q80ZM1; DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 19-MAR-2014, entry version 85. DE RecName: Full=Acyl-coenzyme A oxidase-like protein; DE Short=Acyl-CoA oxidase-like protein; DE EC=1.3.3.-; GN Name=Acoxl; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC STRAIN=C57BL/6J; TISSUE=Lung; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Embryo; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- COFACTOR: FAD (By similarity). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9DBS4-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9DBS4-2; Sequence=VSP_028240; CC -!- SIMILARITY: Belongs to the acyl-CoA oxidase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK004775; BAB23553.1; -; mRNA. DR EMBL; AL805950; CAM14740.1; -; Genomic_DNA. DR EMBL; AL844481; CAM14740.1; JOINED; Genomic_DNA. DR EMBL; AL805950; CAM14741.1; -; Genomic_DNA. DR EMBL; AL844481; CAM14741.1; JOINED; Genomic_DNA. DR EMBL; AL844481; CAM24669.1; -; Genomic_DNA. DR EMBL; AL805950; CAM24669.1; JOINED; Genomic_DNA. DR EMBL; AL844481; CAM24670.1; -; Genomic_DNA. DR EMBL; AL805950; CAM24670.1; JOINED; Genomic_DNA. DR EMBL; BC048717; AAH48717.1; -; mRNA. DR RefSeq; NP_083041.1; NM_028765.3. DR UniGene; Mm.244835; -. DR ProteinModelPortal; Q9DBS4; -. DR SMR; Q9DBS4; 28-596. DR PhosphoSite; Q9DBS4; -. DR PaxDb; Q9DBS4; -. DR PRIDE; Q9DBS4; -. DR Ensembl; ENSMUST00000028859; ENSMUSP00000028859; ENSMUSG00000027380. [Q9DBS4-1] DR Ensembl; ENSMUST00000110344; ENSMUSP00000105973; ENSMUSG00000027380. [Q9DBS4-2] DR GeneID; 74121; -. DR KEGG; mmu:74121; -. DR UCSC; uc008mgg.2; mouse. [Q9DBS4-1] DR CTD; 55289; -. DR MGI; MGI:1921371; Acoxl. DR eggNOG; COG1960; -. DR GeneTree; ENSGT00530000062919; -. DR HOGENOM; HOG000245077; -. DR HOVERGEN; HBG105796; -. DR InParanoid; Q9DBS4; -. DR OMA; HKYLTPM; -. DR OrthoDB; EOG7NSB1S; -. DR TreeFam; TF354292; -. DR NextBio; 339830; -. DR PRO; PR:Q9DBS4; -. DR Bgee; Q9DBS4; -. DR CleanEx; MM_ACOXL; -. DR Genevestigator; Q9DBS4; -. DR GO; GO:0005777; C:peroxisome; IEA:InterPro. DR GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IEA:InterPro. DR GO; GO:0003997; F:acyl-CoA oxidase activity; IEA:InterPro. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. DR GO; GO:0006635; P:fatty acid beta-oxidation; IEA:InterPro. DR Gene3D; 2.40.110.10; -; 1. DR InterPro; IPR006091; Acyl-CoA_Oxase/DH_cen-dom. DR InterPro; IPR012258; Acyl-CoA_oxidase. DR InterPro; IPR002655; Acyl-CoA_oxidase_C. DR InterPro; IPR009075; AcylCo_DH/oxidase_C. DR InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom. DR PANTHER; PTHR10909:SF11; PTHR10909:SF11; 1. DR Pfam; PF01756; ACOX; 1. DR Pfam; PF00441; Acyl-CoA_dh_1; 1. DR Pfam; PF02770; Acyl-CoA_dh_M; 1. DR PIRSF; PIRSF000168; Acyl-CoA_oxidase; 1. DR SUPFAM; SSF47203; SSF47203; 2. DR SUPFAM; SSF56645; SSF56645; 1. PE 2: Evidence at transcript level; KW Alternative splicing; Complete proteome; FAD; Flavoprotein; KW Oxidoreductase; Reference proteome. FT CHAIN 1 632 Acyl-coenzyme A oxidase-like protein. FT /FTId=PRO_0000305101. FT NP_BIND 376 381 FAD (By similarity). FT VAR_SEQ 1 280 Missing (in isoform 2). FT /FTId=VSP_028240. SQ SEQUENCE 632 AA; 70706 MW; 4BA075171EFE56E1 CRC64; MTGWSGLFIE VPLYRLASKV CCHLRGPQGF LQRACQGVCC LPRDSRAAGI MEEKRKSFIS QILILGEVLC MVDVSMSIKC GILFLLFGGA ISNLGSPEHV TKWFWPLKEQ KYTGMFAMTE RGHGSNVRGI QTEATFDLDN QEFVIDMPCE NAHKMYIGNA MHGNYAAVFA QLIIEGKSQG PHCFIVPIRD ENGNLYPGVT AIDMMHKEGM NGVDNGILIF DKVRIPRENL LDKFGSVTPD GQYHSPIQSK NARFNAILAT LTPSRLAVTF QALGAMKLGL MIAIRYSHSR RQFGPKDKEE VKIIEHQMQA LRLMSHLATA LAVTFTSRHA DDILDEDIFQ GRALTNSRSL QALMAGLKAY STWETVSCLQ DCRECTGGMG YMMETRISDL KCDTDVFVTF EGDNVVMLQV VARELLAQYS KQHKKNLLLG VIQNWTATAG DKLRTSFLAF NTDTVGCLAF LLKAVNFRER VLQRSLVSRI YYKVVTKKGD FFSAWNSCMH HVTSLSLAHI HRVALEQFTT AVRQCPNRED QALLMKFCLL YGTKLVFQER GWYLEHKYLT PKASMLIRAQ LLNLCESVKD DALKVISAFN IPHITIRAPK TGIPNPGAAE AAYPAPMQPL VRDAARAQLA KL // ID ACOX2_MOUSE Reviewed; 681 AA. AC Q9QXD1; Q8VCB0; DT 02-NOV-2001, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 2. DT 19-MAR-2014, entry version 103. DE RecName: Full=Peroxisomal acyl-coenzyme A oxidase 2; DE EC=1.17.99.3; DE AltName: Full=3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanoyl-CoA 24-hydroxylase; DE AltName: Full=3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanoyl-CoA oxidase; DE AltName: Full=Trihydroxycoprostanoyl-CoA oxidase; DE Short=THCA-CoA oxidase; DE Short=THCCox; GN Name=Acox2; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Amery L., Van Veldhoven P.P.; RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Liver; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-66; LYS-137; LYS-303; RP LYS-453; LYS-561 AND LYS-667, AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., RA Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). CC -!- FUNCTION: Oxidizes the CoA esters of the bile acid intermediates CC di- and tri-hydroxycoprostanic acids (By similarity). CC -!- CATALYTIC ACTIVITY: (25R)-3-alpha,7-alpha,12-alpha-trihydroxy-5- CC beta-cholestan-26-oyl-CoA + H(2)O + acceptor = (24R,25R)-3- CC alpha,7-alpha,12-alpha,24-tetrahydroxy-5-beta-cholestan-26-oyl-CoA CC + reduced acceptor. CC -!- COFACTOR: FAD (By similarity). CC -!- SUBCELLULAR LOCATION: Peroxisome (By similarity). CC -!- PTM: Acetylation of Lys-667 is observed in liver mitochondria from CC fasted mice but not from fed mice. CC -!- SIMILARITY: Belongs to the acyl-CoA oxidase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJ238492; CAB65251.1; -; mRNA. DR EMBL; BC021339; AAH21339.1; -; mRNA. DR RefSeq; NP_001155139.1; NM_001161667.1. DR RefSeq; NP_444345.2; NM_053115.2. DR RefSeq; XP_006518171.1; XM_006518108.1. DR UniGene; Mm.28700; -. DR ProteinModelPortal; Q9QXD1; -. DR SMR; Q9QXD1; 18-671. DR IntAct; Q9QXD1; 2. DR MINT; MINT-1866639; -. DR STRING; 10090.ENSMUSP00000022271; -. DR PhosphoSite; Q9QXD1; -. DR PaxDb; Q9QXD1; -. DR PRIDE; Q9QXD1; -. DR Ensembl; ENSMUST00000022271; ENSMUSP00000022271; ENSMUSG00000021751. DR Ensembl; ENSMUST00000164598; ENSMUSP00000126464; ENSMUSG00000021751. DR GeneID; 93732; -. DR KEGG; mmu:93732; -. DR UCSC; uc007sey.2; mouse. DR CTD; 8309; -. DR MGI; MGI:1934852; Acox2. DR eggNOG; COG1960; -. DR GeneTree; ENSGT00530000062919; -. DR HOGENOM; HOG000181256; -. DR HOVERGEN; HBG050451; -. DR InParanoid; Q8VCB0; -. DR KO; K10214; -. DR OMA; AFDFTDQ; -. DR OrthoDB; EOG7D59MV; -. DR TreeFam; TF300672; -. DR ChiTaRS; ACOX2; mouse. DR NextBio; 351575; -. DR PRO; PR:Q9QXD1; -. DR ArrayExpress; Q9QXD1; -. DR Bgee; Q9QXD1; -. DR CleanEx; MM_ACOX2; -. DR Genevestigator; Q9QXD1; -. DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell. DR GO; GO:0033791; F:3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoyl-CoA 24-hydroxylase activity; IEA:UniProtKB-EC. DR GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IEA:InterPro. DR GO; GO:0003997; F:acyl-CoA oxidase activity; IEA:InterPro. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. DR GO; GO:0006635; P:fatty acid beta-oxidation; IEA:InterPro. DR Gene3D; 1.10.540.10; -; 1. DR Gene3D; 2.40.110.10; -; 1. DR InterPro; IPR006091; Acyl-CoA_Oxase/DH_cen-dom. DR InterPro; IPR012258; Acyl-CoA_oxidase. DR InterPro; IPR002655; Acyl-CoA_oxidase_C. DR InterPro; IPR009075; AcylCo_DH/oxidase_C. DR InterPro; IPR013786; AcylCoA_DH/ox_N. DR InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom. DR PANTHER; PTHR10909:SF11; PTHR10909:SF11; 1. DR Pfam; PF01756; ACOX; 1. DR PIRSF; PIRSF000168; Acyl-CoA_oxidase; 1. DR SUPFAM; SSF47203; SSF47203; 2. DR SUPFAM; SSF56645; SSF56645; 1. PE 1: Evidence at protein level; KW Acetylation; Complete proteome; FAD; Fatty acid metabolism; KW Flavoprotein; Lipid metabolism; Oxidoreductase; Peroxisome; KW Reference proteome. FT CHAIN 1 681 Peroxisomal acyl-coenzyme A oxidase 2. FT /FTId=PRO_0000204682. FT MOTIF 679 681 Microbody targeting signal (Potential). FT MOD_RES 66 66 N6-succinyllysine. FT MOD_RES 137 137 N6-succinyllysine. FT MOD_RES 303 303 N6-succinyllysine. FT MOD_RES 453 453 N6-succinyllysine. FT MOD_RES 561 561 N6-succinyllysine. FT MOD_RES 667 667 N6-succinyllysine. FT CONFLICT 26 26 R -> W (in Ref. 1; CAB65251). SQ SEQUENCE 681 AA; 76863 MW; 32C65231326BA0FB CRC64; MGNPGDRVSL GETWSREVHP DIDSERHSPS FSVERLTNIL DGGIPNTELR RRVESLIQRD PVFNLKHLYF MTRDELYEDA VQKRFHLEKL AWSLGWSEDG PERIYADRVL AGYNNLNLHG IAMNAIRSLG SDEQIAKWGQ LGKNFQIITT YAQTELGHGT YLQGLETEAT YDATTQEFVI HSPTMTSIKW WPGDLGRTVT HAVVLAHLIC LGARHGMHAF IVPIRSLEDH TPLPGITVGD IGPKMGFENI DNGFLRLNHV RVPRENMLSR FAEVLPDGTY QRLGTPQSNY LGMLVTRVQL LYKGFLPTLQ KACTIAVRYA VIRHQSRLRP SDPEAKILEY QTQQQKLLPQ LAVSYALHFM TTSLLQFFHS SYSDILKRDF SLLPELHALS TGMKAMSSDF CAQGTEICRR ACGGHGYSKL SGLPTLVTQA IASCTYEGEN TVLYLQVARF LMKSYLQAQV SPGSIPQKPL PQSVMYLATP RPARCPAQTA ADFRCPEVYT TAWAYVSARL IRDATQHTQT LMRSGVDQYD AWNQTSVIHL QAAKAHCYFL TVRNFKEAVE KLDNEPEIQR VLQNLCDLYA LNGILTNSGD FLHDGFLSGA QVDMARTAFL DLLPLIRKDA ILLTDAFDFS DHCLNSALGC YDGHVYQRLF EWAQKSPANT QENPAYKKYI RPLMQSWKPK L // ID ACSF4_MOUSE Reviewed; 1100 AA. AC Q80WC9; Q3V3L2; Q505K4; Q8BRP4; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2003, sequence version 1. DT 19-MAR-2014, entry version 92. DE RecName: Full=Acyl-CoA synthetase family member 4; DE EC=6.2.1.-; DE AltName: Full=2-aminoadipic 6-semialdehyde dehydrogenase; DE AltName: Full=Protein LYS2 homolog; DE AltName: Full=Putative aminoadipate-semialdehyde dehydrogenase; DE EC=1.2.1.31; GN Name=Aasdh; Synonyms=Acsf4, U26; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), POSSIBLE FUNCTION, AND RP INDUCTION. RX PubMed=12712191; DOI=10.1038/422832a; RA Kasahara T., Kato T.; RT "Nutritional biochemistry: a new redox-cofactor vitamin for mammals."; RL Nature 422:832-832(2003). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE RP SEQUENCE [LARGE SCALE MRNA] OF 1-645 (ISOFORM 1). RC STRAIN=C57BL/6J; TISSUE=Brain cortex, and Hypothalamus; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Olfactory epithelium; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP COMMENT ON PUBMED:12712191 RESULTS. RX PubMed=15689995; DOI=10.1038/nature03322; RA Felton L.M., Anthony C.; RT "Biochemistry: role of PQQ as a mammalian enzyme cofactor?"; RL Nature 433:E10-E10(2005). RN [5] RP COMMENT ON PUBMED:12712191 RESULTS. RX PubMed=15689994; DOI=10.1038/nature03323; RA Rucker R., Storms D., Sheets A., Tchaparian E., Fascetti A.; RT "Biochemistry: is pyrroloquinoline quinone a vitamin?"; RL Nature 433:E10-E11(2005). RN [6] RP INDUCTION. RX PubMed=17029795; DOI=10.1016/j.bbagen.2006.07.009; RA Bauerly K.A., Storms D.H., Harris C.B., Hajizadeh S., Sun M.Y., RA Cheung C.P., Satre M.A., Fascetti A.J., Tchaparian E., Rucker R.B.; RT "Pyrroloquinoline quinone nutritional status alters lysine metabolism RT and modulates mitochondrial DNA content in the mouse and rat."; RL Biochim. Biophys. Acta 1760:1741-1748(2006). CC -!- FUNCTION: Acyl-CoA synthases catalyze the initial reaction in CC fatty acid metabolism, by forming a thioester with CoA (By CC similarity). Putative 2-aminoadipic 6-semialdehyde dehydrogenase, CC which may be involved in lysine catabolism. CC -!- CATALYTIC ACTIVITY: (S)-2-amino-6-oxohexanoate + NAD(P)(+) + H(2)O CC = L-2-aminoadipate + NAD(P)H. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q80WC9-1; Sequence=Displayed; CC Name=2; CC IsoId=Q80WC9-2; Sequence=VSP_030715; CC Note=No experimental confirmation available; CC Name=3; CC IsoId=Q80WC9-3; Sequence=VSP_030714; CC Note=No experimental confirmation available; CC -!- INDUCTION: According to PubMed:12712191, it is up-regulated by CC lysine-rich diet, while according to PubMed:17029795 levels of CC expression are not significantly changed even when diets differed CC markedly in PQQ and lysine content. CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme CC family. CC -!- SIMILARITY: Contains 1 acyl carrier domain. CC -!- CAUTION: According to PubMed:12712191, it may bind CC pyrroloquinoline quinone (PQQ) cofactor. However, their CC conclusions are based on prediction tools and indirect results and CC are not confirmed by PubMed:15689995 and PubMed:15689994. The CC relevance of PQQ-binding is therefore unclear in vivo. CC -!- CAUTION: In invertebrates, aminoadipate-semialdehyde dehydrogenase CC reaction is a key step of the L-lysine biosynthesis pathway, which CC is not fully conserved in vertebrates. It has been suggested by CC PubMed:12712191 that this protein participates in the reverse CC reaction (i.e. in lysine catabolism), however the relevance of CC this catalytic activity in vivo remains unclear. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AB095954; BAC75954.1; -; mRNA. DR EMBL; AK038779; BAE43303.1; -; mRNA. DR EMBL; AK043807; BAC31660.1; -; mRNA. DR EMBL; BC094507; AAH94507.1; -; mRNA. DR EMBL; BC128330; AAI28331.1; -; mRNA. DR RefSeq; NP_776126.1; NM_173765.3. DR RefSeq; XP_006534916.1; XM_006534853.1. DR UniGene; Mm.39271; -. DR ProteinModelPortal; Q80WC9; -. DR SMR; Q80WC9; 1-606, 753-1091. DR STRING; 10090.ENSMUSP00000113792; -. DR PhosphoSite; Q80WC9; -. DR PRIDE; Q80WC9; -. DR Ensembl; ENSMUST00000069709; ENSMUSP00000069279; ENSMUSG00000055923. [Q80WC9-1] DR Ensembl; ENSMUST00000120963; ENSMUSP00000113792; ENSMUSG00000055923. [Q80WC9-1] DR Ensembl; ENSMUST00000146570; ENSMUSP00000117639; ENSMUSG00000055923. DR GeneID; 231326; -. DR KEGG; mmu:231326; -. DR UCSC; uc008xvi.2; mouse. [Q80WC9-1] DR UCSC; uc008xvk.2; mouse. [Q80WC9-3] DR CTD; 132949; -. DR MGI; MGI:2442517; Aasdh. DR eggNOG; COG1520; -. DR GeneTree; ENSGT00440000033811; -. DR HOGENOM; HOG000033793; -. DR HOVERGEN; HBG057704; -. DR InParanoid; Q80WC9; -. DR KO; K00142; -. DR OMA; TMRATGD; -. DR OrthoDB; EOG77T14J; -. DR TreeFam; TF314245; -. DR ChiTaRS; AASDH; mouse. DR NextBio; 380501; -. DR PRO; PR:Q80WC9; -. DR ArrayExpress; Q80WC9; -. DR Bgee; Q80WC9; -. DR CleanEx; MM_AASDH; -. DR Genevestigator; Q80WC9; -. DR GO; GO:0016878; F:acid-thiol ligase activity; ISS:UniProtKB. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004043; F:L-aminoadipate-semialdehyde dehydrogenase activity; IEA:UniProtKB-EC. DR GO; GO:0006631; P:fatty acid metabolic process; ISS:UniProtKB. DR Gene3D; 1.10.1200.10; -; 1. DR Gene3D; 2.140.10.10; -; 1. DR InterPro; IPR009081; Acyl_carrier_prot-like. DR InterPro; IPR020845; AMP-binding_CS. DR InterPro; IPR000873; AMP-dep_Synth/Lig. DR InterPro; IPR006162; PPantetheine_attach_site. DR InterPro; IPR018391; PQQ_beta_propeller_repeat. DR InterPro; IPR027295; Quinonprotein_ADH-like_fam. DR InterPro; IPR011047; Quinonprotein_ADH-like_supfam. DR Pfam; PF00501; AMP-binding; 1. DR Pfam; PF00550; PP-binding; 1. DR SMART; SM00564; PQQ; 6. DR SUPFAM; SSF47336; SSF47336; 1. DR SUPFAM; SSF50998; SSF50998; 1. DR PROSITE; PS50075; ACP_DOMAIN; 1. DR PROSITE; PS00455; AMP_BINDING; 1. DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1. PE 2: Evidence at transcript level; KW Alternative splicing; ATP-binding; Complete proteome; KW Fatty acid metabolism; Ligase; Lipid metabolism; NAD; KW Nucleotide-binding; Oxidoreductase; Phosphopantetheine; KW Phosphoprotein; Reference proteome. FT CHAIN 1 1100 Acyl-CoA synthetase family member 4. FT /FTId=PRO_0000315804. FT DOMAIN 554 628 Acyl carrier. FT NP_BIND 197 205 ATP (By similarity). FT BINDING 427 427 ATP (By similarity). FT BINDING 441 441 ATP (By similarity). FT BINDING 526 526 ATP (By similarity). FT MOD_RES 591 591 O-(pantetheine 4'-phosphoryl)serine (By FT similarity). FT MOD_RES 651 651 Phosphoserine (By similarity). FT VAR_SEQ 223 1100 Missing (in isoform 3). FT /FTId=VSP_030714. FT VAR_SEQ 368 1100 Missing (in isoform 2). FT /FTId=VSP_030715. SQ SEQUENCE 1100 AA; 121569 MW; 86B303CFF07B234C CRC64; MTLQELVLRT ASVYMDRTAV CFDEGNNQPP VCYSYKALLS AASELSHFLI AHCDFGGIRE IGLYCQPGIN LPSWILGILQ VPAAYAPIDP DSPPSLSTYF MKKCDLKYVL VEKQQLSKFK SSHETVLNYD TVSVEHKDLA LFRLHWEDGR VSTVLGDRAD QHKVTDREDR VSAESRTPEK EHMDMRHDGC LAYVLHTSGT TGTPKIVRVP HACILPNIQH FRSLFDITQE DILFLASPLT FDPSVVEIFV SLSSGACLLI VPTSVKVLPS KLADILFSRH RVTVLQATPT LLRRFGSELI KSTVLSAHTS LRVLALGGEA FPSLTILKSW RGKGNRTQIF NIYGITEVSS WATFYRIPEE ILNSAVKHES PVQLGSPLLG TVIEVRDQNG SPVLEGTGQV FLGGKNRVCF LDDEMTVPLG TMRATGDFVT VKDGEIFFLG RKDSQIKRHG KRLNIALVQQ VAEELRQVES CAVTWYNQER LILFIVSKVD LVKDCIFKEL QKHLPAHALP DDMVLIDTLP FTCHGKVDVS ELNKIYLDYI SSQPRNELHG KEELWGKLQY LWKSILCLPE DPEDTLKVPA NSVFLDSGGD SLKSMRLLSE IERLTGTAIP GLLEVILSSS LLDVYNHIVQ AVFTPEDRKA NRSYTTKRKF SDADPEEASG KPARLESAWP SNHAGETNSV IALSRGSQVL SLGAGRLLTQ LGLCLPVCSL DLIPQTNTQI LKSLSPPAPD ENLEKPPLFQ QGSPVVGAMA MALRERWRSD TGKCVDASPL LVRAAVQDKP STTVYIGSHS HTVKAVDLSS GETRWEQLLG DRIESSACVS KCGNFIVVGC YNGLVYVLKS NSGEKYWTFT TEDAVKSSPA VDPTTGLIYV GSHDQHAYAL DIYEKKCVWK LNCEGALFSS PCVSLSPHHL YCATLGGLLL ALNPASGSTV WKRSCGKPLF SSPRCYQQYI CIGCVDGSLL CFTHSGEQVW RFAAGGPIFS SPCVSAAEQE IFFGSHDCFI YCCSKEGHLR WKFETTARVY ATPFAFSNHP RSDDALLAAA STDGKLWVLE SRSGELRSVY ELPGEVFSSP VVWESMLVIG CRNNYIYCLD LLCGDKNNQV // ID ADH1_MOUSE Reviewed; 375 AA. AC P00329; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 19-MAR-2014, entry version 134. DE RecName: Full=Alcohol dehydrogenase 1; DE EC=1.1.1.1; DE AltName: Full=ADH-A2; DE AltName: Full=Alcohol dehydrogenase A subunit; GN Name=Adh1; Synonyms=Adh-1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=3157987; DOI=10.1073/pnas.82.8.2262; RA Edenberg H.J., Zhang K., Fong K., Bosron W.F., Li T.-K.; RT "Cloning and sequencing of cDNA encoding the complete mouse liver RT alcohol dehydrogenase."; RL Proc. Natl. Acad. Sci. U.S.A. 82:2262-2266(1985). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=2893758; DOI=10.1016/0378-1119(87)90325-8; RA Ceci J.D., Zheng Y.W., Felder M.R.; RT "Molecular analysis of mouse alcohol dehydrogenase: nucleotide RT sequence of the Adh-1 gene and genetic mapping of a related nucleotide RT sequence to chromosome 3."; RL Gene 59:171-182(1987). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=3428612; DOI=10.1016/0378-1119(87)90173-9; RA Zhang K., Bosron W.F., Edenberg H.J.; RT "Structure of the mouse Adh-1 gene and identification of a deletion in RT a long alternating purine-pyrimidine sequence in the first intron of RT strains expressing low alcohol dehydrogenase activity."; RL Gene 57:27-36(1987). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Colon, and Kidney; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 8-51. RX PubMed=7937138; DOI=10.1093/nar/22.20.4132; RA Caubin J., Iglesias T., Bernal J., Munoz A., Marquez G., Barbero J.L., RA Zaballos A.; RT "Isolation of genomic DNA fragments corresponding to genes modulated RT in vivo by a transcription factor."; RL Nucleic Acids Res. 22:4132-4138(1994). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] OF 224-375. RC STRAIN=SWR/J; TISSUE=Liver; RX PubMed=3011597; DOI=10.1016/0378-1119(86)90101-0; RA Ceci J.D., Lawther R., Duester G., Hatfield G.W., Smith M., RA O'Malley M.P., Felder M.R.; RT "Androgen induction of alcohol dehydrogenase in mouse kidney. Studies RT with a cDNA probe confirmed by nucleotide sequence analysis."; RL Gene 41:217-224(1986). RN [7] RP TISSUE SPECIFICITY. RC STRAIN=FVB/N; RX PubMed=7738026; DOI=10.1074/jbc.270.18.10868; RA Zgombic-Knight M., Ang H.L., Foglio M.H., Duester G.; RT "Cloning of the mouse class IV alcohol dehydrogenase (retinol RT dehydrogenase) cDNA and tissue-specific expression patterns of the RT murine ADH gene family."; RL J. Biol. Chem. 270:10868-10877(1995). RN [8] RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-234 AND LYS-340, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., RA Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). CC -!- CATALYTIC ACTIVITY: An alcohol + NAD(+) = an aldehyde or ketone + CC NADH. CC -!- COFACTOR: Binds 2 zinc ions per subunit. CC -!- SUBUNIT: Dimer of identical or non-identical chains of three types CC (A, B, C), which are coded by 3 separate genes at different loci. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- TISSUE SPECIFICITY: Expressed at high levels in the liver, small CC intestine and eye, at moderate levels in kidney, ovary and uterus, CC and at low levels in the spinal cord, thymus, heart, stomach CC mucosa, skin and testis. CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase CC family. Class-I subfamily. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M18480; AAA37178.1; -; Genomic_DNA. DR EMBL; M18472; AAA37178.1; JOINED; Genomic_DNA. DR EMBL; M18473; AAA37178.1; JOINED; Genomic_DNA. DR EMBL; M18474; AAA37178.1; JOINED; Genomic_DNA. DR EMBL; M18475; AAA37178.1; JOINED; Genomic_DNA. DR EMBL; M18476; AAA37178.1; JOINED; Genomic_DNA. DR EMBL; M18477; AAA37178.1; JOINED; Genomic_DNA. DR EMBL; M18478; AAA37178.1; JOINED; Genomic_DNA. DR EMBL; M22679; AAA37179.1; -; Genomic_DNA. DR EMBL; M22671; AAA37179.1; JOINED; Genomic_DNA. DR EMBL; M22672; AAA37179.1; JOINED; Genomic_DNA. DR EMBL; M22673; AAA37179.1; JOINED; Genomic_DNA. DR EMBL; M22674; AAA37179.1; JOINED; Genomic_DNA. DR EMBL; M22675; AAA37179.1; JOINED; Genomic_DNA. DR EMBL; M22676; AAA37179.1; JOINED; Genomic_DNA. DR EMBL; M22677; AAA37179.1; JOINED; Genomic_DNA. DR EMBL; M11307; AAA37180.1; -; mRNA. DR EMBL; BC013477; AAH13477.1; -; mRNA. DR EMBL; BC054467; AAH54467.1; -; mRNA. DR EMBL; Z32540; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; M22611; AAA37181.1; -; mRNA. DR PIR; A27322; DEMSAA. DR RefSeq; NP_031435.1; NM_007409.2. DR UniGene; Mm.2409; -. DR UniGene; Mm.412004; -. DR ProteinModelPortal; P00329; -. DR SMR; P00329; 2-375. DR IntAct; P00329; 4. DR MINT; MINT-1869642; -. DR STRING; 10090.ENSMUSP00000004232; -. DR PhosphoSite; P00329; -. DR PaxDb; P00329; -. DR PRIDE; P00329; -. DR Ensembl; ENSMUST00000004232; ENSMUSP00000004232; ENSMUSG00000074207. DR GeneID; 11522; -. DR KEGG; mmu:11522; -. DR UCSC; uc008rnf.1; mouse. DR CTD; 11522; -. DR MGI; MGI:87921; Adh1. DR eggNOG; COG1062; -. DR HOGENOM; HOG000294674; -. DR HOVERGEN; HBG000195; -. DR InParanoid; P00329; -. DR KO; K13951; -. DR OMA; RENICEN; -. DR OrthoDB; EOG72NRQ6; -. DR TreeFam; TF300429; -. DR SABIO-RK; P00329; -. DR NextBio; 278960; -. DR PRO; PR:P00329; -. DR ArrayExpress; P00329; -. DR Bgee; P00329; -. DR CleanEx; MM_ADH1; -. DR Genevestigator; P00329; -. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR GO; GO:0004022; F:alcohol dehydrogenase (NAD) activity; IDA:MGI. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0048149; P:behavioral response to ethanol; IMP:MGI. DR GO; GO:0006068; P:ethanol catabolic process; IDA:MGI. DR GO; GO:0032526; P:response to retinoic acid; IDA:MGI. DR GO; GO:0033574; P:response to testosterone; IDA:MGI. DR GO; GO:0042573; P:retinoic acid metabolic process; IMP:MGI. DR GO; GO:0042572; P:retinol metabolic process; IMP:MGI. DR Gene3D; 3.40.50.720; -; 1. DR Gene3D; 3.90.180.10; -; 1. DR InterPro; IPR013149; ADH_C. DR InterPro; IPR013154; ADH_GroES-like. DR InterPro; IPR002085; ADH_SF_Zn-type. DR InterPro; IPR002328; ADH_Zn_CS. DR InterPro; IPR011032; GroES-like. DR InterPro; IPR016040; NAD(P)-bd_dom. DR PANTHER; PTHR11695; PTHR11695; 1. DR Pfam; PF08240; ADH_N; 1. DR Pfam; PF00107; ADH_zinc_N; 1. DR SUPFAM; SSF50129; SSF50129; 2. DR PROSITE; PS00059; ADH_ZINC; 1. PE 1: Evidence at protein level; KW Acetylation; Complete proteome; Cytoplasm; Metal-binding; NAD; KW Oxidoreductase; Reference proteome; Zinc. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 375 Alcohol dehydrogenase 1. FT /FTId=PRO_0000160666. FT NP_BIND 200 205 NAD (By similarity). FT NP_BIND 293 295 NAD (By similarity). FT METAL 47 47 Zinc 1; catalytic. FT METAL 68 68 Zinc 1; catalytic. FT METAL 98 98 Zinc 2. FT METAL 101 101 Zinc 2. FT METAL 104 104 Zinc 2. FT METAL 112 112 Zinc 2. FT METAL 175 175 Zinc 1; catalytic. FT BINDING 224 224 NAD (By similarity). FT BINDING 229 229 NAD (By similarity). FT BINDING 370 370 NAD (By similarity). FT MOD_RES 2 2 N-acetylserine (By similarity). FT MOD_RES 234 234 N6-succinyllysine. FT MOD_RES 340 340 N6-succinyllysine. SQ SEQUENCE 375 AA; 39771 MW; 7B8AF94C95D35108 CRC64; MSTAGKVIKC KAAVLWELHK PFTIEDIEVA PPKAHEVRIK MVATGVCRSD DHVVSGTLVT PLPAVLGHEG AGIVESVGEG VTCVKPGDKV IPLFSPQCGE CRICKHPESN FCSRSDLLMP RGTLREGTSR FSCKGKQIHN FISTSTFSQY TVVDDIAVAK IDGASPLDKV CLIGCGFSTG YGSAVKVAKV TPGSTCAVFG LGGVGLSVII GCKAAGAARI IAVDINKDKF AKAKELGATE CINPQDYSKP IQEVLQEMTD GGVDFSFEVI GRLDTMTSAL LSCHAACGVS VVVGVPPNAQ NLSMNPMLLL LGRTWKGAIF GGFKSKDSVP KLVADFMAKK FPLDPLITHV LPFEKINEAF DLLRSGKSIR TVLTF // ID ADH4_MOUSE Reviewed; 377 AA. AC Q9QYY9; Q3V0P5; DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot. DT 28-JUN-2011, sequence version 4. DT 19-FEB-2014, entry version 110. DE RecName: Full=Alcohol dehydrogenase 4; DE EC=1.1.1.1; DE AltName: Full=ADH2; DE AltName: Full=Alcohol dehydrogenase class II; DE Short=Alcohol dehydrogenase II; GN Name=Adh4; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ZINC-BINDING, MUTAGENESIS OF RP PRO-48; ASN-52 AND SER-183, AND TISSUE SPECIFICITY. RC TISSUE=Liver; RX PubMed=10514444; DOI=10.1074/jbc.274.42.29712; RA Svensson S., Stroemberg P., Hoeoeg J.-O.; RT "A novel subtype of class II alcohol dehydrogenase in rodents. Unique RT Pro(47) and Ser(182) modulates hydride transfer in the mouse enzyme."; RL J. Biol. Chem. 274:29712-29719(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Testis; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF WILD-TYPE IN COMPLEX WITH RP NADH AND INHIBITOR AND OF MUTANT HIS-48 IN COMPLEX WITH NADH. RX PubMed=10970744; DOI=10.1006/jmbi.2000.4039; RA Svensson S., Hoeoeg J.-O., Schneider G., Sandalova T.; RT "Crystal structures of mouse class II alcohol dehydrogenase reveal RT determinants of substrate specificity and catalytic efficiency."; RL J. Mol. Biol. 302:441-453(2000). CC -!- FUNCTION: Involved in the reduction of benzoquinones. CC -!- CATALYTIC ACTIVITY: An alcohol + NAD(+) = an aldehyde or ketone + CC NADH. CC -!- COFACTOR: Binds 2 zinc ions per subunit. CC -!- SUBUNIT: Dimer. CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- TISSUE SPECIFICITY: Liver specific. CC -!- MISCELLANEOUS: Has much lower enzymatic activity towards alcohols CC and aldehydes compared to human class II ADH. Strongly inhibited CC by omega-hydroxy fatty acids. CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase CC family. Class-II subfamily. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJ245750; CAB57455.1; -; mRNA. DR EMBL; AK132994; BAE21459.1; -; mRNA. DR RefSeq; NP_036126.2; NM_011996.2. DR UniGene; Mm.158750; -. DR PDB; 1E3E; X-ray; 2.12 A; A/B=2-377. DR PDB; 1E3I; X-ray; 2.08 A; A/B=2-377. DR PDB; 1E3L; X-ray; 2.50 A; A/B=2-377. DR PDBsum; 1E3E; -. DR PDBsum; 1E3I; -. DR PDBsum; 1E3L; -. DR ProteinModelPortal; Q9QYY9; -. DR SMR; Q9QYY9; 2-377. DR IntAct; Q9QYY9; 1. DR MINT; MINT-4087269; -. DR STRING; 10090.ENSMUSP00000013458; -. DR PhosphoSite; Q9QYY9; -. DR PaxDb; Q9QYY9; -. DR PRIDE; Q9QYY9; -. DR Ensembl; ENSMUST00000013458; ENSMUSP00000013458; ENSMUSG00000037797. DR GeneID; 26876; -. DR KEGG; mmu:26876; -. DR UCSC; uc008rnj.1; mouse. DR CTD; 127; -. DR MGI; MGI:1349472; Adh4. DR eggNOG; COG1062; -. DR GeneTree; ENSGT00430000030800; -. DR HOGENOM; HOG000294674; -. DR HOVERGEN; HBG000195; -. DR InParanoid; Q3V0P5; -. DR KO; K13980; -. DR OMA; HKPIQEV; -. DR TreeFam; TF300429; -. DR SABIO-RK; Q9QYY9; -. DR EvolutionaryTrace; Q9QYY9; -. DR NextBio; 304683; -. DR PRO; PR:Q9QYY9; -. DR ArrayExpress; Q9QYY9; -. DR Bgee; Q9QYY9; -. DR Genevestigator; Q9QYY9; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0015630; C:microtubule cytoskeleton; IEA:Ensembl. DR GO; GO:0004024; F:alcohol dehydrogenase activity, zinc-dependent; IDA:MGI. DR GO; GO:0004032; F:alditol:NADP+ 1-oxidoreductase activity; IDA:MGI. DR GO; GO:0005503; F:all-trans retinal binding; IEA:Ensembl. DR GO; GO:0019115; F:benzaldehyde dehydrogenase activity; IEA:Ensembl. DR GO; GO:0051287; F:NAD binding; IEA:Ensembl. DR GO; GO:0003960; F:NADPH:quinone reductase activity; IDA:MGI. DR GO; GO:0019841; F:retinol binding; IEA:Ensembl. DR GO; GO:0004745; F:retinol dehydrogenase activity; IEA:Ensembl. DR GO; GO:0008270; F:zinc ion binding; IEA:Ensembl. DR GO; GO:0046164; P:alcohol catabolic process; IDA:MGI. DR GO; GO:0006081; P:cellular aldehyde metabolic process; IDA:MGI. DR GO; GO:0006067; P:ethanol metabolic process; IDA:MGI. DR GO; GO:0006069; P:ethanol oxidation; IEA:Ensembl. DR GO; GO:1901661; P:quinone metabolic process; IDA:MGI. DR GO; GO:0042572; P:retinol metabolic process; IEA:Ensembl. DR Gene3D; 3.40.50.720; -; 1. DR Gene3D; 3.90.180.10; -; 1. DR InterPro; IPR013149; ADH_C. DR InterPro; IPR013154; ADH_GroES-like. DR InterPro; IPR002085; ADH_SF_Zn-type. DR InterPro; IPR002328; ADH_Zn_CS. DR InterPro; IPR011032; GroES-like. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR028632; Zinc_ADH_II. DR PANTHER; PTHR11695; PTHR11695; 1. DR PANTHER; PTHR11695:SF308; PTHR11695:SF308; 1. DR Pfam; PF08240; ADH_N; 1. DR Pfam; PF00107; ADH_zinc_N; 1. DR SUPFAM; SSF50129; SSF50129; 2. DR PROSITE; PS00059; ADH_ZINC; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Cytoplasm; Metal-binding; NAD; KW Oxidoreductase; Reference proteome; Zinc. FT CHAIN 1 377 Alcohol dehydrogenase 4. FT /FTId=PRO_0000160682. FT NP_BIND 204 209 NAD. FT NP_BIND 297 299 NAD. FT NP_BIND 320 322 NAD. FT METAL 47 47 Zinc 1; catalytic. FT METAL 68 68 Zinc 1; catalytic. FT METAL 98 98 Zinc 2. FT METAL 101 101 Zinc 2. FT METAL 104 104 Zinc 2. FT METAL 112 112 Zinc 2. FT METAL 179 179 Zinc 1; catalytic. FT BINDING 49 49 NAD. FT BINDING 228 228 NAD. FT BINDING 233 233 NAD. FT BINDING 372 372 NAD. FT MUTAGEN 48 48 P->H: Strongly increases enzyme activity, FT serves as proton acceptor. FT MUTAGEN 52 52 N->H: No effect. FT MUTAGEN 183 183 S->T: Strongly increases activity towards FT ethanol, increases KM for benzoquinone FT 10-fold. FT CONFLICT 197 197 S -> G (in Ref. 1; CAB57455). FT CONFLICT 303 303 K -> E (in Ref. 1; CAB57455). FT STRAND 8 15 FT STRAND 23 29 FT STRAND 36 45 FT HELIX 48 52 FT STRAND 62 64 FT STRAND 69 77 FT STRAND 89 92 FT STRAND 99 101 FT HELIX 102 105 FT HELIX 121 123 FT STRAND 134 137 FT STRAND 140 143 FT TURN 146 148 FT STRAND 151 158 FT HELIX 159 161 FT STRAND 162 164 FT HELIX 171 174 FT HELIX 175 178 FT HELIX 180 189 FT TURN 190 192 FT STRAND 199 203 FT HELIX 207 218 FT STRAND 222 227 FT HELIX 231 233 FT HELIX 234 239 FT STRAND 243 246 FT HELIX 248 250 FT HELIX 255 262 FT STRAND 267 274 FT HELIX 277 285 FT TURN 289 291 FT STRAND 293 296 FT STRAND 300 307 FT HELIX 308 312 FT STRAND 316 319 FT HELIX 322 324 FT HELIX 327 339 FT HELIX 345 348 FT STRAND 349 354 FT HELIX 355 357 FT HELIX 358 366 FT STRAND 371 376 SQ SEQUENCE 377 AA; 40211 MW; 5B527E48BB745E14 CRC64; MGTQGKVIKC KAAIAWKTGS PLCIEEIEVS PPKACEVRIQ VIATCVCPTD INATDPKKKA LFPVVLGHEC AGIVESVGPG VTNFKPGDKV IPFFAPQCKR CKLCLSPLTN LCGKLRNFKY PTIDQELMED RTSRFTCKGR SIYHFMGVSS FSQYTVVSEA NLARVDDEAN LERVCLIGCG FSSGYGAAIN TAKVTPSSTC AVFGLGCVGL SAIIGCKIAG ASRIIAIDIN GEKFPKAKAL GATDCLNPRE LDKPVQDVIT ELTAGGVDYS LDCAGTAQTL KAAVDCTVLG WGSCTVVGAK VDKMTIPTVD VILGRSINGT FFGGWKSVDS VPNLVSDYKN KKFDLDLLVT HALPFESIND AIDLMKEGKS IRTILTF // ID ADH7_MOUSE Reviewed; 374 AA. AC Q64437; DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 2. DT 19-MAR-2014, entry version 118. DE RecName: Full=Alcohol dehydrogenase class 4 mu/sigma chain; DE EC=1.1.1.1; DE AltName: Full=ADH-C2; DE AltName: Full=Alcohol dehydrogenase 7; DE AltName: Full=Alcohol dehydrogenase class IV mu/sigma chain; DE AltName: Full=Gastric alcohol dehydrogenase; DE AltName: Full=Retinol dehydrogenase; GN Name=Adh7; Synonyms=Adh-3, Adh3; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=FVB/N; TISSUE=Gastric mucosa; RX PubMed=7738026; DOI=10.1074/jbc.270.18.10868; RA Zgombic-Knight M., Ang H.L., Foglio M.H., Duester G.; RT "Cloning of the mouse class IV alcohol dehydrogenase (retinol RT dehydrogenase) cDNA and tissue-specific expression patterns of the RT murine ADH gene family."; RL J. Biol. Chem. 270:10868-10877(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=129/SvJ; RX PubMed=9126489; DOI=10.1006/geno.1997.4637; RA Zgombic-Knight M., Deltour L., Haselbeck R.J., Foglio M.H., RA Duester G.; RT "Gene structure and promoter for Adh-3 encoding mouse class IV alcohol RT dehydrogenase (retinol dehydrogenase)."; RL Genomics 41:105-109(1997). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). CC -!- FUNCTION: Could function in retinol oxidation for the synthesis of CC retinoic acid, a hormone important for cellular differentiation. CC -!- CATALYTIC ACTIVITY: An alcohol + NAD(+) = an aldehyde or ketone + CC NADH. CC -!- COFACTOR: Binds 2 zinc ions per subunit (By similarity). CC -!- SUBUNIT: Homodimer. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- TISSUE SPECIFICITY: High expression in the stomach mucosa. Lower CC expression in eye, thymus, skin and ovary. Very low expression in CC small intestine, liver and uterus. CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase CC family. Class-IV subfamily. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U20257; AAA76735.1; -; mRNA. DR EMBL; U76734; AAC53124.1; -; Genomic_DNA. DR EMBL; U76728; AAC53124.1; JOINED; Genomic_DNA. DR EMBL; U76729; AAC53124.1; JOINED; Genomic_DNA. DR EMBL; U76730; AAC53124.1; JOINED; Genomic_DNA. DR EMBL; U76727; AAC53124.1; JOINED; Genomic_DNA. DR EMBL; U76731; AAC53124.1; JOINED; Genomic_DNA. DR EMBL; U76733; AAC53124.1; JOINED; Genomic_DNA. DR EMBL; U76732; AAC53124.1; JOINED; Genomic_DNA. DR EMBL; AC079682; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR PIR; A56436; A56436. DR RefSeq; NP_033756.2; NM_009626.4. DR RefSeq; XP_006500982.1; XM_006500919.1. DR UniGene; Mm.8473; -. DR ProteinModelPortal; Q64437; -. DR SMR; Q64437; 2-374. DR PhosphoSite; Q64437; -. DR PaxDb; Q64437; -. DR PRIDE; Q64437; -. DR Ensembl; ENSMUST00000090171; ENSMUSP00000087633; ENSMUSG00000055301. DR GeneID; 11529; -. DR KEGG; mmu:11529; -. DR UCSC; uc008rnd.2; mouse. DR CTD; 131; -. DR MGI; MGI:87926; Adh7. DR eggNOG; COG1062; -. DR HOGENOM; HOG000294674; -. DR HOVERGEN; HBG000195; -. DR InParanoid; Q64437; -. DR KO; K13951; -. DR OMA; RLDTMID; -. DR OrthoDB; EOG72NRQ6; -. DR TreeFam; TF300429; -. DR NextBio; 278964; -. DR PRO; PR:Q64437; -. DR ArrayExpress; Q64437; -. DR Bgee; Q64437; -. DR Genevestigator; Q64437; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005576; C:extracellular region; IEA:Ensembl. DR GO; GO:0005622; C:intracellular; IDA:MGI. DR GO; GO:0005730; C:nucleolus; IEA:Ensembl. DR GO; GO:0004022; F:alcohol dehydrogenase (NAD) activity; IDA:MGI. DR GO; GO:0004024; F:alcohol dehydrogenase activity, zinc-dependent; IEA:Ensembl. DR GO; GO:0004031; F:aldehyde oxidase activity; IEA:Ensembl. DR GO; GO:0035276; F:ethanol binding; IEA:Ensembl. DR GO; GO:0019841; F:retinol binding; IEA:Ensembl. DR GO; GO:0004745; F:retinol dehydrogenase activity; IDA:MGI. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0006068; P:ethanol catabolic process; IMP:MGI. DR GO; GO:0006069; P:ethanol oxidation; IEA:Ensembl. DR GO; GO:1900116; P:extracellular negative regulation of signal transduction; IEA:Ensembl. DR GO; GO:0010430; P:fatty acid omega-oxidation; IEA:Ensembl. DR GO; GO:2000272; P:negative regulation of receptor activity; IEA:GOC. DR GO; GO:0009617; P:response to bacterium; IEA:Ensembl. DR GO; GO:0045471; P:response to ethanol; IEA:Ensembl. DR GO; GO:0042573; P:retinoic acid metabolic process; IMP:MGI. DR GO; GO:0042572; P:retinol metabolic process; IMP:MGI. DR Gene3D; 3.40.50.720; -; 1. DR Gene3D; 3.90.180.10; -; 1. DR InterPro; IPR013149; ADH_C. DR InterPro; IPR013154; ADH_GroES-like. DR InterPro; IPR002085; ADH_SF_Zn-type. DR InterPro; IPR002328; ADH_Zn_CS. DR InterPro; IPR011032; GroES-like. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR028635; Zinc_ADH_IV. DR PANTHER; PTHR11695; PTHR11695; 1. DR PANTHER; PTHR11695:SF306; PTHR11695:SF306; 1. DR Pfam; PF08240; ADH_N; 1. DR Pfam; PF00107; ADH_zinc_N; 1. DR SUPFAM; SSF50129; SSF50129; 2. DR PROSITE; PS00059; ADH_ZINC; 1. PE 2: Evidence at transcript level; KW Complete proteome; Cytoplasm; Metal-binding; NAD; Oxidoreductase; KW Reference proteome; Zinc. FT CHAIN 1 374 Alcohol dehydrogenase class 4 mu/sigma FT chain. FT /FTId=PRO_0000160692. FT NP_BIND 199 204 NAD (By similarity). FT NP_BIND 292 294 NAD (By similarity). FT METAL 47 47 Zinc 1; catalytic (By similarity). FT METAL 68 68 Zinc 1; catalytic (By similarity). FT METAL 98 98 Zinc 2 (By similarity). FT METAL 101 101 Zinc 2 (By similarity). FT METAL 104 104 Zinc 2 (By similarity). FT METAL 112 112 Zinc 2 (By similarity). FT METAL 174 174 Zinc 1; catalytic (By similarity). FT BINDING 223 223 NAD (By similarity). FT BINDING 228 228 NAD (By similarity). FT BINDING 369 369 NAD (By similarity). FT CONFLICT 120 120 R -> C (in Ref. 1; AAA76735 and 2; FT AAC53124). FT CONFLICT 262 262 I -> V (in Ref. 1; AAA76735 and 2; FT AAC53124). SQ SEQUENCE 374 AA; 39904 MW; D615119A23B41843 CRC64; MGTAGKVIKC KAAVLWGVNQ PFSIEEIEVA PPKAKEVRVK ILATGICRTD DHIIKGSMVS KFPVIVGHEA VGVVESVGEG VTTVRPGDKV IPLFLPQCRE CNACLNPEGN LCIRSDLTGR GVLADGTTRF TCKGKPVQHF MNTSTFTEYT VLDESSVAKV DGAAPPEKAC LIGCGFSTGY GAAVKTAKVT PGSTCVVFGL GGVGLSVIMG CKAAGASRII GIDINKDKFQ KALAVGATEC ISPKDSTKPI SEVLSDMTGN TIQYTFEVIG RLETMVDALS SCHMNYGTSV VVGAPPSAKM LTYDPMLLFT GRTWKGCVFG GWKSRDDVPK LVTEFLEKKF DLDQLITHTL PFNNINEGFE LLYSGKSIRT VLTF // ID ADHX_MOUSE Reviewed; 374 AA. AC P28474; Q3TW83; Q8C662; DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 19-MAR-2014, entry version 135. DE RecName: Full=Alcohol dehydrogenase class-3; DE EC=1.1.1.1; DE AltName: Full=Alcohol dehydrogenase 2; DE AltName: Full=Alcohol dehydrogenase 5; DE AltName: Full=Alcohol dehydrogenase B2; DE Short=ADH-B2; DE AltName: Full=Alcohol dehydrogenase class-III; DE AltName: Full=Glutathione-dependent formaldehyde dehydrogenase; DE Short=FALDH; DE Short=FDH; DE Short=GSH-FDH; DE EC=1.1.1.-; DE AltName: Full=S-(hydroxymethyl)glutathione dehydrogenase; DE EC=1.1.1.284; GN Name=Adh5; Synonyms=Adh-2, Adh2; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=2053480; RA Edenberg H.J., Brown C.J., Carr L.G., Ho W.H., Hur M.W.; RT "Alcohol dehydrogenase gene expression and cloning of the mouse chi- RT like ADH."; RL Adv. Exp. Med. Biol. 284:253-262(1991). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=1472709; RA Hur M.W., Ho W.H., Brown C.J., Goldman D., Edenberg H.J.; RT "Molecular cloning of mouse alcohol dehydrogenase-B2 cDNA: nucleotide RT sequences of the class III ADH genes evolve slowly even for silent RT substitutions."; RL DNA Seq. 3:167-175(1992). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=129/SvJ; RX PubMed=8647091; DOI=10.1111/j.1432-1033.1996.0496k.x; RA Foglio M.H., Duester G.; RT "Characterization of the functional gene encoding mouse class III RT alcohol dehydrogenase (glutathione-dependent formaldehyde RT dehydrogenase) and an unexpressed processed pseudogene with an intact RT open reading frame."; RL Eur. J. Biochem. 237:496-504(1996). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Head, and Kidney; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Kidney; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP PROTEIN SEQUENCE OF 234-248, AND MASS SPECTROMETRY. RC STRAIN=OF1; TISSUE=Hippocampus; RA Lubec G., Sunyer B., Chen W.-Q.; RL Submitted (JAN-2009) to UniProtKB. RN [7] RP TISSUE SPECIFICITY. RC STRAIN=FVB/N; RX PubMed=7738026; DOI=10.1074/jbc.270.18.10868; RA Zgombic-Knight M., Ang H.L., Foglio M.H., Duester G.; RT "Cloning of the mouse class IV alcohol dehydrogenase (retinol RT dehydrogenase) cDNA and tissue-specific expression patterns of the RT murine ADH gene family."; RL J. Biol. Chem. 270:10868-10877(1995). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-247, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=17242355; DOI=10.1073/pnas.0609836104; RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; RT "Large-scale phosphorylation analysis of mouse liver."; RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). RN [9] RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-233 AND LYS-315, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., RA Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). CC -!- FUNCTION: Class-III ADH is remarkably ineffective in oxidizing CC ethanol, but it readily catalyzes the oxidation of long-chain CC primary alcohols and the oxidation of S-(hydroxymethyl) CC glutathione. CC -!- CATALYTIC ACTIVITY: An alcohol + NAD(+) = an aldehyde or ketone + CC NADH. CC -!- CATALYTIC ACTIVITY: S-(hydroxymethyl)glutathione + NAD(P)(+) = S- CC formylglutathione + NAD(P)H. CC -!- COFACTOR: Binds 2 zinc ions per subunit (By similarity). CC -!- SUBUNIT: Homodimer. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- TISSUE SPECIFICITY: Ubiquitous. CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase CC family. Class-III subfamily. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M84147; AAA68896.1; -; mRNA. DR EMBL; U48970; AAC52763.1; -; Genomic_DNA. DR EMBL; U48964; AAC52763.1; JOINED; Genomic_DNA. DR EMBL; U48965; AAC52763.1; JOINED; Genomic_DNA. DR EMBL; U48966; AAC52763.1; JOINED; Genomic_DNA. DR EMBL; U48968; AAC52763.1; JOINED; Genomic_DNA. DR EMBL; U48969; AAC52763.1; JOINED; Genomic_DNA. DR EMBL; AK076507; BAC36370.1; -; mRNA. DR EMBL; AK146949; BAE27558.1; -; mRNA. DR EMBL; AK159803; BAE35383.1; -; mRNA. DR EMBL; BC090978; AAH90978.1; -; mRNA. DR PIR; A56643; A56643. DR RefSeq; NP_001275507.1; NM_001288578.1. DR RefSeq; NP_031436.2; NM_007410.3. DR UniGene; Mm.3874; -. DR PDB; 1OTQ; Model; -; A=1-374. DR PDBsum; 1OTQ; -. DR ProteinModelPortal; P28474; -. DR SMR; P28474; 2-374. DR IntAct; P28474; 2. DR MINT; MINT-1869168; -. DR PhosphoSite; P28474; -. DR REPRODUCTION-2DPAGE; P28474; -. DR PaxDb; P28474; -. DR PRIDE; P28474; -. DR Ensembl; ENSMUST00000005964; ENSMUSP00000005964; ENSMUSG00000028138. DR GeneID; 11532; -. DR KEGG; mmu:11532; -. DR UCSC; uc008rnk.1; mouse. DR CTD; 128; -. DR MGI; MGI:87929; Adh5. DR eggNOG; COG1062; -. DR HOGENOM; HOG000294674; -. DR HOVERGEN; HBG000195; -. DR InParanoid; P28474; -. DR KO; K00121; -. DR OMA; IDFAKED; -. DR OrthoDB; EOG72NRQ6; -. DR TreeFam; TF300429; -. DR NextBio; 278968; -. DR PRO; PR:P28474; -. DR ArrayExpress; P28474; -. DR Bgee; P28474; -. DR Genevestigator; P28474; -. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR GO; GO:0005634; C:nucleus; IEA:Ensembl. DR GO; GO:0004022; F:alcohol dehydrogenase (NAD) activity; IDA:MGI. DR GO; GO:0005504; F:fatty acid binding; IEA:Ensembl. DR GO; GO:0018467; F:formaldehyde dehydrogenase activity; IEA:Ensembl. DR GO; GO:0051903; F:S-(hydroxymethyl)glutathione dehydrogenase activity; IMP:MGI. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0007568; P:aging; IEA:Ensembl. DR GO; GO:0006068; P:ethanol catabolic process; IEA:Ensembl. DR GO; GO:0006069; P:ethanol oxidation; IEA:InterPro. DR GO; GO:0046294; P:formaldehyde catabolic process; IMP:MGI. DR GO; GO:0018119; P:peptidyl-cysteine S-nitrosylation; IMP:MGI. DR GO; GO:0045777; P:positive regulation of blood pressure; IMP:MGI. DR GO; GO:0003016; P:respiratory system process; IMP:MGI. DR GO; GO:0032496; P:response to lipopolysaccharide; IMP:MGI. DR GO; GO:0051409; P:response to nitrosative stress; IMP:MGI. DR GO; GO:0051775; P:response to redox state; IEA:Ensembl. DR GO; GO:0001523; P:retinoid metabolic process; IMP:MGI. DR Gene3D; 3.40.50.720; -; 1. DR Gene3D; 3.90.180.10; -; 1. DR InterPro; IPR014183; ADH_3. DR InterPro; IPR013149; ADH_C. DR InterPro; IPR013154; ADH_GroES-like. DR InterPro; IPR002085; ADH_SF_Zn-type. DR InterPro; IPR002328; ADH_Zn_CS. DR InterPro; IPR011032; GroES-like. DR InterPro; IPR016040; NAD(P)-bd_dom. DR PANTHER; PTHR11695; PTHR11695; 1. DR Pfam; PF08240; ADH_N; 1. DR Pfam; PF00107; ADH_zinc_N; 1. DR SUPFAM; SSF50129; SSF50129; 2. DR TIGRFAMs; TIGR02818; adh_III_F_hyde; 1. DR PROSITE; PS00059; ADH_ZINC; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Complete proteome; Cytoplasm; KW Direct protein sequencing; Metal-binding; NAD; Oxidoreductase; KW Phosphoprotein; Reference proteome; Zinc. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 374 Alcohol dehydrogenase class-3. FT /FTId=PRO_0000160760. FT METAL 45 45 Zinc 1; catalytic (By similarity). FT METAL 67 67 Zinc 1; catalytic (By similarity). FT METAL 97 97 Zinc 2 (By similarity). FT METAL 100 100 Zinc 2 (By similarity). FT METAL 103 103 Zinc 2 (By similarity). FT METAL 111 111 Zinc 2 (By similarity). FT METAL 174 174 Zinc 1; catalytic (By similarity). FT SITE 115 115 Important for FDH activity and activation FT by fatty acids (By similarity). FT MOD_RES 2 2 N-acetylalanine (By similarity). FT MOD_RES 233 233 N6-succinyllysine. FT MOD_RES 247 247 Phosphoserine. FT MOD_RES 315 315 N6-succinyllysine. FT CONFLICT 55 55 A -> R (in Ref. 1; no nucleotide entry, FT 2; AAA68896 and 3; AAC52763). FT CONFLICT 133 133 K -> R (in Ref. 4; BAE35383). FT CONFLICT 183 183 A -> T (in Ref. 4; BAE35383). FT CONFLICT 253 253 V -> I (in Ref. 4; BAE35383). FT STRAND 5 12 FT STRAND 20 26 FT STRAND 33 43 FT HELIX 45 52 FT STRAND 60 62 FT STRAND 68 75 FT STRAND 87 90 FT STRAND 97 99 FT HELIX 100 103 FT HELIX 114 118 FT STRAND 128 131 FT TURN 140 142 FT STRAND 146 152 FT HELIX 153 155 FT STRAND 156 158 FT HELIX 165 168 FT HELIX 169 172 FT HELIX 174 183 FT STRAND 193 197 FT HELIX 201 213 FT STRAND 216 221 FT HELIX 225 227 FT HELIX 228 234 FT STRAND 237 240 FT HELIX 242 244 FT HELIX 249 257 FT STRAND 261 266 FT HELIX 271 280 FT TURN 283 285 FT STRAND 287 290 FT HELIX 305 308 FT STRAND 312 315 FT HELIX 318 320 FT HELIX 323 335 FT HELIX 342 344 FT STRAND 347 351 FT HELIX 354 363 FT STRAND 369 372 SQ SEQUENCE 374 AA; 39548 MW; 32A3727B5DAB0919 CRC64; MANQVIRCKA AVAWEAGKPL SIEEIEVAPP KAHEVRIKIL ATAVCHTDAY TLSGADPEGC FPVILGHEGA GIVESVGEGV TKLKAGDTVI PLYIPQCGEC KFCLNPKTNL CQKIRVTQGK GLMPDGTSRF TCKGKSVFHF MGTSTFSEYT VVADISVAKI DPSAPLDKVC LLGCGISTGY GAAVNTAKVE PGSTCAVFGL GGVGLAVIMG CKVAGASRII GIDINKDKFA KAKEFGASEC ISPQDFSKSI QEVLVEMTDG GVDYSFECIG NVKVMRSALE AAHKGWGVSV VVGVAASGEE ISTRPFQLVT GRTWKGTAFG GWKSVESVPK LVSEYMSKKI KVDEFVTGNL SFDQINQAFD LMHSGDSIRT VLKM // ID ADRO_MOUSE Reviewed; 494 AA. AC Q61578; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 19-FEB-2014, entry version 107. DE RecName: Full=NADPH:adrenodoxin oxidoreductase, mitochondrial; DE Short=AR; DE Short=Adrenodoxin reductase; DE EC=1.18.1.6; DE AltName: Full=Ferredoxin--NADP(+) reductase; DE Short=Ferredoxin reductase; DE Flags: Precursor; GN Name=Fdxr; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=C57BL/6; TISSUE=Kidney; RX PubMed=7495857; RA Itoh S., Iemura O., Yamada E., Yoshimura T., Tsujikawa K., Kohama Y., RA Mimura T.; RT "cDNA cloning of mouse ferredoxin reductase from kidney."; RL Biochim. Biophys. Acta 1264:159-162(1995). CC -!- FUNCTION: Serves as the first electron transfer protein in all the CC mitochondrial P450 systems. Including cholesterol side chain CC cleavage in all steroidogenic tissues, steroid 11-beta CC hydroxylation in the adrenal cortex, 25-OH-vitamin D3-24 CC hydroxylation in the kidney, and sterol C-27 hydroxylation in the CC liver. CC -!- CATALYTIC ACTIVITY: 2 reduced adrenodoxin + NADP(+) = 2 oxidized CC adrenodoxin + NADPH. CC -!- COFACTOR: FAD. CC -!- PATHWAY: Steroid metabolism; cholesterol metabolism. CC -!- SUBUNIT: Monomer. Interacts directly with FDX1 (By similarity). CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix. CC -!- TISSUE SPECIFICITY: Expressed in the adrenal, testis and ovary and CC to a lesser extent in the liver and kidney. CC -!- SIMILARITY: Belongs to the ferredoxin--NADP reductase type 1 CC family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; D49920; BAA08659.1; -; mRNA. DR PIR; S60028; S60028. DR RefSeq; NP_032023.1; NM_007997.1. DR UniGene; Mm.4719; -. DR ProteinModelPortal; Q61578; -. DR SMR; Q61578; 40-494. DR IntAct; Q61578; 1. DR MINT; MINT-151907; -. DR PhosphoSite; Q61578; -. DR REPRODUCTION-2DPAGE; Q61578; -. DR PaxDb; Q61578; -. DR PRIDE; Q61578; -. DR Ensembl; ENSMUST00000021078; ENSMUSP00000021078; ENSMUSG00000018861. DR GeneID; 14149; -. DR KEGG; mmu:14149; -. DR UCSC; uc007mgy.1; mouse. DR CTD; 2232; -. DR MGI; MGI:104724; Fdxr. DR eggNOG; COG0493; -. DR GeneTree; ENSGT00390000013574; -. DR HOVERGEN; HBG002132; -. DR InParanoid; Q61578; -. DR KO; K00528; -. DR OMA; VGYKSRP; -. DR OrthoDB; EOG7H1JJX; -. DR TreeFam; TF314193; -. DR UniPathway; UPA00296; -. DR NextBio; 285258; -. DR PRO; PR:Q61578; -. DR ArrayExpress; Q61578; -. DR Bgee; Q61578; -. DR CleanEx; MM_FDXR; -. DR Genevestigator; Q61578; -. DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:MGI. DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell. DR GO; GO:0070402; F:NADPH binding; IEA:Ensembl. DR GO; GO:0015039; F:NADPH-adrenodoxin reductase activity; IEA:Ensembl. DR GO; GO:0008203; P:cholesterol metabolic process; IEA:UniProtKB-UniPathway. DR GO; GO:0070995; P:NADPH oxidation; IEA:Ensembl. DR Gene3D; 3.40.50.720; -; 2. DR InterPro; IPR021163; Adrenodoxin_Rdtase. DR InterPro; IPR016040; NAD(P)-bd_dom. DR PIRSF; PIRSF000362; FNR; 1. PE 2: Evidence at transcript level; KW Cholesterol metabolism; Complete proteome; Electron transport; FAD; KW Flavoprotein; Lipid metabolism; Mitochondrion; NADP; Oxidoreductase; KW Reference proteome; Steroid metabolism; Sterol metabolism; KW Transit peptide; Transport. FT TRANSIT 1 34 Mitochondrion (Potential). FT CHAIN 35 494 NADPH:adrenodoxin oxidoreductase, FT mitochondrial. FT /FTId=PRO_0000019421. FT NP_BIND 187 190 NADP (By similarity). FT NP_BIND 231 232 NADP (By similarity). FT NP_BIND 408 410 FAD (By similarity). FT BINDING 51 51 FAD; via amide nitrogen (By similarity). FT BINDING 72 72 FAD (By similarity). FT BINDING 80 80 FAD; via amide nitrogen (By similarity). FT BINDING 116 116 FAD; via amide nitrogen and carbonyl FT oxygen (By similarity). FT BINDING 243 243 NADP (By similarity). FT BINDING 401 401 FAD; via amide nitrogen (By similarity). FT BINDING 408 408 NADP; via amide nitrogen (By similarity). SQ SEQUENCE 494 AA; 54202 MW; 4BD279DFC606A5C5 CRC64; MAPRCWHWWR WSAWSGLRPS PSRSTPTPGF CQKFSTQEKT PQICVVGSGP AGFYTAQHLL KHHTHAHVDI YEKQLVPFGL VRFGVAPDHP EVKNVINTFT QTARSDRCAF QGNVVVGRDV SVPELREAYH AVVLSYGAED HQPLGIPGEE LPGVVSARAF VGWYNGLPEN QELAPDLSCD TAVILGQGNV ALDVARILLT PPEHLEKTDI TEAALGALRQ SRVKTVWIVG RRGPLQVAFT IKELREMIQL PGTRPILDPS DFLGLQDRIK DVPRPRRRLT ELLLRTATEK PGVEEAARQA LASRAWGLRF FRSPQQVLPT PDGQRVAGIR LAVTSLEGVG ESTRAVPTGD VEDLPCGLLL SSVGYKSRPI DPSVPFDPKL GVIPNTEGRV VNVPGLYCSG WVKRGPTGVI TTTMTDSFLT SQALLEDLKA GLLPSGPRPG YVAIQALLSN RGVRPVSFSD WEKLDAEEVS RGQGTGKPRE KLVDRREMLR LLGH // ID AEDO_MOUSE Reviewed; 256 AA. AC Q6PDY2; Q3U2E1; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 21-FEB-2006, sequence version 2. DT 19-FEB-2014, entry version 82. DE RecName: Full=2-aminoethanethiol dioxygenase; DE EC=1.13.11.19; DE AltName: Full=Cysteamine dioxygenase; GN Name=Ado; Synonyms=Gm237; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=NOD; TISSUE=Dendritic cell; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6; TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP CATALYTIC ACTIVITY, COFACTOR, AND TISSUE SPECIFICITY. RX PubMed=17581819; DOI=10.1074/jbc.M703089200; RA Dominy J.E. Jr., Simmons C.R., Hirschberger L.L., Hwang J., RA Coloso R.M., Stipanuk M.H.; RT "Discovery and characterization of a second mammalian thiol RT dioxygenase, cysteamine dioxygenase."; RL J. Biol. Chem. 282:25189-25198(2007). CC -!- CATALYTIC ACTIVITY: 2-aminoethanethiol + O(2) = hypotaurine. CC -!- COFACTOR: Iron. CC -!- TISSUE SPECIFICITY: Ubiquitous, with highest expression in brain, CC heart and skeletal muscle (at protein level). CC -!- SEQUENCE CAUTION: CC Sequence=AAH57106.1; Type=Erroneous initiation; CC Sequence=AAH58407.1; Type=Erroneous initiation; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK155334; BAE33200.1; -; mRNA. DR EMBL; BC057106; AAH57106.1; ALT_INIT; mRNA. DR EMBL; BC058407; AAH58407.1; ALT_INIT; mRNA. DR RefSeq; NP_001005419.2; NM_001005419.2. DR UniGene; Mm.297250; -. DR UniGene; Mm.491461; -. DR ProteinModelPortal; Q6PDY2; -. DR PhosphoSite; Q6PDY2; -. DR PaxDb; Q6PDY2; -. DR PRIDE; Q6PDY2; -. DR DNASU; 211488; -. DR Ensembl; ENSMUST00000075686; ENSMUSP00000075107; ENSMUSG00000057134. DR GeneID; 211488; -. DR KEGG; mmu:211488; -. DR UCSC; uc007flz.2; mouse. DR CTD; 84890; -. DR MGI; MGI:2685083; Ado. DR eggNOG; NOG301373; -. DR GeneTree; ENSGT00390000014082; -. DR HOGENOM; HOG000037604; -. DR HOVERGEN; HBG050966; -. DR InParanoid; Q6PDY2; -. DR KO; K10712; -. DR OMA; EASGPCV; -. DR OrthoDB; EOG7NKKMH; -. DR TreeFam; TF314673; -. DR NextBio; 373260; -. DR PRO; PR:Q6PDY2; -. DR Bgee; Q6PDY2; -. DR CleanEx; MM_ADO; -. DR Genevestigator; Q6PDY2; -. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR GO; GO:0047800; F:cysteamine dioxygenase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR Gene3D; 2.60.120.10; -; 1. DR InterPro; IPR012864; Cysteamine_dioxygenase. DR InterPro; IPR014710; RmlC-like_jellyroll. DR InterPro; IPR011051; RmlC_Cupin. DR Pfam; PF07847; DUF1637; 1. DR SUPFAM; SSF51182; SSF51182; 1. PE 1: Evidence at protein level; KW Complete proteome; Dioxygenase; Iron; Metal-binding; Oxidoreductase; KW Reference proteome. FT CHAIN 1 256 2-aminoethanethiol dioxygenase. FT /FTId=PRO_0000089785. SQ SEQUENCE 256 AA; 28372 MW; C5E23C4A72A79678 CRC64; MPRDNMASLI QRIARQACLT FRGSSTGSEG PAPGFPENLS LLKSLLTQVR AEDLNIAPRK ALPQPLPRNL PPVTYMHIYE TEGFSLGVFL LKSGTCIPLH DHPGMHGMLK VLYGTVRISC MDKLDTGAGH RRPPPEQQFE PPLQPLEREA VRPGVLRSRA EYTEASGPCV LTPHRDNLHQ IDAVDGPAAF LDILAPPYDP EDGRDCHYYR VVEPIRPKEA SGSACDLPRE VWLLETPQAD DFWCEGEPYP GPKVLP // ID AIFM1_MOUSE Reviewed; 612 AA. AC Q9Z0X1; DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1999, sequence version 1. DT 19-MAR-2014, entry version 129. DE RecName: Full=Apoptosis-inducing factor 1, mitochondrial; DE EC=1.1.1.-; DE AltName: Full=Programmed cell death protein 8; DE Flags: Precursor; GN Name=Aifm1; Synonyms=Aif, Pdcd8; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF N-TERMINUS, PROTEIN RP SEQUENCE OF 322-336, FUNCTION, COFACTOR, MASS SPECTROMETRY, AND RP SUBCELLULAR LOCATION. RX PubMed=9989411; DOI=10.1038/17135; RA Susin S.A., Lorenzo H.K., Zamzami N., Marzo I., Snow B.E., RA Brothers G.M., Mangion J., Jacotot E., Costantini P., Loeffler M., RA Larochette N., Goodlett D.R., Aebersold R., Siderovski D.P., RA Penninger J.M., Kroemer G.; RT "Molecular characterization of mitochondrial apoptosis-inducing RT factor."; RL Nature 397:441-446(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Mammary gland; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP PROTEIN SEQUENCE OF 378-386, AND MASS SPECTROMETRY. RC STRAIN=OF1; TISSUE=Hippocampus; RA Lubec G., Sunyer B., Chen W.-Q.; RL Submitted (JAN-2009) to UniProtKB. RN [4] RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-108, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., RA Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). RN [5] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-387 AND LYS-592, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23576753; DOI=10.1073/pnas.1302961110; RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., RA Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.; RT "Label-free quantitative proteomics of the lysine acetylome in RT mitochondria identifies substrates of SIRT3 in metabolic pathways."; RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013). RN [6] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 108-610 IN COMPLEX WITH FAD, RP NAD-BINDING, AND MUTAGENESIS OF LYS-176 AND GLU-313. RX PubMed=11967568; DOI=10.1038/nsb793; RA Mate M.J., Ortiz-Lombardia M., Boitel B., Haouz A., Tello D., RA Susin S.A., Penninger J., Kroemer G., Alzari P.M.; RT "The crystal structure of the mouse apoptosis-inducing factor AIF."; RL Nat. Struct. Biol. 9:442-446(2002). CC -!- FUNCTION: Functions both as NADH oxidoreductase and as regulator CC of apoptosis. In response to apoptotic stimuli, it is released CC from the mitochondrion intermembrane space into the cytosol and to CC the nucleus, where it functions as a proapoptotic factor in a CC caspase-independent pathway. In contrast, functions as an CC antiapoptotic factor in normal mitochondria via its NADH CC oxidoreductase activity. The soluble form (AIFsol) found in the CC nucleus induces 'parthanatos' i.e. caspase-independent CC fragmentation of chromosomal DNA. Interacts with EIF3G,and thereby CC inhibits the EIF3 machinery and protein synthesis,and activates CC casapse-7 to amplify apoptosis. Plays a critical role in caspase- CC independent, pyknotic cell death in hydrogen peroxide-exposed CC cells. Binds to DNA in a sequence-independent manner (By CC similarity). CC -!- COFACTOR: FAD. CC -!- SUBUNIT: Monomer (oxidized form). Homodimer (reduced form). CC Interacts with XIAP/BIRC4. Interacts (via N-terminus) with EIF3G CC (via C-terminus). Interacts with PRELID1 (By similarity). CC -!- INTERACTION: CC P16104:H2AFX (xeno); NbExp=2; IntAct=EBI-5326677, EBI-494830; CC P27661:H2afx; NbExp=3; IntAct=EBI-773597, EBI-495621; CC Q9EQN3:Tsc22d4; NbExp=4; IntAct=EBI-773597, EBI-7821198; CC -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space. CC Mitochondrion inner membrane (By similarity). Cytoplasm (By CC similarity). Cytoplasm, perinuclear region (By similarity). CC Nucleus. Note=Proteolytic cleavage during or just after CC translocation into the mitochondrial intermembrane space (IMS) CC results in the formation of an inner-membrane-anchored mature form CC (AIFmit). During apoptosis, further proteolytic processing leads CC to a mature form, which is confined to the mitochondrial IMS in a CC soluble form (AIFsol). AIFsol is released to the cytoplasm in CC response to specific death signals, and translocated to the CC nucleus, where it induces nuclear apoptosis. Colocalizes with CC EIF3G in the nucleus and perinuclear region (By similarity). CC -!- PTM: Under normal conditions, a 54-residue N-terminal segment is CC first proteolytically removed during or just after translocation CC into the mitochondrial intermembrane space (IMS) by the CC mitochondrial processing peptidase (MPP) to form the inner- CC membrane-anchored mature form (AIFmit). During apoptosis, it is CC further proteolytically processed at amino-acid position 101 CC leading to the generation of the mature form, which is confined to CC the mitochondrial IMS in a soluble form (AIFsol). AIFsol is CC released to the cytoplasm in response to specific death signals, CC and translocated to the nucleus, where it induces nuclear CC apoptosis in a caspase-independent manner (By similarity). CC -!- PTM: Ubiquitination by XIAP/BIRC4 does not lead to proteasomal CC degradation. Ubiquitination at Lys-254 by XIAP/BIRC4 blocks its CC ability to bind DNA and induce chromatin degradation, thereby CC inhibiting its ability to induce cell death (By similarity). CC -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF100927; AAD16435.1; -; mRNA. DR EMBL; BC003292; AAH03292.1; -; mRNA. DR RefSeq; NP_036149.1; NM_012019.2. DR UniGene; Mm.240434; -. DR PDB; 1GV4; X-ray; 2.00 A; A/B=122-610. DR PDB; 3GD3; X-ray; 2.95 A; A/B/C/D=78-612. DR PDB; 3GD4; X-ray; 2.24 A; A/B=102-612. DR PDBsum; 1GV4; -. DR PDBsum; 3GD3; -. DR PDBsum; 3GD4; -. DR ProteinModelPortal; Q9Z0X1; -. DR SMR; Q9Z0X1; 121-610. DR BioGrid; 205067; 3. DR IntAct; Q9Z0X1; 13. DR MINT; MINT-1862023; -. DR STRING; 10090.ENSMUSP00000041104; -. DR PhosphoSite; Q9Z0X1; -. DR PaxDb; Q9Z0X1; -. DR PRIDE; Q9Z0X1; -. DR Ensembl; ENSMUST00000037349; ENSMUSP00000041104; ENSMUSG00000036932. DR GeneID; 26926; -. DR KEGG; mmu:26926; -. DR UCSC; uc009tcg.1; mouse. DR CTD; 9131; -. DR MGI; MGI:1349419; Aifm1. DR eggNOG; COG0446; -. DR GeneTree; ENSGT00530000063416; -. DR HOGENOM; HOG000264253; -. DR HOVERGEN; HBG053538; -. DR InParanoid; Q9Z0X1; -. DR KO; K04727; -. DR OMA; KDGEEHA; -. DR TreeFam; TF314028; -. DR ChiTaRS; AIFM1; mouse. DR EvolutionaryTrace; Q9Z0X1; -. DR NextBio; 304817; -. DR PRO; PR:Q9Z0X1; -. DR ArrayExpress; Q9Z0X1; -. DR Bgee; Q9Z0X1; -. DR Genevestigator; Q9Z0X1; -. DR GO; GO:0005829; C:cytosol; IDA:UniProtKB. DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005758; C:mitochondrial intermembrane space; ISS:UniProtKB. DR GO; GO:0005741; C:mitochondrial outer membrane; TAS:MGI. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB. DR GO; GO:0004174; F:electron-transferring-flavoprotein dehydrogenase activity; TAS:MGI. DR GO; GO:0071949; F:FAD binding; IDA:UniProtKB. DR GO; GO:0016174; F:NAD(P)H oxidase activity; IDA:UniProtKB. DR GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; ISS:UniProtKB. DR GO; GO:0006309; P:apoptotic DNA fragmentation; IGI:MGI. DR GO; GO:0008637; P:apoptotic mitochondrial changes; TAS:MGI. DR GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro. DR GO; GO:0070059; P:intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress; IMP:UniProtKB. DR GO; GO:0032981; P:mitochondrial respiratory chain complex I assembly; IEA:Ensembl. DR GO; GO:0051402; P:neuron apoptotic process; IGI:MGI. DR GO; GO:0030182; P:neuron differentiation; IEA:Ensembl. DR GO; GO:0043065; P:positive regulation of apoptotic process; TAS:UniProtKB. DR GO; GO:0006979; P:response to oxidative stress; TAS:UniProtKB. DR Gene3D; 3.30.390.30; -; 1. DR InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer. DR InterPro; IPR013027; FAD_pyr_nucl-diS_OxRdtase. DR InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer. DR InterPro; IPR023753; Pyr_nucl-diS_OxRdtase_FAD/NAD. DR InterPro; IPR001327; Pyr_OxRdtase_NAD-bd_dom. DR Pfam; PF00070; Pyr_redox; 1. DR Pfam; PF07992; Pyr_redox_2; 1. DR PRINTS; PR00368; FADPNR. DR SUPFAM; SSF55424; SSF55424; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Apoptosis; Complete proteome; Cytoplasm; KW Direct protein sequencing; DNA-binding; FAD; Flavoprotein; KW Isopeptide bond; Membrane; Mitochondrion; KW Mitochondrion inner membrane; NAD; Nucleus; Oxidoreductase; KW Phosphoprotein; Reference proteome; Transit peptide; Ubl conjugation. FT TRANSIT 1 54 Mitochondrion (By similarity). FT PROPEP 55 101 Removed in mature form. FT /FTId=PRO_0000401936. FT CHAIN 102 612 Apoptosis-inducing factor 1, FT mitochondrial. FT /FTId=PRO_0000022031. FT NP_BIND 137 141 FAD. FT NP_BIND 163 164 FAD. FT NP_BIND 453 454 FAD. FT REGION 133 482 FAD-dependent oxidoreductase. FT MOTIF 445 450 Nuclear localization signal (Potential). FT BINDING 171 171 FAD. FT BINDING 176 176 FAD. FT BINDING 232 232 FAD; via amide nitrogen and carbonyl FT oxygen. FT BINDING 284 284 FAD. FT BINDING 437 437 FAD. FT BINDING 482 482 FAD; via carbonyl oxygen. FT MOD_RES 108 108 N6-succinyllysine. FT MOD_RES 267 267 Phosphoserine (By similarity). FT MOD_RES 387 387 N6-acetyllysine. FT MOD_RES 592 592 N6-acetyllysine. FT CROSSLNK 254 254 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in ubiquitin) (By FT similarity). FT MUTAGEN 176 176 K->A: Increases catalytic efficiency. FT MUTAGEN 313 313 E->A: Increases catalytic efficiency 30- FT fold. Increases affinity for NADH 20- FT fold. FT STRAND 129 137 FT HELIX 140 152 FT STRAND 157 166 FT HELIX 172 175 FT HELIX 177 179 FT HELIX 186 189 FT STRAND 191 193 FT STRAND 199 205 FT HELIX 207 209 FT HELIX 213 218 FT STRAND 223 229 FT STRAND 232 236 FT TURN 237 240 FT STRAND 241 244 FT STRAND 249 257 FT STRAND 261 263 FT HELIX 267 270 FT HELIX 274 277 FT STRAND 280 282 FT HELIX 286 296 FT STRAND 300 305 FT HELIX 309 325 FT STRAND 328 332 FT STRAND 334 337 FT TURN 338 342 FT HELIX 345 356 FT TURN 357 359 FT STRAND 361 363 FT STRAND 368 374 FT STRAND 377 382 FT STRAND 387 395 FT STRAND 399 401 FT HELIX 404 406 FT TURN 407 410 FT TURN 415 417 FT STRAND 419 421 FT STRAND 426 429 FT STRAND 432 434 FT HELIX 436 438 FT STRAND 439 443 FT TURN 444 446 FT STRAND 447 449 FT HELIX 454 468 FT TURN 469 471 FT STRAND 480 486 FT STRAND 490 495 FT STRAND 503 508 FT HELIX 516 523 FT HELIX 528 532 FT STRAND 539 542 FT HELIX 556 558 FT STRAND 561 579 FT HELIX 584 593 FT HELIX 600 604 FT HELIX 605 607 SQ SEQUENCE 612 AA; 66765 MW; A17EDFD5CF77BB85 CRC64; MFRCGGLAGA FKQKLVPLVR TVYVQRPKQR NRLPGNLFQQ WRVPLELQMA RQMASSGSSG GKMDNSVLVL IVGLSTIGAG AYAYKTIKED QKRYNERVMG LGLSPEEKQR RAIASATEGG SVPQIRAPSH VPFLLIGGGT AAFAAARSIR ARDPGARVLI VSEDPELPYM RPPLSKELWF SDDPNVTKTL QFRQWNGKER SIYFQPPSFY VSAQDLPNIE NGGVAVLTGK KVVHLDVRGN MVKLNDGSQI TFEKCLIATG GTPRSLSAID RAGAEVKSRT TLFRKIGDFR ALEKISREVK SITVIGGGFL GSELACALGR KSQASGIEVI QLFPEKGNMG KILPQYLSNW TMEKVKREGV KVMPNAIVQS VGVSGGRLLI KLKDGRKVET DHIVTAVGLE PNVELAKTGG LEIDSDFGGF RVNAELQARS NIWVAGDAAC FYDIKLGRRR VEHHDHAVVS GRLAGENMTG AAKPYWHQSM FWSDLGPDVG YEAIGLVDSS LPTVGVFAKA TAQDNPKSAT EQSGTGIRSE SETESEASEI TIPPSAPAVP QVPVEGEDYG KGVIFYLRDK VVVGIVLWNV FNRMPIARKI IKDGEQHEDL NEVAKLFNIH ED // ID AIFM2_MOUSE Reviewed; 373 AA. AC Q8BUE4; Q8CHZ2; DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 19-MAR-2014, entry version 87. DE RecName: Full=Apoptosis-inducing factor 2; DE EC=1.-.-.-; DE AltName: Full=Apoptosis-inducing factor homologous mitochondrion-associated inducer of death; DE AltName: Full=Apoptosis-inducing factor-like mitochondrion-associated inducer of death; GN Name=Aifm2; Synonyms=Amid; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC STRAIN=C57BL/6J, and NOD; RC TISSUE=Dendritic cell, Mammary gland, and Melanocyte; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC STRAIN=C57BL/6J; TISSUE=Mammary gland; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP TISSUE SPECIFICITY, AND INDUCTION. RX PubMed=16186796; DOI=10.1038/sj.onc.1209121; RA Mei J., Webb S., Zhang B., Shu H.-B.; RT "The p53-inducible apoptotic protein AMID is not required for normal RT development and tumor suppression."; RL Oncogene 25:849-856(2006). CC -!- FUNCTION: Oxidoreductase, which may play a role in mediating a CC p53/TP53-dependent apoptosis response. Probable oxidoreductase CC that acts as a caspase-independent mitochondrial effector of CC apoptotic cell death (By similarity). May contribute to genotoxin- CC induced growth arrest. CC -!- COFACTOR: Binds 6-hydroxy-FAD non-covalently (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm. Mitochondrion outer membrane (By CC similarity). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q8BUE4-1; Sequence=Displayed; CC Note=No experimental confirmation available; CC Name=2; CC IsoId=Q8BUE4-2; Sequence=VSP_052049; CC Note=Ref.3 (AAH38129) sequence differs from that shown due to CC erroneous termination (Translated as Trp in position: CC 339:Stop->W). No experimental confirmation available; CC -!- TISSUE SPECIFICITY: Detected in most normal tissues as two CC transcripts of 1.8 and 4.0 kb in length, respectively. Highly CC expressed in liver, testis, and kidney, and expressed at lower CC levels in pancreas, spleen, brain and lung. CC -!- INDUCTION: Expression is up-regulated in mouse embryonic CC fibroblasts by genotoxic reagents 5-fluorouracil and etoposide. CC -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK085656; BAC39497.1; -; mRNA. DR EMBL; AK155240; BAE33142.1; -; mRNA. DR EMBL; AK147741; BAE28108.1; -; mRNA. DR EMBL; AC153136; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC038129; AAH38129.1; ALT_SEQ; mRNA. DR RefSeq; NP_001034283.1; NM_001039194.3. DR RefSeq; NP_001271229.1; NM_001284300.1. DR RefSeq; NP_722474.2; NM_153779.2. DR RefSeq; NP_835159.1; NM_178058.4. DR RefSeq; XP_006514187.1; XM_006514124.1. DR RefSeq; XP_006514191.1; XM_006514128.1. DR UniGene; Mm.286309; -. DR ProteinModelPortal; Q8BUE4; -. DR SMR; Q8BUE4; 12-315. DR STRING; 10090.ENSMUSP00000078998; -. DR PhosphoSite; Q8BUE4; -. DR PaxDb; Q8BUE4; -. DR PRIDE; Q8BUE4; -. DR Ensembl; ENSMUST00000067857; ENSMUSP00000070054; ENSMUSG00000020085. [Q8BUE4-1] DR Ensembl; ENSMUST00000080099; ENSMUSP00000078998; ENSMUSG00000020085. [Q8BUE4-2] DR Ensembl; ENSMUST00000099706; ENSMUSP00000097297; ENSMUSG00000020085. [Q8BUE4-1] DR Ensembl; ENSMUST00000105455; ENSMUSP00000101095; ENSMUSG00000020085. [Q8BUE4-1] DR GeneID; 71361; -. DR KEGG; mmu:71361; -. DR UCSC; uc007fgi.2; mouse. [Q8BUE4-1] DR UCSC; uc007fgl.1; mouse. [Q8BUE4-2] DR CTD; 84883; -. DR MGI; MGI:1918611; Aifm2. DR eggNOG; COG1252; -. DR GeneTree; ENSGT00390000004582; -. DR HOGENOM; HOG000238788; -. DR HOVERGEN; HBG054912; -. DR OMA; PFTLVDM; -. DR OrthoDB; EOG7J447T; -. DR TreeFam; TF329369; -. DR NextBio; 333621; -. DR PRO; PR:Q8BUE4; -. DR Bgee; Q8BUE4; -. DR Genevestigator; Q8BUE4; -. DR GO; GO:0005829; C:cytosol; ISS:UniProtKB. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005811; C:lipid particle; IEA:Ensembl. DR GO; GO:0005741; C:mitochondrial outer membrane; ISS:UniProtKB. DR GO; GO:0003677; F:DNA binding; ISS:UniProtKB. DR GO; GO:0004174; F:electron-transferring-flavoprotein dehydrogenase activity; ISS:UniProtKB. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; ISS:UniProtKB. DR GO; GO:0008637; P:apoptotic mitochondrial changes; IEA:Ensembl. DR GO; GO:0030261; P:chromosome condensation; ISS:UniProtKB. DR GO; GO:0097194; P:execution phase of apoptosis; ISS:UniProtKB. DR InterPro; IPR013027; FAD_pyr_nucl-diS_OxRdtase. DR InterPro; IPR023753; Pyr_nucl-diS_OxRdtase_FAD/NAD. DR InterPro; IPR001327; Pyr_OxRdtase_NAD-bd_dom. DR InterPro; IPR000103; Pyridine_nuc-diS_OxRdtase_2. DR Pfam; PF00070; Pyr_redox; 1. DR Pfam; PF07992; Pyr_redox_2; 1. DR PRINTS; PR00368; FADPNR. DR PRINTS; PR00469; PNDRDTASEII. PE 2: Evidence at transcript level; KW Alternative splicing; Complete proteome; Cytoplasm; DNA-binding; FAD; KW Flavoprotein; Lipoprotein; Membrane; Mitochondrion; KW Mitochondrion outer membrane; Myristate; Oxidoreductase; KW Reference proteome; Transmembrane; Transmembrane helix. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 373 Apoptosis-inducing factor 2. FT /FTId=PRO_0000238923. FT TRANSMEM 7 27 Helical; (Potential). FT NP_BIND 18 22 6-hydroxy-FAD (Potential). FT BINDING 54 54 6-hydroxy-FAD (Potential). FT BINDING 82 82 6-hydroxy-FAD; via amide nitrogen and FT carbonyl oxygen (Potential). FT BINDING 285 285 6-hydroxy-FAD (Potential). FT LIPID 2 2 N-myristoyl glycine (By similarity). FT VAR_SEQ 324 373 GALTFLLSMGRNDGVGQISGFYVGRLMVRLAKSRDLLISTS FT WKTMRQSPP -> ETDQPPAALSPALLLWTPARKLTLSEGR FT INYLQEAGHVRTLQSMAGLFSDRPCVISL (in isoform FT 2). FT /FTId=VSP_052049. SQ SEQUENCE 373 AA; 40635 MW; A85F02A26C1084BA CRC64; MGSQVSVDTG AVHVVIVGGG FGGIAAASQL QALNVPFMLV DMKDSFHHNV AALRASVESG FAKKTFISYS ATFKDNFRQG KVIGIDLKNR MVLLQGGEAL PFSHLILATG STGPFPGKFN EVSCQQAAIQ AYEDMVKQIQ RSQFIVVVGG GSAGVEMAAE IKTEYPEKEV TLIHSRVPLA DKELLPCVRQ EVKEILLRKG VQLLLSERVS NLEELPRNEY REYIKVETDK GTEVATNMVI VCNGIKINSS AYRSAFESRL ASNGALKVNE FLQVEGYSNI YAIGDCADTK EPKMAYHAGL HANVAVANIV NSMKQRPLKA YKPGALTFLL SMGRNDGVGQ ISGFYVGRLM VRLAKSRDLL ISTSWKTMRQ SPP // ID AIFM3_MOUSE Reviewed; 605 AA. AC Q3TY86; Q0VBD6; Q4VAA4; Q8BWV0; DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2005, sequence version 1. DT 19-MAR-2014, entry version 76. DE RecName: Full=Apoptosis-inducing factor 3; DE EC=1.-.-.-; DE AltName: Full=Apoptosis-inducing factor-like protein; GN Name=Aifm3; Synonyms=Aifl; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3). RC STRAIN=C57BL/6J; TISSUE=Hippocampus, and Visual cortex; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3). RC STRAIN=FVB/N; TISSUE=Brain, and Kidney; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: Induces apoptosis through a caspase dependent pathway. CC Reduces mitochondrial membrane potential (By similarity). CC -!- SUBCELLULAR LOCATION: Mitochondrion. Note=Does not translocate to CC the nucleus upon induction of apoptosis (By similarity). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q3TY86-1; Sequence=Displayed; CC Name=2; CC IsoId=Q3TY86-2; Sequence=VSP_021306; CC Note=No experimental confirmation available; CC Name=3; CC IsoId=Q3TY86-3; Sequence=VSP_021304, VSP_021305; CC -!- DOMAIN: The Rieske domain induces apoptosis (By similarity). CC -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase family. CC -!- SIMILARITY: Contains 1 Rieske domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK049928; BAC33988.1; -; mRNA. DR EMBL; AK158809; BAE34677.1; -; mRNA. DR EMBL; BC096476; AAH96476.1; -; mRNA. DR EMBL; BC120685; AAI20686.1; -; mRNA. DR RefSeq; NP_780387.2; NM_175178.3. DR RefSeq; XP_006522655.1; XM_006522592.1. DR UniGene; Mm.40038; -. DR ProteinModelPortal; Q3TY86; -. DR SMR; Q3TY86; 72-170, 192-562. DR PhosphoSite; Q3TY86; -. DR PaxDb; Q3TY86; -. DR PRIDE; Q3TY86; -. DR Ensembl; ENSMUST00000023448; ENSMUSP00000023448; ENSMUSG00000022763. [Q3TY86-2] DR Ensembl; ENSMUST00000115685; ENSMUSP00000111349; ENSMUSG00000022763. [Q3TY86-1] DR GeneID; 72168; -. DR KEGG; mmu:72168; -. DR UCSC; uc007ykw.1; mouse. [Q3TY86-1] DR UCSC; uc007ykx.1; mouse. [Q3TY86-3] DR UCSC; uc007yky.1; mouse. [Q3TY86-2] DR CTD; 150209; -. DR MGI; MGI:1919418; Aifm3. DR eggNOG; COG0446; -. DR GeneTree; ENSGT00530000063416; -. DR HOGENOM; HOG000276711; -. DR HOVERGEN; HBG052926; -. DR InParanoid; Q3TY86; -. DR OMA; KTGDMSW; -. DR OrthoDB; EOG77DJ5F; -. DR TreeFam; TF314028; -. DR NextBio; 335607; -. DR PRO; PR:Q3TY86; -. DR Bgee; Q3TY86; -. DR Genevestigator; Q3TY86; -. DR GO; GO:0005783; C:endoplasmic reticulum; ISS:HGNC. DR GO; GO:0005743; C:mitochondrial inner membrane; ISS:HGNC. DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW. DR GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro. DR GO; GO:0097194; P:execution phase of apoptosis; ISS:BHF-UCL. DR Gene3D; 2.102.10.10; -; 1. DR Gene3D; 3.30.390.30; -; 1. DR InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer. DR InterPro; IPR013027; FAD_pyr_nucl-diS_OxRdtase. DR InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer. DR InterPro; IPR023753; Pyr_nucl-diS_OxRdtase_FAD/NAD. DR InterPro; IPR001327; Pyr_OxRdtase_NAD-bd_dom. DR InterPro; IPR000103; Pyridine_nuc-diS_OxRdtase_2. DR InterPro; IPR028202; Reductase_C. DR InterPro; IPR017941; Rieske_2Fe-2S. DR Pfam; PF00070; Pyr_redox; 1. DR Pfam; PF07992; Pyr_redox_2; 1. DR Pfam; PF14759; Reductase_C; 1. DR Pfam; PF00355; Rieske; 1. DR PRINTS; PR00368; FADPNR. DR PRINTS; PR00469; PNDRDTASEII. DR SUPFAM; SSF50022; SSF50022; 1. DR SUPFAM; SSF55424; SSF55424; 1. DR PROSITE; PS51296; RIESKE; 1. PE 2: Evidence at transcript level; KW 2Fe-2S; Alternative splicing; Apoptosis; Complete proteome; KW Electron transport; FAD; Flavoprotein; Iron; Iron-sulfur; KW Metal-binding; Mitochondrion; Oxidoreductase; Reference proteome; KW Transport. FT CHAIN 1 605 Apoptosis-inducing factor 3. FT /FTId=PRO_0000255661. FT DOMAIN 70 165 Rieske. FT NP_BIND 201 205 FAD (Potential). FT METAL 109 109 Iron-sulfur (2Fe-2S) (By similarity). FT METAL 111 111 Iron-sulfur (2Fe-2S); via pros nitrogen FT (By similarity). FT METAL 128 128 Iron-sulfur (2Fe-2S) (By similarity). FT METAL 131 131 Iron-sulfur (2Fe-2S); via pros nitrogen FT (By similarity). FT BINDING 235 235 FAD (Potential). FT BINDING 240 240 FAD (Potential). FT BINDING 270 270 FAD; via amide nitrogen and carbonyl FT oxygen (Potential). FT BINDING 467 467 FAD (Potential). FT BINDING 514 514 FAD; via carbonyl oxygen (Potential). FT VAR_SEQ 494 500 RVAAQNM -> MASPEAS (in isoform 3). FT /FTId=VSP_021304. FT VAR_SEQ 501 605 Missing (in isoform 3). FT /FTId=VSP_021305. FT VAR_SEQ 587 593 Missing (in isoform 2). FT /FTId=VSP_021306. FT CONFLICT 138 138 S -> T (in Ref. 1; BAC33988). SQ SEQUENCE 605 AA; 66792 MW; D4811CB2B2CD0739 CRC64; MGGCFSKPKP VELKIEVVLP EKERGKEELS ASGKGSPRGY QGNGTARHFH AEERLPTPQP YPSPQDCVEA TVCHVKDLEN GQMREVELGW GKVLLVKDNG EFHALGHKCP HYGAPLVKGV LSRGRVRCPW HGACFNISTG DLEDFPGLDS LHKFQVKIEK EKVTIRASKQ ALQLQRRTKV MAKCISPSAG HSSSTNVLIV GAGAAGLVCA ETLRQEGFSD RIVLCTLDRH LPYDRAKLSK SLDAQPEQLA LRPKEFFRAY GIEMLTEAQV VTVDVRNKKV VFKDGFKLEY SKLLLAPGSS PKTLTCKGKD VENVFTIRTP EDANRVLRLA RGRNAVVVGA GFLGMEVAAY LTEKAHSVSV VELEETPFRR FLGERVGRAL MKMFENNRVK FYMQTEVSEL RAQEGKLQEV VLKSSKVLRA DVCVLGIGAV PATGFLRQSG IGLDSRGFIP VNKMMQTNVP GVFAAGDAVT FPLAWRNNRK VNIPHWQMAH AQGRVAAQNM LAQEAEINTV PYLWTAMFGK SLRYAGYGEG FDDVIIQGDL EELKFVAFYT KSDEVIAVAS MNYDPIVSKV AEVLASGRAI RKREVELFML HSKTGDMSWL TGKGS // ID AK1A1_MOUSE Reviewed; 325 AA. AC Q9JII6; Q9CQI5; Q9CQT8; Q9CT53; Q9D012; Q9D016; Q9D0I7; Q9D0P3; DT 30-AUG-2002, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 19-MAR-2014, entry version 112. DE RecName: Full=Alcohol dehydrogenase [NADP(+)]; DE EC=1.1.1.2; DE AltName: Full=Aldehyde reductase; DE AltName: Full=Aldo-keto reductase family 1 member A1; GN Name=Akr1a1; Synonyms=Akr1a4; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY. RC TISSUE=Embryo; RX PubMed=10842086; DOI=10.1016/S0925-4773(00)00293-8; RA Allan D., Lohnes D.; RT "Cloning and developmental expression of mouse aldehyde reductase RT (AKR1A4)."; RL Mech. Dev. 94:271-275(2000). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Cerebellum, Embryo, and Tongue; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Mammary gland; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP PROTEIN SEQUENCE OF 2-13 AND 244-251, CLEAVAGE OF INITIATOR RP METHIONINE, ACETYLATION AT THR-2, AND MASS SPECTROMETRY. RC STRAIN=C57BL/6; TISSUE=Liver; RA Bienvenut W.V.; RL Submitted (JUL-2005) to UniProtKB. RN [5] RP PROTEIN SEQUENCE OF 204-218; 222-240 AND 313-325, AND MASS RP SPECTROMETRY. RC TISSUE=Hippocampus; RA Lubec G., Klug S.; RL Submitted (MAR-2007) to UniProtKB. RN [6] RP INDUCTION. RX PubMed=11533224; DOI=10.1101/lm.39401; RA Stork O., Stork S., Pape H.-C., Obata K.; RT "Identification of genes expressed in the amygdala during the RT formation of fear memory."; RL Learn. Memory 8:209-219(2001). RN [7] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-127, SUCCINYLATION [LARGE RP SCALE ANALYSIS] AT LYS-127 AND LYS-145, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic fibroblast, and Liver; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., RA Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). CC -!- FUNCTION: Catalyzes the NADPH-dependent reduction of a variety of CC aromatic and aliphatic aldehydes to their corresponding alcohols. CC Catalyzes the reduction of mevaldate to mevalonic acid and of CC glyceraldehyde to glycerol. Has broad substrate specificity. Plays CC a role in the activation of procarcinogens, such as polycyclic CC aromatic hydrocarbon trans-dihydrodiols, and in the metabolism of CC various xenobiotics and drugs (By similarity). CC -!- CATALYTIC ACTIVITY: An alcohol + NADP(+) = an aldehyde + NADPH. CC -!- SUBUNIT: Monomer (By similarity). CC -!- TISSUE SPECIFICITY: Widely expressed. CC -!- DEVELOPMENTAL STAGE: Detected at high levels in several tissues CC including neural ectoderm, gut endoderm, somites, branchial CC arches, otic vesicles, limb buds and tail bud. CC -!- INDUCTION: Fear memory increases expression 7-fold. CC -!- SIMILARITY: Belongs to the aldo/keto reductase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF225564; AAF67111.1; -; mRNA. DR EMBL; AK011906; BAB27907.1; -; mRNA. DR EMBL; AK009462; BAB26303.1; -; mRNA. DR EMBL; AK011321; BAB27543.1; -; mRNA. DR EMBL; AK011794; BAB27846.1; -; mRNA. DR EMBL; AK011908; BAB27909.1; -; mRNA. DR EMBL; AK011918; BAB27915.1; -; mRNA. DR EMBL; AK011856; BAB27883.1; -; mRNA. DR EMBL; AK011667; BAB27767.1; -; mRNA. DR EMBL; AK011388; BAB27586.1; -; mRNA. DR EMBL; AK011157; BAB27437.1; -; mRNA. DR EMBL; AK011209; BAB27469.1; -; mRNA. DR EMBL; AK005162; BAB23853.1; -; mRNA. DR EMBL; AK011221; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; BC039926; AAH39926.1; -; mRNA. DR RefSeq; NP_067448.1; NM_021473.3. DR UniGene; Mm.30085; -. DR UniGene; Mm.489607; -. DR PDB; 4GAC; X-ray; 1.64 A; A/B=2-325. DR PDBsum; 4GAC; -. DR ProteinModelPortal; Q9JII6; -. DR SMR; Q9JII6; 2-325. DR IntAct; Q9JII6; 4. DR MINT; MINT-1869516; -. DR STRING; 10090.ENSMUSP00000030455; -. DR PhosphoSite; Q9JII6; -. DR REPRODUCTION-2DPAGE; IPI00466128; -. DR REPRODUCTION-2DPAGE; Q9JII6; -. DR PaxDb; Q9JII6; -. DR PRIDE; Q9JII6; -. DR Ensembl; ENSMUST00000030455; ENSMUSP00000030455; ENSMUSG00000028692. DR GeneID; 58810; -. DR KEGG; mmu:58810; -. DR UCSC; uc008uha.2; mouse. DR CTD; 10327; -. DR MGI; MGI:1929955; Akr1a1. DR eggNOG; COG0656; -. DR GeneTree; ENSGT00670000097881; -. DR HOVERGEN; HBG000020; -. DR InParanoid; Q9JII6; -. DR KO; K00002; -. DR OMA; WPYAFER; -. DR OrthoDB; EOG70KGQF; -. DR TreeFam; TF106492; -. DR BRENDA; 1.1.1.2; 3474. DR SABIO-RK; Q9JII6; -. DR NextBio; 314404; -. DR PRO; PR:Q9JII6; -. DR ArrayExpress; Q9JII6; -. DR Bgee; Q9JII6; -. DR Genevestigator; Q9JII6; -. DR GO; GO:0016324; C:apical plasma membrane; IDA:MGI. DR GO; GO:0005829; C:cytosol; IDA:MGI. DR GO; GO:0004032; F:alditol:NADP+ 1-oxidoreductase activity; IDA:MGI. DR GO; GO:0047939; F:L-glucuronate reductase activity; IDA:MGI. DR GO; GO:0046185; P:aldehyde catabolic process; IDA:MGI. DR GO; GO:0042840; P:D-glucuronate catabolic process; IDA:MGI. DR GO; GO:0019853; P:L-ascorbic acid biosynthetic process; IDA:MGI. DR Gene3D; 3.20.20.100; -; 1. DR InterPro; IPR001395; Aldo/ket_red. DR InterPro; IPR018170; Aldo/ket_reductase_CS. DR InterPro; IPR020471; Aldo/keto_reductase_subgr. DR InterPro; IPR023210; NADP_OxRdtase_dom. DR PANTHER; PTHR11732; PTHR11732; 1. DR Pfam; PF00248; Aldo_ket_red; 1. DR PIRSF; PIRSF000097; AKR; 1. DR PRINTS; PR00069; ALDKETRDTASE. DR SUPFAM; SSF51430; SSF51430; 1. DR PROSITE; PS00798; ALDOKETO_REDUCTASE_1; 1. DR PROSITE; PS00062; ALDOKETO_REDUCTASE_2; 1. DR PROSITE; PS00063; ALDOKETO_REDUCTASE_3; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Complete proteome; KW Direct protein sequencing; NADP; Oxidoreductase; Reference proteome. FT INIT_MET 1 1 Removed. FT CHAIN 2 325 Alcohol dehydrogenase [NADP(+)]. FT /FTId=PRO_0000124618. FT NP_BIND 11 20 NADP (Potential). FT NP_BIND 211 273 NADP (By similarity). FT ACT_SITE 50 50 Proton donor (By similarity). FT BINDING 113 113 Substrate (By similarity). FT SITE 80 80 Lowers pKa of active site Tyr (By FT similarity). FT MOD_RES 2 2 N-acetylthreonine. FT MOD_RES 127 127 N6-acetyllysine; alternate. FT MOD_RES 127 127 N6-succinyllysine; alternate. FT MOD_RES 145 145 N6-succinyllysine. FT CONFLICT 54 54 T -> A (in Ref. 2; BAB27586). FT CONFLICT 60 60 L -> P (in Ref. 2; BAB27915). FT CONFLICT 95 95 L -> I (in Ref. 2; BAB27883/BAB27767). FT CONFLICT 120 120 R -> L (in Ref. 2; BAB27909). FT CONFLICT 284 284 E -> G (in Ref. 2; BAB27437). FT STRAND 5 7 FT STRAND 13 17 FT HELIX 26 38 FT STRAND 43 45 FT HELIX 48 50 FT HELIX 53 63 FT STRAND 68 70 FT HELIX 72 74 FT STRAND 76 81 FT HELIX 83 85 FT HELIX 88 102 FT STRAND 107 113 FT STRAND 115 118 FT STRAND 120 122 FT HELIX 140 152 FT STRAND 155 157 FT STRAND 159 163 FT HELIX 166 175 FT STRAND 182 186 FT HELIX 194 202 FT STRAND 206 211 FT HELIX 216 221 FT HELIX 228 230 FT HELIX 232 241 FT HELIX 245 255 FT HELIX 267 273 FT HELIX 283 290 FT STRAND 302 305 FT STRAND 308 313 SQ SEQUENCE 325 AA; 36587 MW; 0097939061DA34CB CRC64; MTASSVLLHT GQKMPLIGLG TWKSEPGQVK AAIKHALSAG YRHIDCASVY GNETEIGEAL KESVGSGKAV PREELFVTSK LWNTKHHPED VEPALRKTLA DLQLEYLDLY LMHWPYAFER GDNPFPKNAD GTVRYDSTHY KETWKALEVL VAKGLVKALG LSNFNSRQID DVLSVASVRP AVLQVECHPY LAQNELIAHC HARGLEVTAY SPLGSSDRAW RHPDEPVLLE EPVVLALAEK HGRSPAQILL RWQVQRKVIC IPKSINPSRI LQNIQVFDFT FSPEEMKQLD ALNKNWRYIV PMITVDGKRV PRDAGHPLYP FNDPY // ID AK1CL_MOUSE Reviewed; 323 AA. AC Q91WR5; Q6P8V0; Q9CX32; DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot. DT 18-MAR-2008, sequence version 2. DT 19-MAR-2014, entry version 90. DE RecName: Full=Aldo-keto reductase family 1 member C21; DE EC=1.1.1.-; DE AltName: Full=17-alpha-hydroxysteroid dehydrogenase; DE Short=17-alpha-HSD; DE AltName: Full=3(or 17)-alpha-hydroxysteroid dehydrogenase; DE EC=1.1.1.209; DE AltName: Full=3-alpha-hydroxysteroid dehydrogenase; DE AltName: Full=Dihydrodiol dehydrogenase type 1; DE Short=DD1; DE AltName: Full=Dihydrodiol dehydrogenase type 3; DE Short=DD3; GN Name=Akr1c21; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, FUNCTION, SUBUNIT, RP ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE RP SPECIFICITY. RC STRAIN=ICR; TISSUE=Kidney; RX PubMed=15577209; DOI=10.1248/bpb.27.1939; RA Ishikura S., Usami N., Nakajima S., Shiraishi H., El-Kabbani O., RA Hara A.; RT "Characterization of two isoforms of mouse 3(17)alpha-hydroxysteroid RT dehydrogenases of the aldo-keto reductase family."; RL Biol. Pharm. Bull. 27:1939-1945(2004). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY. RC STRAIN=C57BL/6; RX PubMed=16018803; DOI=10.1186/1471-2091-6-12; RA Bellemare V., Faucher F., Breton R., Luu-The V.; RT "Characterization of 17alpha-hydroxysteroid dehydrogenase activity RT (17-alpha-HSD) and its involvement in the biosynthesis of RT epitestosterone."; RL BMC Biochem. 6:12-12(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Embryo; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Kidney; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) IN COMPLEX WITH NADP, FUNCTION, RP AND MUTAGENESIS OF ALA-24. RX PubMed=17034817; DOI=10.1016/j.jmb.2006.09.030; RA Faucher F., Pereira de Jesus-Tran K., Cantin L., Luu-The V., RA Labrie F., Breton R.; RT "Crystal structures of mouse 17alpha-hydroxysteroid dehydrogenase RT (apoenzyme and enzyme-NADP(H) binary complex): identification of RT molecular determinants responsible for the unique 17alpha-reductive RT activity of this enzyme."; RL J. Mol. Biol. 364:747-763(2006). RN [6] RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH NADP. RX PubMed=17909281; DOI=10.1107/S1744309107040985; RA Dhagat U., Carbone V., Chung R.P.-T., Schulze-Briese C., Endo S., RA Hara A., El-Kabbani O.; RT "Structure of 3(17)alpha-hydroxysteroid dehydrogenase (AKR1C21) RT holoenzyme from an orthorhombic crystal form: an insight into the RT bifunctionality of the enzyme."; RL Acta Crystallogr. F 63:825-830(2007). RN [7] RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 6-323 IN COMPLEX WITH RP EPITESTOSTERONE, MUTAGENESIS OF LYS-31, BIOPHYSICOCHEMICAL PROPERTIES, RP CATALYTIC ACTIVITY, AND FUNCTION. RX PubMed=17442338; DOI=10.1016/j.jmb.2007.03.058; RA Faucher F., Cantin L., Pereira de Jesus-Tran K., Lemieux M., RA Luu-The V., Labrie F., Breton R.; RT "Mouse 17alpha-hydroxysteroid dehydrogenase (AKR1C21) binds steroids RT differently from other aldo-keto reductases: identification and RT characterization of amino acid residues critical for substrate RT binding."; RL J. Mol. Biol. 369:525-540(2007). RN [8] RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH NADP. RX PubMed=19237748; DOI=10.1107/S0907444908044028; RA Dhagat U., Endo S., Mamiya H., Hara A., El-Kabbani O.; RT "Structure of the G225P/G226P mutant of mouse 3(17)alpha- RT hydroxysteroid dehydrogenase (AKR1C21) ternary complex: implications RT for the binding of inhibitor and substrate."; RL Acta Crystallogr. D 65:257-265(2009). RN [9] RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF MUTANT ASP-224, CATALYTIC RP ACTIVITY, FUNCTION, AND MUTAGENESIS OF GLN-222 AND TYR-224. RX PubMed=20124700; DOI=10.1107/S0907444909051464; RA Dhagat U., Endo S., Mamiya H., Hara A., El-Kabbani O.; RT "Studies on a Tyr residue critical for the binding of coenzyme and RT substrate in mouse 3(17)alpha-hydroxysteroid dehydrogenase (AKR1C21): RT structure of the Y224D mutant enzyme."; RL Acta Crystallogr. D 66:198-204(2010). CC -!- FUNCTION: NADP-dependent 17-alpha-hydroxysteroid dehydrogenase CC that converts 5-alpha-androstane-3,17-dione into androsterone. Has CC lower 3-alpha-hydroxysteroid dehydrogenase activity. Has broad CC substrate specificity and acts on various 17-alpha- CC hydroxysteroids, 17-ketosteroids, 3-alpha hydroxysteroids and 3- CC ketosteroids. Reduction of keto groups is strictly CC stereoselective. Reduction of 17-ketosteroids yields only 17- CC alpha-hydroxysteroids. Likewise, reduction of 3-ketosteroids CC yields only 3-alpha-hydroxysteroids. CC -!- CATALYTIC ACTIVITY: Androsterone + NAD(P)(+) = 5-alpha-androstane- CC 3,17-dione + NAD(P)H. CC -!- ENZYME REGULATION: Inhibited by high concentrations of substrate. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=1.8 uM for NADP; CC KM=19 uM for androstenedione; CC KM=0.5 uM for 5-beta-pregnane-3-alpha,20-alpha-diol; CC KM=0.5 uM for 5-beta-pregnane-3,20-dione; CC KM=0.6 uM for epitestosterone; CC KM=0.3 uM for androst-4-ene-3,17-dione; CC pH dependence: CC Optimum pH is 10.0; CC -!- SUBUNIT: Monomer. CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- TISSUE SPECIFICITY: Detected in kidney and brain. CC -!- SIMILARITY: Belongs to the aldo/keto reductase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AB178898; BAD18929.1; -; mRNA. DR EMBL; AY742217; AAW65159.1; -; mRNA. DR EMBL; AK020439; BAB32101.1; -; mRNA. DR EMBL; BC013531; AAH13531.1; -; mRNA. DR EMBL; BC061057; AAH61057.1; -; mRNA. DR EMBL; BC091761; AAH91761.1; -; mRNA. DR RefSeq; NP_084177.2; NM_029901.2. DR UniGene; Mm.27085; -. DR PDB; 2HE5; X-ray; 2.90 A; A/B/C/D=1-323. DR PDB; 2HE8; X-ray; 1.90 A; A/B=1-323. DR PDB; 2HEJ; X-ray; 1.35 A; A/B=1-323. DR PDB; 2IPF; X-ray; 1.85 A; A/B=6-323. DR PDB; 2IPG; X-ray; 1.90 A; A/B=5-323. DR PDB; 2P5N; X-ray; 1.80 A; A/B=1-323. DR PDB; 3CV6; X-ray; 2.10 A; A/B=1-323. DR PDB; 3FJN; X-ray; 2.30 A; A/B=1-323. DR PDBsum; 2HE5; -. DR PDBsum; 2HE8; -. DR PDBsum; 2HEJ; -. DR PDBsum; 2IPF; -. DR PDBsum; 2IPG; -. DR PDBsum; 2P5N; -. DR PDBsum; 3CV6; -. DR PDBsum; 3FJN; -. DR DisProt; DP00690; -. DR ProteinModelPortal; Q91WR5; -. DR SMR; Q91WR5; 6-323. DR STRING; 10090.ENSMUSP00000021628; -. DR ChEMBL; CHEMBL1075270; -. DR PhosphoSite; Q91WR5; -. DR PaxDb; Q91WR5; -. DR PRIDE; Q91WR5; -. DR Ensembl; ENSMUST00000021628; ENSMUSP00000021628; ENSMUSG00000021207. DR GeneID; 77337; -. DR KEGG; mmu:77337; -. DR UCSC; uc007pjr.1; mouse. DR CTD; 77337; -. DR MGI; MGI:1924587; Akr1c21. DR eggNOG; COG0656; -. DR GeneTree; ENSGT00550000074107; -. DR HOGENOM; HOG000250272; -. DR HOVERGEN; HBG000020; -. DR InParanoid; Q91WR5; -. DR OMA; NTEDHVG; -. DR OrthoDB; EOG70KGQF; -. DR TreeFam; TF106492; -. DR SABIO-RK; Q91WR5; -. DR EvolutionaryTrace; Q91WR5; -. DR NextBio; 346785; -. DR PRO; PR:Q91WR5; -. DR Bgee; Q91WR5; -. DR CleanEx; MM_AKR1C21; -. DR Genevestigator; Q91WR5; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004033; F:aldo-keto reductase (NADP) activity; ISA:MGI. DR GO; GO:0047023; F:androsterone dehydrogenase activity; IDA:UniProtKB. DR GO; GO:0006694; P:steroid biosynthetic process; ISA:MGI. DR Gene3D; 3.20.20.100; -; 1. DR InterPro; IPR001395; Aldo/ket_red. DR InterPro; IPR018170; Aldo/ket_reductase_CS. DR InterPro; IPR020471; Aldo/keto_reductase_subgr. DR InterPro; IPR023210; NADP_OxRdtase_dom. DR PANTHER; PTHR11732; PTHR11732; 1. DR Pfam; PF00248; Aldo_ket_red; 1. DR PIRSF; PIRSF000097; AKR; 1. DR PRINTS; PR00069; ALDKETRDTASE. DR SUPFAM; SSF51430; SSF51430; 1. DR PROSITE; PS00062; ALDOKETO_REDUCTASE_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Cytoplasm; Lipid metabolism; NADP; KW Oxidoreductase; Reference proteome; Steroid metabolism. FT CHAIN 1 323 Aldo-keto reductase family 1 member C21. FT /FTId=PRO_0000326222. FT NP_BIND 20 24 NADP. FT NP_BIND 166 167 NADP. FT NP_BIND 216 224 NADP. FT NP_BIND 270 280 NADP. FT ACT_SITE 55 55 Proton donor. FT BINDING 31 31 Substrate. FT BINDING 50 50 NADP. FT BINDING 117 117 Substrate. FT BINDING 190 190 NADP. FT SITE 84 84 Lowers pKa of active site Tyr (By FT similarity). FT MUTAGEN 24 24 A->Y: Reduces enzyme activity and FT affinity for substrate. Alters the FT stereospecificity, so that FT androstenedione is converted to FT testosterone. FT MUTAGEN 31 31 K->A: No effect on affinity for FT androstenedione. Slight increase of FT catalytic activity. FT MUTAGEN 222 222 Q->N: Decreases affinity for NADP. FT Changes enzyme activity, leading to the FT production of testosterone and FT concomitantly reducing the production of FT epi-testosterone. FT MUTAGEN 224 224 Y->D: Decreases affinity for NADP. FT Changes enzyme activity, leading to the FT production of testosterone and FT concomitantly reducing the production of FT epi-testosterone. FT MUTAGEN 224 224 Y->F: No effect on enzyme activity. FT Decreases affinity for NADP. FT CONFLICT 27 27 L -> V (in Ref. 1; BAD18929 and 4; FT AAH13531/AAH91761). FT CONFLICT 60 60 H -> R (in Ref. 1; BAD18929 and 4; FT AAH13531/AAH91761). FT CONFLICT 91 91 H -> R (in Ref. 1; BAD18929 and 4; FT AAH13531/AAH91761). FT CONFLICT 100 100 E -> V (in Ref. 1; BAD18929 and 4; FT AAH13531/AAH91761). FT CONFLICT 170 170 Y -> S (in Ref. 1; BAD18929 and 4; FT AAH13531/AAH91761). FT CONFLICT 294 294 K -> E (in Ref. 4; AAH61057). FT STRAND 7 9 FT STRAND 15 22 FT STRAND 27 29 FT HELIX 33 44 FT STRAND 48 50 FT HELIX 53 55 FT HELIX 58 70 FT HELIX 76 78 FT STRAND 80 85 FT HELIX 87 89 FT TURN 92 94 FT HELIX 95 106 FT STRAND 111 117 FT STRAND 121 123 FT STRAND 125 129 FT HELIX 144 156 FT STRAND 159 167 FT HELIX 170 177 FT STRAND 187 192 FT STRAND 194 197 FT HELIX 200 208 FT STRAND 212 216 FT TURN 225 227 FT HELIX 228 231 FT HELIX 235 237 FT HELIX 239 248 FT HELIX 252 261 FT TURN 262 264 FT STRAND 266 269 FT HELIX 274 280 FT HELIX 281 285 FT HELIX 290 297 FT HELIX 309 311 FT STRAND 318 321 SQ SEQUENCE 323 AA; 36877 MW; 0D598A0559EFBF11 CRC64; MNSKCHCVIL NDGNFIPVLG FGTALPLECP KSKAKELTKI AIDAGFHHFD SASVYNTEDH VGEAIRSKIA DGTVRREDIF YTSKVWCTSL HPELVRASLE RSLQKLQFDY VDLYLIHYPM ALKPGEENFP VDEHGKLIFD RVDLCATWEA MEKCKDAGLT KSIGVSNFNY RQLEMILNKP GLKYKPVCNQ VECHPYLNQM KLLDFCKSKD IVLVAYGVLG TQRYGGWVDQ NSPVLLDEPV LGSMAKKYNR TPALIALRYQ LQRGIVVLNT SLKEERIKEN MQVFEFQLSS EDMKVLDGLN RNMRYIPAAI FKGHPNWPFL DEY // ID AK1CD_MOUSE Reviewed; 323 AA. AC Q8VC28; Q9D7R9; Q9R0M9; DT 17-JAN-2003, integrated into UniProtKB/Swiss-Prot. DT 17-JAN-2003, sequence version 2. DT 19-FEB-2014, entry version 94. DE RecName: Full=Aldo-keto reductase family 1 member C13; DE EC=1.1.1.-; GN Name=Akr1c13; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Stomach; RX PubMed=10526179; DOI=10.1016/S0014-5793(99)01243-0; RA Ikeda S., Okuda-Ashitaka E., Masu Y., Suzuki T., Watanabe K., RA Nakao M., Shingu K., Ito S.; RT "Cloning and characterization of two novel aldo-keto reductases RT (AKR1C12 and AKR1C13) from mouse stomach."; RL FEBS Lett. 459:433-437(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Stomach; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Liver; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP PROTEIN SEQUENCE OF 201-209, AND MASS SPECTROMETRY. RC STRAIN=C57BL/6; TISSUE=Brain; RA Lubec G., Kang S.U.; RL Submitted (APR-2007) to UniProtKB. RN [5] RP X-RAY CRYSTALLOGRAPHY (1.18 ANGSTROMS) IN COMPLEX WITH NAD. RG Joint center for structural genomics (JCSG); RT "Crystal structure of putative reductase (NP_038806.2) from Mus RT musculus at 1.18 A resolution."; RL Submitted (FEB-2010) to the PDB data bank. CC -!- FUNCTION: Catalyzes the dehydrogenation of 17-beta- CC hydroxysteroids. May also exhibit significant activity with a CC variety of cyclic and alicyclic alcohols. Uses both NAD and NADP, CC but the activity is much greater with NAD than with NADP (By CC similarity). CC -!- SIMILARITY: Belongs to the aldo/keto reductase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AB027125; BAA86850.1; -; mRNA. DR EMBL; AK008949; BAB25986.1; -; mRNA. DR EMBL; BC021937; AAH21937.1; -; mRNA. DR RefSeq; NP_038806.2; NM_013778.2. DR UniGene; Mm.27447; -. DR PDB; 3LN3; X-ray; 1.18 A; A=1-323. DR PDBsum; 3LN3; -. DR ProteinModelPortal; Q8VC28; -. DR SMR; Q8VC28; 5-323. DR IntAct; Q8VC28; 1. DR MINT; MINT-1868613; -. DR STRING; 10090.ENSMUSP00000021634; -. DR PhosphoSite; Q8VC28; -. DR PaxDb; Q8VC28; -. DR PRIDE; Q8VC28; -. DR DNASU; 27384; -. DR Ensembl; ENSMUST00000021634; ENSMUSP00000021634; ENSMUSG00000021213. DR GeneID; 27384; -. DR KEGG; mmu:27384; -. DR UCSC; uc007pjl.2; mouse. DR CTD; 27384; -. DR MGI; MGI:1351662; Akr1c13. DR eggNOG; COG0656; -. DR GeneTree; ENSGT00550000074107; -. DR HOVERGEN; HBG000020; -. DR InParanoid; Q8VC28; -. DR KO; K13374; -. DR OMA; KSGDNDF; -. DR TreeFam; TF106492; -. DR EvolutionaryTrace; Q8VC28; -. DR NextBio; 305324; -. DR PRO; PR:Q8VC28; -. DR ArrayExpress; Q8VC28; -. DR Bgee; Q8VC28; -. DR CleanEx; MM_AKR1C13; -. DR Genevestigator; Q8VC28; -. DR GO; GO:0004033; F:aldo-keto reductase (NADP) activity; ISS:MGI. DR GO; GO:0006805; P:xenobiotic metabolic process; TAS:MGI. DR Gene3D; 3.20.20.100; -; 1. DR InterPro; IPR001395; Aldo/ket_red. DR InterPro; IPR018170; Aldo/ket_reductase_CS. DR InterPro; IPR020471; Aldo/keto_reductase_subgr. DR InterPro; IPR023210; NADP_OxRdtase_dom. DR PANTHER; PTHR11732; PTHR11732; 1. DR Pfam; PF00248; Aldo_ket_red; 1. DR PIRSF; PIRSF000097; AKR; 1. DR PRINTS; PR00069; ALDKETRDTASE. DR SUPFAM; SSF51430; SSF51430; 1. DR PROSITE; PS00798; ALDOKETO_REDUCTASE_1; 1. DR PROSITE; PS00062; ALDOKETO_REDUCTASE_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Direct protein sequencing; NAD; NADP; KW Oxidoreductase; Reference proteome. FT CHAIN 1 323 Aldo-keto reductase family 1 member C13. FT /FTId=PRO_0000124644. FT NP_BIND 20 24 NAD. FT NP_BIND 166 167 NAD. FT NP_BIND 216 224 NAD. FT NP_BIND 270 280 NAD. FT ACT_SITE 55 55 Proton donor (By similarity). FT BINDING 50 50 NAD. FT BINDING 55 55 NAD. FT BINDING 117 117 Substrate (By similarity). FT BINDING 190 190 NAD. FT SITE 84 84 Lowers pKa of active site Tyr (By FT similarity). FT CONFLICT 47 47 R -> L (in Ref. 1; BAA86850). FT CONFLICT 81 81 I -> V (in Ref. 3; AAH21937). FT CONFLICT 183 183 K -> N (in Ref. 2; BAB25986). FT CONFLICT 226 226 E -> K (in Ref. 1; BAA86850). FT STRAND 7 9 FT STRAND 15 22 FT HELIX 31 44 FT STRAND 48 50 FT HELIX 53 55 FT HELIX 58 70 FT HELIX 76 78 FT STRAND 80 85 FT HELIX 87 89 FT HELIX 92 94 FT HELIX 95 106 FT STRAND 111 117 FT HELIX 144 156 FT STRAND 159 167 FT HELIX 170 177 FT STRAND 187 192 FT HELIX 200 208 FT STRAND 212 217 FT TURN 225 227 FT HELIX 235 237 FT HELIX 239 248 FT HELIX 252 262 FT STRAND 266 269 FT HELIX 274 280 FT HELIX 281 285 FT HELIX 290 297 FT HELIX 309 311 SQ SEQUENCE 323 AA; 37058 MW; 8B51A5820402AE5A CRC64; MSSKQHCVKL NDGHLIPALG FGTYKPKEVP KSKSLEAACL ALDVGYRHVD TAYAYQVEEE IGQAIQSKIK AGVVKREDLF ITTKLWCTCF RPELVKPALE KSLKKLQLDY VDLYIMHYPV PMKSGDNDFP VNEQGKSLLD TVDFCDTWER LEECKDAGLV KSIGVSNFNH RQLERILNKP GLKYKPVCNQ VECHLYLNQR KLLDYCESKD IVLVAYGALG TQRYKEWVDQ NSPVLLNDPV LCDVAKKNKR SPALIALRYL IQRGIVPLAQ SFKENEMREN LQVFGFQLSP EDMKTLDGLN KNFRYLPAEF LVDHPEYPFV EEY // ID AK1D1_MOUSE Reviewed; 325 AA. AC Q8VCX1; DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2002, sequence version 1. DT 19-MAR-2014, entry version 85. DE RecName: Full=3-oxo-5-beta-steroid 4-dehydrogenase; DE EC=1.3.1.3; DE AltName: Full=Aldo-keto reductase family 1 member D1; DE AltName: Full=Delta(4)-3-ketosteroid 5-beta-reductase; DE AltName: Full=Delta(4)-3-oxosteroid 5-beta-reductase; GN Name=Akr1d1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Liver; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: Efficiently catalyzes the reduction of progesterone, CC androstenedione, 17-alpha-hydroxyprogesterone and testosterone to CC 5-beta-reduced metabolites. The bile acid intermediates 7- CC alpha,12-alpha-dihydroxy-4-cholesten-3-one and 7-alpha-hydroxy-4- CC cholesten-3-one can also act as substrates. CC -!- CATALYTIC ACTIVITY: 5-beta-cholestan-3-one + NADP(+) = cholest-4- CC en-3-one + NADPH. CC -!- CATALYTIC ACTIVITY: 17,21-dihydroxy-5-beta-pregnane-3,11,20-trione CC + NADP(+) = cortisone. CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the aldo/keto reductase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BC018333; AAH18333.1; -; mRNA. DR RefSeq; NP_663339.1; NM_145364.2. DR RefSeq; XP_006505888.1; XM_006505825.1. DR UniGene; Mm.262635; -. DR ProteinModelPortal; Q8VCX1; -. DR SMR; Q8VCX1; 2-325. DR IntAct; Q8VCX1; 3. DR MINT; MINT-1868906; -. DR STRING; 10090.ENSMUSP00000048830; -. DR PhosphoSite; Q8VCX1; -. DR PaxDb; Q8VCX1; -. DR PRIDE; Q8VCX1; -. DR Ensembl; ENSMUST00000040987; ENSMUSP00000048830; ENSMUSG00000038641. DR GeneID; 208665; -. DR KEGG; mmu:208665; -. DR UCSC; uc009bjg.2; mouse. DR CTD; 6718; -. DR MGI; MGI:2384785; Akr1d1. DR eggNOG; COG0656; -. DR GeneTree; ENSGT00550000074107; -. DR HOGENOM; HOG000250272; -. DR HOVERGEN; HBG000020; -. DR InParanoid; Q8VCX1; -. DR KO; K00251; -. DR OMA; XVNISSP; -. DR OrthoDB; EOG70KGQF; -. DR TreeFam; TF106492; -. DR ChiTaRS; AKR1D1; mouse. DR NextBio; 372375; -. DR PRO; PR:Q8VCX1; -. DR ArrayExpress; Q8VCX1; -. DR Bgee; Q8VCX1; -. DR CleanEx; MM_AKR1D1; -. DR Genevestigator; Q8VCX1; -. DR GO; GO:0005829; C:cytosol; IEA:Ensembl. DR GO; GO:0047787; F:delta4-3-oxosteroid 5beta-reductase activity; IEA:UniProtKB-EC. DR GO; GO:0008209; P:androgen metabolic process; IEA:Ensembl. DR GO; GO:0006699; P:bile acid biosynthetic process; IEA:Ensembl. DR GO; GO:0030573; P:bile acid catabolic process; IEA:UniProtKB-KW. DR GO; GO:0008207; P:C21-steroid hormone metabolic process; IEA:Ensembl. DR GO; GO:0006707; P:cholesterol catabolic process; IEA:Ensembl. DR GO; GO:0007586; P:digestion; IEA:Ensembl. DR Gene3D; 3.20.20.100; -; 1. DR InterPro; IPR001395; Aldo/ket_red. DR InterPro; IPR018170; Aldo/ket_reductase_CS. DR InterPro; IPR020471; Aldo/keto_reductase_subgr. DR InterPro; IPR023210; NADP_OxRdtase_dom. DR PANTHER; PTHR11732; PTHR11732; 1. DR Pfam; PF00248; Aldo_ket_red; 1. DR PIRSF; PIRSF000097; AKR; 1. DR PRINTS; PR00069; ALDKETRDTASE. DR SUPFAM; SSF51430; SSF51430; 1. DR PROSITE; PS00798; ALDOKETO_REDUCTASE_1; 1. DR PROSITE; PS00062; ALDOKETO_REDUCTASE_2; 1. DR PROSITE; PS00063; ALDOKETO_REDUCTASE_3; 1. PE 2: Evidence at transcript level; KW Bile acid catabolism; Complete proteome; Cytoplasm; Lipid degradation; KW Lipid metabolism; NADP; Oxidoreductase; Reference proteome; KW Steroid metabolism. FT CHAIN 1 325 3-oxo-5-beta-steroid 4-dehydrogenase. FT /FTId=PRO_0000124670. FT NP_BIND 22 26 NADP (By similarity). FT NP_BIND 168 169 NADP (By similarity). FT NP_BIND 218 223 NADP (By similarity). FT NP_BIND 272 282 NADP (By similarity). FT ACT_SITE 57 57 Proton donor (By similarity). FT BINDING 26 26 Substrate (By similarity). FT BINDING 52 52 NADP (By similarity). FT BINDING 57 57 Substrate (By similarity). FT BINDING 88 88 Substrate (By similarity). FT BINDING 119 119 Substrate (By similarity). FT BINDING 131 131 Substrate (By similarity). FT BINDING 192 192 NADP (By similarity). FT BINDING 229 229 Substrate (By similarity). SQ SEQUENCE 325 AA; 37290 MW; 1866A0DA4C5DDA98 CRC64; MNLSAAHHQI SLSDGNNIPL IGLGTYSDPR PVPGKTYVAV KTAIDEGYRH IDGAYVYHNE HEVGEAIREK IAEGKVKREE IFYCGKLWNT EHVPSMVLPA LERTLKALKL DYIDLYIIEL PMAFKPGKEI YPRDENGRII YDKTNLCATW EALEACKDAG LVKSLGVSNF NRRQLELILN KPGLKYKPVT NQVECHPYFT QTKLLKFCQQ HDIVIVAHSP LGTCRNPSWV NVSSPPLLND ELLTSLGKKY NKTQAQIVLR FNIQRGIVVI PKSFTPERIK ENFQIFDFSL TEEEMKDIDA LNKNVRYVEL LMWSDHPEYP FHDEY // ID AKC1H_MOUSE Reviewed; 323 AA. AC Q8K023; Q99N44; DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot. DT 07-JUN-2005, sequence version 2. DT 19-MAR-2014, entry version 95. DE RecName: Full=Aldo-keto reductase family 1 member C18; DE EC=1.1.-.-; DE AltName: Full=20-alpha-hydroxysteroid dehydrogenase; DE Short=20-alpha-HSD; DE EC=1.1.1.149; GN Name=Akr1c18; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC STRAIN=ICR; TISSUE=Ovary; RA Ishida M., Chang K., Hirabayashi K., Nishihara M., Takahashi M.; RT "Cloning of mouse 20alpha-hydroxysteroid dehydrogenase cDNA and its RT mRNA localization during pregnancy."; RL J. Reprod. Dev. 45:321-329(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC STRAIN=FVB/N; TISSUE=Kidney; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: Catalyzes the conversion of progesterone into 20-alpha- CC dihydroprogesterone (20 alpha-OHP). CC -!- CATALYTIC ACTIVITY: 17-alpha,20-alpha-dihydroxypregn-4-en-3-one + CC NAD(P)(+) = 17-alpha-hydroxyprogesterone + NAD(P)H. CC -!- SUBUNIT: Monomer (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q8K023-1; Sequence=Displayed; CC Name=2; CC IsoId=Q8K023-2; Sequence=VSP_014039; CC Note=No experimental confirmation available; CC -!- SIMILARITY: Belongs to the aldo/keto reductase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AB059565; BAB40958.1; -; mRNA. DR EMBL; BC034259; AAH34259.1; -; mRNA. DR RefSeq; NP_598827.1; NM_134066.2. DR UniGene; Mm.41337; -. DR ProteinModelPortal; Q8K023; -. DR SMR; Q8K023; 6-319. DR IntAct; Q8K023; 2. DR MINT; MINT-1866370; -. DR PhosphoSite; Q8K023; -. DR PaxDb; Q8K023; -. DR PRIDE; Q8K023; -. DR Ensembl; ENSMUST00000021635; ENSMUSP00000021635; ENSMUSG00000021214. [Q8K023-1] DR Ensembl; ENSMUST00000110704; ENSMUSP00000106332; ENSMUSG00000021214. [Q8K023-2] DR GeneID; 105349; -. DR KEGG; mmu:105349; -. DR UCSC; uc007pjj.1; mouse. [Q8K023-1] DR UCSC; uc007pjk.1; mouse. [Q8K023-2] DR CTD; 105349; -. DR MGI; MGI:2145420; Akr1c18. DR eggNOG; COG0656; -. DR GeneTree; ENSGT00550000074107; -. DR HOGENOM; HOG000250272; -. DR HOVERGEN; HBG000020; -. DR InParanoid; Q8K023; -. DR KO; K05295; -. DR OMA; VRPSLEN; -. DR OrthoDB; EOG70KGQF; -. DR TreeFam; TF106492; -. DR NextBio; 357616; -. DR PRO; PR:Q8K023; -. DR ArrayExpress; Q8K023; -. DR Bgee; Q8K023; -. DR CleanEx; MM_AKR1C18; -. DR Genevestigator; Q8K023; -. DR GO; GO:0005829; C:cytosol; IEA:Ensembl. DR GO; GO:0047006; F:17-alpha,20-alpha-dihydroxypregn-4-en-3-one dehydrogenase activity; IDA:MGI. DR GO; GO:0007567; P:parturition; IMP:MGI. DR GO; GO:0006709; P:progesterone catabolic process; IDA:MGI. DR GO; GO:0050810; P:regulation of steroid biosynthetic process; IEA:Ensembl. DR Gene3D; 3.20.20.100; -; 1. DR InterPro; IPR001395; Aldo/ket_red. DR InterPro; IPR018170; Aldo/ket_reductase_CS. DR InterPro; IPR020471; Aldo/keto_reductase_subgr. DR InterPro; IPR023210; NADP_OxRdtase_dom. DR PANTHER; PTHR11732; PTHR11732; 1. DR Pfam; PF00248; Aldo_ket_red; 1. DR PIRSF; PIRSF000097; AKR; 1. DR PRINTS; PR00069; ALDKETRDTASE. DR SUPFAM; SSF51430; SSF51430; 1. DR PROSITE; PS00062; ALDOKETO_REDUCTASE_2; 1. DR PROSITE; PS00063; ALDOKETO_REDUCTASE_3; 1. PE 2: Evidence at transcript level; KW Alternative splicing; Complete proteome; Cytoplasm; NADP; KW Oxidoreductase; Reference proteome. FT CHAIN 1 323 Aldo-keto reductase family 1 member C18. FT /FTId=PRO_0000124649. FT NP_BIND 20 24 NADP (By similarity). FT NP_BIND 166 167 NADP (By similarity). FT NP_BIND 216 221 NADP (By similarity). FT NP_BIND 270 280 NADP (By similarity). FT ACT_SITE 55 55 Proton donor (By similarity). FT BINDING 50 50 NADP (By similarity). FT BINDING 117 117 Substrate (By similarity). FT BINDING 190 190 NADP (By similarity). FT SITE 54 54 Important for substrate specificity (By FT similarity). FT SITE 84 84 Lowers pKa of active site Tyr (By FT similarity). FT VAR_SEQ 124 149 Missing (in isoform 2). FT /FTId=VSP_014039. SQ SEQUENCE 323 AA; 37177 MW; F2732C09C60B4544 CRC64; MNSKIQKIEL NDGHSIPVLG FGTYATEEHL KKKSMESTKI AIDVGFCHID CSHLYQNEEE IGQAILSKIE DGTVKREDIF YTSKLWSTSH RPELVRPSLE NSLRKLNLDY VDLYLIHFPV SLKPGNELLP KDEHGNLIFD TVDLCDTWEA MEKCKDAGLA KSIGVSNFNR RQLEMILNKP GLKYKPVCNQ VECHLYLNQS KLLAYCKMND IVLVAYGALG TQRYKYCINE DTPVLLDDPV LCAMAKKYKR TPALIALRYQ LDRGIVALAK SFNEERIREN MQVFDFQLAS DDMKILDGLD RNLRYFPADM FKAHPNFPFF DEY // ID AKCL2_MOUSE Reviewed; 301 AA. AC Q9DCT1; O09125; DT 10-MAY-2002, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 19-FEB-2014, entry version 95. DE RecName: Full=1,5-anhydro-D-fructose reductase; DE Short=AF reductase; DE EC=1.1.1.263; DE AltName: Full=Aldo-keto reductase family 1 member C-like protein 2; DE AltName: Full=Aldo-keto reductase family 1 member E1; DE AltName: Full=Aldo-keto reductase family 1 member E2; GN Name=Akr1e2; Synonyms=Akr1cl2, Akr1e1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION. RC STRAIN=129/Sv; TISSUE=Liver; RA Bohren K.M., Barski O.A., Gabbay K.H.; RT "Characterization of a novel murine aldo-keto reductase."; RL (In) Weiner H. (eds.); RL Enzymology and molecular biology of carbonyl metabolism 6, pp.1-1, RL Plenum Press, New York (1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Kidney; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Mammary tumor; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, AND BIOPHYSICOCHEMICAL RP PROPERTIES. RC STRAIN=C57BL/6J; RX PubMed=18323634; DOI=10.1271/bbb.70612; RA Sakuma M., Kubota S.; RT "Mouse AKR1E1 is an ortholog of pig liver NADPH dependent 1,5-anhydro- RT D-fructose reductase."; RL Biosci. Biotechnol. Biochem. 72:872-876(2008). CC -!- FUNCTION: Catalyzes the NADPH-dependent reduction of 1,5-anhydro- CC D-fructose (AF) to 1,5-anhydro-D-glucitol. Can also catalyze the CC reduction of various aldehydes and quinones. CC -!- CATALYTIC ACTIVITY: 1,5-anhydro-D-glucitol + NADP(+) = 1,5- CC anhydro-D-fructose + NADPH. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=1.02 mM for 1,5-anhydro-D-fructose; CC Vmax=0.57 umol/min/mg enzyme; CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the aldo/keto reductase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U68535; AAB37274.1; -; mRNA. DR EMBL; AK002507; BAB22152.1; -; mRNA. DR EMBL; BC012692; AAH12692.1; -; mRNA. DR RefSeq; NP_061347.2; NM_018859.2. DR UniGene; Mm.251908; -. DR ProteinModelPortal; Q9DCT1; -. DR SMR; Q9DCT1; 3-301. DR IntAct; Q9DCT1; 1. DR MINT; MINT-4087401; -. DR PhosphoSite; Q9DCT1; -. DR PaxDb; Q9DCT1; -. DR PRIDE; Q9DCT1; -. DR DNASU; 56043; -. DR Ensembl; ENSMUST00000091848; ENSMUSP00000089459; ENSMUSG00000045410. DR GeneID; 56043; -. DR KEGG; mmu:56043; -. DR UCSC; uc007pjs.1; mouse. DR CTD; 56043; -. DR MGI; MGI:1914758; Akr1e1. DR eggNOG; COG0656; -. DR GeneTree; ENSGT00670000097881; -. DR HOGENOM; HOG000250272; -. DR KO; K13981; -. DR OMA; TFPITEN; -. DR TreeFam; TF106492; -. DR SABIO-RK; Q9DCT1; -. DR NextBio; 311808; -. DR PRO; PR:Q9DCT1; -. DR ArrayExpress; Q9DCT1; -. DR Bgee; Q9DCT1; -. DR CleanEx; MM_AKR1E1; -. DR Genevestigator; Q9DCT1; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0050571; F:1,5-anhydro-D-fructose reductase activity; IEA:UniProtKB-EC. DR Gene3D; 3.20.20.100; -; 1. DR InterPro; IPR001395; Aldo/ket_red. DR InterPro; IPR018170; Aldo/ket_reductase_CS. DR InterPro; IPR020471; Aldo/keto_reductase_subgr. DR InterPro; IPR023210; NADP_OxRdtase_dom. DR PANTHER; PTHR11732; PTHR11732; 1. DR Pfam; PF00248; Aldo_ket_red; 1. DR PIRSF; PIRSF000097; AKR; 1. DR PRINTS; PR00069; ALDKETRDTASE. DR SUPFAM; SSF51430; SSF51430; 1. DR PROSITE; PS00798; ALDOKETO_REDUCTASE_1; 1. DR PROSITE; PS00062; ALDOKETO_REDUCTASE_2; 1. DR PROSITE; PS00063; ALDOKETO_REDUCTASE_3; 1. PE 1: Evidence at protein level; KW Complete proteome; Cytoplasm; NADP; Oxidoreductase; KW Reference proteome. FT CHAIN 1 301 1,5-anhydro-D-fructose reductase. FT /FTId=PRO_0000124673. FT NP_BIND 250 258 NADP (By similarity). FT ACT_SITE 40 40 Proton donor (By similarity). FT BINDING 35 35 NADP (By similarity). FT BINDING 102 102 Substrate (By similarity). FT BINDING 174 174 NADP (By similarity). FT SITE 69 69 Lowers pKa of active site Tyr (By FT similarity). FT CONFLICT 105 105 M -> I (in Ref. 1; AAB37274). FT CONFLICT 283 283 L -> F (in Ref. 1; AAB37274). SQ SEQUENCE 301 AA; 34461 MW; 5633663685EF32CA CRC64; MENIPTVGLG TWKASPGEVT DAVKLAINLG YRHFDCAYLY HNESEVGMGI SEKIKEGVVK REDLFVVSKL WCTCHKKSLV KTACTNTLEA LNLDYLDLYL IHWPMGFKPG EKDIPLDRNG KVIPSHTSFL DTWEAMEDLV FEGLVKNLGV SNFNHEQLER LLDKPGLRVR PITNQIECHP YLNQKKLIDF CHKRNVSVTA YRPLGGSGGG FHLMDDTVIR KIAKKHGKSP AQILIRFQIQ RNLIVIPKSV TPSRIRENIQ VFDFELTEKD MEELLSLDKN LRLATFPTTE NHQDYPFHIE Y // ID AL1A7_MOUSE Reviewed; 501 AA. AC O35945; Q80ZX7; DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1998, sequence version 1. DT 19-FEB-2014, entry version 92. DE RecName: Full=Aldehyde dehydrogenase, cytosolic 1; DE EC=1.2.1.3; DE AltName: Full=ALDH class 1; DE AltName: Full=ALDH-E1; DE AltName: Full=ALHDII; DE AltName: Full=Aldehyde dehydrogenase family 1 member A7; DE AltName: Full=Aldehyde dehydrogenase phenobarbital-inducible; GN Name=Aldh1a7; Synonyms=Aldh-pb; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY. RC STRAIN=C57BL/6; TISSUE=Liver; RX PubMed=10191271; DOI=10.1042/0264-6021:3390387; RA Hsu L.C., Chang W.C., Hoffmann I., Duester G.; RT "Molecular analysis of two closely related mouse aldehyde RT dehydrogenase genes: identification of a role for Aldh1, but not Aldh- RT pb, in the biosynthesis of retinoic acid."; RL Biochem. J. 339:387-395(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6; TISSUE=Olfactory epithelium; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: Can oxidize benzaldehyde, propionaldehyde and CC acetaldehyde (By similarity). No detectable activity with retinal. CC -!- CATALYTIC ACTIVITY: An aldehyde + NAD(+) + H(2)O = a carboxylate + CC NADH. CC -!- PATHWAY: Alcohol metabolism; ethanol degradation; acetate from CC ethanol: step 2/2. CC -!- SUBUNIT: Homotetramer (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- TISSUE SPECIFICITY: Highest level in liver, high level in lung, CC low level in kidney and testis. CC -!- MISCELLANEOUS: Xenopus embryos injected with Aldh1a7 mRNA failed CC to produce retinoic acid in contrast to embryos injected with CC Aldh1a1. CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U96401; AAB64411.1; -; mRNA. DR EMBL; BC046315; AAH46315.2; -; mRNA. DR RefSeq; NP_036051.1; NM_011921.2. DR UniGene; Mm.14609; -. DR ProteinModelPortal; O35945; -. DR SMR; O35945; 9-501. DR IntAct; O35945; 2. DR MINT; MINT-1869840; -. DR PhosphoSite; O35945; -. DR PaxDb; O35945; -. DR PRIDE; O35945; -. DR Ensembl; ENSMUST00000025656; ENSMUSP00000025656; ENSMUSG00000024747. DR GeneID; 26358; -. DR KEGG; mmu:26358; -. DR UCSC; uc008gyn.1; mouse. DR CTD; 26358; -. DR MGI; MGI:1347050; Aldh1a7. DR eggNOG; COG1012; -. DR GeneTree; ENSGT00550000074289; -. DR HOGENOM; HOG000271505; -. DR HOVERGEN; HBG000097; -. DR InParanoid; O35945; -. DR KO; K07249; -. DR OMA; SEESTLM; -. DR OrthoDB; EOG7PS1F7; -. DR TreeFam; TF300455; -. DR UniPathway; UPA00780; UER00768. DR ChiTaRS; Aldh1a7; mouse. DR NextBio; 304207; -. DR PRO; PR:O35945; -. DR ArrayExpress; O35945; -. DR Bgee; O35945; -. DR CleanEx; MM_ALDH1A7; -. DR Genevestigator; O35945; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004029; F:aldehyde dehydrogenase (NAD) activity; IEA:UniProtKB-EC. DR GO; GO:0006068; P:ethanol catabolic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.309.10; -; 1. DR Gene3D; 3.40.605.10; -; 1. DR InterPro; IPR016161; Ald_DH/histidinol_DH. DR InterPro; IPR016163; Ald_DH_C. DR InterPro; IPR016160; Ald_DH_CS. DR InterPro; IPR016162; Ald_DH_N. DR InterPro; IPR015590; Aldehyde_DH_dom. DR Pfam; PF00171; Aldedh; 1. DR SUPFAM; SSF53720; SSF53720; 1. DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1. DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1. PE 2: Evidence at transcript level; KW Complete proteome; Cytoplasm; NAD; Oxidoreductase; Reference proteome. FT CHAIN 1 501 Aldehyde dehydrogenase, cytosolic 1. FT /FTId=PRO_0000291264. FT NP_BIND 246 251 NAD (By similarity). FT ACT_SITE 269 269 Proton acceptor (By similarity). FT ACT_SITE 303 303 Nucleophile (By similarity). FT SITE 170 170 Transition state stabilizer (By FT similarity). SQ SEQUENCE 501 AA; 54588 MW; 42DE97962799237B CRC64; MSSPAQPAVP APLANLKIQH TKIFINNEWH DSVSSKKFPV LNPATEEVIC HVEEGDKADV DKAVKAARQA FQIGSPWRTM DASERGRLLN KLADLMERDR LLLATMESMN AGKVFAHAYL LDVEISIKAL QYFAGWADKI HGQTIPSDGN IFTYTRREPI GVCGQIIPWN GPLIIFTWKL GPALSCGNTV VVKPAEQTPL TALHMASLIK EAGFPPGVVN IVPGYGPTAG GAISSHMDID KVSFTGSTEV GKLIKEAAGK SNLKRVTLEL GGKSPCIVFA DADLDSAVEF AHQGVFFHQG QICVAASRLF VEESIYDEFV RRSVERAKKY ILGNPLNSGI NQGPQIDKEQ HNKILGLIES GKKEGAKLEC GGGRWGNKGF FVQPTVFSNV TDEMRIAKEE IFGPVQQIMK FKSMDDVIKR ANNTTYGLAA GVFTKDLDKA ITVSSALQAG MVWVNCYLAV PVQCPFGGFK MSGNGRELGE HGLYEYTELK TVAMQISQKN S // ID AL1A1_MOUSE Reviewed; 501 AA. AC P24549; Q7TQJ0; Q811J0; DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 5. DT 19-FEB-2014, entry version 137. DE RecName: Full=Retinal dehydrogenase 1; DE Short=RALDH 1; DE Short=RalDH1; DE EC=1.2.1.36; DE AltName: Full=ALDH-E1; DE AltName: Full=ALHDII; DE AltName: Full=Aldehyde dehydrogenase family 1 member A1; DE AltName: Full=Aldehyde dehydrogenase, cytosolic; GN Name=Aldh1a1; Synonyms=Ahd-2, Ahd2, Aldh1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. RC STRAIN=BALB/c, and C57BL/6; TISSUE=Liver; RX PubMed=2055490; DOI=10.1016/0378-1119(91)90421-7; RA Rongnoparut P., Weaver S.; RT "Isolation and characterization of a cytosolic aldehyde dehydrogenase- RT encoding cDNA from mouse liver."; RL Gene 101:261-265(1991). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. RC STRAIN=129/ReJ, BALB/c, and C57BL/6J; TISSUE=Liver; RX PubMed=7993664; DOI=10.1006/bmmb.1994.1048; RA Bond S.L., Singh S.M.; RT "DNA sequence analysis of the cytosolic acetaldehyde dehydrogenase RT gene (Ahd-2) in mouse strains with variable ethanol preferences."; RL Biochem. Med. Metab. Biol. 52:155-159(1994). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Colon, and Liver; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP PROTEIN SEQUENCE OF 23-52; 140-156; 211-230; 309-320; 330-349; RP 400-410; 421-435 AND 477-490. RC TISSUE=Embryonic retina; RX PubMed=1935685; RA McCaffery P., Tempst P., Lara G., Drager U.C.; RT "Aldehyde dehydrogenase is a positional marker in the retina."; RL Development 112:693-702(1991). CC -!- FUNCTION: In addition to the activity on acetaldehyde and related CC substrates, is also involved in the oxidation of aldehydes derived CC from biogenic amines such as epinephrine and norepinephrine, as CC well as the aldehydes generated via lipid peroxidation. Binds free CC retinal and cellular retinol-binding protein-bound retinal. Can CC convert/oxidize retinaldehyde to retinoic acid (By similarity). CC -!- CATALYTIC ACTIVITY: Retinal + NAD(+) + H(2)O = retinoate + NADH. CC -!- PATHWAY: Cofactor metabolism; retinol metabolism. CC -!- SUBUNIT: Homodimer. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- TISSUE SPECIFICITY: Expressed in the liver, lung, and testis. CC Apparently not expressed at detectable levels in kidney, stomach, CC ovary, heart, and brain. CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family. CC -!- SEQUENCE CAUTION: CC Sequence=AAH44729.1; Type=Erroneous initiation; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M74570; AAA37202.1; -; mRNA. DR EMBL; M74571; AAA37203.1; -; Genomic_DNA. DR EMBL; S75713; AAB32754.2; -; mRNA. DR EMBL; S77047; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC044729; AAH44729.1; ALT_INIT; mRNA. DR EMBL; BC054386; AAH54386.1; -; mRNA. DR PIR; JQ1004; JQ1004. DR RefSeq; NP_038495.2; NM_013467.3. DR UniGene; Mm.250866; -. DR ProteinModelPortal; P24549; -. DR SMR; P24549; 9-501. DR IntAct; P24549; 4. DR MINT; MINT-1859401; -. DR PhosphoSite; P24549; -. DR REPRODUCTION-2DPAGE; IPI00626662; -. DR REPRODUCTION-2DPAGE; P24549; -. DR SWISS-2DPAGE; P24549; -. DR PaxDb; P24549; -. DR PRIDE; P24549; -. DR Ensembl; ENSMUST00000087638; ENSMUSP00000084918; ENSMUSG00000053279. DR GeneID; 11668; -. DR KEGG; mmu:11668; -. DR UCSC; uc008gym.1; mouse. DR CTD; 216; -. DR MGI; MGI:1353450; Aldh1a1. DR eggNOG; COG1012; -. DR GeneTree; ENSGT00550000074289; -. DR HOGENOM; HOG000271505; -. DR HOVERGEN; HBG000097; -. DR InParanoid; P24549; -. DR KO; K07249; -. DR OMA; YMGSLIK; -. DR OrthoDB; EOG7PS1F7; -. DR TreeFam; TF300455; -. DR BRENDA; 1.2.1.36; 3474. DR SABIO-RK; P24549; -. DR UniPathway; UPA00912; -. DR NextBio; 279287; -. DR PRO; PR:P24549; -. DR Bgee; P24549; -. DR CleanEx; MM_ALDH1A1; -. DR Genevestigator; P24549; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005634; C:nucleus; IEA:Ensembl. DR GO; GO:0004028; F:3-chloroallyl aldehyde dehydrogenase activity; IDA:MGI. DR GO; GO:0018479; F:benzaldehyde dehydrogenase (NAD+) activity; IEA:Ensembl. DR GO; GO:0001758; F:retinal dehydrogenase activity; IEA:UniProtKB-EC. DR GO; GO:0042904; P:9-cis-retinoic acid biosynthetic process; IDA:MGI. DR GO; GO:0060206; P:estrous cycle phase; IEA:Ensembl. DR GO; GO:0001822; P:kidney development; IEA:Ensembl. DR GO; GO:0001889; P:liver development; IEA:Ensembl. DR GO; GO:0007494; P:midgut development; IEA:Ensembl. DR GO; GO:0002072; P:optic cup morphogenesis involved in camera-type eye development; IGI:MGI. DR GO; GO:0043065; P:positive regulation of apoptotic process; IGI:MGI. DR GO; GO:0051289; P:protein homotetramerization; IEA:Ensembl. DR GO; GO:0042493; P:response to drug; IDA:MGI. DR GO; GO:0032355; P:response to estradiol; IEA:Ensembl. DR GO; GO:0045471; P:response to ethanol; IEA:Ensembl. DR GO; GO:0006979; P:response to oxidative stress; IEA:Ensembl. DR GO; GO:0032526; P:response to retinoic acid; IEA:Ensembl. DR GO; GO:0042572; P:retinol metabolic process; IMP:MGI. DR Gene3D; 3.40.309.10; -; 1. DR Gene3D; 3.40.605.10; -; 1. DR InterPro; IPR016161; Ald_DH/histidinol_DH. DR InterPro; IPR016163; Ald_DH_C. DR InterPro; IPR016160; Ald_DH_CS. DR InterPro; IPR016162; Ald_DH_N. DR InterPro; IPR015590; Aldehyde_DH_dom. DR Pfam; PF00171; Aldedh; 1. DR SUPFAM; SSF53720; SSF53720; 1. DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1. DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1. PE 1: Evidence at protein level; KW Acetylation; Complete proteome; Cytoplasm; Direct protein sequencing; KW NAD; Oxidoreductase; Reference proteome. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 501 Retinal dehydrogenase 1. FT /FTId=PRO_0000056417. FT NP_BIND 246 251 NAD (By similarity). FT REGION 300 305 Antabuse binding. FT ACT_SITE 269 269 Proton acceptor (By similarity). FT ACT_SITE 303 303 Nucleophile (By similarity). FT BINDING 456 456 NAD (By similarity). FT SITE 170 170 Transition state stabilizer (By FT similarity). FT MOD_RES 2 2 N-acetylserine (By similarity). FT MOD_RES 91 91 N6-acetyllysine (By similarity). FT MOD_RES 128 128 N6-acetyllysine (By similarity). FT MOD_RES 252 252 N6-acetyllysine (By similarity). FT MOD_RES 353 353 N6-acetyllysine (By similarity). FT MOD_RES 367 367 N6-acetyllysine (By similarity). FT MOD_RES 410 410 N6-acetyllysine (By similarity). FT MOD_RES 419 419 N6-acetyllysine (By similarity). FT MOD_RES 435 435 N6-acetyllysine (By similarity). FT MOD_RES 495 495 N6-acetyllysine (By similarity). FT CONFLICT 8 8 A -> R (in Ref. 1; AAA37202/AAA37203). FT CONFLICT 45 45 T -> S (in Ref. 2; AAB32754). FT CONFLICT 51 51 H -> Q (in Ref. 2; AAB32754). FT CONFLICT 87 87 R -> C (in Ref. 1; AAA37202). FT CONFLICT 140 140 I -> Y (in Ref. 4; AA sequence). FT CONFLICT 458 458 M -> I (in Ref. 1; AAA37202). SQ SEQUENCE 501 AA; 54468 MW; 0E428151B799BD1D CRC64; MSSPAQPAVP APLADLKIQH TKIFINNEWH NSVSGKKFPV LNPATEEVIC HVEEGDKADV DKAVKAARQA FQIGSPWRTM DASERGRLLN KLADLMERDR LLLATMEALN GGKVFANAYL SDLGGCIKAL KYCAGWADKI HGQTIPSDGD IFTYTRREPI GVCGQIIPWN FPMLMFIWKI GPALSCGNTV VVKPAEQTPL TALHLASLIK EAGFPPGVVN IVPGYGPTAG AAISSHMDVD KVAFTGSTQV GKLIKEAAGK SNLKRVTLEL GGKSPCIVFA DADLDIAVEF AHHGVFYHQG QCCVAASRIF VEESVYDEFV KRSVERAKKY VLGNPLTPGI NQGPQIDKEQ HDKILDLIES GKKEGAKLEC GGGRWGNKGF FVQPTVFSNV TDEMRIAKEE IFGPVQQIMK FKSVDDVIKR ANNTTYGLAA GLFTKDLDKA ITVSSALQAG VVWVNCYMML SAQCPFGGFK MSGNGRELGE HGLYEYTELK TVAMKISQKN S // ID AL1B1_MOUSE Reviewed; 519 AA. AC Q9CZS1; Q3UAH5; DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 19-MAR-2014, entry version 103. DE RecName: Full=Aldehyde dehydrogenase X, mitochondrial; DE EC=1.2.1.3; DE AltName: Full=Aldehyde dehydrogenase family 1 member B1; DE Flags: Precursor; GN Name=Aldh1b1; Synonyms=Aldhx; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J, and NOD; TISSUE=Bone marrow, Embryo, and Thymus; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6, and FVB/N; TISSUE=Brain, and Colon; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-54; LYS-83; LYS-366; RP LYS-385; LYS-401; LYS-416 AND LYS-428, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., RA Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). RN [4] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-53; LYS-54; LYS-366; RP LYS-385; LYS-401; LYS-416; LYS-428 AND LYS-431, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23576753; DOI=10.1073/pnas.1302961110; RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., RA Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.; RT "Label-free quantitative proteomics of the lysine acetylome in RT mitochondria identifies substrates of SIRT3 in metabolic pathways."; RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013). CC -!- FUNCTION: ALDHs play a major role in the detoxification of CC alcohol-derived acetaldehyde. They are involved in the metabolism CC of corticosteroids, biogenic amines, neurotransmitters, and lipid CC peroxidation (By similarity). CC -!- CATALYTIC ACTIVITY: An aldehyde + NAD(+) + H(2)O = a carboxylate + CC NADH. CC -!- PATHWAY: Alcohol metabolism; ethanol degradation; acetate from CC ethanol: step 2/2. CC -!- SUBUNIT: Homotetramer (By similarity). CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix (By similarity). CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK012213; BAB28101.1; -; mRNA. DR EMBL; AK088396; BAC40326.1; -; mRNA. DR EMBL; AK150992; BAE30016.1; -; mRNA. DR EMBL; AK151349; BAE30325.1; -; mRNA. DR EMBL; AK151364; BAE30339.1; -; mRNA. DR EMBL; AK153416; BAE31976.1; -; mRNA. DR EMBL; BC020001; AAH20001.1; -; mRNA. DR EMBL; BC086768; AAH86768.1; -; mRNA. DR RefSeq; NP_082546.1; NM_028270.4. DR UniGene; Mm.331583; -. DR ProteinModelPortal; Q9CZS1; -. DR SMR; Q9CZS1; 34-519. DR IntAct; Q9CZS1; 1. DR MINT; MINT-1869729; -. DR STRING; 10090.ENSMUSP00000041260; -. DR PhosphoSite; Q9CZS1; -. DR PaxDb; Q9CZS1; -. DR PRIDE; Q9CZS1; -. DR Ensembl; ENSMUST00000044384; ENSMUSP00000041260; ENSMUSG00000035561. DR GeneID; 72535; -. DR KEGG; mmu:72535; -. DR UCSC; uc008ssx.1; mouse. DR CTD; 219; -. DR MGI; MGI:1919785; Aldh1b1. DR eggNOG; COG1012; -. DR GeneTree; ENSGT00550000074289; -. DR HOGENOM; HOG000271505; -. DR HOVERGEN; HBG000097; -. DR InParanoid; Q9CZS1; -. DR KO; K00128; -. DR OMA; DNGRDKG; -. DR OrthoDB; EOG7PS1F7; -. DR TreeFam; TF300455; -. DR UniPathway; UPA00780; UER00768. DR NextBio; 336439; -. DR PRO; PR:Q9CZS1; -. DR ArrayExpress; Q9CZS1; -. DR Bgee; Q9CZS1; -. DR CleanEx; MM_ALDH1B1; -. DR Genevestigator; Q9CZS1; -. DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR GO; GO:0005634; C:nucleus; IEA:Ensembl. DR GO; GO:0004029; F:aldehyde dehydrogenase (NAD) activity; IEA:UniProtKB-EC. DR GO; GO:0006068; P:ethanol catabolic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.309.10; -; 1. DR Gene3D; 3.40.605.10; -; 1. DR InterPro; IPR016161; Ald_DH/histidinol_DH. DR InterPro; IPR016163; Ald_DH_C. DR InterPro; IPR016160; Ald_DH_CS. DR InterPro; IPR016162; Ald_DH_N. DR InterPro; IPR015590; Aldehyde_DH_dom. DR Pfam; PF00171; Aldedh; 1. DR SUPFAM; SSF53720; SSF53720; 1. DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1. DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1. PE 1: Evidence at protein level; KW Acetylation; Complete proteome; Mitochondrion; NAD; Oxidoreductase; KW Reference proteome; Transit peptide. FT TRANSIT 1 19 Mitochondrion (Potential). FT CHAIN 20 519 Aldehyde dehydrogenase X, mitochondrial. FT /FTId=PRO_0000271411. FT NP_BIND 264 269 NAD (By similarity). FT ACT_SITE 287 287 Proton acceptor (By similarity). FT ACT_SITE 321 321 Nucleophile (By similarity). FT SITE 188 188 Transition state stabilizer (By FT similarity). FT MOD_RES 53 53 N6-acetyllysine. FT MOD_RES 54 54 N6-acetyllysine; alternate. FT MOD_RES 54 54 N6-succinyllysine; alternate. FT MOD_RES 83 83 N6-succinyllysine. FT MOD_RES 366 366 N6-acetyllysine; alternate. FT MOD_RES 366 366 N6-succinyllysine; alternate. FT MOD_RES 385 385 N6-acetyllysine; alternate. FT MOD_RES 385 385 N6-succinyllysine; alternate. FT MOD_RES 401 401 N6-acetyllysine; alternate. FT MOD_RES 401 401 N6-succinyllysine; alternate. FT MOD_RES 416 416 N6-acetyllysine; alternate. FT MOD_RES 416 416 N6-succinyllysine; alternate. FT MOD_RES 428 428 N6-acetyllysine; alternate. FT MOD_RES 428 428 N6-succinyllysine; alternate. FT MOD_RES 431 431 N6-acetyllysine. FT CONFLICT 146 146 K -> R (in Ref. 1; BAE30339). FT CONFLICT 261 261 A -> T (in Ref. 1; BAE30339). SQ SEQUENCE 519 AA; 57553 MW; 69222D7409BFEEF3 CRC64; MLTARLLLPR LLCLQGRTTS YSTAAALPNP IPNPEICYNK LFINNEWHDA VSKKTFPTVN PTTGEVIGHV AEGDRADVDL AVKAAREAFR LGSPWRRMDA SERGRLLNRL ADLVERDRVY LASLETLDNG KPFQESYVLD LDEVIKVYRY FAGWADKWHG KTIPMDGEHF CFTRHEPVGV CGQIIPWNFP LVMQGWKLAP ALATGNTVVM KVAEQTPLSA LYLASLIKEA GFPPGVVNII TGYGPTAGAA IAQHMDVDKV AFTGSTEVGH LIQKAAGESN LKRVTLELGG KSPSIVLADA DMEHAVDQCH EALFFNMGQC CCAGSRTFVE ESIYREFLER TVEKAKQRKV GNPFELDTQQ GPQVDKEQFE RILGYIRLGQ KEGAKLLCGG ERLGERGFFI KPTVFGDVQD GMRIAKEEIF GPVQPLFKFK KIEEVIQRAN NTRYGLAAAV FTRDLDKAIY FTQALQAGTV WVNTYNIVTC HTPFGGFKES GNGRELGEDG LRAYTEVKTV TIKVPEKNS // ID AL1L1_MOUSE Reviewed; 902 AA. AC Q8R0Y6; DT 25-OCT-2002, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2002, sequence version 1. DT 19-MAR-2014, entry version 112. DE RecName: Full=Cytosolic 10-formyltetrahydrofolate dehydrogenase; DE Short=10-FTHFDH; DE Short=FDH; DE EC=1.5.1.6; DE AltName: Full=Aldehyde dehydrogenase family 1 member L1; GN Name=Aldh1l1; Synonyms=Fthfd; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Liver; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [2] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-354, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=17242355; DOI=10.1073/pnas.0609836104; RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; RT "Large-scale phosphorylation analysis of mouse liver."; RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). RN [3] RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-38 AND LYS-767, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., RA Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). CC -!- CATALYTIC ACTIVITY: 10-formyltetrahydrofolate + NADP(+) + H(2)O = CC tetrahydrofolate + CO(2) + NADPH. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: In the N-terminal section; belongs to the GART family. CC -!- SIMILARITY: In the C-terminal section; belongs to the aldehyde CC dehydrogenase family. ALDH1L subfamily. CC -!- SIMILARITY: Contains 1 acyl carrier domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BC025939; AAH25939.1; -; mRNA. DR EMBL; BC028817; AAH28817.1; -; mRNA. DR EMBL; BC030722; AAH30722.1; -; mRNA. DR EMBL; BC030723; AAH30723.1; -; mRNA. DR EMBL; BC030727; AAH30727.1; -; mRNA. DR EMBL; BC030730; AAH30730.1; -; mRNA. DR RefSeq; NP_081682.1; NM_027406.1. DR RefSeq; XP_006505342.1; XM_006505279.1. DR UniGene; Mm.30035; -. DR ProteinModelPortal; Q8R0Y6; -. DR SMR; Q8R0Y6; 1-402, 405-902. DR BioGrid; 223535; 1. DR IntAct; Q8R0Y6; 7. DR MINT; MINT-1856176; -. DR STRING; 10090.ENSMUSP00000032175; -. DR PhosphoSite; Q8R0Y6; -. DR PaxDb; Q8R0Y6; -. DR PRIDE; Q8R0Y6; -. DR Ensembl; ENSMUST00000032175; ENSMUSP00000032175; ENSMUSG00000030088. DR Ensembl; ENSMUST00000130418; ENSMUSP00000114304; ENSMUSG00000030088. DR GeneID; 107747; -. DR KEGG; mmu:107747; -. DR UCSC; uc009cxl.1; mouse. DR CTD; 10840; -. DR MGI; MGI:1340024; Aldh1l1. DR eggNOG; COG1012; -. DR GeneTree; ENSGT00740000115528; -. DR HOVERGEN; HBG051668; -. DR InParanoid; Q8R0Y6; -. DR KO; K00289; -. DR OMA; MASTFGD; -. DR OrthoDB; EOG7MSMN7; -. DR TreeFam; TF354242; -. DR ChiTaRS; ALDH1L1; mouse. DR NextBio; 359368; -. DR PRO; PR:Q8R0Y6; -. DR ArrayExpress; Q8R0Y6; -. DR Bgee; Q8R0Y6; -. DR CleanEx; MM_ALDH1L1; -. DR Genevestigator; Q8R0Y6; -. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR GO; GO:0016155; F:formyltetrahydrofolate dehydrogenase activity; IEA:UniProtKB-EC. DR GO; GO:0016742; F:hydroxymethyl-, formyl- and related transferase activity; IEA:InterPro. DR GO; GO:0008168; F:methyltransferase activity; IEA:InterPro. DR GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IEA:InterPro. DR GO; GO:0009258; P:10-formyltetrahydrofolate catabolic process; IEA:InterPro. DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro. DR GO; GO:0032259; P:methylation; IEA:GOC. DR GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW. DR Gene3D; 1.10.1200.10; -; 1. DR Gene3D; 3.10.25.10; -; 1. DR Gene3D; 3.40.309.10; -; 1. DR Gene3D; 3.40.50.170; -; 1. DR Gene3D; 3.40.605.10; -; 1. DR InterPro; IPR011407; 10_FTHF_DH. DR InterPro; IPR009081; Acyl_carrier_prot-like. DR InterPro; IPR016161; Ald_DH/histidinol_DH. DR InterPro; IPR016163; Ald_DH_C. DR InterPro; IPR016160; Ald_DH_CS. DR InterPro; IPR016162; Ald_DH_N. DR InterPro; IPR015590; Aldehyde_DH_dom. DR InterPro; IPR005793; Formyl_trans_C. DR InterPro; IPR002376; Formyl_transf_N. DR InterPro; IPR011034; Formyl_transferase_C-like. DR InterPro; IPR001555; GART_AS. DR Pfam; PF00171; Aldedh; 1. DR Pfam; PF02911; Formyl_trans_C; 1. DR Pfam; PF00551; Formyl_trans_N; 1. DR Pfam; PF00550; PP-binding; 1. DR PIRSF; PIRSF036489; 10-FTHFDH; 1. DR SUPFAM; SSF47336; SSF47336; 1. DR SUPFAM; SSF50486; SSF50486; 1. DR SUPFAM; SSF53328; SSF53328; 1. DR SUPFAM; SSF53720; SSF53720; 1. DR PROSITE; PS50075; ACP_DOMAIN; 1. DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1. DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1. DR PROSITE; PS00373; GART; 1. PE 1: Evidence at protein level; KW Complete proteome; Cytoplasm; NADP; One-carbon metabolism; KW Oxidoreductase; Phosphopantetheine; Phosphoprotein; KW Reference proteome. FT CHAIN 1 902 Cytosolic 10-formyltetrahydrofolate FT dehydrogenase. FT /FTId=PRO_0000199420. FT DOMAIN 323 392 Acyl carrier. FT NP_BIND 571 573 NADP (By similarity). FT NP_BIND 597 600 NADP (By similarity). FT NP_BIND 630 635 NADP (By similarity). FT NP_BIND 650 651 NADP (By similarity). FT NP_BIND 804 806 NADP (By similarity). FT REGION 1 203 GART. FT REGION 88 90 Substrate binding (By similarity). FT REGION 417 902 Aldehyde dehydrogenase. FT ACT_SITE 106 106 Proton donor (By similarity). FT ACT_SITE 673 673 Proton acceptor (By similarity). FT ACT_SITE 707 707 Proton donor (By similarity). FT BINDING 142 142 Substrate (By similarity). FT BINDING 757 757 NADP (By similarity). FT SITE 142 142 Essential for catalytic activity (By FT similarity). FT MOD_RES 38 38 N6-succinyllysine. FT MOD_RES 354 354 O-(pantetheine 4'-phosphoryl)serine; FT alternate (By similarity). FT MOD_RES 354 354 Phosphoserine; alternate. FT MOD_RES 767 767 N6-succinyllysine. SQ SEQUENCE 902 AA; 98709 MW; 9B5526A7FB41909E CRC64; MKIAVIGQSL FGQEVYCQLR KEGHEVVGVF TIPDKDGKAD PLGLEAEKDG VPVFKFPRWR ARGQALPEVV AKYQALGAEL NVLPFCSQFI PMEVINAPRH GSIIYHPSLL PRHRGASAIN WTLIHGDKKG GFTIFWADDG LDTGDLLLQK ECDVLPDDTV STLYNRFLFP EGIKGMVQAV RLIAEGTAPR RPQPEEGATY EGIQKKETAM INWDQPAEAI HNWIRGNDKV PGAWTEACGQ KLTFFNSTLN TSGLVAQGEA LPIPGAHRPG LVTKAGLILF GNDDRMLLVK NIQLEDGKMM PASQFFKGSA SSALELTEEE LATAEAVRSS WMRILPNVPE VEDSTDFFKS GAASVDVVRL VEEVKELCDG LELENEDVYM ATTFGDFIQL LVRKLRGEDG ESECVINYVE KAVKKLTLQM PYQLFIGGEF VDAEGAKTYS TINPTDGSVI CQVSLAQVSD VDKAVAAAKE AFENGLWGKI NARDRGRLLY RLADLMEQHQ EELATIEALD AGAVYTLALK THVGMSIQTF RYFAGWCDKI QGATIPINQA RPNRNLTLTK KEPVGVCGIV IPWNYPLMML SWKTAACLAA GNTVVIKPAQ VTPLTALKFA ELTLKAGIPK GVVNILPGSG SLVGQRLSDH PDVRKIGFTG STEVGKHIMK SCALSNVKKV SLELGGKSPL IIFADCDLNK AVQMGMSSVF FNKGENCIAA GRLFVEDSIH DQFVQKVVEE VGKMKIGNPL DRDTNHGPQN HEAHLRKLVE YCQRGVKEGA TLVCGGNQVP RPGFFFQPTV FTDVEDHMYI AKEESFGPIM IISRFADGDV DAVLSRANAT EFGLASGVFT RDINKALYVS DKLQAGTVFV NTYNKTDVAA PFGGFKQSGF GKDLGEAALN EYLRIKTVTF EY // ID AL1A3_MOUSE Reviewed; 512 AA. AC Q9JHW9; Q9EQP7; Q9JI72; DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 19-FEB-2014, entry version 106. DE RecName: Full=Aldehyde dehydrogenase family 1 member A3; DE EC=1.2.1.5; DE AltName: Full=Aldehyde dehydrogenase 6; DE AltName: Full=Retinaldehyde dehydrogenase 3; DE Short=RALDH-3; DE Short=RalDH3; GN Name=Aldh1a3; Synonyms=Aldh6, Raldh3; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY. RC STRAIN=B6/D2; RX PubMed=10906479; DOI=10.1016/S0925-4773(00)00352-X; RA Li H., Wagner E., McCaffery P., Smith D., Andreadis A., Drager U.C.; RT "A retinoic acid synthesizing enzyme in ventral retina and RT telencephalon of the embryonic mouse."; RL Mech. Dev. 95:283-289(2000). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DEVELOPMENTAL STAGE, AND TISSUE RP SPECIFICITY. RC STRAIN=C57BL/6 X 129/SvJ; TISSUE=Kidney; RX PubMed=11025231; DOI=10.1016/S0925-4773(00)00434-2; RA Mic F.A., Molotkov A., Fan X., Cuenca A.E., Duester G.; RT "RALDH3, a retinaldehyde dehydrogenase that generates retinoic acid, RT is expressed in the ventral retina, otic vesicle and olfactory pit RT during mouse development."; RL Mech. Dev. 97:227-230(2000). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY. RC STRAIN=C57BL/6J; TISSUE=Retina; RX PubMed=11044606; DOI=10.1016/S0925-4773(00)00450-0; RA Suzuki R., Shintani T., Sakuta H., Kato A., Ohkawara T., Osumi N., RA Noda M.; RT "Identification of RALDH-3, a novel retinaldehyde dehydrogenase, RT expressed in the ventral region of the retina."; RL Mech. Dev. 98:37-50(2000). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE RP SPECIFICITY. RX PubMed=11013254; DOI=10.1074/jbc.M007376200; RA Grun F., Hirose Y., Kawauchi S., Ogura T., Umesono K.; RT "Aldehyde dehydrogenase 6, a cytosolic retinaldehyde dehydrogenase RT prominently expressed in sensory neuroepithelia during development."; RL J. Biol. Chem. 275:41210-41218(2000). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Mammary tumor; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: Recognizes as substrates free retinal and cellular CC retinol-binding protein-bound retinal. Seems to be the key enzyme CC in the formation of an RA gradient along the dorso-ventral axis CC during the early eye development and also in the development of CC the olfactory system. CC -!- CATALYTIC ACTIVITY: An aldehyde + NAD(P)(+) + H(2)O = a CC carboxylate + NAD(P)H. CC -!- PATHWAY: Cofactor metabolism; retinol metabolism. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- TISSUE SPECIFICITY: Ventral retina. CC -!- DEVELOPMENTAL STAGE: In mouse embryos, RALDH3 expression is first CC noticed in the ventral optic eminence at E8.75, then in the optic CC vesicle/cup, otic vesicle and olfactory placode/pit from E9.5 to CC E11.5. CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF253409; AAF67736.1; -; mRNA. DR EMBL; AF280404; AAF86980.1; -; mRNA. DR EMBL; AF246711; AAG38488.1; -; mRNA. DR EMBL; AF152359; AAG33935.1; -; mRNA. DR EMBL; BC058277; AAH58277.1; -; mRNA. DR RefSeq; NP_444310.3; NM_053080.3. DR UniGene; Mm.140988; -. DR ProteinModelPortal; Q9JHW9; -. DR SMR; Q9JHW9; 20-511. DR BioGrid; 208193; 1. DR PhosphoSite; Q9JHW9; -. DR PaxDb; Q9JHW9; -. DR PRIDE; Q9JHW9; -. DR Ensembl; ENSMUST00000015278; ENSMUSP00000015278; ENSMUSG00000015134. DR GeneID; 56847; -. DR KEGG; mmu:56847; -. DR UCSC; uc009hhi.2; mouse. DR CTD; 220; -. DR MGI; MGI:1861722; Aldh1a3. DR eggNOG; COG1012; -. DR GeneTree; ENSGT00550000074289; -. DR HOGENOM; HOG000271505; -. DR HOVERGEN; HBG000097; -. DR InParanoid; Q9JHW9; -. DR KO; K00129; -. DR OMA; NSMKIMQ; -. DR OrthoDB; EOG7PS1F7; -. DR TreeFam; TF300455; -. DR BRENDA; 1.2.1.36; 3474. DR SABIO-RK; Q9JHW9; -. DR UniPathway; UPA00912; -. DR NextBio; 313405; -. DR PRO; PR:Q9JHW9; -. DR ArrayExpress; Q9JHW9; -. DR Bgee; Q9JHW9; -. DR CleanEx; MM_ALDH1A3; -. DR Genevestigator; Q9JHW9; -. DR GO; GO:0005737; C:cytoplasm; IDA:MGI. DR GO; GO:0004028; F:3-chloroallyl aldehyde dehydrogenase activity; TAS:MGI. DR GO; GO:0004029; F:aldehyde dehydrogenase (NAD) activity; IDA:MGI. DR GO; GO:0004030; F:aldehyde dehydrogenase [NAD(P)+] activity; IDA:MGI. DR GO; GO:0070403; F:NAD+ binding; IDA:MGI. DR GO; GO:0070324; F:thyroid hormone binding; IPI:MGI. DR GO; GO:0060324; P:face development; IGI:MGI. DR GO; GO:0042472; P:inner ear morphogenesis; IMP:MGI. DR GO; GO:0007626; P:locomotory behavior; IMP:MGI. DR GO; GO:0050885; P:neuromuscular process controlling balance; IMP:MGI. DR GO; GO:0021768; P:nucleus accumbens development; IMP:MGI. DR GO; GO:0060166; P:olfactory pit development; IMP:MGI. DR GO; GO:0002072; P:optic cup morphogenesis involved in camera-type eye development; IGI:MGI. DR GO; GO:0043065; P:positive regulation of apoptotic process; IMP:MGI. DR GO; GO:0048386; P:positive regulation of retinoic acid receptor signaling pathway; ISA:MGI. DR GO; GO:0042574; P:retinal metabolic process; IEA:Ensembl. DR GO; GO:0002138; P:retinoic acid biosynthetic process; IDA:MGI. DR GO; GO:0042572; P:retinol metabolic process; IEA:UniProtKB-UniPathway. DR GO; GO:0060013; P:righting reflex; IMP:MGI. DR Gene3D; 3.40.309.10; -; 1. DR Gene3D; 3.40.605.10; -; 1. DR InterPro; IPR016161; Ald_DH/histidinol_DH. DR InterPro; IPR016163; Ald_DH_C. DR InterPro; IPR016160; Ald_DH_CS. DR InterPro; IPR016162; Ald_DH_N. DR InterPro; IPR015590; Aldehyde_DH_dom. DR Pfam; PF00171; Aldedh; 1. DR SUPFAM; SSF53720; SSF53720; 1. DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1. DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1. PE 2: Evidence at transcript level; KW Acetylation; Complete proteome; Cytoplasm; NAD; Oxidoreductase; KW Reference proteome. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 512 Aldehyde dehydrogenase family 1 member FT A3. FT /FTId=PRO_0000056479. FT NP_BIND 257 262 NAD (By similarity). FT ACT_SITE 280 280 Proton acceptor (By similarity). FT ACT_SITE 314 314 Nucleophile (By similarity). FT SITE 181 181 Transition state stabilizer (By FT similarity). FT MOD_RES 2 2 N-acetylalanine (By similarity). FT CONFLICT 91 91 L -> V (in Ref. 1; AAF67736). FT CONFLICT 208 208 Q -> R (in Ref. 4; AAG33935). FT CONFLICT 223 223 V -> E (in Ref. 1; AAF67736). FT CONFLICT 341 341 R -> S (in Ref. 4; AAG33935). FT CONFLICT 407 407 I -> R (in Ref. 1; AAF67736). SQ SEQUENCE 512 AA; 56157 MW; 5BBC6DEE41E58CFE CRC64; MATTNGAVEN GQPDGKPPAL PRPIRNLEVK FTKIFINNDW HESKSGRKFA TYNPSTLEKI CEVEEGDKPD VDKAVEAAQA AFQRGSPWRR LDALSRGQLL HQLADLVERD RAILATLETM DTGKPFLHAF FVDLEGCIKT FRYFAGWADK IQGRTIPTDD NVVCFTRHEP IGVCGAITPW NFPLLMLAWK LAPALCCGNT VVLKPAEQTP LTALYLASLI KEVGFPPGVV NIVPGFGPTV GAAISSHPQI NKIAFTGSTE VGKLVREAAS RSNLKRVTLE LGGKNPCIVC ADADLDLAVE CAHQGVFFNQ GQCCTAASRV FVEEQVYGEF VRRSVEFAKK RPVGDPFDAK TEQGPQIDQK QFDKILELIE SGKKEGAKLE CGGSAMEDRG LFIKPTVFSD VTDNMRIAKE EIFGPVQPIL KFKNLEEVIK RANSTDYGLT AAVFTKNLDK ALKLAAALES GTVWINCYNA FYAQAPFGGF KMSGNGRELG EYALAEYTEV KTVTIKLEEK NP // ID AL1A2_MOUSE Reviewed; 518 AA. AC Q62148; Q6DI79; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 07-MAR-2006, sequence version 2. DT 19-FEB-2014, entry version 125. DE RecName: Full=Retinal dehydrogenase 2; DE Short=RALDH 2; DE Short=RalDH2; DE EC=1.2.1.36; DE AltName: Full=Aldehyde dehydrogenase family 1 member A2; DE AltName: Full=Retinaldehyde-specific dehydrogenase type 2; DE Short=RALDH(II); GN Name=Aldh1a2; Synonyms=Aldh1a7, Raldh2; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=C3H/He; RX PubMed=8797830; DOI=10.1111/j.1432-1033.1996.0015h.x; RA Zhao D., McCaffery P., Ivins K.J., Neve R.L., Hogan P., Chin W.W., RA Draeger U.C.; RT "Molecular identification of a major retinoic-acid-synthesizing RT enzyme, a retinaldehyde-specific dehydrogenase."; RL Eur. J. Biochem. 240:15-22(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Kidney; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-518. RC STRAIN=C57BL/6J; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). CC -!- FUNCTION: Recognizes as substrates free retinal and cellular CC retinol-binding protein-bound retinal. Does metabolize octanal and CC decanal but does not metabolize citral, benzaldehyde, acetaldehyde CC and propanal efficiently (By similarity). CC -!- CATALYTIC ACTIVITY: Retinal + NAD(+) + H(2)O = retinoate + NADH. CC -!- PATHWAY: Cofactor metabolism; retinol metabolism. CC -!- SUBUNIT: Homotetramer (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family. CC -!- SEQUENCE CAUTION: CC Sequence=BAC37332.1; Type=Erroneous initiation; CC Sequence=CAA67666.1; Type=Erroneous initiation; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X99273; CAA67666.1; ALT_INIT; mRNA. DR EMBL; BC075704; AAH75704.1; -; mRNA. DR EMBL; AK078553; BAC37332.1; ALT_INIT; mRNA. DR PIR; S74224; S74224. DR RefSeq; NP_033048.2; NM_009022.4. DR UniGene; Mm.42016; -. DR ProteinModelPortal; Q62148; -. DR SMR; Q62148; 20-518. DR IntAct; Q62148; 1. DR MINT; MINT-4087503; -. DR PhosphoSite; Q62148; -. DR REPRODUCTION-2DPAGE; IPI00122212; -. DR REPRODUCTION-2DPAGE; Q62148; -. DR PaxDb; Q62148; -. DR PRIDE; Q62148; -. DR Ensembl; ENSMUST00000034723; ENSMUSP00000034723; ENSMUSG00000013584. DR GeneID; 19378; -. DR KEGG; mmu:19378; -. DR UCSC; uc009qox.2; mouse. DR CTD; 8854; -. DR MGI; MGI:107928; Aldh1a2. DR eggNOG; COG1012; -. DR GeneTree; ENSGT00550000074289; -. DR HOGENOM; HOG000271505; -. DR HOVERGEN; HBG000097; -. DR InParanoid; Q62148; -. DR KO; K07249; -. DR OMA; NELAMIV; -. DR OrthoDB; EOG7PS1F7; -. DR TreeFam; TF300455; -. DR BRENDA; 1.2.1.36; 3474. DR UniPathway; UPA00912; -. DR NextBio; 296481; -. DR PRO; PR:Q62148; -. DR ArrayExpress; Q62148; -. DR Bgee; Q62148; -. DR CleanEx; MM_ALDH1A2; -. DR CleanEx; MM_ALDH1A7; -. DR Genevestigator; Q62148; -. DR GO; GO:0005829; C:cytosol; IEA:Ensembl. DR GO; GO:0005634; C:nucleus; IEA:Ensembl. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl. DR GO; GO:0004028; F:3-chloroallyl aldehyde dehydrogenase activity; IDA:MGI. DR GO; GO:0016918; F:retinal binding; IEA:Ensembl. DR GO; GO:0001758; F:retinal dehydrogenase activity; IDA:MGI. DR GO; GO:0042904; P:9-cis-retinoic acid biosynthetic process; IDA:MGI. DR GO; GO:0009952; P:anterior/posterior pattern specification; IMP:MGI. DR GO; GO:0001568; P:blood vessel development; IMP:MGI. DR GO; GO:0048738; P:cardiac muscle tissue development; IMP:MGI. DR GO; GO:0071300; P:cellular response to retinoic acid; IEP:UniProtKB. DR GO; GO:0031076; P:embryonic camera-type eye development; IGI:MGI. DR GO; GO:0048566; P:embryonic digestive tract development; IMP:MGI. DR GO; GO:0035115; P:embryonic forelimb morphogenesis; IMP:MGI. DR GO; GO:0060324; P:face development; IMP:MGI. DR GO; GO:0030900; P:forebrain development; IMP:MGI. DR GO; GO:0001947; P:heart looping; TAS:DFLAT. DR GO; GO:0030902; P:hindbrain development; IMP:MGI. DR GO; GO:0001822; P:kidney development; IEA:Ensembl. DR GO; GO:0001889; P:liver development; IEA:Ensembl. DR GO; GO:0030324; P:lung development; IMP:MGI. DR GO; GO:0007494; P:midgut development; IEA:Ensembl. DR GO; GO:0016331; P:morphogenesis of embryonic epithelium; IMP:MGI. DR GO; GO:0008285; P:negative regulation of cell proliferation; IEA:Ensembl. DR GO; GO:0014032; P:neural crest cell development; IMP:MGI. DR GO; GO:0021915; P:neural tube development; IEA:Ensembl. DR GO; GO:0030182; P:neuron differentiation; IMP:MGI. DR GO; GO:0031016; P:pancreas development; IMP:MGI. DR GO; GO:0021983; P:pituitary gland development; IEA:Ensembl. DR GO; GO:0043065; P:positive regulation of apoptotic process; IMP:MGI. DR GO; GO:0008284; P:positive regulation of cell proliferation; IMP:MGI. DR GO; GO:0010628; P:positive regulation of gene expression; IMP:MGI. DR GO; GO:0009954; P:proximal/distal pattern formation; IMP:MGI. DR GO; GO:0001936; P:regulation of endothelial cell proliferation; IMP:MGI. DR GO; GO:0034097; P:response to cytokine; IEA:Ensembl. DR GO; GO:0032355; P:response to estradiol; IEA:Ensembl. DR GO; GO:0033189; P:response to vitamin A; IEA:Ensembl. DR GO; GO:0042574; P:retinal metabolic process; IDA:MGI. DR GO; GO:0048384; P:retinoic acid receptor signaling pathway; IMP:MGI. DR GO; GO:0042572; P:retinol metabolic process; IEA:UniProtKB-UniPathway. DR GO; GO:0035799; P:ureter maturation; IMP:MGI. DR Gene3D; 3.40.309.10; -; 1. DR Gene3D; 3.40.605.10; -; 1. DR InterPro; IPR016161; Ald_DH/histidinol_DH. DR InterPro; IPR016163; Ald_DH_C. DR InterPro; IPR016160; Ald_DH_CS. DR InterPro; IPR016162; Ald_DH_N. DR InterPro; IPR015590; Aldehyde_DH_dom. DR Pfam; PF00171; Aldedh; 1. DR SUPFAM; SSF53720; SSF53720; 1. DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1. DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1. PE 2: Evidence at transcript level; KW Complete proteome; Cytoplasm; NAD; Oxidoreductase; Reference proteome. FT CHAIN 1 518 Retinal dehydrogenase 2. FT /FTId=PRO_0000056423. FT NP_BIND 263 268 NAD (By similarity). FT ACT_SITE 286 286 Proton acceptor (By similarity). FT ACT_SITE 320 320 Nucleophile (By similarity). FT SITE 187 187 Transition state stabilizer (By FT similarity). SQ SEQUENCE 518 AA; 56626 MW; 2BC35B5C90046ABC CRC64; MTSSEIAMPG EVKADPAALM ASLQLLPSPT PNLEIKYTKI FINNEWQNSE SGRVFPVCNP ATGEQVCEVQ EADKVDIDKA VQAARLAFSL GSVWRRMDAS ERGRLLDKLA DLVERDRATL ATMESLNGGK PFLQAFYIDL QGVIKTLRYY AGWADKIHGM TIPVDGDYFT FTRHEPIGVC GQIIPWNFPL LMFTWKIAPA LCCGNTVVIK PAEQTPLSAL YMGALIKEAG FPPGVVNILP GYGPTAGAAI ASHIGIDKIA FTGSTEVGKL IQEAAGRSNL KRVTLELGGK SPNIIFADAD LDYAVEQAHQ GVFFNQGQCC TAGSRIFVEE SIYEEFVKRS VERAKRRIVG SPFDPTTEQG PQIDKKQYNK VLELIQSGVA EGAKLECGGK GLGRKGFFIE PTVFSNVTDD MRIAKEEIFG PVQEILRFKT MDEVIERANN SDFGLVAAVF TNDINKALMV SSAMQAGTVW INCYNALNAQ SPFGGFKMSG NGREMGEFGL REYSEVKTVT VKIPQKNS // ID AL3A2_MOUSE Reviewed; 484 AA. AC P47740; Q99L64; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 2. DT 19-FEB-2014, entry version 112. DE RecName: Full=Fatty aldehyde dehydrogenase; DE EC=1.2.1.3; DE AltName: Full=Aldehyde dehydrogenase 3; DE AltName: Full=Aldehyde dehydrogenase family 3 member A2; GN Name=Aldh3a2; Synonyms=Ahd-3, Ahd3, Aldh3, Aldh4; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=C57BL/6 X CBA; TISSUE=Liver; RX PubMed=8634152; DOI=10.1089/dna.1996.15.235; RA Vasiliou V., Kozak C.A., Lindahl R., Nebert D.W.; RT "Mouse microsomal class 3 aldehyde dehydrogenase: AHD3 cDNA sequence, RT inducibility by dioxin and clofibrate, and genetic mapping."; RL DNA Cell Biol. 15:235-245(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J, and NOD; RC TISSUE=Head, Spinal cord, Stomach, and Thymus; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Mammary tumor; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: Catalyzes the oxidation of long-chain aliphatic CC aldehydes to fatty acids. Responsible for conversion of the CC sphingosine 1-phosphate (S1P) degradation product hexadecenal to CC hexadecenoic acid (By similarity). CC -!- CATALYTIC ACTIVITY: An aldehyde + NAD(+) + H(2)O = a carboxylate + CC NADH. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass CC membrane protein; Cytoplasmic side. CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U14390; AAB06232.1; -; mRNA. DR EMBL; AK079639; BAC37712.1; -; mRNA. DR EMBL; AK140932; BAE24523.1; -; mRNA. DR EMBL; AK159246; BAE34928.1; -; mRNA. DR EMBL; AK163040; BAE37166.1; -; mRNA. DR EMBL; AK169157; BAE40936.1; -; mRNA. DR EMBL; AK170195; BAE41628.1; -; mRNA. DR EMBL; AL672172; CAI24063.1; -; Genomic_DNA. DR EMBL; BC003797; AAH03797.1; -; mRNA. DR RefSeq; NP_031463.2; NM_007437.4. DR UniGene; Mm.398221; -. DR ProteinModelPortal; P47740; -. DR SMR; P47740; 1-443. DR IntAct; P47740; 4. DR MINT; MINT-4087555; -. DR STRING; 10090.ENSMUSP00000067767; -. DR PhosphoSite; P47740; -. DR PaxDb; P47740; -. DR PRIDE; P47740; -. DR Ensembl; ENSMUST00000074127; ENSMUSP00000073764; ENSMUSG00000010025. DR GeneID; 11671; -. DR KEGG; mmu:11671; -. DR UCSC; uc007jhf.1; mouse. DR CTD; 224; -. DR MGI; MGI:1353452; Aldh3a2. DR eggNOG; COG1012; -. DR GeneTree; ENSGT00390000002825; -. DR HOGENOM; HOG000271515; -. DR HOVERGEN; HBG050483; -. DR KO; K00128; -. DR TreeFam; TF314264; -. DR ChiTaRS; ALDH3A2; mouse. DR NextBio; 279299; -. DR PRO; PR:P47740; -. DR ArrayExpress; P47740; -. DR Bgee; P47740; -. DR CleanEx; MM_ALDH3A2; -. DR Genevestigator; P47740; -. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:MGI. DR GO; GO:0005777; C:peroxisome; IEA:Ensembl. DR GO; GO:0004030; F:aldehyde dehydrogenase [NAD(P)+] activity; IEA:InterPro. DR GO; GO:0046577; F:long-chain-alcohol oxidase activity; IEA:Ensembl. DR GO; GO:0050061; F:long-chain-aldehyde dehydrogenase activity; IEA:Ensembl. DR GO; GO:0052814; F:medium-chain-aldehyde dehydrogenase activity; IEA:Ensembl. DR GO; GO:0006081; P:cellular aldehyde metabolic process; IEA:InterPro. DR GO; GO:0007417; P:central nervous system development; IEA:Ensembl. DR GO; GO:0008544; P:epidermis development; IEA:Ensembl. DR GO; GO:0007422; P:peripheral nervous system development; IEA:Ensembl. DR GO; GO:0033306; P:phytol metabolic process; IEA:Ensembl. DR GO; GO:0006714; P:sesquiterpenoid metabolic process; IEA:Ensembl. DR Gene3D; 3.40.309.10; -; 1. DR Gene3D; 3.40.605.10; -; 1. DR InterPro; IPR016161; Ald_DH/histidinol_DH. DR InterPro; IPR016163; Ald_DH_C. DR InterPro; IPR016160; Ald_DH_CS. DR InterPro; IPR016162; Ald_DH_N. DR InterPro; IPR015590; Aldehyde_DH_dom. DR InterPro; IPR012394; Aldehyde_DH_NAD(P). DR PANTHER; PTHR11699:SF15; PTHR11699:SF15; 1. DR Pfam; PF00171; Aldedh; 1. DR PIRSF; PIRSF036492; ALDH; 1. DR SUPFAM; SSF53720; SSF53720; 1. DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1. DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1. PE 2: Evidence at transcript level; KW Complete proteome; Endoplasmic reticulum; Membrane; NAD; KW Oxidoreductase; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 484 Fatty aldehyde dehydrogenase. FT /FTId=PRO_0000056475. FT TOPO_DOM 1 463 Cytoplasmic. FT TRANSMEM 464 480 Helical; (Potential). FT NP_BIND 185 190 NAD (Potential). FT MOTIF 481 484 Prevents secretion from ER (By FT similarity). FT ACT_SITE 207 207 By similarity. FT ACT_SITE 241 241 By similarity. FT CONFLICT 19 19 P -> L (in Ref. 1; AAB06232). FT CONFLICT 229 229 I -> V (in Ref. 1; AAB06232). FT CONFLICT 418 418 T -> A (in Ref. 1; AAB06232). SQ SEQUENCE 484 AA; 53971 MW; DFC67C96C757832A CRC64; MERQVLRLRQ AFRSGRSRPL RFRLQQLEAL RRMVQEREKE ILAAIAADLS KSELNAYSHE VITILGEIDF MLGNLPELAS ARPAKKNLLT MMDEAYVQPE PLGVVLIIGA WNYPFVLTMQ PLVGAIAAGN AAIVKPSELS ENTAKILAEL LPQYLDQDLY AIVNGGIPET TELLKQRFDH ILYTGNTAVG KIVMEAAAKH LTPVTLELGG KSPCYIDRDC DLDVACRRIA WGKYMNCGQT CIAPDYILCE ASLQNQIVQK IKETVKDFYG ENIKASPDYE RIINLRHFKR LQSLLKGQKI AFGGEMDEAT RYLAPTILTD VDPNSKVMQE EIFGPILPIV SVKNVDEAIN FINDREKPLA LYVFSRNNKL IKRVIDETSS GGVTGNDVIM HFTVNSLPFG GVGASGMGAY HGKYSFDTFS HQRPCLLKGL KGESVNKLRY PPNSESKVSW AKFFLLKQFN KGRLGMLLFV CLVAVAAVIV KDQL // ID AL1L2_MOUSE Reviewed; 923 AA. AC Q8K009; E9QLV8; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 2. DT 19-MAR-2014, entry version 99. DE RecName: Full=Mitochondrial 10-formyltetrahydrofolate dehydrogenase; DE Short=Mitochondrial 10-FTHFDH; DE Short=mtFDH; DE EC=1.5.1.6; DE AltName: Full=Aldehyde dehydrogenase family 1 member L2; GN Name=Aldh1l2; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Salivary gland; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-681, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic fibroblast; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., RA Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). CC -!- CATALYTIC ACTIVITY: 10-formyltetrahydrofolate + NADP(+) + H(2)O = CC tetrahydrofolate + CO(2) + NADPH. CC -!- SUBCELLULAR LOCATION: Mitochondrion (By similarity). CC -!- SIMILARITY: In the N-terminal section; belongs to the GART family. CC -!- SIMILARITY: In the C-terminal section; belongs to the aldehyde CC dehydrogenase family. ALDH1L subfamily. CC -!- SIMILARITY: Contains 1 acyl carrier domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AC113014; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC034531; AAH34531.1; -; mRNA. DR RefSeq; NP_705771.2; NM_153543.2. DR UniGene; Mm.263138; -. DR ProteinModelPortal; Q8K009; -. DR SMR; Q8K009; 23-923. DR STRING; 10090.ENSMUSP00000020497; -. DR PhosphoSite; Q8K009; -. DR PaxDb; Q8K009; -. DR PRIDE; Q8K009; -. DR Ensembl; ENSMUST00000020497; ENSMUSP00000020497; ENSMUSG00000020256. DR GeneID; 216188; -. DR KEGG; mmu:216188; -. DR UCSC; uc007gkh.2; mouse. DR CTD; 160428; -. DR MGI; MGI:2444680; Aldh1l2. DR eggNOG; COG1012; -. DR GeneTree; ENSGT00740000115528; -. DR HOGENOM; HOG000006902; -. DR HOVERGEN; HBG051668; -. DR InParanoid; Q8K009; -. DR KO; K00289; -. DR OMA; THIGMSV; -. DR OrthoDB; EOG7MSMN7; -. DR TreeFam; TF354242; -. DR NextBio; 375062; -. DR PRO; PR:Q8K009; -. DR ArrayExpress; Q8K009; -. DR Bgee; Q8K009; -. DR CleanEx; MM_ALDH1L2; -. DR Genevestigator; Q8K009; -. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR GO; GO:0016155; F:formyltetrahydrofolate dehydrogenase activity; IEA:UniProtKB-EC. DR GO; GO:0016742; F:hydroxymethyl-, formyl- and related transferase activity; IEA:InterPro. DR GO; GO:0008168; F:methyltransferase activity; IEA:InterPro. DR GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IEA:InterPro. DR GO; GO:0009258; P:10-formyltetrahydrofolate catabolic process; IEA:InterPro. DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro. DR GO; GO:0032259; P:methylation; IEA:GOC. DR GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW. DR Gene3D; 1.10.1200.10; -; 1. DR Gene3D; 3.10.25.10; -; 1. DR Gene3D; 3.40.309.10; -; 1. DR Gene3D; 3.40.50.170; -; 1. DR Gene3D; 3.40.605.10; -; 1. DR InterPro; IPR011407; 10_FTHF_DH. DR InterPro; IPR009081; Acyl_carrier_prot-like. DR InterPro; IPR016161; Ald_DH/histidinol_DH. DR InterPro; IPR016163; Ald_DH_C. DR InterPro; IPR016160; Ald_DH_CS. DR InterPro; IPR016162; Ald_DH_N. DR InterPro; IPR015590; Aldehyde_DH_dom. DR InterPro; IPR005793; Formyl_trans_C. DR InterPro; IPR002376; Formyl_transf_N. DR InterPro; IPR011034; Formyl_transferase_C-like. DR InterPro; IPR001555; GART_AS. DR InterPro; IPR006162; PPantetheine_attach_site. DR Pfam; PF00171; Aldedh; 1. DR Pfam; PF02911; Formyl_trans_C; 1. DR Pfam; PF00551; Formyl_trans_N; 1. DR Pfam; PF00550; PP-binding; 1. DR PIRSF; PIRSF036489; 10-FTHFDH; 1. DR SUPFAM; SSF47336; SSF47336; 1. DR SUPFAM; SSF50486; SSF50486; 1. DR SUPFAM; SSF53328; SSF53328; 1. DR SUPFAM; SSF53720; SSF53720; 1. DR PROSITE; PS50075; ACP_DOMAIN; 1. DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1. DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1. DR PROSITE; PS00373; GART; 1. DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1. PE 1: Evidence at protein level; KW Acetylation; Complete proteome; Mitochondrion; NADP; KW One-carbon metabolism; Oxidoreductase; Phosphopantetheine; KW Phosphoprotein; Reference proteome; Transit peptide. FT CHAIN 1 923 Mitochondrial 10-formyltetrahydrofolate FT dehydrogenase. FT /FTId=PRO_0000316002. FT TRANSIT 1 19 Mitochondrion; not cleaved (By FT similarity). FT DOMAIN 344 413 Acyl carrier. FT REGION 23 225 GART. FT REGION 438 923 Aldehyde dehydrogenase. FT ACT_SITE 128 128 Proton donor (By similarity). FT ACT_SITE 694 694 By similarity. FT ACT_SITE 728 728 By similarity. FT SITE 164 164 Essential for catalytic activity (By FT similarity). FT MOD_RES 375 375 O-(pantetheine 4'-phosphoryl)serine (By FT similarity). FT MOD_RES 681 681 N6-succinyllysine. FT MOD_RES 903 903 N6-acetyllysine (By similarity). FT CONFLICT 476 476 Y -> H (in Ref. 2; AAH34531). SQ SEQUENCE 923 AA; 101590 MW; 57CB83C38FAFB0D2 CRC64; MLWRGSQALR HFSTSRVYFK NKLKLALIGQ SLFGQEVYSQ LLKEGHRVVG VFTVPDKDGK ADPLALAAEK DGTPVFKFPR WRLKGKTIKE VAEAYQSVGA ELNVLPFCTQ FIPMDVIDSP KHGSIIYHPS LLPRHRGASA INWTLIMGDK KAGFSVFWAD DGLDTGPILL QRSCDVKPND TVDSLYNRFL FPEGIKAMVE AVQLIADGKA PRTPQPEEGA TYEGIQKKEN AEVSWDQPAE GLHNWIRGHD KVPGAWAEIN GQMVTFYGSS LLTSSVPSGE PLDIRGAKKP GLVTKNGLVL FGNDGKALMV RNLQFEDGKM IPASQYFSAG ETSVVELTAE ELKVAETIKV IWARILSNTP VIEDSTDFFK SGASSMDVVR LVEEIRQSCG GLQLQNEDVY MATKFGDFIQ KVVRRLRGED EEAEMVVDYV SKEVNGMTVK IPYQCFINGQ FVDAEDGETY ATVNPTDGTT ICRVSYASLA DVDRAVAAAK DAFENGEWGR MNARDRGRLM YRLADLMEEN QEELATIEAL DSGAVYTLAL KTHIGMSVQT FRYFAGWCDK IQGSTIPINQ ARPNYNLTFT KKEPLGACAI IIPWNYPLMM LAWKSAACLA AGNTLVLKPA QVTPLTALKF AELTVKAGFP KGVINIIPGS GGVAGQRLSQ HPDIRKLGFT GSTSVGKQIM KSCAVSNLKK VSLELGGKSP LIIFSDCDLE KAVRMGMGAV FFNKGENCIA AGRLFVEEAI HDEFVTRVVE EIKKMKIGDP LDRSTDHGPQ NHRAHLEKLL QYCETGVQEG ATLVYGGRQV QRPGFFMEPT VFTGVEDHMY LAKEESFGPI MVISKFQNGD IDGVLQRANN TEYGLASGVF TRDINKAMYV SDKLEAGTVF INTYNKTDVA APFGGMKQSG FGKDLGEEAL NEYLKIKTVT LEY // ID AL3B1_MOUSE Reviewed; 468 AA. AC Q80VQ0; Q63ZW3; Q8VHW0; Q9CW05; DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2003, sequence version 1. DT 19-MAR-2014, entry version 93. DE RecName: Full=Aldehyde dehydrogenase family 3 member B1; DE EC=1.2.1.5; DE AltName: Full=Aldehyde dehydrogenase 7; DE Flags: Precursor; GN Name=Aldh3b1; Synonyms=Aldh7; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Olfactory epithelium; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] OF 20-468. RA Vasiliou V., Pappa A., Manzer R.; RL Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 331-468. RC STRAIN=C57BL/6J; TISSUE=Testis; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [4] RP TISSUE SPECIFICITY. RX PubMed=17382292; DOI=10.1016/j.bbrc.2007.03.046; RA Marchitti S.A., Orlicky D.J., Vasiliou V.; RT "Expression and initial characterization of human ALDH3B1."; RL Biochem. Biophys. Res. Commun. 356:792-798(2007). CC -!- FUNCTION: Oxidizes medium and long chain saturated and unsaturated CC aldehydes (By similarity). Metabolizes also benzaldehyde (By CC similarity). Low activity towards acetaldehyde and 3,4- CC dihydroxyphenylacetaldehyde (By similarity). May not metabolize CC short chain aldehydes (By similarity). May use both NADP(+) and CC NAD(+) as cofactors (By similarity). May have a protective role CC against the cytotoxicity induced by lipid peroxidation (By CC similarity). CC -!- CATALYTIC ACTIVITY: An aldehyde + NAD(P)(+) + H(2)O = a CC carboxylate + NAD(P)H. CC -!- PATHWAY: Alcohol metabolism; ethanol degradation; acetate from CC ethanol: step 2/2. CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor (By similarity). CC Note=Primarily in the plasma membrane as well as in some punctate CC structures in the cytoplasm (By similarity). CC -!- TISSUE SPECIFICITY: Highly expressed in kidney and liver. In brain CC is expressed at moderate levels in cortex, striatum and CC hippocampus, and at lower levels in brainstem and cerebellum. CC -!- PTM: Dually lipadated in the C-terminus; prenylation occurs prior, CC and is a prerequisite for palmitoylation, it is also required for CC activity towards long-chain substrates (By similarity). CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BC046597; AAH46597.1; -; mRNA. DR EMBL; BC082792; AAH82792.1; -; mRNA. DR EMBL; AF362571; AAL56246.1; -; mRNA. DR EMBL; AK005615; BAB24152.2; -; mRNA. DR RefSeq; NP_080592.2; NM_026316.2. DR RefSeq; XP_006531893.1; XM_006531830.1. DR UniGene; Mm.109341; -. DR ProteinModelPortal; Q80VQ0; -. DR SMR; Q80VQ0; 6-445. DR IntAct; Q80VQ0; 1. DR MINT; MINT-4120234; -. DR PhosphoSite; Q80VQ0; -. DR PaxDb; Q80VQ0; -. DR PRIDE; Q80VQ0; -. DR Ensembl; ENSMUST00000051803; ENSMUSP00000056276; ENSMUSG00000024885. DR GeneID; 67689; -. DR KEGG; mmu:67689; -. DR UCSC; uc008fxq.1; mouse. DR CTD; 221; -. DR MGI; MGI:1914939; Aldh3b1. DR eggNOG; COG1012; -. DR GeneTree; ENSGT00390000002825; -. DR HOGENOM; HOG000271515; -. DR HOVERGEN; HBG050483; -. DR InParanoid; Q80VQ0; -. DR KO; K00129; -. DR OMA; PGMEKIN; -. DR OrthoDB; EOG73RBB3; -. DR TreeFam; TF314264; -. DR UniPathway; UPA00780; UER00768. DR NextBio; 325269; -. DR PRO; PR:Q80VQ0; -. DR ArrayExpress; Q80VQ0; -. DR Bgee; Q80VQ0; -. DR CleanEx; MM_ALDH3B1; -. DR Genevestigator; Q80VQ0; -. DR GO; GO:0005829; C:cytosol; IDA:MGI. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0004030; F:aldehyde dehydrogenase [NAD(P)+] activity; ISO:MGI. DR GO; GO:0046185; P:aldehyde catabolic process; IEA:Ensembl. DR GO; GO:0034599; P:cellular response to oxidative stress; IEA:Ensembl. DR GO; GO:0006068; P:ethanol catabolic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.309.10; -; 1. DR Gene3D; 3.40.605.10; -; 1. DR InterPro; IPR016161; Ald_DH/histidinol_DH. DR InterPro; IPR016163; Ald_DH_C. DR InterPro; IPR016160; Ald_DH_CS. DR InterPro; IPR016162; Ald_DH_N. DR InterPro; IPR015590; Aldehyde_DH_dom. DR InterPro; IPR012394; Aldehyde_DH_NAD(P). DR PANTHER; PTHR11699:SF15; PTHR11699:SF15; 1. DR Pfam; PF00171; Aldedh; 1. DR PIRSF; PIRSF036492; ALDH; 1. DR SUPFAM; SSF53720; SSF53720; 1. DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1. DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1. PE 2: Evidence at transcript level; KW Acetylation; Cell membrane; Complete proteome; Lipoprotein; Membrane; KW NAD; Oxidoreductase; Palmitate; Prenylation; Reference proteome. FT CHAIN 1 465 Aldehyde dehydrogenase family 3 member FT B1. FT /FTId=PRO_0000056482. FT PROPEP 466 468 Removed in mature form (Probable). FT /FTId=PRO_0000424194. FT NP_BIND 188 193 NAD (By similarity). FT ACT_SITE 210 210 By similarity. FT ACT_SITE 244 244 By similarity. FT MOD_RES 1 1 N-acetylmethionine (By similarity). FT LIPID 463 463 S-palmitoyl cysteine (By similarity). FT LIPID 465 465 S-farnesyl cysteine (By similarity). SQ SEQUENCE 468 AA; 52292 MW; 715B01070A3F7E23 CRC64; MDSFEDKLQQ LREAFKEGRT RSAEFRAAQL QGLSHFLRDN KQQLQEALAQ DLHKSAFEAE VSEIAISQAE VDLALRNLRS WMKDEKVSKN LATQLDSAFI RKEPFGLVLI IVPWNYPINL TLVPLVGAIA AGNCVVLKPS EISKATEKIL AEVLPRYLDQ SCFTVVLGGR QETGQLLEHK FDYIFFTGNA YVGKIVMAAA AKHLTPITLE LGGKNPCYVD DNCDPQIVAN RVAWFRYFNA GQTCVAPDYI LCSQEMQERL VPALQNAITR FYGDNPQTSP NLGRIINQKH FKRLQGLLGC GRVAIGGQSD EGERYIAPTV LVDVQETEPV MQEEIFGPIL PLVTVRSLDE AIEFMNRREK PLALYAFSKR SQVIKQVLAR TSSGGFCGND GFMHMTLSSL PFGGVGTSGM GRYHGKFSFD TFSNQRACLL RSPGMEKIND LRYPPYSSRN LRVLLVAMEE RCCSCTLL // ID AL3A1_MOUSE Reviewed; 453 AA. AC P47739; B1ATI7; Q9R203; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 03-OCT-2012, sequence version 2. DT 19-MAR-2014, entry version 117. DE RecName: Full=Aldehyde dehydrogenase, dimeric NADP-preferring; DE EC=1.2.1.5; DE AltName: Full=Aldehyde dehydrogenase 4; DE AltName: Full=Aldehyde dehydrogenase family 3 member A1; DE AltName: Full=Dioxin-inducible aldehyde dehydrogenase 3; GN Name=Aldh3a1; Synonyms=Ahd-4, Ahd4, Aldh3, Aldh4; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=C3H; RX PubMed=8148869; RA Vasiliou V., Reuter S.F., Kozak C.A., Nebert D.W.; RT "Mouse dioxin-inducible cytosolic aldehyde dehydrogenase-3: AHD4 cDNA RT sequence, genetic mapping, and differences in mRNA levels."; RL Pharmacogenetics 3:281-290(1993). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Vasiliou V., Reuter S.F., Nebert D.W.; RT "Organization and characterization of the murine cytosolic TCDD- RT inducible aldehyde dehydrogenase gene (ahd4)."; RL Toxicologist 14:410-410(1994). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND VARIANTS RP ALD3A1C ASN-154; ARG-305 AND VAL-352. RC STRAIN=DBA/2, and SWR/J; RX PubMed=10376761; RA Shiao T., Tran P., Siegel D., Lee J., Vasiliou V.; RT "Four amino acid changes are associated with the Aldh3a1 locus RT polymorphism in mice which may be responsible for corneal sensitivity RT to ultraviolet light."; RL Pharmacogenetics 9:145-153(1999). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [5] RP FUNCTION. RC STRAIN=CD-1; RX PubMed=11784860; DOI=10.1128/MCB.22.3.849-855.2002; RA Nees D.W., Wawrousek E.F., Robison W.G. Jr., Piatigorsky J.; RT "Structurally normal corneas in aldehyde dehydrogenase 3a1-deficient RT mice."; RL Mol. Cell. Biol. 22:849-855(2002). CC -!- FUNCTION: ALDHs play a major role in the detoxification of CC alcohol-derived acetaldehyde. They are involved in the metabolism CC of corticosteroids, biogenic amines, neurotransmitters, and lipid CC peroxidation. This protein preferentially oxidizes aromatic CC aldehyde substrates. It may play a role in the oxidation of toxic CC aldehydes and in preventing corneal damage caused by ultraviolet CC light. CC -!- CATALYTIC ACTIVITY: An aldehyde + NAD(P)(+) + H(2)O = a CC carboxylate + NAD(P)H. CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- TISSUE SPECIFICITY: Constitutively expressed in cornea, stomach, CC skin, bladder and lungs. Lowest expression levels in lungs and CC bladder. CC -!- POLYMORPHISM: There are two alleles, Ald3a1a and Ald3a1c. Ald3a1c CC codes for a low activity enzyme and is associated with extensive CC corneal clouding after exposure to ultraviolet light. Ald3a1a CC encodes the high activity enzyme. CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U12785; AAA20670.1; -; mRNA. DR EMBL; AF072815; AAD15964.1; -; mRNA. DR EMBL; AL646093; CAI25900.1; -; Genomic_DNA. DR RefSeq; NP_001106196.1; NM_001112725.1. DR RefSeq; NP_031462.2; NM_007436.2. DR RefSeq; XP_006532089.1; XM_006532026.1. DR RefSeq; XP_006532090.1; XM_006532027.1. DR UniGene; Mm.4257; -. DR ProteinModelPortal; P47739; -. DR SMR; P47739; 3-448. DR IntAct; P47739; 1. DR MINT; MINT-4087533; -. DR PhosphoSite; P47739; -. DR PaxDb; P47739; -. DR PRIDE; P47739; -. DR Ensembl; ENSMUST00000019246; ENSMUSP00000019246; ENSMUSG00000019102. DR Ensembl; ENSMUST00000108716; ENSMUSP00000104356; ENSMUSG00000019102. DR GeneID; 11670; -. DR KEGG; mmu:11670; -. DR UCSC; uc007jhd.2; mouse. DR CTD; 218; -. DR MGI; MGI:1353451; Aldh3a1. DR eggNOG; COG1012; -. DR GeneTree; ENSGT00390000002825; -. DR HOVERGEN; HBG050483; -. DR InParanoid; P47739; -. DR KO; K00129; -. DR OMA; HHFQRVM; -. DR TreeFam; TF314264; -. DR NextBio; 279295; -. DR PRO; PR:P47739; -. DR ArrayExpress; P47739; -. DR CleanEx; MM_ALDH3A1; -. DR Genevestigator; P47739; -. DR GO; GO:0005829; C:cytosol; ISS:UniProtKB. DR GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl. DR GO; GO:0004028; F:3-chloroallyl aldehyde dehydrogenase activity; IDA:MGI. DR GO; GO:0008106; F:alcohol dehydrogenase (NADP+) activity; ISS:UniProtKB. DR GO; GO:0004029; F:aldehyde dehydrogenase (NAD) activity; ISS:UniProtKB. DR GO; GO:0004030; F:aldehyde dehydrogenase [NAD(P)+] activity; IEA:UniProtKB-EC. DR GO; GO:0007568; P:aging; IEA:Ensembl. DR GO; GO:0006081; P:cellular aldehyde metabolic process; ISS:UniProtKB. DR GO; GO:0008284; P:positive regulation of cell proliferation; IEA:Ensembl. DR GO; GO:0051591; P:response to cAMP; IEA:Ensembl. DR GO; GO:0042493; P:response to drug; IEA:Ensembl. DR GO; GO:0051384; P:response to glucocorticoid; IEA:Ensembl. DR GO; GO:0001666; P:response to hypoxia; IEA:Ensembl. DR GO; GO:0007584; P:response to nutrient; IEA:Ensembl. DR Gene3D; 3.40.309.10; -; 1. DR Gene3D; 3.40.605.10; -; 1. DR InterPro; IPR016161; Ald_DH/histidinol_DH. DR InterPro; IPR016163; Ald_DH_C. DR InterPro; IPR016160; Ald_DH_CS. DR InterPro; IPR016162; Ald_DH_N. DR InterPro; IPR015590; Aldehyde_DH_dom. DR InterPro; IPR012394; Aldehyde_DH_NAD(P). DR PANTHER; PTHR11699:SF15; PTHR11699:SF15; 1. DR Pfam; PF00171; Aldedh; 1. DR PIRSF; PIRSF036492; ALDH; 1. DR SUPFAM; SSF53720; SSF53720; 1. DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1. DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1. PE 2: Evidence at transcript level; KW Acetylation; Complete proteome; Cytoplasm; NAD; NADP; Oxidoreductase; KW Polymorphism; Reference proteome. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 453 Aldehyde dehydrogenase, dimeric NADP- FT preferring. FT /FTId=PRO_0000056471. FT NP_BIND 188 193 NAD or NADP (By similarity). FT ACT_SITE 210 210 By similarity. FT ACT_SITE 244 244 By similarity. FT MOD_RES 2 2 N-acetylserine (By similarity). FT MOD_RES 178 178 N6-acetyllysine (By similarity). FT MOD_RES 194 194 N6-acetyllysine (By similarity). FT VARIANT 154 154 I -> N (in allele Ald3a1c). FT VARIANT 305 305 H -> R (in allele Ald3a1c). FT VARIANT 352 352 I -> V (in allele Ald3a1c). FT CONFLICT 88 88 A -> G (in Ref. 1; AAA20670). FT CONFLICT 88 88 A -> R (in Ref. 3; AAD15964). SQ SEQUENCE 453 AA; 50481 MW; 7B4EA1CC56B5FAA1 CRC64; MSNISSIVNR ARDAFNSGKT RPLQFRVEQL EALQRMINEN LKGISKALAS NLRKNEWTSY YEEVAHVLDE IDFTIKGLSD WAEDEPVAKT RQTQEDDLYI HSEPLGVVLV IGAWNYPFNL TIQPMVGAIA AGNAVVLKPS EVSDHMADLL STLIPQYMDK DLYPVIKGGV PETTELLKEK FDHIMYTGST AVGKIVMAAA AKHLTPVTLE LGGKSPCYVD KDCDLDVACR RIAWGKFMNS GQTCVAPDYI LCDPSIQNEI VEKLKKSLKD FYGEDAKQSH DYGRIINDRH FQRVINLIDS KKVAHGGTWD QPSRYIAPTI LVDVDPQSPV MQEEIFGPVM PIVCVRSLDE AIKFINQREK PLALYVFSNN DKVIKKMIAE TSSGGVTAND VIVHITVPTL PFGGVGNSGM GAYHGKKSFE TFSHRRSCLV RSLRNEEANK ARYPPSPAKM PRH // ID AL4A1_MOUSE Reviewed; 562 AA. AC Q8CHT0; B1AXW8; Q7TND0; Q8BXM3; Q8R0N1; Q8R1S2; DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 3. DT 19-MAR-2014, entry version 105. DE RecName: Full=Delta-1-pyrroline-5-carboxylate dehydrogenase, mitochondrial; DE Short=P5C dehydrogenase; DE EC=1.2.1.88; DE AltName: Full=Aldehyde dehydrogenase family 4 member A1; DE AltName: Full=L-glutamate gamma-semialdehyde dehydrogenase; DE Flags: Precursor; GN Name=Aldh4a1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Retina; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Kidney, and Liver; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-30; LYS-92; LYS-98; RP LYS-113; LYS-129; LYS-174; LYS-346; LYS-357; LYS-394 AND LYS-508, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., RA Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). RN [6] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-51; LYS-92; LYS-98; LYS-113; RP LYS-129; LYS-174; LYS-317; LYS-357; LYS-364; LYS-375; LYS-461; RP LYS-508; LYS-530 AND LYS-551, AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23576753; DOI=10.1073/pnas.1302961110; RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., RA Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.; RT "Label-free quantitative proteomics of the lysine acetylome in RT mitochondria identifies substrates of SIRT3 in metabolic pathways."; RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013). RN [7] RP X-RAY CRYSTALLOGRAPHY (1.24 ANGSTROMS) OF 21-562. RX PubMed=22868767; DOI=10.1107/S0907444912019580; RA Pemberton T.A., Still B.R., Christensen E.M., Singh H., Srivastava D., RA Tanner J.J.; RT "Proline: Mother Nature's cryoprotectant applied to protein RT crystallography."; RL Acta Crystallogr. D 68:1010-1018(2012). RN [8] RP X-RAY CRYSTALLOGRAPHY (1.30 ANGSTROMS) OF 21-562 IN COMPLEXES WITH RP GLUTAMATE AND NAD, SUBUNIT, AND ACTIVE SITE. RX PubMed=22516612; DOI=10.1016/j.jmb.2012.04.010; RA Srivastava D., Singh R.K., Moxley M.A., Henzl M.T., Becker D.F., RA Tanner J.J.; RT "The three-dimensional structural basis of type II hyperprolinemia."; RL J. Mol. Biol. 420:176-189(2012). CC -!- FUNCTION: Irreversible conversion of delta-1-pyrroline-5- CC carboxylate (P5C), derived either from proline or ornithine, to CC glutamate. This is a necessary step in the pathway interconnecting CC the urea and tricarboxylic acid cycles. The preferred substrate is CC glutamic gamma-semialdehyde, other substrates include succinic, CC glutaric and adipic semialdehydes (By similarity). CC -!- CATALYTIC ACTIVITY: L-glutamate 5-semialdehyde + NAD(+) + H(2)O = CC L-glutamate + NADH. CC -!- PATHWAY: Amino-acid degradation; L-proline degradation into L- CC glutamate; L-glutamate from L-proline: step 2/2. CC -!- SUBUNIT: Homodimer. CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix (By similarity). CC -!- PTM: Acetylation of Lys-98, Lys-113 and Lys-401 is observed in CC liver mitochondria from fasted mice but not from fed mice. CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK044712; BAC32045.1; -; mRNA. DR EMBL; AL831790; CAM21310.1; -; Genomic_DNA. DR EMBL; CH466615; EDL13315.1; -; Genomic_DNA. DR EMBL; BC024133; AAH24133.1; -; mRNA. DR EMBL; BC026589; AAH26589.1; -; mRNA. DR EMBL; BC039281; AAH39281.2; -; mRNA. DR EMBL; BC056226; AAH56226.1; -; mRNA. DR RefSeq; NP_780647.3; NM_175438.4. DR UniGene; Mm.273571; -. DR PDB; 3V9J; X-ray; 1.30 A; A/B=21-562. DR PDB; 3V9K; X-ray; 1.50 A; A/B=21-562. DR PDB; 3V9L; X-ray; 1.50 A; A/B=21-562. DR PDB; 4E3X; X-ray; 1.24 A; A/B=21-562. DR PDB; 4LGZ; X-ray; 1.68 A; A/B=21-562. DR PDB; 4LH0; X-ray; 1.67 A; A/B=21-562. DR PDB; 4LH1; X-ray; 1.67 A; A/B=21-562. DR PDB; 4LH2; X-ray; 1.67 A; A/B=21-562. DR PDB; 4LH3; X-ray; 1.81 A; A/B=21-562. DR PDBsum; 3V9J; -. DR PDBsum; 3V9K; -. DR PDBsum; 3V9L; -. DR PDBsum; 4E3X; -. DR PDBsum; 4LGZ; -. DR PDBsum; 4LH0; -. DR PDBsum; 4LH1; -. DR PDBsum; 4LH2; -. DR PDBsum; 4LH3; -. DR ProteinModelPortal; Q8CHT0; -. DR SMR; Q8CHT0; 21-562. DR IntAct; Q8CHT0; 3. DR MINT; MINT-1859863; -. DR PhosphoSite; Q8CHT0; -. DR PaxDb; Q8CHT0; -. DR PRIDE; Q8CHT0; -. DR Ensembl; ENSMUST00000039818; ENSMUSP00000043821; ENSMUSG00000028737. DR GeneID; 212647; -. DR KEGG; mmu:212647; -. DR UCSC; uc012dnu.1; mouse. DR CTD; 8659; -. DR MGI; MGI:2443883; Aldh4a1. DR eggNOG; COG1012; -. DR GeneTree; ENSGT00560000077335; -. DR HOGENOM; HOG000271511; -. DR HOVERGEN; HBG050484; -. DR InParanoid; B1AXW8; -. DR KO; K00294; -. DR OMA; LRWKHTS; -. DR OrthoDB; EOG7T1R9D; -. DR TreeFam; TF300481; -. DR UniPathway; UPA00261; UER00374. DR ChiTaRS; ALDH4A1; mouse. DR NextBio; 373656; -. DR PRO; PR:Q8CHT0; -. DR ArrayExpress; Q8CHT0; -. DR Bgee; Q8CHT0; -. DR CleanEx; MM_ALDH4A1; -. DR Genevestigator; Q8CHT0; -. DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR GO; GO:0003842; F:1-pyrroline-5-carboxylate dehydrogenase activity; IEA:Ensembl. DR GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IEA:InterPro. DR GO; GO:0006561; P:proline biosynthetic process; IEA:InterPro. DR GO; GO:0010133; P:proline catabolic process to glutamate; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.309.10; -; 1. DR Gene3D; 3.40.605.10; -; 1. DR InterPro; IPR005931; 1-pyrroline-5-COlate_DH. DR InterPro; IPR016161; Ald_DH/histidinol_DH. DR InterPro; IPR016163; Ald_DH_C. DR InterPro; IPR016160; Ald_DH_CS. DR InterPro; IPR016162; Ald_DH_N. DR InterPro; IPR015590; Aldehyde_DH_dom. DR Pfam; PF00171; Aldedh; 1. DR SUPFAM; SSF53720; SSF53720; 1. DR TIGRFAMs; TIGR01236; D1pyr5carbox1; 1. DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1. DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Complete proteome; Mitochondrion; NAD; KW Oxidoreductase; Proline metabolism; Reference proteome; KW Transit peptide. FT TRANSIT 1 23 Mitochondrion (By similarity). FT CHAIN 24 562 Delta-1-pyrroline-5-carboxylate FT dehydrogenase, mitochondrial. FT /FTId=PRO_0000007174. FT NP_BIND 285 289 NAD. FT ACT_SITE 313 313 Proton acceptor. FT ACT_SITE 347 347 Nucleophile. FT BINDING 207 207 NAD. FT BINDING 232 232 NAD. FT BINDING 446 446 NAD. FT BINDING 512 512 Substrate. FT SITE 210 210 Transition state stabilizer (By FT similarity). FT MOD_RES 30 30 N6-succinyllysine. FT MOD_RES 51 51 N6-acetyllysine. FT MOD_RES 92 92 N6-acetyllysine; alternate. FT MOD_RES 92 92 N6-succinyllysine; alternate. FT MOD_RES 98 98 N6-acetyllysine; alternate. FT MOD_RES 98 98 N6-succinyllysine; alternate. FT MOD_RES 113 113 N6-acetyllysine; alternate. FT MOD_RES 113 113 N6-succinyllysine; alternate. FT MOD_RES 129 129 N6-acetyllysine; alternate. FT MOD_RES 129 129 N6-succinyllysine; alternate. FT MOD_RES 174 174 N6-acetyllysine; alternate. FT MOD_RES 174 174 N6-succinyllysine; alternate. FT MOD_RES 317 317 N6-acetyllysine. FT MOD_RES 346 346 N6-succinyllysine. FT MOD_RES 357 357 N6-acetyllysine; alternate. FT MOD_RES 357 357 N6-succinyllysine; alternate. FT MOD_RES 364 364 N6-acetyllysine. FT MOD_RES 375 375 N6-acetyllysine. FT MOD_RES 394 394 N6-succinyllysine. FT MOD_RES 461 461 N6-acetyllysine. FT MOD_RES 508 508 N6-acetyllysine; alternate. FT MOD_RES 508 508 N6-succinyllysine; alternate. FT MOD_RES 530 530 N6-acetyllysine. FT MOD_RES 551 551 N6-acetyllysine. FT CONFLICT 18 18 G -> S (in Ref. 1; BAC32045 and 4; FT AAH56226/AAH39281/AAH24133). FT CONFLICT 32 32 T -> A (in Ref. 1; BAC32045 and 4; FT AAH56226/AAH39281/AAH24133). FT CONFLICT 47 47 D -> G (in Ref. 1; BAC32045). FT CONFLICT 60 60 M -> T (in Ref. 1; BAC32045 and 4; FT AAH56226/AAH39281/AAH24133). FT CONFLICT 467 467 Q -> K (in Ref. 1; BAC32045 and 4; FT AAH56226/AAH39281/AAH24133/AAH26589). FT HELIX 44 54 FT TURN 55 58 FT STRAND 65 67 FT STRAND 70 72 FT STRAND 77 82 FT STRAND 85 94 FT HELIX 98 117 FT HELIX 120 135 FT TURN 136 138 FT HELIX 139 150 FT HELIX 154 160 FT HELIX 163 179 FT STRAND 190 195 FT STRAND 200 206 FT HELIX 212 224 FT STRAND 229 232 FT HELIX 235 237 FT HELIX 238 250 FT STRAND 257 260 FT HELIX 265 272 FT STRAND 278 285 FT HELIX 287 299 FT TURN 300 303 FT STRAND 309 313 FT STRAND 318 322 FT HELIX 328 340 FT HELIX 341 344 FT STRAND 350 356 FT HELIX 357 359 FT HELIX 360 372 FT TURN 379 381 FT HELIX 393 408 FT STRAND 412 416 FT STRAND 423 425 FT STRAND 431 436 FT HELIX 441 443 FT STRAND 449 457 FT HELIX 459 461 FT HELIX 462 471 FT STRAND 472 482 FT HELIX 486 495 FT TURN 496 499 FT STRAND 501 507 FT TURN 514 516 FT HELIX 536 540 FT STRAND 544 549 FT HELIX 559 561 SQ SEQUENCE 562 AA; 61841 MW; 4D8A0C9C68A99478 CRC64; MLPLPSLRRS LLSHAWRGAG LRWKHTSSLK VTNEPILAFS QGSPERDALQ KALKDLKGQM EAIPCVVGDE EVWTSDIQYQ LSPFNHAHKV AKFCYADKAL LNRAIDAALA ARKEWDLKPM ADRAQVFLKA ADMLSGPRRA EVLAKTMVGQ GKTVIQAEID AAAELIDFFR FNAKFAVELE GEQPISVPPS TNHTVYRGLE GFVAAISPFN FTAIGGNLAG APALMGNVVL WKPSDTAMLA SYAVYRILRE AGLPPNIIQF VPADGPTFGD TVTSSEHLCG INFTGSVPTF KHLWRQVAQN LDRFRTFPRL AGECGGKNFH FVHSSADVDS VVSGTLRSAF EYGGQKCSAC SRLYVPKSLW PQIKGRLLEE HSRIKVGDPA EDFGTFFSAV IDAKAFARIK KWLEHARSSP SLSILAGGQC NESVGYYVEP CIIESKDPQE PIMKEEIFGP VLTVYVYPDD KYRETLQLVD STTSYGLTGA VFAQDKAIVQ EATRMLRNAA GNFYINDKST GSVVGQQPFG GARASGTNDK PGGPHYILRW TSPQVIKETH KPLGDWRYSY MQ // ID AL8A1_MOUSE Reviewed; 487 AA. AC Q8BH00; Q91WS6; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 19-MAR-2014, entry version 89. DE RecName: Full=Aldehyde dehydrogenase family 8 member A1; DE EC=1.2.1.-; DE AltName: Full=Retinal dehydrogenase 4; GN Name=Aldh8a1; Synonyms=Raldh4; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RC TISSUE=Embryo; RX PubMed=12519776; DOI=10.1074/jbc.M211417200; RA Lin M., Zhang M., Abraham M., Smith S.M., Napoli J.L.; RT "Mouse retinal dehydrogenase 4 (RALDH4), molecular cloning, cellular RT expression, and activity in 9-cis-retinoic acid biosynthesis in intact RT cells."; RL J. Biol. Chem. 278:9856-9861(2003). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Liver tumor, and Spleen; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLY-145. RC STRAIN=FVB/N; TISSUE=Kidney; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: Converts 9-cis-retinal to 9-cis-retinoic acid. Has lower CC activity towards 13-cis-retinal. Has much lower activity towards CC all-trans-retinal. Has a preference for NAD, but shows CC considerable activity with NADP (in vitro) (By similarity). CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=2.3 uM for 9-cis-retinal; CC Vmax=3.4 nmol/min/mg enzyme; CC Note=Activity was measured with total soluble protein; CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- TISSUE SPECIFICITY: Detected in hepatocytes and in proximal and CC distal convoluted tubules in kidney cortex (at protein level). CC Highly expressed in adult liver and in kidney cortex. First CC detected in embryonic liver after 15 days of development. CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF510322; AAO64246.1; -; mRNA. DR EMBL; AK050298; BAC34173.1; -; mRNA. DR EMBL; AK143752; BAE25524.1; -; mRNA. DR EMBL; BC013511; AAH13511.1; -; mRNA. DR EMBL; BC038493; AAH38493.1; -; mRNA. DR RefSeq; NP_848828.1; NM_178713.4. DR UniGene; Mm.90181; -. DR ProteinModelPortal; Q8BH00; -. DR SMR; Q8BH00; 10-487. DR IntAct; Q8BH00; 4. DR MINT; MINT-4110439; -. DR STRING; 10090.ENSMUSP00000038878; -. DR PhosphoSite; Q8BH00; -. DR PaxDb; Q8BH00; -. DR PRIDE; Q8BH00; -. DR Ensembl; ENSMUST00000042699; ENSMUSP00000038878; ENSMUSG00000037542. DR GeneID; 237320; -. DR KEGG; mmu:237320; -. DR UCSC; uc007eoq.1; mouse. DR CTD; 64577; -. DR MGI; MGI:2653900; Aldh8a1. DR eggNOG; COG1012; -. DR GeneTree; ENSGT00720000108597; -. DR HOGENOM; HOG000271505; -. DR HOVERGEN; HBG000097; -. DR InParanoid; Q8BH00; -. DR OMA; CMTEEIF; -. DR OrthoDB; EOG7FV3Q2; -. DR TreeFam; TF314129; -. DR NextBio; 383298; -. DR PRO; PR:Q8BH00; -. DR ArrayExpress; Q8BH00; -. DR Bgee; Q8BH00; -. DR CleanEx; MM_ALDH8A1; -. DR Genevestigator; Q8BH00; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005622; C:intracellular; ISS:UniProtKB. DR GO; GO:0001758; F:retinal dehydrogenase activity; ISS:UniProtKB. DR GO; GO:0042904; P:9-cis-retinoic acid biosynthetic process; IDA:MGI. DR GO; GO:0042574; P:retinal metabolic process; ISS:UniProtKB. DR Gene3D; 3.40.309.10; -; 1. DR Gene3D; 3.40.605.10; -; 1. DR InterPro; IPR016161; Ald_DH/histidinol_DH. DR InterPro; IPR016163; Ald_DH_C. DR InterPro; IPR016160; Ald_DH_CS. DR InterPro; IPR016162; Ald_DH_N. DR InterPro; IPR015590; Aldehyde_DH_dom. DR Pfam; PF00171; Aldedh; 1. DR SUPFAM; SSF53720; SSF53720; 1. DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1. DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1. PE 1: Evidence at protein level; KW Complete proteome; Cytoplasm; NAD; Oxidoreductase; Reference proteome. FT CHAIN 1 487 Aldehyde dehydrogenase family 8 member FT A1. FT /FTId=PRO_0000312955. FT NP_BIND 231 236 NAD (By similarity). FT ACT_SITE 253 253 Proton acceptor (By similarity). FT ACT_SITE 287 287 Nucleophile (By similarity). FT SITE 155 155 Transition state stabilizer (By FT similarity). FT VARIANT 145 145 V -> G (in strain: FVB/N). SQ SEQUENCE 487 AA; 53664 MW; 5E205A495BD61ED7 CRC64; MAGKRELLML ENFIGGKFLP CNSYIDSYDP STGEVYCKVP NSGKEEIEAA VEAAREAFPA WSSRSPQERS LVLNRLADVL EQSLEELAQA ESKDQGKTLT LARTMDIPRS VLNFRFFASS NLHHVSECTQ MSHLGCMHYT VRTPVGIAGL ISPWNLPLYL LTWKIAPAIA AGNTVIAKPS EMTSVTAWMF CKLLDKAGVP PGVINIVFGT GPRVGEALVS HPEVPLISFT GSQPTAERIT QLSAPHCKKL SLELGGKNPA IIFEDANLEE CIPATVRSSF ANQGEICLCT SRIFVQRSIY SEFLKRFVEA TRKWKVGVPS DPSANMGALI SKAHLEKVRS YVLKAQTEGA RILCGEGVDQ LSLPLRNQAG YFMLPTVITD IKDESRCMTE EIFGPVTCVV PFDSEEEVIT RANSVRYGLA ATVWSKDVGR IHRVAKKLQS GLVWTNCWLI RELNLPFGGM KSSGIGREGA KDSYDFFTEI KTITIKY // ID AL9A1_MOUSE Reviewed; 494 AA. AC Q9JLJ2; DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 19-MAR-2014, entry version 104. DE RecName: Full=4-trimethylaminobutyraldehyde dehydrogenase; DE Short=TMABADH; DE EC=1.2.1.47; DE AltName: Full=Aldehyde dehydrogenase family 9 member A1; DE EC=1.2.1.3; GN Name=Aldh9a1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Liver; RX PubMed=10702312; DOI=10.1074/jbc.275.10.7390; RA Vaz F.M., Fouchier S.W., Ofman R., Sommer M., Wanders R.J.A.; RT "Molecular and biochemical characterization of rat gamma- RT trimethylaminobutyraldehyde dehydrogenase and evidence for the RT involvement of human aldehyde dehydrogenase 9 in carnitine RT biosynthesis."; RL J. Biol. Chem. 275:7390-7394(2000). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Mammary tumor; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP PROTEIN SEQUENCE OF 39-59; 74-82; 88-101; 228-239; 247-274; 317-338; RP 348-366; 412-426 AND 472-494, AND MASS SPECTROMETRY. RC STRAIN=OF1; TISSUE=Hippocampus; RA Lubec G., Sunyer B., Chen W.-Q.; RL Submitted (JAN-2009) to UniProtKB. RN [4] RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-30; LYS-59 AND LYS-303, RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., RA Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). RN [5] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-30; LYS-298; LYS-303 AND RP LYS-344, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Liver; RX PubMed=23576753; DOI=10.1073/pnas.1302961110; RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., RA Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.; RT "Label-free quantitative proteomics of the lysine acetylome in RT mitochondria identifies substrates of SIRT3 in metabolic pathways."; RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013). CC -!- FUNCTION: Converts gamma-trimethylaminobutyraldehyde into gamma- CC butyrobetaine (By similarity). CC -!- CATALYTIC ACTIVITY: 4-trimethylammoniobutanal + NAD(+) + H(2)O = CC 4-trimethylammoniobutanoate + NADH. CC -!- CATALYTIC ACTIVITY: An aldehyde + NAD(+) + H(2)O = a carboxylate + CC NADH. CC -!- PATHWAY: Amine and polyamine biosynthesis; carnitine biosynthesis. CC -!- SUBUNIT: Homotetramer (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF170919; AAF43599.1; -; mRNA. DR EMBL; BC003297; AAH03297.1; -; mRNA. DR RefSeq; NP_064377.2; NM_019993.3. DR UniGene; Mm.330055; -. DR ProteinModelPortal; Q9JLJ2; -. DR SMR; Q9JLJ2; 2-494. DR IntAct; Q9JLJ2; 3. DR MINT; MINT-4087568; -. DR PhosphoSite; Q9JLJ2; -. DR REPRODUCTION-2DPAGE; Q9JLJ2; -. DR PaxDb; Q9JLJ2; -. DR PRIDE; Q9JLJ2; -. DR GeneID; 56752; -. DR KEGG; mmu:56752; -. DR CTD; 223; -. DR MGI; MGI:1861622; Aldh9a1. DR eggNOG; COG1012; -. DR HOVERGEN; HBG000097; -. DR InParanoid; Q9JLJ2; -. DR KO; K00149; -. DR UniPathway; UPA00118; -. DR NextBio; 313278; -. DR PRO; PR:Q9JLJ2; -. DR ArrayExpress; Q9JLJ2; -. DR Bgee; Q9JLJ2; -. DR CleanEx; MM_ALDH9A1; -. DR Genevestigator; Q9JLJ2; -. DR GO; GO:0005829; C:cytosol; IDA:MGI. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl. DR GO; GO:0047105; F:4-trimethylammoniobutyraldehyde dehydrogenase activity; IEA:UniProtKB-EC. DR GO; GO:0043176; F:amine binding; IEA:Ensembl. DR GO; GO:0019145; F:aminobutyraldehyde dehydrogenase activity; IEA:Ensembl. DR GO; GO:0051287; F:NAD binding; IEA:Ensembl. DR GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IDA:MGI. DR GO; GO:0045329; P:carnitine biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0009437; P:carnitine metabolic process; IDA:MGI. DR GO; GO:0006081; P:cellular aldehyde metabolic process; IEA:Ensembl. DR GO; GO:0001822; P:kidney development; IEA:Ensembl. DR GO; GO:0001889; P:liver development; IEA:Ensembl. DR GO; GO:0042136; P:neurotransmitter biosynthetic process; IEA:Ensembl. DR Gene3D; 3.40.309.10; -; 1. DR Gene3D; 3.40.605.10; -; 1. DR InterPro; IPR016161; Ald_DH/histidinol_DH. DR InterPro; IPR016163; Ald_DH_C. DR InterPro; IPR016160; Ald_DH_CS. DR InterPro; IPR016162; Ald_DH_N. DR InterPro; IPR015590; Aldehyde_DH_dom. DR Pfam; PF00171; Aldedh; 1. DR SUPFAM; SSF53720; SSF53720; 1. DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1. DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1. PE 1: Evidence at protein level; KW Acetylation; Complete proteome; Cytoplasm; Direct protein sequencing; KW NAD; Oxidoreductase; Reference proteome. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 494 4-trimethylaminobutyraldehyde FT dehydrogenase. FT /FTId=PRO_0000056486. FT NP_BIND 232 237 NAD (By similarity). FT ACT_SITE 254 254 Potential. FT ACT_SITE 288 288 Potential. FT MOD_RES 2 2 N-acetylserine (By similarity). FT MOD_RES 30 30 N6-acetyllysine; alternate. FT MOD_RES 30 30 N6-succinyllysine; alternate. FT MOD_RES 59 59 N6-succinyllysine. FT MOD_RES 298 298 N6-acetyllysine. FT MOD_RES 303 303 N6-acetyllysine; alternate. FT MOD_RES 303 303 N6-succinyllysine; alternate. FT MOD_RES 344 344 N6-acetyllysine. SQ SEQUENCE 494 AA; 53515 MW; CBB27755330E0A23 CRC64; MSTGTFVVSQ PLNYRGGARV EPVDASGTEK AFEPATGRVI ATFACSGEKE VNLAVENAKA AFKLWSKKSG LERCQVLLEA ARIIKERKDE IATVETINNG KSIFEARLDV DTCWQCLEYY AGLAASMAGE HIQLPGGSFG YTRREPLGVC VGIGAWNYPF QIACWKSAPA LACGNAMIFK PSPFTPVSAL LLAEIYTKAG APPGLFNVVQ GGAATGQFLC HHREVAKISF TGSVPTGVKI MEMSAKGVKP ITLELGGKSP LIIFSDCNME NAVKGALMAN FLTQGQVCCN GTRVFVQKEI ADKFINEVVK QTQKIKLGDP LLEDTRMGPL INAPHLERVL GFVKLAKEQG ATVLCGGEVY VPEDPKLKHG YYMTPCILTN CRDDMTCVKE EIFGPVMSIL TFGTEAEVLE RANDTTFGLA AGVFTRDIQR AHRVAAELQA GTCYINNYNV SPVELPFGGY KKSGFGRENG RVTIEYYSQL KTVCVEMGDV ESAF // ID AL7A1_MOUSE Reviewed; 539 AA. AC Q9DBF1; Q3TFC7; Q3TVH7; Q3UKT6; DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot. DT 20-APR-2010, sequence version 4. DT 19-MAR-2014, entry version 112. DE RecName: Full=Alpha-aminoadipic semialdehyde dehydrogenase; DE Short=Alpha-AASA dehydrogenase; DE EC=1.2.1.31; DE AltName: Full=Aldehyde dehydrogenase family 7 member A1; DE EC=1.2.1.3; DE AltName: Full=Antiquitin-1; DE AltName: Full=Betaine aldehyde dehydrogenase; DE EC=1.2.1.8; DE AltName: Full=Delta1-piperideine-6-carboxylate dehydrogenase; DE Short=P6c dehydrogenase; DE Flags: Precursor; GN Name=Aldh7a1; Synonyms=Ald7a1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC STRAIN=C57BL/6J; TISSUE=Liver; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Salivary gland; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION. RX PubMed=20207735; DOI=10.1074/jbc.M109.077925; RA Brocker C., Lassen N., Estey T., Pappa A., Cantore M., Orlova V.V., RA Chavakis T., Kavanagh K.L., Oppermann U., Vasiliou V.; RT "Aldehyde dehydrogenase 7A1 (ALDH7A1) is a novel enzyme involved in RT cellular defense against hyperosmotic stress."; RL J. Biol. Chem. 285:18452-18463(2010). RN [4] RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-86; LYS-94; LYS-97 AND RP LYS-537, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Liver; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., RA Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). RN [5] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-86; LYS-94; LYS-97; LYS-462 RP AND LYS-500, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Liver; RX PubMed=23576753; DOI=10.1073/pnas.1302961110; RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., RA Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.; RT "Label-free quantitative proteomics of the lysine acetylome in RT mitochondria identifies substrates of SIRT3 in metabolic pathways."; RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013). CC -!- FUNCTION: Multifunctional enzyme mediating important protective CC effects. Metabolizes betaine aldehyde to betaine, an important CC cellular osmolyte and methyl donor. Protects cells from oxidative CC stress by metabolizing a number of lipid peroxidation-derived CC aldehydes. Involved in lysine catabolism (By similarity). CC -!- CATALYTIC ACTIVITY: (S)-2-amino-6-oxohexanoate + NAD(P)(+) + H(2)O CC = L-2-aminoadipate + NAD(P)H. CC -!- CATALYTIC ACTIVITY: Betaine aldehyde + NAD(+) + H(2)O = betaine + CC NADH. CC -!- CATALYTIC ACTIVITY: An aldehyde + NAD(+) + H(2)O = a carboxylate + CC NADH. CC -!- PATHWAY: Amine and polyamine biosynthesis; betaine biosynthesis CC via choline pathway; betaine from betaine aldehyde: step 1/1. CC -!- SUBUNIT: Homotetramer (By similarity). CC -!- SUBCELLULAR LOCATION: Mitochondrion. Nucleus. Cytoplasm, cytosol. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9DBF1-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9DBF1-2; Sequence=VSP_038989; CC -!- TISSUE SPECIFICITY: Present in liver, kidney, brain and pancreas, CC and at lower levels in jejunum, duodenum, stomach and testes (at CC protein level). CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family. CC -!- SEQUENCE CAUTION: CC Sequence=AAH12407.1; Type=Erroneous initiation; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK004991; BAB23726.1; -; mRNA. DR EMBL; AK145873; BAE26715.1; -; mRNA. DR EMBL; AK160117; BAE35641.1; -; mRNA. DR EMBL; AK169195; BAE40971.1; -; mRNA. DR EMBL; BC012407; AAH12407.1; ALT_INIT; mRNA. DR RefSeq; NP_001120810.1; NM_001127338.1. DR RefSeq; NP_613066.2; NM_138600.4. DR UniGene; Mm.30250; -. DR ProteinModelPortal; Q9DBF1; -. DR SMR; Q9DBF1; 30-527. DR IntAct; Q9DBF1; 4. DR MINT; MINT-1859388; -. DR STRING; 10090.ENSMUSP00000112334; -. DR PhosphoSite; Q9DBF1; -. DR REPRODUCTION-2DPAGE; Q9DBF1; -. DR PaxDb; Q9DBF1; -. DR PRIDE; Q9DBF1; -. DR Ensembl; ENSMUST00000066208; ENSMUSP00000065089; ENSMUSG00000053644. [Q9DBF1-1] DR Ensembl; ENSMUST00000174518; ENSMUSP00000133372; ENSMUSG00000053644. [Q9DBF1-2] DR GeneID; 110695; -. DR KEGG; mmu:110695; -. DR UCSC; uc008eyn.2; mouse. [Q9DBF1-1] DR CTD; 501; -. DR MGI; MGI:108186; Aldh7a1. DR eggNOG; COG1012; -. DR GeneTree; ENSGT00720000108597; -. DR HOGENOM; HOG000271511; -. DR HOVERGEN; HBG050485; -. DR InParanoid; Q3UKT6; -. DR KO; K14085; -. DR OMA; WNNAIAL; -. DR OrthoDB; EOG78D7JV; -. DR TreeFam; TF300388; -. DR UniPathway; UPA00529; UER00386. DR NextBio; 364487; -. DR PRO; PR:Q9DBF1; -. DR ArrayExpress; Q9DBF1; -. DR Bgee; Q9DBF1; -. DR CleanEx; MM_ALDH7A1; -. DR Genevestigator; Q9DBF1; -. DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0008802; F:betaine-aldehyde dehydrogenase activity; IEA:UniProtKB-EC. DR GO; GO:0004043; F:L-aminoadipate-semialdehyde dehydrogenase activity; IEA:UniProtKB-EC. DR GO; GO:0019285; P:glycine betaine biosynthetic process from choline; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.309.10; -; 1. DR Gene3D; 3.40.605.10; -; 1. DR InterPro; IPR016161; Ald_DH/histidinol_DH. DR InterPro; IPR016163; Ald_DH_C. DR InterPro; IPR016160; Ald_DH_CS. DR InterPro; IPR016162; Ald_DH_N. DR InterPro; IPR015590; Aldehyde_DH_dom. DR Pfam; PF00171; Aldedh; 1. DR SUPFAM; SSF53720; SSF53720; 1. DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1. PE 1: Evidence at protein level; KW Acetylation; Alternative splicing; Complete proteome; Cytoplasm; KW Mitochondrion; NAD; Nucleus; Oxidoreductase; Reference proteome; KW Transit peptide. FT TRANSIT 1 26 Mitochondrion (Potential). FT CHAIN 27 539 Alpha-aminoadipic semialdehyde FT dehydrogenase. FT /FTId=PRO_0000056491. FT NP_BIND 274 279 NAD (By similarity). FT ACT_SITE 296 296 Proton acceptor (By similarity). FT ACT_SITE 330 330 Nucleophile (By similarity). FT SITE 195 195 Transition state stabilizer (By FT similarity). FT MOD_RES 86 86 N6-acetyllysine; alternate. FT MOD_RES 86 86 N6-succinyllysine; alternate. FT MOD_RES 94 94 N6-acetyllysine; alternate. FT MOD_RES 94 94 N6-succinyllysine; alternate. FT MOD_RES 97 97 N6-acetyllysine; alternate. FT MOD_RES 97 97 N6-succinyllysine; alternate. FT MOD_RES 462 462 N6-acetyllysine. FT MOD_RES 500 500 N6-acetyllysine. FT MOD_RES 537 537 N6-succinyllysine. FT VAR_SEQ 1 28 Missing (in isoform 2). FT /FTId=VSP_038989. FT CONFLICT 164 164 I -> M (in Ref. 1; BAE26715). FT CONFLICT 467 467 I -> V (in Ref. 1; BAE35641). FT CONFLICT 491 491 E -> G (in Ref. 1; BAE35641). SQ SEQUENCE 539 AA; 58861 MW; 7591EE5652F2577E CRC64; MWRVPRRLCV QSVKTSKLSG PWSRPAAHMS TLLIHHPQYA WLQDLGLRED NEGVYNGSWG GRGEVITTYC PANNEPIARV RQASLKDYEE TIGKAKKAWN IWADIPAPKR GEIVRKIGDA FREKIQLLGR LVSLEMGKIL VEGIGEVQEY VDVCDYAAGL SRMIGGPTLP SERPGHALIE MWNPLGLVGI ITAFNFPVAV FGWNNAIALI TGNVCLWKGA PTTSLVSVAV TKIIAQVLED NLLPGAICSL VCGGADIGTT MARDERVNLL SFTGSTQVGK EVALMVQERF GKSLLELGGN NAIIAFEDAD LSLVVPSVLF AAVGTAGQRC TTVRRLFLHE SIHNEVVDRL RSAYSQIRVG NPWDPNILYG PLHTKQAVSM FVRAVEEAKK QGGTVVYGGK VMDHPGNYVE PTIVTGLAHD APIVHQETFA PILYVFKFQD EEEVFEWNNE VKQGLSSSIF TKDLGRIFRW LGPKGSDCGI VNVNIPTSGA EIGGAFGGEK HTGGGRESGS DAWKQYMRRS TCTINYSTSL PLAQGIKFQ // ID ALD2_MOUSE Reviewed; 316 AA. AC P45377; Q99JN4; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 19-FEB-2014, entry version 113. DE RecName: Full=Aldose reductase-related protein 2; DE Short=AR; DE EC=1.1.1.21; DE AltName: Full=Aldehyde reductase; DE AltName: Full=Fibroblast growth factor-regulated protein; DE AltName: Full=Protein FR-1; GN Name=Akr1b8; Synonyms=Fgfrp; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=BALB/c; RX PubMed=7510692; RA Donohue P.J., Alberts G.F., Hampton B.S., Winkles J.A.; RT "A delayed-early gene activated by fibroblast growth factor-1 encodes RT a protein related to aldose reductase."; RL J. Biol. Chem. 269:8604-8609(1994). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Mammary gland; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH NADPH AND RP INHIBITOR. RX PubMed=7578036; DOI=10.1021/bi00044a009; RA Wilson D.K., Nakano T., Petrash M., Quiocho F.A.; RT "1.7-A structure of FR-1, a fibroblast growth factor-induced member of RT the aldo-keto reductase family, complexed with coenzyme and RT inhibitor."; RL Biochemistry 34:14323-14330(1995). CC -!- CATALYTIC ACTIVITY: Alditol + NAD(P)(+) = aldose + NAD(P)H. CC -!- SUBUNIT: Monomer (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- INDUCTION: By FGF-1. CC -!- SIMILARITY: Belongs to the aldo/keto reductase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U04204; AAA16953.1; -; mRNA. DR EMBL; BC005789; AAH05789.1; -; mRNA. DR PIR; A53440; A53440. DR RefSeq; NP_032038.1; NM_008012.1. DR UniGene; Mm.5378; -. DR PDB; 1FRB; X-ray; 1.70 A; A=2-316. DR PDBsum; 1FRB; -. DR ProteinModelPortal; P45377; -. DR SMR; P45377; 2-315. DR IntAct; P45377; 1. DR MINT; MINT-4087589; -. DR STRING; 10090.ENSMUSP00000040244; -. DR PhosphoSite; P45377; -. DR REPRODUCTION-2DPAGE; IPI00273096; -. DR REPRODUCTION-2DPAGE; P45377; -. DR PaxDb; P45377; -. DR PRIDE; P45377; -. DR Ensembl; ENSMUST00000038406; ENSMUSP00000040244; ENSMUSG00000029762. DR GeneID; 14187; -. DR KEGG; mmu:14187; -. DR UCSC; uc009bgz.1; mouse. DR CTD; 14187; -. DR MGI; MGI:107673; Akr1b8. DR eggNOG; COG0656; -. DR GeneTree; ENSGT00670000097881; -. DR HOGENOM; HOG000250272; -. DR HOVERGEN; HBG000020; -. DR InParanoid; P45377; -. DR KO; K00011; -. DR OMA; YPFDAEY; -. DR OrthoDB; EOG70KGQF; -. DR TreeFam; TF106492; -. DR EvolutionaryTrace; P45377; -. DR NextBio; 285402; -. DR PRO; PR:P45377; -. DR Bgee; P45377; -. DR Genevestigator; P45377; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004032; F:alditol:NADP+ 1-oxidoreductase activity; IEA:UniProtKB-EC. DR Gene3D; 3.20.20.100; -; 1. DR InterPro; IPR001395; Aldo/ket_red. DR InterPro; IPR018170; Aldo/ket_reductase_CS. DR InterPro; IPR020471; Aldo/keto_reductase_subgr. DR InterPro; IPR023210; NADP_OxRdtase_dom. DR PANTHER; PTHR11732; PTHR11732; 1. DR Pfam; PF00248; Aldo_ket_red; 1. DR PIRSF; PIRSF000097; AKR; 1. DR PRINTS; PR00069; ALDKETRDTASE. DR SUPFAM; SSF51430; SSF51430; 1. DR PROSITE; PS00798; ALDOKETO_REDUCTASE_1; 1. DR PROSITE; PS00062; ALDOKETO_REDUCTASE_2; 1. DR PROSITE; PS00063; ALDOKETO_REDUCTASE_3; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Cytoplasm; NADP; Oxidoreductase; KW Reference proteome. FT CHAIN 1 316 Aldose reductase-related protein 2. FT /FTId=PRO_0000124631. FT NP_BIND 211 273 NADP. FT ACT_SITE 49 49 Proton donor. FT BINDING 111 111 Substrate. FT SITE 78 78 Lowers pKa of active site Tyr (By FT similarity). FT CONFLICT 242 242 E -> K (in Ref. 2; AAH05789). FT STRAND 4 6 FT STRAND 12 16 FT HELIX 25 37 FT STRAND 42 44 FT HELIX 47 49 FT HELIX 52 64 FT HELIX 70 72 FT STRAND 74 79 FT HELIX 81 83 FT HELIX 86 100 FT STRAND 105 110 FT HELIX 138 150 FT STRAND 153 161 FT HELIX 164 171 FT STRAND 182 186 FT HELIX 194 202 FT STRAND 206 211 FT TURN 228 230 FT HELIX 232 240 FT HELIX 245 254 FT TURN 255 257 FT HELIX 267 274 FT HELIX 283 290 FT HELIX 302 304 SQ SEQUENCE 316 AA; 36121 MW; 0C6F0A7BA806497C CRC64; MATFVELSTK AKMPIVGLGT WKSPPNQVKE AVKAAIDAGY RHIDCAYAYC NENEVGEAIQ EKIKEKAVQR EDLFIVSKLW PTCFEKKLLK EAFQKTLTDL KLDYLDLYLI HWPQGLQPGK ELFPKDDQGR ILTSKTTFLE AWEGMEELVD QGLVKALGVS NFNHFQIERL LNKPGLKHKP VTNQVECHPY LTQEKLIQYC HSKGISVTAY SPLGSPDRPS AKPEDPSLLE DPKIKEIAAK HEKTSAQVLI RFHIQRNVVV IPKSVTPSRI QENIQVFDFQ LSDEEMATIL SFNRNWRACL LPETVNMEEY PYDAEY // ID ALD1_MOUSE Reviewed; 316 AA. AC P21300; DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 4. DT 19-FEB-2014, entry version 115. DE RecName: Full=Aldose reductase-related protein 1; DE EC=1.1.1.21; DE AltName: Full=Aldehyde reductase; DE Short=AR; DE AltName: Full=Aldo-keto reductase family 1 member B7; DE AltName: Full=MVDP; DE AltName: Full=Vas deferens androgen-dependent protein; GN Name=Akr1b7; Synonyms=Avdp; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC TISSUE=Vas deferens; RX PubMed=1637719; DOI=10.1016/0960-0760(92)90445-O; RA Pailhoux E.A., Veyssiere G.M., Fabre S., Tournaire C., Jean C.G.; RT "The genomic organization and DNA sequence of the mouse vas deferens RT androgen regulated protein gene."; RL J. Steroid Biochem. Mol. Biol. 42:561-568(1992). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=CD-1; TISSUE=Vas deferens; RX PubMed=2123194; RA Pailhoux E.A., Martinez A., Veyssiere G.M., Jean C.G.; RT "Androgen-dependent protein from mouse vas deferens. cDNA cloning and RT protein homology with the aldo-keto reductase superfamily."; RL J. Biol. Chem. 265:19932-19936(1990). CC -!- FUNCTION: Reduces a broad range of aliphatic and aromatic CC aldehydes to the corresponding alcohols. May play a role in the CC metabolism of xenobiotic aromatic aldehydes (By similarity). The CC role of MVDP in sperm maturation and storage may be related to its CC potential capacity to produce fructose, or MVDP may play an CC osmoregulatory role by producing sorbitol. CC -!- CATALYTIC ACTIVITY: Alditol + NAD(P)(+) = aldose + NAD(P)H. CC -!- SUBUNIT: Monomer (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- INDUCTION: Castration resulted in a marked decrease in the level CC of the mRNA coding for the protein, whereas administration of CC testosterone to castrated males resulted in a marked increase. CC -!- SIMILARITY: Belongs to the aldo/keto reductase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M81448; AAA39774.1; -; Genomic_DNA. DR EMBL; J05663; AAA39773.1; -; mRNA. DR PIR; A37990; A37990. DR RefSeq; NP_033861.2; NM_009731.2. DR UniGene; Mm.482073; -. DR ProteinModelPortal; P21300; -. DR SMR; P21300; 3-316. DR REPRODUCTION-2DPAGE; P21300; -. DR PaxDb; P21300; -. DR PRIDE; P21300; -. DR DNASU; 11997; -. DR Ensembl; ENSMUST00000007449; ENSMUSP00000007449; ENSMUSG00000052131. DR GeneID; 11997; -. DR KEGG; mmu:11997; -. DR UCSC; uc009bhd.2; mouse. DR CTD; 11997; -. DR MGI; MGI:101918; Akr1b7. DR eggNOG; COG0656; -. DR HOGENOM; HOG000250272; -. DR HOVERGEN; HBG000020; -. DR InParanoid; P21300; -. DR KO; K00011; -. DR OMA; FYENQHE; -. DR OrthoDB; EOG70KGQF; -. DR TreeFam; TF106492; -. DR NextBio; 280181; -. DR PRO; PR:P21300; -. DR ArrayExpress; P21300; -. DR Bgee; P21300; -. DR CleanEx; MM_AKR1B7; -. DR Genevestigator; P21300; -. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR GO; GO:0004032; F:alditol:NADP+ 1-oxidoreductase activity; IEA:UniProtKB-EC. DR GO; GO:0044255; P:cellular lipid metabolic process; TAS:MGI. DR Gene3D; 3.20.20.100; -; 1. DR InterPro; IPR001395; Aldo/ket_red. DR InterPro; IPR018170; Aldo/ket_reductase_CS. DR InterPro; IPR020471; Aldo/keto_reductase_subgr. DR InterPro; IPR023210; NADP_OxRdtase_dom. DR PANTHER; PTHR11732; PTHR11732; 1. DR Pfam; PF00248; Aldo_ket_red; 1. DR PIRSF; PIRSF000097; AKR; 1. DR PRINTS; PR00069; ALDKETRDTASE. DR SUPFAM; SSF51430; SSF51430; 1. DR PROSITE; PS00798; ALDOKETO_REDUCTASE_1; 1. DR PROSITE; PS00062; ALDOKETO_REDUCTASE_2; 1. DR PROSITE; PS00063; ALDOKETO_REDUCTASE_3; 1. PE 2: Evidence at transcript level; KW Complete proteome; Cytoplasm; NADP; Oxidoreductase; KW Reference proteome. FT CHAIN 1 316 Aldose reductase-related protein 1. FT /FTId=PRO_0000124629. FT NP_BIND 20 21 NADP (By similarity). FT NP_BIND 160 161 NADP (By similarity). FT NP_BIND 210 215 NADP (By similarity). FT NP_BIND 263 269 NADP (By similarity). FT ACT_SITE 49 49 Proton donor (By similarity). FT BINDING 44 44 NADP (By similarity). FT BINDING 111 111 Substrate (By similarity). FT BINDING 184 184 NADP (By similarity). FT BINDING 273 273 NADP (By similarity). FT SITE 78 78 Lowers pKa of active site Tyr (By FT similarity). FT CONFLICT 94 94 Q -> D (in Ref. 2; AAA39773). SQ SEQUENCE 316 AA; 35988 MW; 6BC46B6076969742 CRC64; MATFVELSTK AKMPLVGLGT WKSSPGQVKE AVKAAIDAGY RHIDCAYVYH NENEVGEAIQ EKIKENAVKR EDLFIVSKLW ATFFEKSLVK KAFQNTLSDL KLDYLDLYLV HWPQGFQAGN ALLPKDNKGK VLLSKSTFLD AWEAMEELVD QGLVKALGIS NFNHFQIERL LNKPGLKHKP VTNQIESHPY LTQEKLIQYC QSKGIAVTAY SPLGSPDRPY AKPEDPVVME IPKIKEIAAK HKKTVAQVLI RFHVQRNVVV IPKSVTPSRI QENLQVFDFQ LSEEDMAAIL SFNRNWRACD LLDARTEEDY PFHEEY // ID ALDH2_MOUSE Reviewed; 519 AA. AC P47738; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 19-MAR-2014, entry version 120. DE RecName: Full=Aldehyde dehydrogenase, mitochondrial; DE EC=1.2.1.3; DE AltName: Full=AHD-M1; DE AltName: Full=ALDH class 2; DE AltName: Full=ALDH-E2; DE AltName: Full=ALDHI; DE Flags: Precursor; GN Name=Aldh2; Synonyms=Ahd-1, Ahd1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=C57BL/6J; RX PubMed=7958964; DOI=10.1016/0378-1119(94)90708-0; RA Chang C., Yoshida A.; RT "Cloning and characterization of the gene encoding mouse mitochondrial RT aldehyde dehydrogenase."; RL Gene 148:331-336(1994). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=8058062; RA Chen M., Achkar C., Gudas L.J.; RT "Enzymatic conversion of retinaldehyde to retinoic acid by cloned RT murine cytosolic and mitochondrial aldehyde dehydrogenases."; RL Mol. Pharmacol. 46:88-96(1994). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Mammary gland; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP PROTEIN SEQUENCE OF 54-80; 87-96; 162-174; 198-228; 260-282; 327-340; RP 349-370; 386-409; 417-428; 431-438 AND 444-453, AND MASS SPECTROMETRY. RC STRAIN=C57BL/6, and OF1; TISSUE=Brain, and Hippocampus; RA Lubec G., Kang S.U., Klug S., Sunyer B., Chen W.-Q.; RL Submitted (JAN-2009) to UniProtKB. RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 472-509. RX PubMed=7937138; DOI=10.1093/nar/22.20.4132; RA Caubin J., Iglesias T., Bernal J., Munoz A., Marquez G., Barbero J.L., RA Zaballos A.; RT "Isolation of genomic DNA fragments corresponding to genes modulated RT in vivo by a transcription factor."; RL Nucleic Acids Res. 22:4132-4138(1994). RN [6] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-430, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic fibroblast; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., RA Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). RN [7] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-54; LYS-75; LYS-80; LYS-161; RP LYS-370; LYS-377; LYS-385; LYS-409; LYS-428; LYS-430; LYS-443 AND RP LYS-453, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Liver; RX PubMed=23576753; DOI=10.1073/pnas.1302961110; RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., RA Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.; RT "Label-free quantitative proteomics of the lysine acetylome in RT mitochondria identifies substrates of SIRT3 in metabolic pathways."; RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013). CC -!- FUNCTION: Is capable of converting retinaldehyde to retinoic acid. CC -!- CATALYTIC ACTIVITY: An aldehyde + NAD(+) + H(2)O = a carboxylate + CC NADH. CC -!- PATHWAY: Alcohol metabolism; ethanol degradation; acetate from CC ethanol: step 2/2. CC -!- SUBUNIT: Homotetramer (By similarity). CC -!- INTERACTION: CC Q8R104:Sirt3; NbExp=2; IntAct=EBI-2308120, EBI-6999888; CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix. CC -!- INDUCTION: By retinoic acid; 3-5 fold increase. CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U07235; AAA64636.1; -; mRNA. DR EMBL; S71509; AAC60691.1; -; mRNA. DR EMBL; BC005476; AAH05476.1; -; mRNA. DR EMBL; Z32545; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR PIR; I48966; I48966. DR RefSeq; NP_033786.1; NM_009656.3. DR UniGene; Mm.284446; -. DR ProteinModelPortal; P47738; -. DR SMR; P47738; 26-519. DR IntAct; P47738; 5. DR MINT; MINT-1859437; -. DR PhosphoSite; P47738; -. DR REPRODUCTION-2DPAGE; P47738; -. DR SWISS-2DPAGE; P47738; -. DR UCD-2DPAGE; P47738; -. DR PaxDb; P47738; -. DR PRIDE; P47738; -. DR Ensembl; ENSMUST00000031411; ENSMUSP00000031411; ENSMUSG00000029455. DR GeneID; 11669; -. DR KEGG; mmu:11669; -. DR UCSC; uc008zjt.1; mouse. DR CTD; 217; -. DR MGI; MGI:99600; Aldh2. DR eggNOG; COG1012; -. DR HOGENOM; HOG000271505; -. DR HOVERGEN; HBG000097; -. DR InParanoid; P47738; -. DR KO; K00128; -. DR OMA; VAYHIYE; -. DR OrthoDB; EOG7PS1F7; -. DR TreeFam; TF300455; -. DR UniPathway; UPA00780; UER00768. DR ChiTaRS; ALDH2; mouse. DR NextBio; 279291; -. DR PRO; PR:P47738; -. DR ArrayExpress; P47738; -. DR Bgee; P47738; -. DR CleanEx; MM_ALDH2; -. DR Genevestigator; P47738; -. DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR GO; GO:0004029; F:aldehyde dehydrogenase (NAD) activity; IEA:UniProtKB-EC. DR GO; GO:0006068; P:ethanol catabolic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.309.10; -; 1. DR Gene3D; 3.40.605.10; -; 1. DR InterPro; IPR016161; Ald_DH/histidinol_DH. DR InterPro; IPR016163; Ald_DH_C. DR InterPro; IPR016160; Ald_DH_CS. DR InterPro; IPR016162; Ald_DH_N. DR InterPro; IPR015590; Aldehyde_DH_dom. DR Pfam; PF00171; Aldedh; 1. DR SUPFAM; SSF53720; SSF53720; 1. DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1. DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1. PE 1: Evidence at protein level; KW Acetylation; Complete proteome; Direct protein sequencing; KW Mitochondrion; NAD; Oxidoreductase; Reference proteome; KW Transit peptide. FT TRANSIT 1 19 Mitochondrion (By similarity). FT CHAIN 20 519 Aldehyde dehydrogenase, mitochondrial. FT /FTId=PRO_0000007169. FT NP_BIND 264 269 NAD (By similarity). FT ACT_SITE 287 287 Proton acceptor (By similarity). FT ACT_SITE 321 321 Nucleophile (By similarity). FT SITE 188 188 Transition state stabilizer (By FT similarity). FT MOD_RES 20 20 N-acetylserine (Probable). FT MOD_RES 54 54 N6-acetyllysine. FT MOD_RES 75 75 N6-acetyllysine. FT MOD_RES 80 80 N6-acetyllysine. FT MOD_RES 161 161 N6-acetyllysine. FT MOD_RES 370 370 N6-acetyllysine. FT MOD_RES 377 377 N6-acetyllysine. FT MOD_RES 385 385 N6-acetyllysine. FT MOD_RES 409 409 N6-acetyllysine. FT MOD_RES 428 428 N6-acetyllysine. FT MOD_RES 430 430 N6-acetyllysine. FT MOD_RES 443 443 N6-acetyllysine. FT MOD_RES 453 453 N6-acetyllysine. FT CONFLICT 88 89 AF -> C (in Ref. 2; AAC60691). FT CONFLICT 181 181 Missing (in Ref. 2; AAC60691). FT CONFLICT 227 227 I -> S (in Ref. 2; AAC60691). FT CONFLICT 344 344 R -> G (in Ref. 2; AAC60691). FT CONFLICT 370 370 K -> N (in Ref. 2; AAC60691). FT CONFLICT 378 378 S -> M (in Ref. 2; AAC60691). FT CONFLICT 476 476 D -> V (in Ref. 2; AAC60691). SQ SEQUENCE 519 AA; 56538 MW; 200806F63D48F4DA CRC64; MLRAALTTVR RGPRLSRLLS AAATSAVPAP NHQPEVFCNQ IFINNEWHDA VSRKTFPTVN PSTGEVICQV AEGNKEDVDK AVKAARAAFQ LGSPWRRMDA SDRGRLLYRL ADLIERDRTY LAALETLDNG KPYVISYLVD LDMVLKCLRY YAGWADKYHG KTIPIDGDFF SYTRHEPVGV CGQIIPWNFP LLMQAWKLGP ALATGNVVVM KVAEQTPLTA LYVANLIKEA GFPPGVVNIV PGFGPTAGAA IASHEGVDKV AFTGSTEVGH LIQVAAGSSN LKRVTLELGG KSPNIIMSDA DMDWAVEQAH FALFFNQGQC CCAGSRTFVQ ENVYDEFVER SVARAKSRVV GNPFDSRTEQ GPQVDETQFK KILGYIKSGQ QEGAKLLCGG GAAADRGYFI QPTVFGDVKD GMTIAKEEIF GPVMQILKFK TIEEVVGRAN DSKYGLAAAV FTKDLDKANY LSQALQAGTV WINCYDVFGA QSPFGGYKMS GSGRELGEYG LQAYTEVKTV TVKVPQKNS // ID ALDR_MOUSE Reviewed; 316 AA. AC P45376; O70130; Q99KC9; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 19-FEB-2014, entry version 122. DE RecName: Full=Aldose reductase; DE Short=AR; DE EC=1.1.1.21; DE AltName: Full=Aldehyde reductase; GN Name=Akr1b1; Synonyms=Akr1b3, Aldor1, Aldr1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=C57BL/6; TISSUE=Kidney; RX PubMed=7851421; DOI=10.1111/j.1432-1033.1995.tb20408.x; RA Gui T., Tanimoto T., Kokai Y., Nishimura C.; RT "Presence of a closely related subgroup in the aldo-ketoreductase RT family of the mouse."; RL Eur. J. Biochem. 227:448-453(1995). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=ICR X Swiss Webster; TISSUE=Liver; RA Iwata T., Carper D.; RL Submitted (MAR-1995) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=CD-1; TISSUE=Kidney; RA Daoudal S., Berger M., Pailhoux E., Tournaire C., Veyssiere G., RA Jean C.; RL Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=129/Ola; RX PubMed=9485485; RA McGowan M.H., Iwata T., Carper D.A.; RT "Characterization of the mouse aldose reductase gene and promoter in a RT lens epithelial cell line."; RL Mol. Vis. 4:2-2(1998). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=129/SvJ; RX PubMed=10092857; DOI=10.1046/j.1432-1327.1999.00110.x; RA Ho H.T.B., Jenkins N.A., Copeland N.G., Gilbert D.J., Winkles J.A., RA Louie H.W.Y., Lee F.K., Chung S.S.M., Chung S.K.; RT "Comparisons of genomic structures and chromosomal locations of the RT mouse aldose reductase and aldose reductase-like genes."; RL Eur. J. Biochem. 259:726-730(1999). RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=BALB/c; RX PubMed=10049784; DOI=10.1006/bbrc.1999.0164; RA Li H., Nobukuni Y., Gui T., Yabe-Nishimura C.; RT "Characterization of genomic regions directing the cell-specific RT expression of the mouse aldose reductase gene."; RL Biochem. Biophys. Res. Commun. 255:759-764(1999). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Mammary tumor; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [8] RP PROTEIN SEQUENCE OF 156-169. RC TISSUE=Brain; RA Lubec G., Yang J.W., Zigmond M.; RL Submitted (JUL-2007) to UniProtKB. CC -!- FUNCTION: Catalyzes the NADPH-dependent reduction of a wide CC variety of carbonyl-containing compounds to their corresponding CC alcohols with a broad range of catalytic efficiencies. CC -!- CATALYTIC ACTIVITY: Alditol + NAD(P)(+) = aldose + NAD(P)H. CC -!- SUBUNIT: Monomer. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- TISSUE SPECIFICITY: Abundant in the testis, skeletal muscle and CC kidney. CC -!- SIMILARITY: Belongs to the aldo/keto reductase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; D32250; BAA06980.1; -; mRNA. DR EMBL; L39795; AAA62176.1; -; mRNA. DR EMBL; U29152; AAA69958.1; -; mRNA. DR EMBL; U89150; AAC13358.1; -; Genomic_DNA. DR EMBL; U89140; AAC13358.1; JOINED; Genomic_DNA. DR EMBL; U89142; AAC13358.1; JOINED; Genomic_DNA. DR EMBL; U89143; AAC13358.1; JOINED; Genomic_DNA. DR EMBL; U89144; AAC13358.1; JOINED; Genomic_DNA. DR EMBL; U89145; AAC13358.1; JOINED; Genomic_DNA. DR EMBL; U89146; AAC13358.1; JOINED; Genomic_DNA. DR EMBL; U89147; AAC13358.1; JOINED; Genomic_DNA. DR EMBL; U89148; AAC13358.1; JOINED; Genomic_DNA. DR EMBL; U89149; AAC13358.1; JOINED; Genomic_DNA. DR EMBL; U93231; AAD32300.1; -; Genomic_DNA. DR EMBL; U93230; AAD32300.1; JOINED; Genomic_DNA. DR EMBL; AB016665; BAA76413.1; -; Genomic_DNA. DR EMBL; BC004725; AAH04725.1; -; mRNA. DR EMBL; BC021655; AAH21655.1; -; mRNA. DR PIR; I49484; I49484. DR RefSeq; NP_033788.3; NM_009658.3. DR UniGene; Mm.389126; -. DR UniGene; Mm.451; -. DR ProteinModelPortal; P45376; -. DR SMR; P45376; 2-315. DR BioGrid; 198069; 2. DR IntAct; P45376; 6. DR MINT; MINT-1869603; -. DR PhosphoSite; P45376; -. DR COMPLUYEAST-2DPAGE; P45376; -. DR REPRODUCTION-2DPAGE; IPI00223757; -. DR REPRODUCTION-2DPAGE; P45376; -. DR SWISS-2DPAGE; P45376; -. DR PaxDb; P45376; -. DR PRIDE; P45376; -. DR DNASU; 11677; -. DR Ensembl; ENSMUST00000102980; ENSMUSP00000100045; ENSMUSG00000001642. DR GeneID; 11677; -. DR KEGG; mmu:11677; -. DR UCSC; uc009bgy.2; mouse. DR CTD; 11677; -. DR MGI; MGI:1353494; Akr1b3. DR eggNOG; COG0656; -. DR HOGENOM; HOG000250272; -. DR HOVERGEN; HBG000020; -. DR InParanoid; P45376; -. DR KO; K00011; -. DR OMA; DFLDTWT; -. DR OrthoDB; EOG70KGQF; -. DR TreeFam; TF106492; -. DR NextBio; 279311; -. DR PRO; PR:P45376; -. DR ArrayExpress; P45376; -. DR Bgee; P45376; -. DR Genevestigator; P45376; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005634; C:nucleus; IEA:Ensembl. DR GO; GO:0004032; F:alditol:NADP+ 1-oxidoreductase activity; IDA:MGI. DR GO; GO:0043795; F:glyceraldehyde oxidoreductase activity; IEA:Ensembl. DR GO; GO:0044597; P:daunorubicin metabolic process; IEA:Ensembl. DR GO; GO:0044598; P:doxorubicin metabolic process; IEA:Ensembl. DR Gene3D; 3.20.20.100; -; 1. DR InterPro; IPR001395; Aldo/ket_red. DR InterPro; IPR018170; Aldo/ket_reductase_CS. DR InterPro; IPR020471; Aldo/keto_reductase_subgr. DR InterPro; IPR023210; NADP_OxRdtase_dom. DR PANTHER; PTHR11732; PTHR11732; 1. DR Pfam; PF00248; Aldo_ket_red; 1. DR PIRSF; PIRSF000097; AKR; 1. DR PRINTS; PR00069; ALDKETRDTASE. DR SUPFAM; SSF51430; SSF51430; 1. DR PROSITE; PS00798; ALDOKETO_REDUCTASE_1; 1. DR PROSITE; PS00062; ALDOKETO_REDUCTASE_2; 1. DR PROSITE; PS00063; ALDOKETO_REDUCTASE_3; 1. PE 1: Evidence at protein level; KW Acetylation; Complete proteome; Cytoplasm; Direct protein sequencing; KW NADP; Oxidoreductase; Reference proteome. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 316 Aldose reductase. FT /FTId=PRO_0000124624. FT NP_BIND 10 19 NADP (Potential). FT NP_BIND 211 273 NADP (By similarity). FT ACT_SITE 49 49 Proton donor (By similarity). FT BINDING 111 111 Substrate (By similarity). FT SITE 78 78 Lowers pKa of active site Tyr (By FT similarity). FT MOD_RES 2 2 N-acetylalanine (By similarity). FT MOD_RES 95 95 N6-acetyllysine (By similarity). FT MOD_RES 222 222 N6-acetyllysine (By similarity). FT MOD_RES 263 263 N6-acetyllysine (By similarity). FT CONFLICT 46 46 A -> S (in Ref. 1; BAA06980). FT CONFLICT 221 221 A -> G (in Ref. 4; AAC13358). FT CONFLICT 281 281 V -> L (in Ref. 7; AAH04725/AAH21655). SQ SEQUENCE 316 AA; 35732 MW; E18759AD160B4A0E CRC64; MASHLELNNG TKMPTLGLGT WKSPPGQVTE AVKVAIDLGY RHIDCAQVYQ NEKEVGVALQ EKLKEQVVKR QDLFIVSKLW CTFHDKSMVK GAFQKTLSDL QLDYLDLYLI HWPTGFKPGP DYFPLDASGN VIPSDTDFVD TWTAMEQLVD EGLVKTIGVS NFNPLQIERI LNKPGLKYKP AVNQIECHPY LTQEKLIEYC HSKGIVVTAY SPLGSPDRPW AKPEDPSLLE DPRIKAIAAK YNKTTAQVLI RFPIQRNLVV IPKSVTPVRI AENLKVFDFE VSSEDMATLL SYNRNWRVCA LMSCAKHKDY PFHAEV // ID ALKB3_MOUSE Reviewed; 286 AA. AC Q8K1E6; DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2002, sequence version 1. DT 19-MAR-2014, entry version 90. DE RecName: Full=Alpha-ketoglutarate-dependent dioxygenase alkB homolog 3; DE EC=1.14.11.-; DE AltName: Full=Alkylated DNA repair protein alkB homolog 3; GN Name=Alkbh3; Synonyms=Abh3; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Mammary tumor; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [2] RP FUNCTION, MUTAGENESIS OF ASP-193 AND HIS-257, AND TISSUE SPECIFICITY. RX PubMed=16174769; DOI=10.1074/jbc.M509881200; RA Lee D.-H., Jin S.-G., Cai S., Chen Y., Pfeifer G.P., O'Connor T.R.; RT "Repair of methylation damage in DNA and RNA by mammalian AlkB RT homologues."; RL J. Biol. Chem. 280:39448-39459(2005). RN [3] RP DISRUPTION PHENOTYPE. RX PubMed=16642038; DOI=10.1038/sj.emboj.7601109; RA Ringvoll J., Nordstrand L.M., Vaagboe C.B., Talstad V., Reite K., RA Aas P.A., Lauritzen K.H., Liabakk N.B., Bjoerk A., Doughty R.W., RA Falnes P.O., Krokan H.E., Klungland A.; RT "Repair deficient mice reveal mABH2 as the primary oxidative RT demethylase for repairing 1meA and 3meC lesions in DNA."; RL EMBO J. 25:2189-2198(2006). RN [4] RP DISRUPTION PHENOTYPE. RX PubMed=18519673; DOI=10.1158/0008-5472.CAN-08-0796; RA Ringvoll J., Moen M.N., Nordstrand L.M., Meira L.B., Pang B., RA Bekkelund A., Dedon P.C., Bjelland S., Samson L.D., Falnes P.O., RA Klungland A.; RT "AlkB homologue 2-mediated repair of ethenoadenine lesions in RT mammalian DNA."; RL Cancer Res. 68:4142-4149(2008). CC -!- FUNCTION: Dioxygenase that repairs alkylated DNA containing 1- CC methyladenine (1meA) and 3-methylcytosine (3meC) by oxidative CC demethylation. Has a strong preference for single-stranded DNA. CC Able to process alkylated 3mC within double-stranded regions via CC its interaction with ASCC3, which promotes DNA unwinding to CC generate single-stranded substrate needed for ALKHB3. May also act CC on RNA. Requires molecular oxygen, alpha-ketoglutarate and iron. CC -!- COFACTOR: Binds 1 Fe(2+) ion per subunit. CC -!- ENZYME REGULATION: Activated by ascorbate (By similarity). CC -!- SUBUNIT: Interacts with the TRIP4 complex, notably composed of CC ASCC3 (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus (By similarity). CC -!- TISSUE SPECIFICITY: Detected in testis, kidney, liver and heart. CC -!- DISRUPTION PHENOTYPE: No visible phenotype. CC -!- SIMILARITY: Belongs to the alkB family. CC -!- SIMILARITY: Contains 1 Fe2OG dioxygenase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BC018196; AAH18196.1; -; mRNA. DR RefSeq; NP_081220.1; NM_026944.1. DR RefSeq; XP_006500186.1; XM_006500123.1. DR UniGene; Mm.272498; -. DR ProteinModelPortal; Q8K1E6; -. DR SMR; Q8K1E6; 70-279. DR PhosphoSite; Q8K1E6; -. DR PaxDb; Q8K1E6; -. DR PRIDE; Q8K1E6; -. DR Ensembl; ENSMUST00000040005; ENSMUSP00000038721; ENSMUSG00000040174. DR GeneID; 69113; -. DR KEGG; mmu:69113; -. DR UCSC; uc008lgn.1; mouse. DR CTD; 221120; -. DR MGI; MGI:1916363; Alkbh3. DR eggNOG; COG3145; -. DR GeneTree; ENSGT00530000063618; -. DR HOGENOM; HOG000207105; -. DR HOVERGEN; HBG056732; -. DR KO; K10860; -. DR NextBio; 328628; -. DR PRO; PR:Q8K1E6; -. DR ArrayExpress; Q8K1E6; -. DR Bgee; Q8K1E6; -. DR CleanEx; MM_ALKBH3; -. DR Genevestigator; Q8K1E6; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0051747; F:cytosine C-5 DNA demethylase activity; IDA:MGI. DR GO; GO:0043734; F:DNA-N1-methyladenine dioxygenase activity; ISS:UniProtKB. DR GO; GO:0008198; F:ferrous iron binding; ISS:UniProtKB. DR GO; GO:0008283; P:cell proliferation; ISS:UniProtKB. DR GO; GO:0006307; P:DNA dealkylation involved in DNA repair; ISS:UniProtKB. DR GO; GO:0035552; P:oxidative single-stranded DNA demethylation; ISS:UniProtKB. DR Gene3D; 2.60.120.590; -; 1. DR InterPro; IPR027450; AlkB-like. DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase. DR Pfam; PF13532; 2OG-FeII_Oxy_2; 1. DR PROSITE; PS51471; FE2OG_OXY; 1. PE 1: Evidence at protein level; KW Complete proteome; Cytoplasm; Dioxygenase; DNA damage; DNA repair; KW Iron; Metal-binding; Nucleus; Oxidoreductase; Reference proteome. FT CHAIN 1 286 Alpha-ketoglutarate-dependent dioxygenase FT alkB homolog 3. FT /FTId=PRO_0000239279. FT DOMAIN 172 278 Fe2OG dioxygenase. FT REGION 141 143 Substrate binding (By similarity). FT REGION 179 181 Alpha-ketoglutarate binding (By FT similarity). FT REGION 269 275 Alpha-ketoglutarate binding (By FT similarity). FT METAL 191 191 Iron; catalytic (By similarity). FT METAL 193 193 Iron; catalytic (By similarity). FT METAL 257 257 Iron; catalytic (By similarity). FT BINDING 115 115 Substrate (By similarity). FT BINDING 194 194 Substrate (By similarity). FT MUTAGEN 193 193 D->A: Loss of activity. FT MUTAGEN 257 257 H->A: Reduced activity. SQ SEQUENCE 286 AA; 33061 MW; 2480D0D20A9893F4 CRC64; MEDKRQRARV QGGWATPTKS QSATQPASPA RSRLSQTAGP AWRSKEQQQC DRQFVFKEPQ LVVRAAPEPR VIDREGVYEI SLSPTGVSRV CLYPGFVDLK EADWILEQLC KDVPWKQRMG IREDVTYPQP RLTAWYGELP YTYSRITMEP NPHWLPVLWT LKSRIEENTS HTFNSLLCNF YRDEKDSVDW HSDDEPSLGS CPVIASLSFG ATRTFEMRKK PPPEENGDYT YVERVKIPLD HGTLLIMEGA TQADWQHRVP KEYHSRQPRV NLTFRTVYPD PRGAPR // ID ALKB5_MOUSE Reviewed; 395 AA. AC Q3TSG4; Q80US0; Q8BKB9; Q8BKC1; DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2006, sequence version 2. DT 19-MAR-2014, entry version 72. DE RecName: Full=RNA demethylase ALKBH5; DE EC=1.14.11.-; DE AltName: Full=Alkylated DNA repair protein alkB homolog 5; DE AltName: Full=Alpha-ketoglutarate-dependent dioxygenase alkB homolog 5; GN Name=Alkbh5; Synonyms=Abh5, Ofoxd; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Egg, and Eye; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6; TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-362; SER-372 AND RP SER-385, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Liver; RX PubMed=17242355; DOI=10.1073/pnas.0609836104; RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; RT "Large-scale phosphorylation analysis of mouse liver."; RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). RN [5] RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE. RX PubMed=23177736; DOI=10.1016/j.molcel.2012.10.015; RA Zheng G., Dahl J.A., Niu Y., Fedorcsak P., Huang C.M., Li C.J., RA Vagbo C.B., Shi Y., Wang W.L., Song S.H., Lu Z., Bosmans R.P., Dai Q., RA Hao Y.J., Yang X., Zhao W.M., Tong W.M., Wang X.J., Bogdan F., RA Furu K., Fu Y., Jia G., Zhao X., Liu J., Krokan H.E., Klungland A., RA Yang Y.G., He C.; RT "ALKBH5 is a mammalian RNA demethylase that impacts RNA metabolism and RT mouse fertility."; RL Mol. Cell 49:18-29(2013). CC -!- FUNCTION: Dioxygenase that demethylates RNA by oxidative CC demethylation: specifically demethylates N(6)-methyladenosine CC (m6A) RNA, the most prevalent internal modification of messenger CC RNA (mRNA) in higher eukaryotes. Requires molecular oxygen, alpha- CC ketoglutarate and iron (By similarity). Demethylation of m6A mRNA CC affects mRNA processing and export and is required for CC spermatogenesis. CC -!- COFACTOR: Binds 1 Fe(2+) ion per subunit (By similarity). CC -!- SUBCELLULAR LOCATION: Nucleus speckle (By similarity). CC -!- TISSUE SPECIFICITY: Widely expressed, with highest expression in CC testis. CC -!- DISRUPTION PHENOTYPE: Mice are viable, anatomically normal and CC reach adulthood but display impaired fertility resulting from CC apoptosis that affects meiotic metaphase-stage spermatocytes. Male CC mice have increased m6A in mRNA. Testes are significantly smaller CC and histological analysis of testis sections reveal aberrant CC tubular architecture and size. The number of spermatozoa released CC from cauda epididymes is dramatically reduced, and the spermatozoa CC are morphologically abnormal with greatly compromised motility. CC -!- SIMILARITY: Belongs to the alkB family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK053695; BAC35478.1; -; mRNA. DR EMBL; AK053700; BAC35481.1; -; mRNA. DR EMBL; AK162072; BAE36711.1; -; mRNA. DR EMBL; AK163294; BAE37281.1; -; mRNA. DR EMBL; AL596386; CAI35332.1; -; Genomic_DNA. DR EMBL; BC052076; AAH52076.1; -; mRNA. DR RefSeq; NP_766531.2; NM_172943.4. DR UniGene; Mm.262056; -. DR ProteinModelPortal; Q3TSG4; -. DR SMR; Q3TSG4; 86-287. DR PhosphoSite; Q3TSG4; -. DR PaxDb; Q3TSG4; -. DR PRIDE; Q3TSG4; -. DR Ensembl; ENSMUST00000044250; ENSMUSP00000049116; ENSMUSG00000042650. DR GeneID; 268420; -. DR KEGG; mmu:268420; -. DR UCSC; uc007jgd.2; mouse. DR CTD; 54890; -. DR MGI; MGI:2144489; Alkbh5. DR eggNOG; NOG264303; -. DR GeneTree; ENSGT00390000009298; -. DR HOGENOM; HOG000007505; -. DR HOVERGEN; HBG080833; -. DR InParanoid; Q3TSG4; -. DR KO; K10767; -. DR OMA; GAKRKYQ; -. DR OrthoDB; EOG7SBNNR; -. DR TreeFam; TF329212; -. DR NextBio; 392283; -. DR PRO; PR:Q3TSG4; -. DR Bgee; Q3TSG4; -. DR CleanEx; MM_ALKBH5; -. DR Genevestigator; Q3TSG4; -. DR GO; GO:0016607; C:nuclear speck; ISS:UniProtKB. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0035515; F:oxidative RNA demethylase activity; ISS:UniProtKB. DR GO; GO:0016706; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors; ISS:UniProtKB. DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW. DR GO; GO:0006406; P:mRNA export from nucleus; ISS:UniProtKB. DR GO; GO:0006397; P:mRNA processing; ISS:UniProtKB. DR GO; GO:0035553; P:oxidative single-stranded RNA demethylation; ISS:UniProtKB. DR GO; GO:0001666; P:response to hypoxia; ISS:UniProtKB. DR GO; GO:0007283; P:spermatogenesis; IMP:UniProtKB. DR Gene3D; 2.60.120.590; -; 1. DR InterPro; IPR027450; AlkB-like. DR Pfam; PF13532; 2OG-FeII_Oxy_2; 1. PE 1: Evidence at protein level; KW Acetylation; Coiled coil; Complete proteome; Differentiation; KW Dioxygenase; Iron; Metal-binding; Nucleus; Oxidoreductase; KW Phosphoprotein; Reference proteome; Spermatogenesis. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 395 RNA demethylase ALKBH5. FT /FTId=PRO_0000239284. FT COILED 68 117 Potential. FT COMPBIAS 30 48 Ala-rich. FT METAL 205 205 Iron; catalytic (By similarity). FT METAL 207 207 Iron; catalytic (By similarity). FT METAL 267 267 Iron; catalytic (By similarity). FT MOD_RES 2 2 N-acetylalanine (By similarity). FT MOD_RES 65 65 Phosphoserine (By similarity). FT MOD_RES 70 70 Phosphoserine (By similarity). FT MOD_RES 72 72 Phosphotyrosine (By similarity). FT MOD_RES 133 133 N6-acetyllysine (By similarity). FT MOD_RES 362 362 Phosphoserine. FT MOD_RES 372 372 Phosphoserine. FT MOD_RES 375 375 Phosphoserine (By similarity). FT MOD_RES 385 385 Phosphoserine. FT CONFLICT 67 67 P -> S (in Ref. 1; BAC35481). FT CONFLICT 85 85 K -> Q (in Ref. 1; BAC35481). FT CONFLICT 185 185 E -> K (in Ref. 3; AAH52076). FT CONFLICT 203 203 V -> L (in Ref. 1; BAC35481). FT CONFLICT 231 232 CK -> WQ (in Ref. 1; BAE36711). SQ SEQUENCE 395 AA; 44411 MW; 2822BF4BFFFEE7EF CRC64; MAAASGYTDL REKLKSMTSR DNYKAGSREA AAAAAAAVAA AAAAAAAAEP YPASGTTKRK YQEDSDPERS DYEEHQLQKE EEARKVKSGI RQIRLFSQDE CSKIEARIDE VVSRAEKGLY NEHTVDRAPL RNKYFFGEGY TYGAQLQKRG PGQERLYPPG DVDEIPDWVH QLVIQKLVEH RVIPEGFVNS AVINDYQPGG CIVSHVDPIH IFERPIVSVS FFSDSALCFG CKFQFKPIRV SEPVLSLPVR RGSVTVLSGY AADEITHCIR PQDIKERRAV IILRKTRLDA PRLETKSLSS STLPPSYASD RLSGNTRDPA LKPKRSHRKA DPDAAHRPRI LEMDKEENRR SVLLPTHRRR GSFSSENYWR KSYESSEDCP EAASSPTRKV KMRRH // ID ALKB2_MOUSE Reviewed; 239 AA. AC Q6P6J4; Q8C591; DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 19-MAR-2014, entry version 80. DE RecName: Full=Alpha-ketoglutarate-dependent dioxygenase alkB homolog 2; DE EC=1.14.11.33; DE AltName: Full=Alkylated DNA repair protein alkB homolog 2; DE AltName: Full=DNA oxidative demethylase ALKBH2; GN Name=Alkbh2; Synonyms=Abh2; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Urinary bladder; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Jaw; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP FUNCTION, MUTAGENESIS OF ASP-151 AND HIS-214, AND TISSUE SPECIFICITY. RX PubMed=16174769; DOI=10.1074/jbc.M509881200; RA Lee D.-H., Jin S.-G., Cai S., Chen Y., Pfeifer G.P., O'Connor T.R.; RT "Repair of methylation damage in DNA and RNA by mammalian AlkB RT homologues."; RL J. Biol. Chem. 280:39448-39459(2005). RN [4] RP DISRUPTION PHENOTYPE, FUNCTION, ENZYME REGULATION, SUBCELLULAR RP LOCATION, AND TISSUE SPECIFICITY. RX PubMed=16642038; DOI=10.1038/sj.emboj.7601109; RA Ringvoll J., Nordstrand L.M., Vaagboe C.B., Talstad V., Reite K., RA Aas P.A., Lauritzen K.H., Liabakk N.B., Bjoerk A., Doughty R.W., RA Falnes P.O., Krokan H.E., Klungland A.; RT "Repair deficient mice reveal mABH2 as the primary oxidative RT demethylase for repairing 1meA and 3meC lesions in DNA."; RL EMBO J. 25:2189-2198(2006). RN [5] RP DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, FUNCTION, AND TISSUE RP SPECIFICITY. RX PubMed=18519673; DOI=10.1158/0008-5472.CAN-08-0796; RA Ringvoll J., Moen M.N., Nordstrand L.M., Meira L.B., Pang B., RA Bekkelund A., Dedon P.C., Bjelland S., Samson L.D., Falnes P.O., RA Klungland A.; RT "AlkB homologue 2-mediated repair of ethenoadenine lesions in RT mammalian DNA."; RL Cancer Res. 68:4142-4149(2008). CC -!- FUNCTION: Dioxygenase that repairs alkylated DNA and RNA CC containing 1-methyladenine and 3-methylcytosine by oxidative CC demethylation. Can also repair alkylated DNA containing 1- CC ethenoadenine. Has strong preference for double-stranded DNA. Has CC low efficiency with single-stranded substrates. Requires molecular CC oxygen, alpha-ketoglutarate and iron. CC -!- CATALYTIC ACTIVITY: DNA-base-CH(3) + 2-oxoglutarate + O(2) = DNA- CC base + formaldehyde + succinate + CO(2). CC -!- COFACTOR: Binds 1 Fe(2+) ion per subunit. CC -!- ENZYME REGULATION: Activated by magnesium ions. CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- TISSUE SPECIFICITY: Detected in liver, testis and kidney (at CC protein level). Detected in heart and testis. CC -!- DISRUPTION PHENOTYPE: No visible phenotype, and no effect on the CC level of 1-ethenoadenine in genomic DNA in aging mice. In CC contrast, the levels of 1-methyladenine in genomic DNA increase CC over time in aging adults. CC -!- SIMILARITY: Belongs to the alkB family. CC -!- SIMILARITY: Contains 1 Fe2OG dioxygenase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK079195; BAC37576.1; -; mRNA. DR EMBL; BC062188; AAH62188.1; -; mRNA. DR RefSeq; NP_778181.2; NM_175016.2. DR RefSeq; XP_006530352.1; XM_006530289.1. DR RefSeq; XP_006530353.1; XM_006530290.1. DR RefSeq; XP_006530354.1; XM_006530291.1. DR RefSeq; XP_006530355.1; XM_006530292.1. DR UniGene; Mm.332593; -. DR ProteinModelPortal; Q6P6J4; -. DR SMR; Q6P6J4; 35-235. DR STRING; 10090.ENSMUSP00000107898; -. DR PhosphoSite; Q6P6J4; -. DR PRIDE; Q6P6J4; -. DR DNASU; 231642; -. DR Ensembl; ENSMUST00000053657; ENSMUSP00000056043; ENSMUSG00000044339. DR Ensembl; ENSMUST00000112279; ENSMUSP00000107898; ENSMUSG00000044339. DR GeneID; 231642; -. DR KEGG; mmu:231642; -. DR UCSC; uc008yzd.1; mouse. DR CTD; 121642; -. DR MGI; MGI:2141032; Alkbh2. DR eggNOG; COG3145; -. DR GeneTree; ENSGT00530000063618; -. DR HOGENOM; HOG000207105; -. DR HOVERGEN; HBG080832; -. DR InParanoid; Q6P6J4; -. DR KO; K10859; -. DR OMA; HRDDEKE; -. DR OrthoDB; EOG77T159; -. DR TreeFam; TF331732; -. DR NextBio; 380677; -. DR PRO; PR:Q6P6J4; -. DR Bgee; Q6P6J4; -. DR CleanEx; MM_ALKBH2; -. DR Genevestigator; Q6P6J4; -. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0051747; F:cytosine C-5 DNA demethylase activity; ISS:UniProtKB. DR GO; GO:0043734; F:DNA-N1-methyladenine dioxygenase activity; ISS:UniProtKB. DR GO; GO:0008198; F:ferrous iron binding; ISS:UniProtKB. DR GO; GO:0006307; P:DNA dealkylation involved in DNA repair; ISS:UniProtKB. DR GO; GO:0035511; P:oxidative DNA demethylation; ISS:UniProtKB. DR Gene3D; 2.60.120.590; -; 1. DR InterPro; IPR027450; AlkB-like. DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase. DR Pfam; PF13532; 2OG-FeII_Oxy_2; 1. DR PROSITE; PS51471; FE2OG_OXY; 1. PE 1: Evidence at protein level; KW Complete proteome; Dioxygenase; DNA damage; DNA repair; Iron; KW Magnesium; Metal-binding; Nucleus; Oxidoreductase; Reference proteome. FT CHAIN 1 239 Alpha-ketoglutarate-dependent dioxygenase FT alkB homolog 2. FT /FTId=PRO_0000239276. FT DOMAIN 130 235 Fe2OG dioxygenase. FT REGION 80 82 Substrate binding (By similarity). FT REGION 100 102 Substrate binding (By similarity). FT REGION 137 139 Alpha-ketoglutarate binding (By FT similarity). FT REGION 226 232 Alpha-ketoglutarate binding (By FT similarity). FT METAL 149 149 Iron; catalytic (By similarity). FT METAL 151 151 Iron; catalytic (By similarity). FT METAL 214 214 Iron; catalytic (By similarity). FT BINDING 152 152 Substrate (By similarity). FT MUTAGEN 151 151 D->A: Loss of activity. FT MUTAGEN 214 214 H->A: Reduces activity. FT CONFLICT 149 149 H -> Q (in Ref. 1; BAC37576). SQ SEQUENCE 239 AA; 27129 MW; A38259C6B1472095 CRC64; MDKFLVRPDL RDLQGGGEEP APTGGASGDL KSPDWRHLRA EGLSCDYTVL FGKAEADKIF RELEQEVEYF TGALAKVQVF GKWHSVPRKQ ATYGDAGLTY TFSGLTLTPK PWVPVLERVR DRVCEVTGQT FNFVLVNRYK DGCDHIGEHR DDERELAPGS PIASVSFGAC RDFIFRHKDS RGKRPRRTVE VVRLQLAHGS LLMMNPPTNT HWYHSLPIRK RVLAPRVNLT FRKILPTKK // ID ALKB4_MOUSE Reviewed; 300 AA. AC Q9D8F1; Q8R1Y9; DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 19-MAR-2014, entry version 77. DE RecName: Full=Alpha-ketoglutarate-dependent dioxygenase alkB homolog 4; DE EC=1.14.11.-; DE AltName: Full=Alkylated DNA repair protein alkB homolog 4; GN Name=Alkbh4; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC STRAIN=C57BL/6J; TISSUE=Small intestine; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Eye; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP DISRUPTION PHENOTYPE. RX PubMed=23673617; DOI=10.1038/ncomms2863; RA Li M.M., Nilsen A., Shi Y., Fusser M., Ding Y.H., Fu Y., Liu B., RA Niu Y., Wu Y.S., Huang C.M., Olofsson M., Jin K.X., Lv Y., Xu X.Z., RA He C., Dong M.Q., Rendtlew Danielsen J.M., Klungland A., Yang Y.G.; RT "ALKBH4-dependent demethylation of actin regulates actomyosin RT dynamics."; RL Nat. Commun. 4:1832-1832(2013). CC -!- FUNCTION: Dioxygenase that mediates demethylation of actin CC monomethylated at 'Lys-84' (K84me1), thereby acting as a regulator CC of actomyosin-processes. Demethylation of actin K84me1 is required CC for maintaining actomyosin dynamics supporting normal cleavage CC furrow ingression during cytokinesis and cell migration. May be CC involved in transcription regulation (By similarity). CC -!- COFACTOR: Binds 1 Fe(2+) ion per subunit (By similarity). CC -!- SUBUNIT: Interacts with ZFHX3, MLLT3, MLLT1, HSF4, EP300, TES, CC EIF3C, MTMR6 and PSMA6 (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By CC similarity). Midbody (By similarity). Note=Associates with the CC contractile ring and midbody (By similarity). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9D8F1-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9D8F1-2; Sequence=VSP_019129; CC Note=No experimental confirmation available; CC -!- DISRUPTION PHENOTYPE: Embryonic lethality. CC -!- SIMILARITY: Belongs to the alkB family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK008083; BAB25449.1; -; mRNA. DR EMBL; GL456122; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC022729; AAH22729.1; -; mRNA. DR RefSeq; NP_082346.1; NM_028070.1. DR RefSeq; XP_006504565.1; XM_006504502.1. DR RefSeq; XP_006504566.1; XM_006504503.1. DR RefSeq; XP_006504567.1; XM_006504504.1. DR RefSeq; XP_006504568.1; XM_006504505.1. DR UniGene; Mm.486605; -. DR ProteinModelPortal; Q9D8F1; -. DR SMR; Q9D8F1; 68-273. DR PRIDE; Q9D8F1; -. DR Ensembl; ENSMUST00000041100; ENSMUSP00000040403; ENSMUSG00000039754. [Q9D8F1-1] DR Ensembl; ENSMUST00000100568; ENSMUSP00000098134; ENSMUSG00000039754. [Q9D8F1-2] DR GeneID; 72041; -. DR KEGG; mmu:72041; -. DR UCSC; uc009aaa.1; mouse. [Q9D8F1-1] DR CTD; 54784; -. DR MGI; MGI:1919291; Alkbh4. DR eggNOG; NOG255556; -. DR GeneTree; ENSGT00390000006344; -. DR HOGENOM; HOG000015835; -. DR HOVERGEN; HBG062006; -. DR InParanoid; Q9D8F1; -. DR KO; K10766; -. DR OMA; DRDPWKL; -. DR TreeFam; TF314885; -. DR NextBio; 335284; -. DR PRO; PR:Q9D8F1; -. DR ArrayExpress; Q9D8F1; -. DR Bgee; Q9D8F1; -. DR CleanEx; MM_ALKBH4; -. DR Genevestigator; Q9D8F1; -. DR GO; GO:0070938; C:contractile ring; ISS:UniProtKB. DR GO; GO:0030496; C:midbody; ISS:UniProtKB. DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0003779; F:actin binding; ISS:UniProtKB. DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0031032; P:actomyosin structure organization; ISS:UniProtKB. DR GO; GO:0036090; P:cleavage furrow ingression; ISS:UniProtKB. DR GO; GO:0006482; P:protein demethylation; ISS:UniProtKB. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 2.60.120.590; -; 1. DR InterPro; IPR027450; AlkB-like. DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase. DR Pfam; PF03171; 2OG-FeII_Oxy; 1. PE 2: Evidence at transcript level; KW Acetylation; Actin-binding; Alternative splicing; Complete proteome; KW Cytoplasm; Dioxygenase; Iron; Metal-binding; Nucleus; Oxidoreductase; KW Reference proteome; Transcription; Transcription regulation. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 300 Alpha-ketoglutarate-dependent dioxygenase FT alkB homolog 4. FT /FTId=PRO_0000239282. FT METAL 167 167 Iron; catalytic (By similarity). FT METAL 169 169 Iron; catalytic (By similarity). FT METAL 252 252 Iron; catalytic (By similarity). FT BINDING 263 263 2-oxoglutarate (Potential). FT MOD_RES 2 2 N-acetylalanine (By similarity). FT VAR_SEQ 2 85 Missing (in isoform 2). FT /FTId=VSP_019129. SQ SEQUENCE 300 AA; 33394 MW; C19FBBB89095B6ED CRC64; MAAAAEVSLL QECGCKGIRT CLICERQRHR DPPWQICLQK KCCFLYCPDT GWAAGAEGSD LEGWAFPFPG VTLIQDFVTP EEEAEMVRLM DCDPWKLSQS GRKKQDYGPK VNFRKQKLKM AGFQGLPGFS QKVVQRMGLY PGLEDFQPVE QCNLDYSPER GSAIDPHLDD AWLWGERLVS LNLLSATVVS MSPEAPGSLL LCSAPSVRPD AFEDSLVAPS RSVPCQEVEV AITVPRRSLL VLTGAARHQW THAIHRRHIK ARRVCATFRE LSSEFLPGGK QQELGQELLQ AALSFQGRPV // ID ALKB6_MOUSE Reviewed; 238 AA. AC Q8K2U2; G3X994; DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot. DT 18-SEP-2013, sequence version 3. DT 19-FEB-2014, entry version 70. DE RecName: Full=Alpha-ketoglutarate-dependent dioxygenase alkB homolog 6; DE EC=1.14.11.-; DE AltName: Full=Alkylated DNA repair protein alkB homolog 6; GN Name=Alkbh6; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Mammary tumor; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: Probable dioxygenase that requires molecular oxygen, CC alpha-ketoglutarate and iron (By similarity). CC -!- COFACTOR: Binds 1 Fe(2+) ion per subunit (By similarity). CC -!- SUBUNIT: Interacts with VCPKMT (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By CC similarity). CC -!- SIMILARITY: Belongs to the alkB family. CC -!- SIMILARITY: Contains 1 Fe2OG dioxygenase domain. CC -!- SEQUENCE CAUTION: CC Sequence=AAH29805.1; Type=Frameshift; Positions=7, 210, 221, 227, 231; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AC149067; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH466593; EDL24033.1; -; Genomic_DNA. DR EMBL; BC029805; AAH29805.1; ALT_FRAME; mRNA. DR RefSeq; NP_932144.2; NM_198027.2. DR UniGene; Mm.276277; -. DR ProteinModelPortal; Q8K2U2; -. DR STRING; 10090.ENSMUSP00000051515; -. DR PhosphoSite; Q8K2U2; -. DR PaxDb; Q8K2U2; -. DR PRIDE; Q8K2U2; -. DR Ensembl; ENSMUST00000060834; ENSMUSP00000051515; ENSMUSG00000042831. DR GeneID; 233065; -. DR KEGG; mmu:233065; -. DR UCSC; uc009geb.1; mouse. DR CTD; 84964; -. DR MGI; MGI:2142037; Alkbh6. DR eggNOG; NOG254390; -. DR GeneTree; ENSGT00510000048626; -. DR HOGENOM; HOG000210721; -. DR HOVERGEN; HBG056765; -. DR InParanoid; Q8K2U2; -. DR KO; K10768; -. DR OMA; GKTANHV; -. DR OrthoDB; EOG74J98M; -. DR TreeFam; TF314467; -. DR ChiTaRS; ALKBH6; mouse. DR NextBio; 381519; -. DR PRO; PR:Q8K2U2; -. DR CleanEx; MM_ALKBH6; -. DR Genevestigator; Q8K2U2; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR Gene3D; 2.60.120.590; -; 1. DR InterPro; IPR027450; AlkB-like. DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase. DR Pfam; PF13532; 2OG-FeII_Oxy_2; 1. DR PROSITE; PS51471; FE2OG_OXY; 1. PE 2: Evidence at transcript level; KW Complete proteome; Cytoplasm; Dioxygenase; Iron; Metal-binding; KW Nucleus; Oxidoreductase; Reference proteome. FT CHAIN 1 238 Alpha-ketoglutarate-dependent dioxygenase FT alkB homolog 6. FT /FTId=PRO_0000323717. FT DOMAIN 96 227 Fe2OG dioxygenase. FT REGION 103 105 Alpha-ketoglutarate binding (By FT similarity). FT REGION 218 224 Alpha-ketoglutarate binding (By FT similarity). FT METAL 114 114 Iron; catalytic (By similarity). FT METAL 116 116 Iron; catalytic (By similarity). FT METAL 182 182 Iron; catalytic (By similarity). SQ SEQUENCE 238 AA; 26776 MW; E67EA27846A9121D CRC64; MEEQDARVPA LEPFRVEQAP PLIYYVPDFI SKEEEEYLLR QVFNAPKPKW TQLSGRKLQN WGGLPHPRGM VPERLPPWLQ RYVDKVSDLS LFGGLPANHV LVNQYLPGEG IMPHEDGPLY YPTVSTISLG SHTVLDFYEP RQPDDDVPME QPRPPQRPIT SLLVEPRSLL VLRGTAYTRL LHGISATRVD ELDATSLPPN ATACKSALPG AHLVRGTRVS LTIRRVPRVL RASLLLSK // ID ALKB8_MOUSE Reviewed; 664 AA. AC Q80Y20; Q3TUG4; Q8BV08; Q9CX44; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2003, sequence version 1. DT 19-MAR-2014, entry version 90. DE RecName: Full=Alkylated DNA repair protein alkB homolog 8; DE EC=1.14.11.-; DE AltName: Full=Probable alpha-ketoglutarate-dependent dioxygenase ABH8; DE AltName: Full=S-adenosyl-L-methionine-dependent tRNA methyltransferase ABH8; DE AltName: Full=tRNA (carboxymethyluridine(34)-5-O)-methyltransferase ABH8; DE EC=2.1.1.-; DE EC=2.1.1.229; GN Name=Alkbh8; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3). RC STRAIN=C57BL/6J; TISSUE=Head, and Testis; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Embryo; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: Catalyzes the methylation of 5-carboxymethyl uridine to CC 5-methylcarboxymethyl uridine at the wobble position of the CC anticodon loop in tRNA. Catalyzes the last step in the formation CC of 5-methylcarboxymethyl uridine at the wobble position of the CC anticodon loop in target tRNA. Has a preference for tRNA(Arg) and CC tRNA(Glu), and does not bind tRNA(Lys). Required for normal CC survival after DNA damage. May inhibit apoptosis and promote cell CC survival and angiogenesis (By similarity). CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + CC carboxymethyluridine(34) in tRNA = S-adenosyl-L-homocysteine + 5- CC (2-methoxy-2-oxoethyl)uridine(34) in tRNA. CC -!- SUBUNIT: Interacts with TRMT112 (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By CC similarity). Note=Predominantly cytoplasmic (By similarity). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q80Y20-1; Sequence=Displayed; CC Name=2; CC IsoId=Q80Y20-2; Sequence=VSP_033931; CC Note=No experimental confirmation available; CC Name=3; CC IsoId=Q80Y20-3; Sequence=VSP_033929, VSP_033930; CC Note=No experimental confirmation available; CC -!- SIMILARITY: Belongs to the alkB family. CC -!- SIMILARITY: Contains 1 Fe2OG dioxygenase domain. CC -!- SIMILARITY: Contains 1 RRM (RNA recognition motif) domain. CC -!- SEQUENCE CAUTION: CC Sequence=BAC38223.1; Type=Frameshift; Positions=121; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK020197; BAB32026.1; -; mRNA. DR EMBL; AK081459; BAC38223.1; ALT_FRAME; mRNA. DR EMBL; AK160783; BAE36007.1; -; mRNA. DR EMBL; BC050863; AAH50863.1; -; mRNA. DR RefSeq; NP_080579.1; NM_026303.1. DR RefSeq; XP_006509943.1; XM_006509880.1. DR UniGene; Mm.116968; -. DR UniGene; Mm.440994; -. DR ProteinModelPortal; Q80Y20; -. DR SMR; Q80Y20; 23-545. DR PhosphoSite; Q80Y20; -. DR PaxDb; Q80Y20; -. DR PRIDE; Q80Y20; -. DR Ensembl; ENSMUST00000053407; ENSMUSP00000061511; ENSMUSG00000025899. [Q80Y20-1] DR Ensembl; ENSMUST00000165105; ENSMUSP00000125996; ENSMUSG00000025899. [Q80Y20-1] DR GeneID; 67667; -. DR KEGG; mmu:67667; -. DR UCSC; uc009oat.1; mouse. [Q80Y20-1] DR UCSC; uc009oau.1; mouse. [Q80Y20-3] DR UCSC; uc012gnj.1; mouse. [Q80Y20-2] DR CTD; 91801; -. DR MGI; MGI:1914917; Alkbh8. DR eggNOG; COG0500; -. DR GeneTree; ENSGT00530000063536; -. DR HOGENOM; HOG000007984; -. DR HOVERGEN; HBG067234; -. DR InParanoid; Q80Y20; -. DR KO; K10770; -. DR OMA; PCNCSYP; -. DR OrthoDB; EOG780RMC; -. DR TreeFam; TF316056; -. DR NextBio; 325193; -. DR PRO; PR:Q80Y20; -. DR Bgee; Q80Y20; -. DR Genevestigator; Q80Y20; -. DR GO; GO:0005829; C:cytosol; ISS:UniProtKB. DR GO; GO:0015630; C:microtubule cytoskeleton; IEA:Ensembl. DR GO; GO:0005634; C:nucleus; ISS:UniProtKB. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro. DR GO; GO:0016706; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors; IEA:InterPro. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW. DR GO; GO:0016300; F:tRNA (uracil) methyltransferase activity; ISS:UniProtKB. DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB. DR Gene3D; 2.60.120.590; -; 1. DR Gene3D; 3.30.70.330; -; 1. DR InterPro; IPR027450; AlkB-like. DR InterPro; IPR015095; AlkB_hom8_N. DR InterPro; IPR013216; Methyltransf_11. DR InterPro; IPR012677; Nucleotide-bd_a/b_plait. DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase. DR InterPro; IPR000504; RRM_dom. DR Pfam; PF13532; 2OG-FeII_Oxy_2; 1. DR Pfam; PF09004; DUF1891; 1. DR Pfam; PF08241; Methyltransf_11; 1. DR Pfam; PF00076; RRM_1; 1. DR SMART; SM00360; RRM; 1. DR PROSITE; PS51471; FE2OG_OXY; 1. DR PROSITE; PS50102; RRM; 1. PE 2: Evidence at transcript level; KW Alternative splicing; Complete proteome; Cytoplasm; Iron; KW Metal-binding; Methyltransferase; Multifunctional enzyme; Nucleus; KW Oxidoreductase; Reference proteome; RNA-binding; KW S-adenosyl-L-methionine; Transferase. FT CHAIN 1 664 Alkylated DNA repair protein alkB homolog FT 8. FT /FTId=PRO_0000337127. FT DOMAIN 45 120 RRM. FT DOMAIN 220 337 Fe2OG dioxygenase. FT REGION 227 229 Alpha-ketoglutarate binding (By FT similarity). FT REGION 328 334 Alpha-ketoglutarate binding (By FT similarity). FT REGION 411 664 Methyltransferase domain (By similarity). FT METAL 238 238 Iron; catalytic (By similarity). FT METAL 240 240 Iron; catalytic (By similarity). FT METAL 292 292 Iron; catalytic (By similarity). FT VAR_SEQ 123 169 AQWKNMGLEALPPGLLVVEEIISSEEEKKLLESVNWTEDTG FT NQNFQR -> GTLTLASFNLLFLCEFSSYRESLSIILYVWE FT VCAGVLDHAVPVGVKG (in isoform 3). FT /FTId=VSP_033929. FT VAR_SEQ 170 664 Missing (in isoform 3). FT /FTId=VSP_033930. FT VAR_SEQ 199 233 Missing (in isoform 2). FT /FTId=VSP_033931. FT CONFLICT 88 88 Q -> H (in Ref. 1; BAC38223). FT CONFLICT 132 132 A -> T (in Ref. 1; BAC38223). FT CONFLICT 151 151 K -> R (in Ref. 1; BAC38223). SQ SEQUENCE 664 AA; 74768 MW; 624A9F48768A903E CRC64; MNINHKGVLK LTKMEKKFLR KQSKARHVLL KHEGIQAVSY PTQSLVIANG GLGNGVSRKQ LLLTLEKCGP VEALLMPPNK PYAFVIFQTI EESKKAYFTL NGKEIIDDLG QKIFLYLNFV EKAQWKNMGL EALPPGLLVV EEIISSEEEK KLLESVNWTE DTGNQNFQRS LKHRRVKHFG YEFHYESNTV DKDKPLPGGL PEVCSSILEK LLKEGYIKHK PDQLTINQYE PGHGIPAHID THSAFEDEII SLSLGSAIVM DFKHPEGVTV QVMLPRRSLL VMTGESRYLW THGITPRKFD TVQASEQFKG GIITSDIGDL TLSKRGMRTS FTFRKVRRMP CNCSYSSVCD RQRKATPPSL TESSKEALEL EQKHVHQVYN EIASHFSSTR HSPWPRIVEF LKALPSGSIV ADIGCGNGKY LGINKDLYMI GCDRSQNLVD ICRERQFQAL VCDALAVPVR SGSCDACISI AVIHHFATAE RRVEALQELA RLLRPGGQAL IYVWAMEQEY KNQKSKYLRG KRISQGDKDE LNSATSTEEF LVNQTPEGVN EDPALSVNSS SITKEEEYKS RKVPNSELPI HINRTCFHSQ DVLVPWHLKR NPGKDKAIEP SGVAGCPDPS PVFHRYYHVF CDGELEASCQ AVGDVSILQS YYDQGNWCVV LQKV // ID ALKB7_MOUSE Reviewed; 221 AA. AC Q9D6Z0; Q8K1H3; Q9CY41; Q9D942; DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 19-MAR-2014, entry version 76. DE RecName: Full=Alpha-ketoglutarate-dependent dioxygenase alkB homolog 7, mitochondrial; DE EC=1.14.11.-; DE AltName: Full=Alkylated DNA repair protein alkB homolog 7; DE Flags: Precursor; GN Name=Alkbh7; Synonyms=Spata11; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC STRAIN=C57BL/6J; TISSUE=Liver, Pancreas, and Tongue; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4-221 (ISOFORM 1). RC TISSUE=Eye; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND TISSUE RP SPECIFICITY. RX PubMed=23572141; DOI=10.1093/jmcb/mjt012; RA Solberg A., Robertson A.B., Aronsen J.M., Rognmo O., Sjaastad I., RA Wisloff U., Klungland A.; RT "Deletion of mouse Alkbh7 leads to obesity."; RL J. Mol. Cell Biol. 5:194-203(2013). CC -!- FUNCTION: Probable dioxygenase required to induce programmed CC necrosis in response to DNA damage caused by cytotoxic alkylating CC agents. Acts by triggering the collapse of mitochondrial membrane CC potential and loss of mitochondrial function that leads to energy CC depletion and cell death. ALKBH7-mediated necrosis is probably CC required to prevent the accumulation of cells with DNA damage. CC Does not display DNA demethylase activity (By similarity). CC Involved in fatty acid metabolism. CC -!- COFACTOR: Binds 1 Fe(2+) ion per subunit (By similarity). CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9D6Z0-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9D6Z0-2; Sequence=VSP_019132; CC Note=No experimental confirmation available; CC -!- TISSUE SPECIFICITY: Widely expressed. CC -!- DISRUPTION PHENOTYPE: Increased body weight and body fat, a CC phenotype amplified under high-fat diet. CC -!- SIMILARITY: Belongs to the alkB family. CC -!- SEQUENCE CAUTION: CC Sequence=AAH29677.1; Type=Erroneous initiation; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK007380; BAB24999.1; -; mRNA. DR EMBL; AK009812; BAB26517.1; -; mRNA. DR EMBL; AK010930; BAB27274.1; -; mRNA. DR EMBL; GL456179; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC029677; AAH29677.1; ALT_INIT; mRNA. DR RefSeq; NP_079814.1; NM_025538.3. DR RefSeq; NP_081648.1; NM_027372.1. DR UniGene; Mm.196150; -. DR ProteinModelPortal; Q9D6Z0; -. DR STRING; 10090.ENSMUSP00000002737; -. DR PaxDb; Q9D6Z0; -. DR PRIDE; Q9D6Z0; -. DR Ensembl; ENSMUST00000002737; ENSMUSP00000002737; ENSMUSG00000002661. [Q9D6Z0-1] DR Ensembl; ENSMUST00000074141; ENSMUSP00000073775; ENSMUSG00000002661. [Q9D6Z0-2] DR GeneID; 66400; -. DR KEGG; mmu:66400; -. DR UCSC; uc008ddn.2; mouse. [Q9D6Z0-1] DR UCSC; uc012avz.1; mouse. [Q9D6Z0-2] DR CTD; 84266; -. DR MGI; MGI:1913650; Alkbh7. DR eggNOG; NOG299394; -. DR GeneTree; ENSGT00390000014585; -. DR HOGENOM; HOG000018442; -. DR HOVERGEN; HBG054357; -. DR InParanoid; Q9D6Z0; -. DR KO; K10769; -. DR OMA; DGVIKPH; -. DR OrthoDB; EOG7M0NT9; -. DR TreeFam; TF314197; -. DR NextBio; 321567; -. DR PRO; PR:Q9D6Z0; -. DR Bgee; Q9D6Z0; -. DR CleanEx; MM_ALKBH7; -. DR Genevestigator; Q9D6Z0; -. DR GO; GO:0005759; C:mitochondrial matrix; IDA:UniProtKB. DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB. DR GO; GO:0006631; P:fatty acid metabolic process; IMP:UniProtKB. DR GO; GO:0070265; P:necrotic cell death; ISS:UniProtKB. DR GO; GO:0012501; P:programmed cell death; IEA:UniProtKB-KW. DR GO; GO:0010883; P:regulation of lipid storage; IMP:UniProtKB. DR Gene3D; 2.60.120.590; -; 1. DR InterPro; IPR027450; AlkB-like. DR Pfam; PF13532; 2OG-FeII_Oxy_2; 1. PE 2: Evidence at transcript level; KW Alternative splicing; Complete proteome; Dioxygenase; Iron; KW Metal-binding; Mitochondrion; Necrosis; Oxidoreductase; KW Reference proteome; Transit peptide. FT TRANSIT 1 23 Mitochondrion (Potential). FT CHAIN 24 221 Alpha-ketoglutarate-dependent dioxygenase FT alkB homolog 7, mitochondrial. FT /FTId=PRO_0000239289. FT METAL 121 121 Iron; catalytic (By similarity). FT METAL 123 123 Iron; catalytic (By similarity). FT METAL 177 177 Iron; catalytic (By similarity). FT BINDING 197 197 2-oxoglutarate (Potential). FT VAR_SEQ 69 126 Missing (in isoform 2). FT /FTId=VSP_019132. FT CONFLICT 191 191 R -> L (in Ref. 1; BAB24999). SQ SEQUENCE 221 AA; 24970 MW; 7961509733692740 CRC64; MAGSRRLAMR LLSGCAWVRG SDSAVLGRLR DEAVVHPGFL SQEEEDTLTR ELEPQLRRRR YEYDHWDAAI HGFRETEKSC WSDASQVILQ RVRAAAFGPD QSLLSPVHVL DLEPRGYIKP HVDSVKFCGS TIAGLSLLSP SVMKLVHTQE PEQWLELLLE PGSLYILRGS ARYDFSHEIL RDEESFFGEH RVPRGRRISV ICRSLPEGMG PGRPEEPPPA C // ID ALKB1_MOUSE Reviewed; 389 AA. AC P0CB42; DT 13-OCT-2009, integrated into UniProtKB/Swiss-Prot. DT 13-OCT-2009, sequence version 1. DT 19-MAR-2014, entry version 38. DE RecName: Full=Alkylated DNA repair protein alkB homolog 1; DE EC=1.14.11.33; DE AltName: Full=Alpha-ketoglutarate-dependent dioxygenase ABH1; DE AltName: Full=DNA lyase ABH1; DE EC=4.2.99.18; DE AltName: Full=DNA oxidative demethylase ALKBH1; GN Name=Alkbh1; Synonyms=Abh, Alkbh; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [2] RP FUNCTION, INTERACTION WITH DNAJB6, SUBCELLULAR LOCATION, DEVELOPMENTAL RP STAGE, AND DISRUPTION PHENOTYPE. RX PubMed=18163532; DOI=10.1002/dvdy.21418; RA Pan Z., Sikandar S., Witherspoon M., Dizon D., Nguyen T., RA Benirschke K., Wiley C., Vrana P., Lipkin S.M.; RT "Impaired placental trophoblast lineage differentiation in Alkbh1(-/-) RT mice."; RL Dev. Dyn. 237:316-327(2008). CC -!- FUNCTION: Dioxygenase that repairs alkylated single-stranded DNA CC and RNA containing 3-methylcytosine by oxidative demethylation. CC Requires molecular oxygen, alpha-ketoglutarate and iron. Has DNA CC lyase activity and introduces double-stranded breaks at abasic CC sites. Cleaves both single-stranded DNA and double-stranded DNA at CC abasic sites, with the greatest activity towards double-stranded CC DNA with two abasic sites. DNA lyase activity does not require CC alpha-ketoglutarate and iron (By similarity). May have a role in CC placental trophoblast lineage differentiation. CC -!- CATALYTIC ACTIVITY: The C-O-P bond 3' to the apurinic or CC apyrimidinic site in DNA is broken by a beta-elimination reaction, CC leaving a 3'-terminal unsaturated sugar and a product with a CC terminal 5'-phosphate. CC -!- CATALYTIC ACTIVITY: DNA-base-CH(3) + 2-oxoglutarate + O(2) = DNA- CC base + formaldehyde + succinate + CO(2). CC -!- COFACTOR: Binds 1 Fe(2+) ion per subunit. CC -!- SUBUNIT: Monomer (By similarity). Interacts with DNAJB6. CC -!- SUBCELLULAR LOCATION: Nucleus. Mitochondrion (By similarity). CC Note=Mainly localizes in euchromatin, largely excluded from CC heterochromatin and nucleoli. CC -!- DEVELOPMENTAL STAGE: At E8.5 is highly expressed in the chorion CC and the ectoplacental cone. At E10.5 is highly expressed in CC multiple trophoblast lineages (spongiotrophoblasts, giant cell CC trophoblasts, glycogen cells, and labyrinthine trophoblasts). The CC highest placental level is at E9.5 and subsequently decreases CC until parturition. CC -!- DISRUPTION PHENOTYPE: Intrauterine growth retardation and CC placental defects. Fertile. Altered expression of trophoblast CC lineage-specific genes. CC -!- SIMILARITY: Contains 1 Fe2OG dioxygenase domain. CC -!- CAUTION: Localizes to the nucleus when expressed as fusion protein CC with an N-terminal tag (PubMed:18163532). Experiments with the CC human protein show that the endogenous, unmodified protein CC localizes to mitochondria (PubMed:18603530), but that a fusion CC protein with an N-terminal tag is localized in cytoplasm and CC nucleus (PubMed:18603530). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CT030249; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; NP_001096035.1; NM_001102565.1. DR UniGene; Mm.486235; -. DR ProteinModelPortal; P0CB42; -. DR SMR; P0CB42; 96-346. DR STRING; 10090.ENSMUSP00000105782; -. DR PRIDE; P0CB42; -. DR Ensembl; ENSMUST00000162961; ENSMUSP00000124565; ENSMUSG00000079036. DR GeneID; 211064; -. DR KEGG; mmu:211064; -. DR UCSC; uc007oix.1; mouse. DR CTD; 8846; -. DR MGI; MGI:2384034; Alkbh1. DR eggNOG; COG3145; -. DR GeneTree; ENSGT00390000004599; -. DR HOGENOM; HOG000033905; -. DR KO; K10765; -. DR OMA; KKYSADH; -. DR OrthoDB; EOG71P2CK; -. DR TreeFam; TF314609; -. DR ChiTaRS; ALKBH1; mouse. DR NextBio; 373138; -. DR PRO; PR:P0CB42; -. DR ArrayExpress; P0CB42; -. DR Bgee; P0CB42; -. DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB. DR GO; GO:0005719; C:nuclear euchromatin; IDA:MGI. DR GO; GO:0042056; F:chemoattractant activity; IDA:MGI. DR GO; GO:0003906; F:DNA-(apurinic or apyrimidinic site) lyase activity; ISS:UniProtKB. DR GO; GO:0008198; F:ferrous iron binding; ISS:UniProtKB. DR GO; GO:0070579; F:methylcytosine dioxygenase activity; ISS:UniProtKB. DR GO; GO:0048589; P:developmental growth; IMP:MGI. DR GO; GO:0006307; P:DNA dealkylation involved in DNA repair; ISS:UniProtKB. DR GO; GO:0080111; P:DNA demethylation; ISS:UniProtKB. DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI. DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IDA:MGI. DR GO; GO:0001764; P:neuron migration; IDA:MGI. DR GO; GO:0031175; P:neuron projection development; IDA:MGI. DR GO; GO:0070989; P:oxidative demethylation; ISS:UniProtKB. DR GO; GO:0001890; P:placenta development; IMP:MGI. DR GO; GO:0042245; P:RNA repair; ISS:UniProtKB. DR Gene3D; 2.60.120.590; -; 2. DR InterPro; IPR004574; Alkb. DR InterPro; IPR027450; AlkB-like. DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase. DR Pfam; PF13532; 2OG-FeII_Oxy_2; 1. DR TIGRFAMs; TIGR00568; alkb; 1. DR PROSITE; PS51471; FE2OG_OXY; 1. PE 1: Evidence at protein level; KW Complete proteome; Dioxygenase; DNA damage; DNA repair; Iron; Lyase; KW Metal-binding; Mitochondrion; Multifunctional enzyme; Nucleus; KW Oxidoreductase; Reference proteome; RNA repair. FT CHAIN 1 389 Alkylated DNA repair protein alkB homolog FT 1. FT /FTId=PRO_0000386453. FT DOMAIN 213 347 Fe2OG dioxygenase. FT REGION 1 127 Interaction with DNAJB6. FT REGION 177 179 Substrate binding (By similarity). FT REGION 220 222 Alpha-ketoglutarate binding (By FT similarity). FT REGION 338 344 Alpha-ketoglutarate binding (By FT similarity). FT METAL 231 231 Iron; catalytic (By similarity). FT METAL 233 233 Iron; catalytic (By similarity). FT METAL 287 287 Iron; catalytic (By similarity). FT BINDING 170 170 Substrate (By similarity). FT BINDING 261 261 Substrate (By similarity). SQ SEQUENCE 389 AA; 43746 MW; D18C019F0CB9C0A5 CRC64; MGKMAAAVAS LATLAAEPRE DAFRKLFRFY RQSRPGTADL GAVIDFSEAH LARSPKPGVP QVVRFPLNVS SVTERDAERV GLEPVSKWRA YGLEGYPGFI FIPNPFLPGC QRHWVKQCLK LYSQKPNVCN LDKHMTKEET QGLWEQSKEV LRSKEVTKRR PRSLLERLRW VTLGYHYNWD SKKYSADHYT PFPSDLAFLS EQVATACGFQ GFQAEAGILN YYRLDSTLGI HVDRSELDHS KPLLSFSFGQ SAIFLLGGLK RDEAPTAMFM HSGDIMVMSG FSRLLNHAVP RVLPHPDGEC LPHCLETPLP AVLPSNSLVE PCSVEDWQVC ATYLRTARVN MTVRQVLATG QDFPLEPVEE TKRDIAADGL CHLHDPNSPV KRKRLNPNS // ID ALKMO_MOUSE Reviewed; 447 AA. AC Q8BS35; Q3TR15; Q8C7H5; Q8CAA6; DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 19-MAR-2014, entry version 77. DE RecName: Full=Alkylglycerol monooxygenase; DE EC=1.14.16.5; DE AltName: Full=Transmembrane protein 195; GN Name=Agmo; Synonyms=Tmem195; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 10-447 (ISOFORM 3). RC STRAIN=C57BL/6J; RC TISSUE=Aorta, Cerebellum, Hypothalamus, Liver, and Vein; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP TISSUE SPECIFICITY. RX PubMed=20643956; DOI=10.1073/pnas.1002404107; RA Watschinger K., Keller M.A., Golderer G., Hermann M., Maglione M., RA Sarg B., Lindner H.H., Hermetter A., Werner-Felmayer G., Konrat R., RA Hulo N., Werner E.R.; RT "Identification of the gene encoding alkylglycerol monooxygenase RT defines a third class of tetrahydrobiopterin-dependent enzymes."; RL Proc. Natl. Acad. Sci. U.S.A. 107:13672-13677(2010). CC -!- FUNCTION: Glyceryl-ether monooxygenase that cleaves the O-alkyl CC bond of ether lipids. Ether lipids are essential components of CC brain membranes (By similarity). CC -!- CATALYTIC ACTIVITY: 1-alkyl-sn-glycerol + tetrahydrobiopterin + CC O(2) = 1-O-alkyl-sn-glycerol + dihydrobiopterin + H(2)O. CC -!- COFACTOR: Iron (By similarity). CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass CC membrane protein (By similarity). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q8BS35-1; Sequence=Displayed; CC Name=2; CC IsoId=Q8BS35-2; Sequence=VSP_027599; CC Note=May be produced at very low levels due to a premature stop CC codon in the mRNA, leading to nonsense-mediated mRNA decay. No CC experimental confirmation available; CC Name=3; CC IsoId=Q8BS35-3; Sequence=VSP_027600; CC Note=No experimental confirmation available; CC -!- TISSUE SPECIFICITY: Highly expressed in lever and small intestine. CC -!- SIMILARITY: Belongs to the sterol desaturase family. TMEM195 CC subfamily. CC -!- SEQUENCE CAUTION: CC Sequence=BAC30271.1; Type=Erroneous initiation; CC Sequence=BAC34143.1; Type=Miscellaneous discrepancy; Note=Intron retention; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK039191; BAC30271.1; ALT_INIT; mRNA. DR EMBL; AK040702; BAC30675.1; -; mRNA. DR EMBL; AK050246; BAC34143.1; ALT_SEQ; mRNA. DR EMBL; AK163155; BAE37216.1; -; mRNA. DR RefSeq; NP_848882.2; NM_178767.5. DR RefSeq; XP_006515177.1; XM_006515114.1. DR UniGene; Mm.485540; -. DR PaxDb; Q8BS35; -. DR PRIDE; Q8BS35; -. DR DNASU; 319660; -. DR Ensembl; ENSMUST00000049874; ENSMUSP00000051441; ENSMUSG00000050103. [Q8BS35-1] DR Ensembl; ENSMUST00000159998; ENSMUSP00000123801; ENSMUSG00000050103. [Q8BS35-2] DR Ensembl; ENSMUST00000160390; ENSMUSP00000125639; ENSMUSG00000050103. [Q8BS35-3] DR GeneID; 319660; -. DR KEGG; mmu:319660; -. DR UCSC; uc007nkg.1; mouse. [Q8BS35-1] DR CTD; 392636; -. DR MGI; MGI:2442495; Agmo. DR eggNOG; COG3000; -. DR GeneTree; ENSGT00440000033807; -. DR HOVERGEN; HBG097659; -. DR InParanoid; Q8BS35; -. DR KO; K15537; -. DR OMA; QGFRMLF; -. DR OrthoDB; EOG7HQN81; -. DR TreeFam; TF314881; -. DR NextBio; 395170; -. DR PRO; PR:Q8BS35; -. DR ArrayExpress; Q8BS35; -. DR Bgee; Q8BS35; -. DR CleanEx; MM_TMEM195; -. DR Genevestigator; Q8BS35; -. DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0050479; F:glyceryl-ether monooxygenase activity; ISS:UniProtKB. DR GO; GO:0005506; F:iron ion binding; ISS:UniProtKB. DR GO; GO:0046485; P:ether lipid metabolic process; ISS:UniProtKB. DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro. DR GO; GO:0006643; P:membrane lipid metabolic process; ISS:UniProtKB. DR InterPro; IPR006694; Fatty_acid_hydroxylase. DR Pfam; PF04116; FA_hydroxylase; 1. PE 2: Evidence at transcript level; KW Alternative splicing; Complete proteome; Endoplasmic reticulum; Iron; KW Membrane; Oxidoreductase; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 447 Alkylglycerol monooxygenase. FT /FTId=PRO_0000299301. FT TRANSMEM 43 63 Helical; (Potential). FT TRANSMEM 111 131 Helical; (Potential). FT TRANSMEM 170 190 Helical; (Potential). FT TRANSMEM 340 360 Helical; (Potential). FT TRANSMEM 363 383 Helical; (Potential). FT TRANSMEM 413 433 Helical; (Potential). FT MOTIF 132 136 Histidine box-1. FT MOTIF 145 149 Histidine box-2. FT MOTIF 221 225 Histidine box-3. FT VAR_SEQ 422 447 IFFSVCIAFWGVRSITQLTSGSWKKP -> IPQLSVLTFVV FT T (in isoform 2). FT /FTId=VSP_027599. FT VAR_SEQ 422 447 IFFSVCIAFWGVRSITQLTSGSWKKP -> GWCTEVWSSAL FT PPS (in isoform 3). FT /FTId=VSP_027600. SQ SEQUENCE 447 AA; 51778 MW; 6712E58FC3FD18FD CRC64; MRSPGAQDNV SVSQGMRAMF YMMEPSETAF QTVEEVPDYV KKATPFFIFL ILLELVISWI LKGKPSGRLD DALTSISAGV VSRLPSLFFR SLEVTSYIYI WENYRLLELP WDSTWTWYFT FLGVDFGYYW FHRMAHEINI FWAAHQAHHS SEDYNLSTAL RQSVLQQYSS WVFYCPLALF IPPSVFAVHI QFNLLYQFWI HTEIIRTLGP LEVILNTPSH HRVHHGRNRY CIDKNYAGTL IIWDRIFGTF EAENEQVIYG LTHPIGTFEP FNVQFHHLLY IWTTFWTTPG FCHKFSVLFK GPGWGPGKPR LGLSEEIPEV TGQEVPFSSS ASQLLKIYTV LQFAVMLAFY EETFANTAVL SQVTLLLRIF FFILTLTSIG FLLDQRSKAA TMETFRCLLF LTLHRFGHLK PLIPSLSFAF EIFFSVCIAF WGVRSITQLT SGSWKKP // ID ALOX8_MOUSE Reviewed; 677 AA. AC O35936; B1ASX5; DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1998, sequence version 1. DT 19-FEB-2014, entry version 123. DE RecName: Full=Arachidonate 8S-lipoxygenase; DE Short=8-LOX; DE Short=8S-LOX; DE EC=1.13.11.-; DE AltName: Full=15-lipoxygenase 2; DE Short=15-LOX-2; DE AltName: Full=Arachidonate 15-lipoxygenase B; DE Short=15-LOX-B; GN Name=Alox8; Synonyms=Alox15b; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION IN ARACHIDONATE AND LINOLEATE RP METABOLISM, INDUCTION BY PHORBOL ESTER, AND TISSUE SPECIFICITY. RC TISSUE=Epidermis; RX PubMed=9305900; DOI=10.1074/jbc.272.39.24410; RA Jisaka M., Kim R.B., Boeglin W.E., Nanney L.B., Brash A.R.; RT "Molecular cloning and functional expression of a phorbol ester- RT inducible 8S-lipoxygenase from mouse skin."; RL J. Biol. Chem. 272:24410-24416(1997). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY. RC STRAIN=NMRI; TISSUE=Epidermis; RX PubMed=9518531; DOI=10.1016/S0005-2760(97)00214-2; RA Krieg P., Kinzig A., Heidt M., Marks F., Fuerstenberger G.; RT "cDNA cloning of a 8-lipoxygenase and a novel epidermis-type RT lipoxygenase from phorbol ester-treated mouse skin."; RL Biochim. Biophys. Acta 1391:7-12(1998). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Skin; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Kidney; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP FUNCTION IN KERATINOCYTE DIFFERENTIATION. RX PubMed=10965849; RA Muga S.J., Thuillier P., Pavone A., Rundhaug J.E., Boeglin W.E., RA Jisaka M., Brash A.R., Fischer S.M.; RT "8S-lipoxygenase products activate peroxisome proliferator-activated RT receptor alpha and induce differentiation in murine keratinocytes."; RL Cell Growth Differ. 11:447-454(2000). RN [7] RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF TYR-603 AND HIS-604. RX PubMed=10625675; DOI=10.1074/jbc.275.2.1287; RA Jisaka M., Kim R.B., Boeglin W.E., Brash A.R.; RT "Identification of amino acid determinants of the positional RT specificity of mouse 8S-lipoxygenase and human 15S-lipoxygenase-2."; RL J. Biol. Chem. 275:1287-1293(2000). RN [8] RP MUTAGENESIS OF SER-558. RX PubMed=11368335; DOI=10.1006/abbi.2000.2175; RA Jisaka M., Boeglin W.E., Kim R.B., Brash A.R.; RT "Site-directed mutagenesis studies on a putative fifth iron ligand of RT mouse 8S-lipoxygenase: retention of catalytic activity on mutation of RT serine-558 to asparagine, histidine, or alanine."; RL Arch. Biochem. Biophys. 386:136-142(2001). RN [9] RP FUNCTION AS A 8S-LIPOXYGENASE, CATALYTIC ACTIVITY, AND MUTAGENESIS OF RP HIS-374. RX PubMed=16143298; DOI=10.1016/j.bbrc.2005.08.099; RA Kawajiri H., Piao Y., Takahashi Y., Murakami T., Hamanaka N., RA Yoshimoto T.; RT "Synthesis of 8,9-leukotriene A4 by murine 8-lipoxygenase."; RL Biochem. Biophys. Res. Commun. 338:144-148(2005). RN [10] RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND KINETIC RP PARAMETERS. RX PubMed=16112079; DOI=10.1016/j.bbrc.2005.08.029; RA Jisaka M., Iwanaga C., Takahashi N., Goto T., Kawada T., Yamamoto T., RA Ikeda I., Nishimura K., Nagaya T., Fushiki T., Yokota K.; RT "Double dioxygenation by mouse 8S-lipoxygenase: specific formation of RT a potent peroxisome proliferator-activated receptor alpha agonist."; RL Biochem. Biophys. Res. Commun. 338:136-143(2005). CC -!- FUNCTION: Non-heme iron-containing dioxygenase that catalyzes the CC stereo-specific peroxidation of free and esterified CC polyunsaturated fatty acids generating a spectrum of bioactive CC lipid mediators. Catalyzes the peroxidation of arachidonate and CC linoleate into (8S)-HPETE and (9S)-HPODE respectively. From CC arachidonate mainly produces (8S)-HPETE and in addition, minor CC products derived from (8S)-HPETE itself that may include CC leukotriene A4 and 8,15-diHPETE. With arachidonate as substrate, CC has no detectable 15S-lipoxygenase activity and only displays a CC 8S-lipoxygenase activity. However, it may have a 15S-lipoxygenase CC activity with (8S)-HPETE to produce (8S,15S)-diHPETE. May also CC catalyze (15S)-HPETE peroxidation to produce 8,15-diHPETE. May CC play a role in keratinocyte differentiation through activation of CC the peroxisome proliferator activated receptor signaling pathway. CC -!- CATALYTIC ACTIVITY: Arachidonate + O(2) = (5Z,9E,11Z,14Z)-8- CC hydroperoxyicosa-5,9,11,14-tetraenoate. CC -!- COFACTOR: Binds 1 iron ion per subunit (By similarity). CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=1.2 uM for arachidonate (at pH 7.4 and 25 degrees Celsius); CC KM=2.1 uM for (8S)-HPETE (at pH 7.4 and 25 degrees Celsius); CC KM=5.7 uM for (8S)-HETE (at pH 7.4 and 25 degrees Celsius); CC KM=39 uM for (15S)-HPETE (at pH 7.4 and 25 degrees Celsius); CC KM=15 uM for (15S)-HETE (at pH 7.4 and 25 degrees Celsius); CC Note=The highest catalytic efficiency is observed with CC arachidonate followed by (8S)-HPETE and(15S)-HPETE with similar CC efficiencies; CC -!- PATHWAY: Lipid metabolism; hydroperoxy eicosatetraenoic acid CC biosynthesis. CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol (By similarity). CC -!- TISSUE SPECIFICITY: Expressed in epidermis and brain. No CC expression found in heart, spleen, liver, skeletal muscle, kidney CC or testis. CC -!- INDUCTION: By phorbol ester. CC -!- SIMILARITY: Belongs to the lipoxygenase family. CC -!- SIMILARITY: Contains 1 lipoxygenase domain. CC -!- SIMILARITY: Contains 1 PLAT domain. CC -!- CAUTION: Despite its homology with human ALOX15B (AC O15296), it CC seems not to have any 15S-lipoxygenase activity on arachidonate. CC Based on its catalytic activity it is referred to as the mouse CC arachidonate 8S-lipoxygenase. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U93277; AAC53356.1; -; mRNA. DR EMBL; Y14696; CAA75003.1; -; mRNA. DR EMBL; AK028724; BAC26085.1; -; mRNA. DR EMBL; AL645527; CAI35251.1; -; Genomic_DNA. DR EMBL; BC015253; AAH15253.1; -; mRNA. DR RefSeq; NP_033791.1; NM_009661.4. DR UniGene; Mm.289672; -. DR ProteinModelPortal; O35936; -. DR SMR; O35936; 6-677. DR PhosphoSite; O35936; -. DR PaxDb; O35936; -. DR PRIDE; O35936; -. DR Ensembl; ENSMUST00000021262; ENSMUSP00000021262; ENSMUSG00000020891. DR GeneID; 11688; -. DR KEGG; mmu:11688; -. DR UCSC; uc007jpl.1; mouse. DR CTD; 11688; -. DR MGI; MGI:1098228; Alox8. DR eggNOG; NOG69653; -. DR GeneTree; ENSGT00550000074415; -. DR HOGENOM; HOG000234358; -. DR HOVERGEN; HBG005150; -. DR InParanoid; B1ASX5; -. DR KO; K08022; -. DR OMA; IQTNVIN; -. DR OrthoDB; EOG7B05CG; -. DR TreeFam; TF105320; -. DR UniPathway; UPA00881; -. DR NextBio; 279335; -. DR PRO; PR:O35936; -. DR ArrayExpress; O35936; -. DR Bgee; O35936; -. DR CleanEx; MM_ALOX8; -. DR Genevestigator; O35936; -. DR GO; GO:0005856; C:cytoskeleton; IEA:Ensembl. DR GO; GO:0005829; C:cytosol; ISS:UniProtKB. DR GO; GO:0005634; C:nucleus; IEA:Ensembl. DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl. DR GO; GO:0050473; F:arachidonate 15-lipoxygenase activity; IEA:Ensembl. DR GO; GO:0036403; F:arachidonate 8(S)-lipoxygenase activity; IDA:UniProtKB. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0016165; F:linoleate 13S-lipoxygenase activity; IEA:Ensembl. DR GO; GO:0019369; P:arachidonic acid metabolic process; IDA:UniProtKB. DR GO; GO:0043651; P:linoleic acid metabolic process; IDA:UniProtKB. DR GO; GO:0019372; P:lipoxygenase pathway; IDA:UniProtKB. DR GO; GO:0045786; P:negative regulation of cell cycle; IEA:Ensembl. DR GO; GO:0008285; P:negative regulation of cell proliferation; IEA:Ensembl. DR GO; GO:0045926; P:negative regulation of growth; IEA:Ensembl. DR GO; GO:0090197; P:positive regulation of chemokine secretion; IEA:Ensembl. DR GO; GO:0045618; P:positive regulation of keratinocyte differentiation; IMP:UniProtKB. DR GO; GO:0010744; P:positive regulation of macrophage derived foam cell differentiation; IEA:Ensembl. DR GO; GO:0035360; P:positive regulation of peroxisome proliferator activated receptor signaling pathway; IMP:UniProtKB. DR Gene3D; 2.60.60.20; -; 1. DR InterPro; IPR008976; Lipase_LipOase. DR InterPro; IPR000907; LipOase. DR InterPro; IPR013819; LipOase_C. DR InterPro; IPR020834; LipOase_CS. DR InterPro; IPR020833; LipOase_Fe_BS. DR InterPro; IPR001885; LipOase_mml. DR InterPro; IPR001024; PLAT/LH2_dom. DR PANTHER; PTHR11771; PTHR11771; 1. DR Pfam; PF00305; Lipoxygenase; 1. DR Pfam; PF01477; PLAT; 1. DR PRINTS; PR00087; LIPOXYGENASE. DR PRINTS; PR00467; MAMLPOXGNASE. DR SMART; SM00308; LH2; 1. DR SUPFAM; SSF48484; SSF48484; 1. DR SUPFAM; SSF49723; SSF49723; 1. DR PROSITE; PS00711; LIPOXYGENASE_1; 1. DR PROSITE; PS00081; LIPOXYGENASE_2; 1. DR PROSITE; PS51393; LIPOXYGENASE_3; 1. DR PROSITE; PS50095; PLAT; 1. PE 1: Evidence at protein level; KW Complete proteome; Cytoplasm; Dioxygenase; Iron; Metal-binding; KW Oxidoreductase; Polymorphism; Reference proteome. FT CHAIN 1 677 Arachidonate 8S-lipoxygenase. FT /FTId=PRO_0000220701. FT DOMAIN 2 125 PLAT. FT DOMAIN 126 677 Lipoxygenase. FT METAL 374 374 Iron; catalytic (By similarity). FT METAL 379 379 Iron; catalytic (By similarity). FT METAL 554 554 Iron; catalytic (By similarity). FT METAL 677 677 Iron; via carboxylate; catalytic (By FT similarity). FT VARIANT 32 32 E -> G (in clone K12). FT VARIANT 38 38 L -> M (in clone G2). FT VARIANT 58 58 P -> R (in clone K12). FT VARIANT 76 76 V -> A (in clones G2, G5, G11 and K1). FT VARIANT 413 413 I -> V (in clone K7). FT VARIANT 536 536 R -> Q (in clones G2, G5 and G11). FT MUTAGEN 374 374 H->L: Loss of enzymatic activity. FT MUTAGEN 558 558 S->A,H,N: Retains catalytic activity FT indicating it is not required for iron FT ligand-binding. FT MUTAGEN 603 603 Y->D: Changes the stereoselectivity of FT the oxygenation reaction to produce FT (15S)-HPETE instead of (8S)-HPETE. FT Completely changes the stereoselectivity; FT when associated with V-604. FT MUTAGEN 604 604 H->V: Changes the stereoselectivity of FT the oxygenation reaction to produce FT (15S)-HPETE instead of (8S)-HPETE. FT Completely changes the stereoselectivity; FT when associated with D-603. SQ SEQUENCE 677 AA; 76230 MW; 78DB1AC9C2F68399 CRC64; MAKCRVRVST GEACGAGTWD KVSVSIVGTH GESPLVPLDH LGKEFSAGAE EDFEVTLPQD VGTVLMLRVH KAPPEVSLPL MSFRSDAWFC RWFELEWLPG AALHFPCYQW LEGAGELVLR EGAAKVSWQD HHPTLQDQRQ KELESRQKMY SWKTYIEGWP RCLDHETVKD LDLNIKYSAM KNAKLFFKAH SAYTELKVKG LLDRTGLWRS LREMRRLFNF RKTPAAEYVF AHWQEDAFFA SQFLNGINPV LIRRCHSLPN NFPVTDEMVA PVLGPGTSLQ AELEKGSLFL VDHGILSGVH TNILNGKPQF SAAPMTLLHQ SSGSGPLLPI AIQLKQTPGP DNPIFLPSDD TWDWLLAKTW VRNSEFYIHE AVTHLLHAHL IPEVFALATL RQLPRCHPLF KLLIPHIRYT LHINTLAREL LVAPGKLIDK STGLGTGGFS DLIKRNMEQL NYSVLCLPED IRARGVEDIP GYYYRDDGMQ IWGAIKSFVS EIVSIYYPSD TSVQDDQELQ AWVREIFSEG FLGRESSGMP SLLDTREALV QYITMVIFTC SAKHAAVSSG QFDSCVWMPN LPPTMQLPPP TSKGQARPES FIATLPAVNS SSYHIIALWL LSAEPGDQRP LGHYPDEHFT EDAPRRSVAA FQRKLIQISK GIRERNRGLA LPYTYLDPPL IENSVSI // ID ALR_MOUSE Reviewed; 198 AA. AC P56213; Q8CIF8; Q9JJE6; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 16-DEC-2008, sequence version 2. DT 19-MAR-2014, entry version 89. DE RecName: Full=FAD-linked sulfhydryl oxidase ALR; DE EC=1.8.3.2; DE AltName: Full=Augmenter of liver regeneration; GN Name=Gfer; Synonyms=Alr; ORFNames=MNCb-0663; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY. RC STRAIN=C57BL/6 X CBA; RX PubMed=8900538; RA Giorda R., Hagiya M., Seki T., Shimonishi M., Sakai H., Michaelson J., RA Francavilla A., Starzl T.E., Trucco M.; RT "Analysis of the structure and expression of the augmenter of liver RT regeneration (ALR) gene."; RL Mol. Med. 2:97-108(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6; TISSUE=Brain; RA Osada N., Kusuda J., Tanuma R., Ito A., Hirata M., Sugano S., RA Hashimoto K.; RT "Isolation of full-length cDNA clones from mouse brain cDNA library RT made by oligo-capping method."; RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Kidney; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Mammary tumor; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] OF 45-198. RC STRAIN=C57BL/6 X CBA; RA Cheng J., Zhong Y.W., Liu Y., Dong J., Yang J.Z., Chen J.M.; RT "Cloning and sequence analysis of a mouse cDNA coding for augmenter of RT liver regeneration."; RL Zhonghua Gan Zang Bing Za Zhi 4:138-140(1999). CC -!- FUNCTION: FAD-dependent sulfhydryl oxidase that regenerates the CC redox-active disulfide bonds in CHCHD4/MIA40, a chaperone CC essential for disulfide bond formation and protein folding in the CC mitochondrial intermembrane space. The reduced form of CC CHCHD4/MIA40 forms a transient intermolecular disulfide bridge CC with GFER/ERV1, resulting in regeneration of the essential CC disulfide bonds in CHCHD4/MIA40, while GFER/ERV1 becomes re- CC oxidized by donating electrons to cytochrome c or molecular oxygen CC (By similarity). CC -!- CATALYTIC ACTIVITY: 2 R'C(R)SH + O(2) = R'C(R)S-S(R)CR' + CC H(2)O(2). CC -!- COFACTOR: FAD (By similarity). CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm. Mitochondrion intermembrane space CC (By similarity). CC -!- TISSUE SPECIFICITY: Preferentially expressed in the liver and in CC testis. CC -!- SIMILARITY: Contains 1 ERV/ALR sulfhydryl oxidase domain. CC -!- SEQUENCE CAUTION: CC Sequence=AAD36987.1; Type=Erroneous initiation; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U40494; AAD10339.1; -; Genomic_DNA. DR EMBL; AB041561; BAA95045.1; -; mRNA. DR EMBL; AK146579; BAE27275.1; -; mRNA. DR EMBL; CH466606; EDL22354.1; -; Genomic_DNA. DR EMBL; BC023941; AAH23941.1; -; mRNA. DR EMBL; AF148688; AAD36987.1; ALT_INIT; mRNA. DR RefSeq; NP_075527.2; NM_023040.3. DR UniGene; Mm.28124; -. DR ProteinModelPortal; P56213; -. DR SMR; P56213; 9-197. DR IntAct; P56213; 2. DR MINT; MINT-4129999; -. DR PhosphoSite; P56213; -. DR PaxDb; P56213; -. DR PRIDE; P56213; -. DR Ensembl; ENSMUST00000046839; ENSMUSP00000049186; ENSMUSG00000040888. DR GeneID; 11692; -. DR KEGG; mmu:11692; -. DR UCSC; uc008axr.1; mouse. DR CTD; 2671; -. DR MGI; MGI:107757; Gfer. DR eggNOG; COG5054; -. DR GeneTree; ENSGT00390000001979; -. DR HOGENOM; HOG000195924; -. DR HOVERGEN; HBG000235; -. DR InParanoid; Q9JJE6; -. DR KO; K17783; -. DR OMA; QKRDSKF; -. DR OrthoDB; EOG7HMS2X; -. DR TreeFam; TF105271; -. DR NextBio; 279349; -. DR PRO; PR:P56213; -. DR Bgee; P56213; -. DR Genevestigator; P56213; -. DR GO; GO:0005758; C:mitochondrial intermembrane space; IEA:UniProtKB-SubCell. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; ISS:UniProtKB. DR GO; GO:0015035; F:protein disulfide oxidoreductase activity; ISS:UniProtKB. DR GO; GO:0016972; F:thiol oxidase activity; IEA:UniProtKB-EC. DR Gene3D; 1.20.120.310; -; 1. DR InterPro; IPR017905; ERV/ALR_sulphydryl_oxidase. DR Pfam; PF04777; Evr1_Alr; 1. DR SUPFAM; SSF69000; SSF69000; 1. DR PROSITE; PS51324; ERV_ALR; 1. PE 2: Evidence at transcript level; KW Complete proteome; Cytoplasm; Disulfide bond; FAD; Flavoprotein; KW Growth factor; Mitochondrion; Oxidoreductase; Reference proteome. FT CHAIN 1 198 FAD-linked sulfhydryl oxidase ALR. FT /FTId=PRO_0000208549. FT DOMAIN 88 188 ERV/ALR sulfhydryl oxidase. FT NP_BIND 92 100 FAD (By similarity). FT NP_BIND 164 176 FAD (By similarity). FT NP_BIND 187 188 FAD (By similarity). FT BINDING 104 104 FAD (By similarity). FT BINDING 133 133 FAD (By similarity). FT DISULFID 88 88 Interchain (with C-197) (By similarity). FT DISULFID 135 138 Redox-active (By similarity). FT DISULFID 164 181 By similarity. FT DISULFID 197 197 Interchain (with C-88) (By similarity). FT CONFLICT 40 40 A -> P (in Ref. 1; AAD10339). FT CONFLICT 49 49 A -> S (in Ref. 1; AAD10339, 5; AAH23941 FT and 6; AAD36987). SQ SEQUENCE 198 AA; 22877 MW; 4828C5D5B2F61054 CRC64; MAAPSEPAGF PRGSRFSFLP GGARSEMTDD LVTDARGRGA RHRDDTTPAA APAPQGLEHG KRPCRACVDF KSWMRTQQKR DIKFREDCPQ DREELGRHTW AFLHTLAAYY PDRPTPEQQQ DMAQFIHIFS KFYPCEECAE DIRKRIGRNQ PDTSTRVSFS QWLCRLHNEV NRKLGKPDFD CSRVDERWRD GWKDGSCD // ID AMD_MOUSE Reviewed; 979 AA. AC P97467; E9QL07; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 2. DT 19-MAR-2014, entry version 125. DE RecName: Full=Peptidyl-glycine alpha-amidating monooxygenase; DE Short=PAM; DE Includes: DE RecName: Full=Peptidylglycine alpha-hydroxylating monooxygenase; DE Short=PHM; DE EC=1.14.17.3; DE Includes: DE RecName: Full=Peptidyl-alpha-hydroxyglycine alpha-amidating lyase; DE EC=4.3.2.5; DE AltName: Full=Peptidylamidoglycolate lyase; DE Short=PAL; DE Flags: Precursor; GN Name=Pam; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Jeong J.H., Baek S.J., Park D.H.; RL Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). CC -!- FUNCTION: Bifunctional enzyme that catalyzes 2 sequential steps in CC C-terminal alpha-amidation of peptides. The monooxygenase part CC produces an unstable peptidyl(2-hydroxyglycine) intermediate that CC is dismutated to glyoxylate and the corresponding desglycine CC peptide amide by the lyase part. C-terminal amidation of peptides CC such as neuropeptides is essential for full biological activity CC (By similarity). CC -!- CATALYTIC ACTIVITY: Peptidylglycine + ascorbate + O(2) = CC peptidyl(2-hydroxyglycine) + dehydroascorbate + H(2)O. CC -!- CATALYTIC ACTIVITY: Peptidylamidoglycolate = peptidyl amide + CC glyoxylate. CC -!- COFACTOR: Zinc; for the lyase reaction (By similarity). CC -!- COFACTOR: Binds 2 copper ions per subunit; For the monoxygenase CC reaction (By similarity). CC -!- SUBUNIT: Monomer. Interacts with RASSF9 (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle CC membrane; Single-pass membrane protein (By similarity). CC Note=Secretory granules. CC -!- SIMILARITY: In the C-terminal section; belongs to the peptidyl- CC alpha-hydroxyglycine alpha-amidating lyase family. CC -!- SIMILARITY: In the N-terminal section; belongs to the copper type CC II ascorbate-dependent monooxygenase family. CC -!- SIMILARITY: Contains 5 NHL repeats. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U79523; AAB38364.1; -; mRNA. DR EMBL; AC102191; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC157923; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; NP_038654.2; NM_013626.3. DR RefSeq; XP_006529307.1; XM_006529244.1. DR UniGene; Mm.441453; -. DR UniGene; Mm.5121; -. DR ProteinModelPortal; P97467; -. DR SMR; P97467; 44-355, 498-823. DR IntAct; P97467; 2. DR PhosphoSite; P97467; -. DR PaxDb; P97467; -. DR PRIDE; P97467; -. DR DNASU; 18484; -. DR Ensembl; ENSMUST00000058762; ENSMUSP00000057112; ENSMUSG00000026335. DR GeneID; 18484; -. DR KEGG; mmu:18484; -. DR UCSC; uc007cfp.1; mouse. DR CTD; 5066; -. DR MGI; MGI:97475; Pam. DR eggNOG; COG3391; -. DR GeneTree; ENSGT00730000111058; -. DR HOGENOM; HOG000293368; -. DR HOVERGEN; HBG004218; -. DR InParanoid; P97467; -. DR KO; K00504; -. DR OMA; TVHHMLL; -. DR OrthoDB; EOG70ZZNT; -. DR TreeFam; TF320698; -. DR ChiTaRS; PAM; mouse. DR NextBio; 294198; -. DR PRO; PR:P97467; -. DR ArrayExpress; P97467; -. DR Bgee; P97467; -. DR CleanEx; MM_PAM; -. DR Genevestigator; P97467; -. DR GO; GO:0005829; C:cytosol; TAS:MGI. DR GO; GO:0005887; C:integral component of plasma membrane; TAS:MGI. DR GO; GO:0030658; C:transport vesicle membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005507; F:copper ion binding; IEA:InterPro. DR GO; GO:0031418; F:L-ascorbic acid binding; IEA:UniProtKB-KW. DR GO; GO:0004598; F:peptidylamidoglycolate lyase activity; IEA:UniProtKB-EC. DR GO; GO:0004504; F:peptidylglycine monooxygenase activity; TAS:MGI. DR GO; GO:0006518; P:peptide metabolic process; TAS:MGI. DR Gene3D; 2.120.10.30; -; 2. DR Gene3D; 2.60.120.230; -; 1. DR Gene3D; 2.60.120.310; -; 1. DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like. DR InterPro; IPR014784; Cu2_ascorb_mOase-like_C. DR InterPro; IPR020611; Cu2_ascorb_mOase_CS-1. DR InterPro; IPR014783; Cu2_ascorb_mOase_CS-2. DR InterPro; IPR000323; Cu2_ascorb_mOase_N. DR InterPro; IPR001258; NHL_repeat. DR InterPro; IPR013017; NHL_repeat_subgr. DR InterPro; IPR000720; Pep_amidat_mOase. DR InterPro; IPR008977; PHM/PNGase_F_dom. DR Pfam; PF01082; Cu2_monooxygen; 1. DR Pfam; PF01436; NHL; 4. DR PRINTS; PR00790; PAMONOXGNASE. DR SUPFAM; SSF49742; SSF49742; 2. DR PROSITE; PS00084; CU2_MONOOXYGENASE_1; 1. DR PROSITE; PS00085; CU2_MONOOXYGENASE_2; 1. DR PROSITE; PS51125; NHL; 5. PE 1: Evidence at protein level; KW Cleavage on pair of basic residues; Complete proteome; Copper; KW Cytoplasmic vesicle; Disulfide bond; Glycoprotein; Lyase; Membrane; KW Metal-binding; Monooxygenase; Multifunctional enzyme; Oxidoreductase; KW Phosphoprotein; Reference proteome; Repeat; Signal; Transmembrane; KW Transmembrane helix; Vitamin C; Zinc. FT SIGNAL 1 24 By similarity. FT PROPEP 25 34 By similarity. FT /FTId=PRO_0000006363. FT CHAIN 35 979 Peptidyl-glycine alpha-amidating FT monooxygenase. FT /FTId=PRO_0000006364. FT TOPO_DOM 35 869 Intragranular (Potential). FT TRANSMEM 870 893 Helical; (Potential). FT TOPO_DOM 894 979 Cytoplasmic (Potential). FT REPEAT 501 544 NHL 1. FT REPEAT 570 611 NHL 2. FT REPEAT 620 665 NHL 3. FT REPEAT 673 717 NHL 4. FT REPEAT 769 812 NHL 5. FT REGION 1 497 Peptidylglycine alpha-hydroxylating FT monooxygenase (By similarity). FT REGION 498 823 Peptidyl-alpha-hydroxyglycine alpha- FT amidating lyase (By similarity). FT REGION 931 948 Interaction with RASSF9 (By similarity). FT METAL 106 106 Copper A (By similarity). FT METAL 107 107 Copper A (By similarity). FT METAL 171 171 Copper A (By similarity). FT METAL 241 241 Copper B (By similarity). FT METAL 243 243 Copper B (By similarity). FT METAL 313 313 Copper B (By similarity). FT MOD_RES 935 935 Phosphoserine (By similarity). FT MOD_RES 948 948 Phosphoserine (By similarity). FT MOD_RES 949 949 Phosphothreonine (By similarity). FT MOD_RES 952 952 Phosphoserine; by UHMK1. FT CARBOHYD 765 765 N-linked (GlcNAc...) (Potential). FT DISULFID 46 185 By similarity. FT DISULFID 80 125 By similarity. FT DISULFID 113 130 By similarity. FT DISULFID 226 333 By similarity. FT DISULFID 292 314 By similarity. FT DISULFID 634 655 By similarity. FT DISULFID 702 713 By similarity. FT CONFLICT 970 970 A -> R (in Ref. 1; AAB38364). SQ SEQUENCE 979 AA; 108963 MW; 1F4C7276567A741A CRC64; MAGRARSRLL LLLGLLALQS SCLAFRSPLS VFKRFKETTR SFSNECLGTT RPITPIDSSD FTLDIRMPGV TPKESDTYFC MSMRLPVDEE AFVIDFKPRA SMDTVHHMLL FGCNMPSSTG SYWFCDEGTC TDKANILYAW ARNAPPTRLP KGVGFRVGGE TGSKYFVLQV HYGDISAFRD NHKDCSGVSL HLTRVPQPLI AGMYLMMSVN TVIPPGEKVV NSDISCHYKM YPMHVFAYRV HTHHLGKVVS GYRVRNGQWT LIGRQSPQLP QAFYPVEHPV DVAFGDILAA RCVFTGEGRT EATHIGGTSS DEMCNLYIMY YMEAKHAVSF MTCTQNVAPD MFRTIPEEAN IPIPVKSDMV MIHGHHKETE NKEKSALIQQ PKQGEEEAFE QGDFYSLLSK LLGEREDVVH VHKYNPTEKT ESGSDLVAEI ANVVQKKDLG RSDAREGAEH EEGGNAILVR DRIHKFHRLE STLRPAESRA LSFQQPGEGP WEPELAGDFH VEEALEWPGV YLLPGQVSGV ALDSKNNLVI FHRGDHVWDG NSFDSKFVYQ QRGLGPIEED TILVIDPNKA EILQSSGKNL FYLPHGLSID TDGNYWVTDV ALHQVFKLEP RSKEGPLLVL GRSMQPGSDQ NHFCQPTDVA VEPSTGAVFV SDGYCNSRIV QFSPSGKFIT QWGEESSGSS PKPGQFSVPH SLALVPHLNQ LCVADRENGR IQCFKTDTKE FVREIKHASF GRNVFAISYI PGFLFAVNGK PYFGDQEPVQ GFVMNFSSGE IIDVFKPVRK HFDMPHDIVA SEDGTVYIGD AHTNTVWKFT LTESRLEVEH RSVKKAGIEV PEIKEAEAVV EPKVKNKPTS SELQKMQEKK KLIKDPGSGV PVVLITTLLV IPVVVLLAIA MFIRWKKSRA FGDHDRKLES SSGRVLGRLR GKGSSGLNLG NFFASRKGYS RKGFDRVSTE GSDQEKDEDD GSESEEEYSA PLPTPAPSS // ID AOC2_MOUSE Reviewed; 757 AA. AC Q812C9; A2A4J0; Q80WP3; DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 2. DT 19-FEB-2014, entry version 88. DE RecName: Full=Retina-specific copper amine oxidase; DE Short=RAO; DE EC=1.4.3.21; DE AltName: Full=Amine oxidase [copper-containing]; DE Flags: Precursor; GN Name=Aoc2; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. RX PubMed=14585497; DOI=10.1016/S0378-1119(03)00753-4; RA Zhang Q., Mashima Y., Noda S., Imamura Y., Kudoh J., Shimizu N., RA Nishiyama T., Umeda S., Oguchi Y., Tanaka Y., Iwata T.; RT "Characterization of AOC2 gene encoding a copper-binding amine oxidase RT expressed specifically in retina."; RL Gene 318:45-53(2003). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: Has a monoamine oxidase activity with substrate CC specificity for 2-phenylethylamine and tryptamine. May play a role CC in adipogenesis. May be a critical modulator of signal CC transmission in retina (By similarity). CC -!- CATALYTIC ACTIVITY: RCH(2)NH(2) + H(2)O + O(2) = RCHO + NH(3) + CC H(2)O(2). CC -!- COFACTOR: Binds 1 copper ion per subunit (By similarity). CC -!- COFACTOR: Binds 2 calcium ions per subunit (By similarity). CC -!- COFACTOR: Contains 1 topaquinone per subunit (By similarity). CC -!- SUBUNIT: Forms a heterodimer with AOC3 (By similarity). CC -!- TISSUE SPECIFICITY: Significantly much highly expressed in retina. CC -!- PTM: Topaquinone (TPQ) is generated by copper-dependent CC autoxidation of a specific tyrosyl residue. CC -!- SIMILARITY: Belongs to the copper/topaquinone oxidase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF350445; AAK58864.2; -; mRNA. DR EMBL; AF350446; AAK58865.1; -; Genomic_DNA. DR EMBL; AL590969; CAM19554.1; -; Genomic_DNA. DR EMBL; BC150843; AAI50844.1; -; mRNA. DR EMBL; BC150848; AAI50849.1; -; mRNA. DR RefSeq; NP_849263.1; NM_178932.1. DR UniGene; Mm.302277; -. DR ProteinModelPortal; Q812C9; -. DR SMR; Q812C9; 52-757. DR PhosphoSite; Q812C9; -. DR PaxDb; Q812C9; -. DR PRIDE; Q812C9; -. DR Ensembl; ENSMUST00000041095; ENSMUSP00000040255; ENSMUSG00000078651. DR GeneID; 237940; -. DR KEGG; mmu:237940; -. DR UCSC; uc007loo.1; mouse. DR CTD; 314; -. DR MGI; MGI:2668431; Aoc2. DR eggNOG; COG3733; -. DR GeneTree; ENSGT00510000046461; -. DR HOGENOM; HOG000233919; -. DR HOVERGEN; HBG004164; -. DR InParanoid; A2A4J0; -. DR KO; K00276; -. DR OMA; PLESDME; -. DR OrthoDB; EOG7353W8; -. DR TreeFam; TF314750; -. DR NextBio; 383590; -. DR PRO; PR:Q812C9; -. DR ArrayExpress; Q812C9; -. DR Bgee; Q812C9; -. DR Genevestigator; Q812C9; -. DR GO; GO:0052595; F:aliphatic-amine oxidase activity; IEA:UniProtKB-EC. DR GO; GO:0052594; F:aminoacetone:oxygen oxidoreductase(deaminating) activity; IEA:UniProtKB-EC. DR GO; GO:0005507; F:copper ion binding; IEA:InterPro. DR GO; GO:0052596; F:phenethylamine:oxygen oxidoreductase (deaminating) activity; IEA:UniProtKB-EC. DR GO; GO:0008131; F:primary amine oxidase activity; IEA:UniProtKB-EC. DR GO; GO:0048038; F:quinone binding; IEA:InterPro. DR GO; GO:0052593; F:tryptamine:oxygen oxidoreductase (deaminating) activity; IEA:UniProtKB-EC. DR GO; GO:0009308; P:amine metabolic process; IEA:InterPro. DR GO; GO:0006584; P:catecholamine metabolic process; IEA:UniProtKB-KW. DR Gene3D; 2.70.98.20; -; 1. DR Gene3D; 3.10.450.40; -; 2. DR InterPro; IPR000269; Cu_amine_oxidase. DR InterPro; IPR015798; Cu_amine_oxidase_C. DR InterPro; IPR016182; Cu_amine_oxidase_N-reg. DR InterPro; IPR015800; Cu_amine_oxidase_N2. DR InterPro; IPR015801; Cu_amine_oxidase_N2/3. DR InterPro; IPR015802; Cu_amine_oxidase_N3. DR PANTHER; PTHR10638; PTHR10638; 1. DR Pfam; PF01179; Cu_amine_oxid; 1. DR Pfam; PF02727; Cu_amine_oxidN2; 1. DR Pfam; PF02728; Cu_amine_oxidN3; 1. DR PRINTS; PR00766; CUDAOXIDASE. DR SUPFAM; SSF49998; SSF49998; 1. DR SUPFAM; SSF54416; SSF54416; 2. DR PROSITE; PS01164; COPPER_AMINE_OXID_1; 1. DR PROSITE; PS01165; COPPER_AMINE_OXID_2; 1. PE 2: Evidence at transcript level; KW Calcium; Catecholamine metabolism; Complete proteome; Copper; KW Glycoprotein; Metal-binding; Oxidoreductase; Reference proteome; KW Signal; TPQ. FT SIGNAL 1 32 Potential. FT CHAIN 33 757 Retina-specific copper amine oxidase (By FT similarity). FT /FTId=PRO_0000035672. FT ACT_SITE 381 381 Proton acceptor (By similarity). FT ACT_SITE 466 466 Schiff-base intermediate with substrate; FT via topaquinone (By similarity). FT METAL 517 517 Copper (By similarity). FT METAL 519 519 Copper (By similarity). FT METAL 526 526 Calcium 1 (By similarity). FT METAL 527 527 Calcium 1; via carbonyl oxygen (By FT similarity). FT METAL 528 528 Calcium 1 (By similarity). FT METAL 569 569 Calcium 2 (By similarity). FT METAL 635 635 Calcium 2 (By similarity). FT METAL 660 660 Calcium 2; via carbonyl oxygen (By FT similarity). FT METAL 662 662 Calcium 2 (By similarity). FT METAL 664 664 Calcium 2 (By similarity). FT METAL 670 670 Calcium 1 (By similarity). FT METAL 671 671 Calcium 1; via carbonyl oxygen (By FT similarity). FT METAL 681 681 Copper (By similarity). FT MOD_RES 466 466 2',4',5'-topaquinone (By similarity). FT CARBOHYD 133 133 N-linked (GlcNAc...) (Potential). FT CARBOHYD 198 198 N-linked (GlcNAc...) (Potential). FT CARBOHYD 226 226 N-linked (GlcNAc...) (Potential). FT CARBOHYD 589 589 N-linked (GlcNAc...) (Potential). FT CARBOHYD 663 663 N-linked (GlcNAc...) (Potential). FT CONFLICT 53 53 S -> N (in Ref. 1; AAK58865). FT CONFLICT 117 117 V -> A (in Ref. 1; AAK58865). SQ SEQUENCE 757 AA; 83583 MW; 4D93D9839AD57159 CRC64; MNLKVLLLLL GLSFLTVFAL VYVLLTRQGS FSQSPRCPSI PPRIHPWTHP SQSQLFADLT PEELTAVMSF LTKHLGPGLV DAAQARPSDN CVFSVELQLP AKAAALAHLD RGGPPPVREA LAIIFFGGQP KPNVSELVVG PLPHPSYMRD VTVERHGGPL PYYRRPMQKT EFVQIWRHLK EVELPKAPTF LASVLNYNGS TLAPLHSTAS GFHAGDRATW IALYHNISGL GVFLHPVGLE LLLDHGALDP ADWVVQQVFY LGHYYADLAQ LEWEFKVGRL EVIRVPLPTP GGASSLRPRV TPDPPLPPLQ FSLQGPQYNI QGNSVTSPLW TFTFGHGVFS GLRIFDIRFK GERVAYEVSV QECLTVYGAD SPKTMTIRYL DSSYGLGLNS RALVRGVDCP YQATMVDIHV LVGTGSVQLL PGAVCVFEEA QGLPLRRHHN GIGGHFYGGL ASSSLVVRSV SSVGNYDYIW DFMLHPTGAL EARVHATGYI NTAFMSGGAE SLLFGNRVGE RVLGAVHTHA FHFKLDLDVA GLKNWVIAED AVFKPVAAPW NPELQLQRPQ LTRQVLSRED LAAFPWGSPL PRYLYLATNQ TNAWGHQRGY RIQIHSPPGV HVPLESSEER ALSWGRYQLV VTQRKEAEPH SSSIYYQNDM RSPATVFADF INNETLLGED LVAWVTASFL HIPHAEDIPN TVTVGNRVGF LLRPYNFFNE DPSIFSPGSV YFERDQDAGL CSINPVACTQ QLADCVPNLP SFSYEGL // ID AOC1_MOUSE Reviewed; 751 AA. AC Q8JZQ5; Q8R229; Q8VC36; DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2002, sequence version 1. DT 22-JAN-2014, entry version 91. DE RecName: Full=Amiloride-sensitive amine oxidase [copper-containing]; DE Short=DAO; DE Short=Diamine oxidase; DE EC=1.4.3.22; DE AltName: Full=Amiloride-binding protein 1; DE AltName: Full=Amine oxidase copper domain-containing protein 1; DE AltName: Full=Histaminase; DE Flags: Precursor; GN Name=Aoc1; Synonyms=Abp1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Colon; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: Catalyzes the degradation of compounds such as CC putrescine, histamine, spermine, and spermidine, substances CC involved in allergic and immune responses, cell proliferation, CC tissue differentiation, tumor formation, and possibly apoptosis CC (By similarity). CC -!- CATALYTIC ACTIVITY: Histamine + H(2)O + O(2) = (imidazol-4- CC yl)acetaldehyde + NH(3) + H(2)O(2). CC -!- COFACTOR: Binds 1 copper ion per subunit (By similarity). CC -!- COFACTOR: Binds 2 calcium ions per subunit (By similarity). CC -!- COFACTOR: Contains 1 topaquinone per subunit (By similarity). CC -!- SUBUNIT: Homodimer; disulfide-linked (By similarity). CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space (By CC similarity). CC -!- PTM: Topaquinone (TPQ) is generated by copper-dependent CC autoxidation of a specific tyrosyl residue. CC -!- MISCELLANEOUS: Inhibited by amiloride in a competitive manner (By CC similarity). CC -!- SIMILARITY: Belongs to the copper/topaquinone oxidase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BC021880; AAH21880.1; -; mRNA. DR EMBL; BC022627; AAH22627.1; -; mRNA. DR EMBL; BC034215; AAH34215.1; -; mRNA. DR UniGene; Mm.213898; -. DR ProteinModelPortal; Q8JZQ5; -. DR SMR; Q8JZQ5; 29-751. DR IntAct; Q8JZQ5; 1. DR MINT; MINT-4086577; -. DR PhosphoSite; Q8JZQ5; -. DR PaxDb; Q8JZQ5; -. DR PRIDE; Q8JZQ5; -. DR MGI; MGI:1923757; Aoc1. DR eggNOG; COG3733; -. DR HOVERGEN; HBG004164; -. DR InParanoid; Q8JZQ5; -. DR PRO; PR:Q8JZQ5; -. DR ArrayExpress; Q8JZQ5; -. DR Bgee; Q8JZQ5; -. DR Genevestigator; Q8JZQ5; -. DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB. DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB. DR GO; GO:0005923; C:tight junction; ISS:UniProtKB. DR GO; GO:0005261; F:cation channel activity; ISS:UniProtKB. DR GO; GO:0005507; F:copper ion binding; ISS:UniProtKB. DR GO; GO:0052597; F:diamine oxidase activity; ISS:UniProtKB. DR GO; GO:0008144; F:drug binding; ISS:UniProtKB. DR GO; GO:0008201; F:heparin binding; ISS:UniProtKB. DR GO; GO:0052598; F:histamine oxidase activity; IEA:UniProtKB-EC. DR GO; GO:0052599; F:methylputrescine oxidase activity; IEA:UniProtKB-EC. DR GO; GO:0008131; F:primary amine oxidase activity; ISS:UniProtKB. DR GO; GO:0052600; F:propane-1,3-diamine oxidase activity; IEA:UniProtKB-EC. DR GO; GO:0032403; F:protein complex binding; ISS:UniProtKB. DR GO; GO:0048038; F:quinone binding; ISS:UniProtKB. DR GO; GO:0004872; F:receptor activity; ISS:UniProtKB. DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB. DR GO; GO:0009308; P:amine metabolic process; IEA:InterPro. DR GO; GO:0097185; P:cellular response to azide; ISS:UniProtKB. DR GO; GO:0071280; P:cellular response to copper ion; ISS:UniProtKB. DR GO; GO:0035874; P:cellular response to copper ion starvation; ISS:UniProtKB. DR GO; GO:0071420; P:cellular response to histamine; ISS:UniProtKB. DR GO; GO:0046677; P:response to antibiotic; ISS:UniProtKB. DR GO; GO:0042493; P:response to drug; ISS:UniProtKB. DR Gene3D; 2.70.98.20; -; 1. DR Gene3D; 3.10.450.40; -; 1. DR InterPro; IPR000269; Cu_amine_oxidase. DR InterPro; IPR015798; Cu_amine_oxidase_C. DR InterPro; IPR016182; Cu_amine_oxidase_N-reg. DR InterPro; IPR015800; Cu_amine_oxidase_N2. DR InterPro; IPR015801; Cu_amine_oxidase_N2/3. DR InterPro; IPR015802; Cu_amine_oxidase_N3. DR PANTHER; PTHR10638; PTHR10638; 1. DR Pfam; PF01179; Cu_amine_oxid; 1. DR Pfam; PF02727; Cu_amine_oxidN2; 1. DR Pfam; PF02728; Cu_amine_oxidN3; 1. DR PRINTS; PR00766; CUDAOXIDASE. DR SUPFAM; SSF49998; SSF49998; 1. DR SUPFAM; SSF54416; SSF54416; 2. DR PROSITE; PS01164; COPPER_AMINE_OXID_1; 1. DR PROSITE; PS01165; COPPER_AMINE_OXID_2; 1. PE 2: Evidence at transcript level; KW Calcium; Complete proteome; Copper; Disulfide bond; Glycoprotein; KW Heparin-binding; Metal-binding; Oxidoreductase; Reference proteome; KW Secreted; Signal; TPQ. FT SIGNAL 1 22 Potential. FT CHAIN 23 751 Amiloride-sensitive amine oxidase FT [copper-containing] (By similarity). FT /FTId=PRO_0000035667. FT REGION 568 575 Heparin-binding (By similarity). FT ACT_SITE 373 373 Proton acceptor (By similarity). FT ACT_SITE 461 461 Schiff-base intermediate with substrate; FT via topaquinone (By similarity). FT METAL 510 510 Copper (By similarity). FT METAL 512 512 Copper (By similarity). FT METAL 519 519 Calcium 1 (By similarity). FT METAL 520 520 Calcium 1; via carbonyl oxygen (By FT similarity). FT METAL 521 521 Calcium 1 (By similarity). FT METAL 562 562 Calcium 2 (By similarity). FT METAL 653 653 Calcium 2; via carbonyl oxygen (By FT similarity). FT METAL 656 656 Calcium 2 (By similarity). FT METAL 658 658 Calcium 2 (By similarity). FT METAL 664 664 Calcium 1 (By similarity). FT METAL 665 665 Calcium 1; via carbonyl oxygen (By FT similarity). FT METAL 675 675 Copper (By similarity). FT MOD_RES 461 461 2',4',5'-topaquinone (By similarity). FT CARBOHYD 61 61 N-linked (GlcNAc...) (Potential). FT CARBOHYD 110 110 N-linked (GlcNAc...) (Potential). FT CARBOHYD 538 538 N-linked (GlcNAc...) (Potential). FT CARBOHYD 745 745 N-linked (GlcNAc...) (Potential). FT DISULFID 391 417 By similarity. FT DISULFID 736 736 Interchain (By similarity). FT CONFLICT 20 20 A -> P (in Ref. 1; AAH21880). SQ SEQUENCE 751 AA; 85424 MW; 4E9682DA7C967AC7 CRC64; MSLAFGWAAV ILLLQTADTA SAVTTPHDKA RIFADLSPQE IKAVHSFLMS RKELGLESSK NLTLAKNSVF LIEMLLPKKK NVLKFLDEGR KSPVREARAI IFFGAQDHPN VTEFAVGPLP RPCYVQALSP RPGHHLSWSS RPISTAEYDL LYHMLNRAIT PLHQFFLDTT GFSFLGCDDR FLTFTDVAPR GVESGQRRSW LIVQRYVEGY FLHPTGLEIL VDHSSTDVQD WRVEQLWYNG KFYNSPEELA QKYAVGEVEA VVLEEVVLED PLPGATEQPP LFSSYKPRGE FHTPVTVAGP HVVQPSGPRY KLEGNVVLYG DWSFSYRLRS SSGLQIFNVL FGGERVAYEV SVQEAVALYG GHTPAGMQTK YIDVGWGLGS VTHELAPGID CPETATFLDA FHYYDSDGPV LYPRALCLFE MPTGVPLRRH FDSNFKGGFN FYAGLKGYVL VLRTTSTVYN YDYIWDFIFY PNGVMETKMH ATGYVHATFY TPEGLRHGTR LQTHLLGNIH THLVHYRVDL DVAGTKNSFR TLKTKLENIT NPWSPSHSLV QPTLEQTQYS HEHQAAFRFG QTLPKYLLFS SPQKNRWGHR RSYRLQIHSM AEQVLPPGWQ EERAVTWARY PLAVTKYRES ERYSSSLYNQ NDPWDPPVVF EEFLRNNENI ENEDLVAWVT VGFLHIPHSE DVPNTATPGN CVGFLIRPFN FFEEDPSLAS RDTVIVWPQD NGLNHVQRWI PENRDCLVSP PFSYNGTYKP V // ID AOFA_MOUSE Reviewed; 526 AA. AC Q64133; B1AX52; Q8K0Z8; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 3. DT 19-FEB-2014, entry version 112. DE RecName: Full=Amine oxidase [flavin-containing] A; DE EC=1.4.3.4; DE AltName: Full=Monoamine oxidase type A; DE Short=MAO-A; GN Name=Maoa; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Mammary tumor; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 19-40. RX PubMed=7792602; DOI=10.1126/science.7792602; RA Cases O., Seif I., Grimsby J., Gaspar P., Chen K., Pournin S., RA Mueller U., Aguet M., Babinet C., Shih J.C., de Maeyer E.; RT "Aggressive behavior and altered amounts of brain serotonin and RT norepinephrine in mice lacking MAOA."; RL Science 268:1763-1766(1995). RN [5] RP PROTEIN SEQUENCE OF 137-147; 207-217; 268-280 AND 380-395, AND MASS RP SPECTROMETRY. RC STRAIN=C57BL/6; TISSUE=Brain; RA Lubec G., Kang S.U.; RL Submitted (APR-2007) to UniProtKB. CC -!- FUNCTION: Catalyzes the oxidative deamination of biogenic and CC xenobiotic amines and has important functions in the metabolism of CC neuroactive and vasoactive amines in the central nervous system CC and peripheral tissues. MAOA preferentially oxidizes biogenic CC amines such as 5-hydroxytryptamine (5-HT), norepinephrine and CC epinephrine (By similarity). CC -!- CATALYTIC ACTIVITY: RCH(2)NHR' + H(2)O + O(2) = RCHO + R'NH(2) + CC H(2)O(2). CC -!- COFACTOR: FAD. CC -!- SUBUNIT: Monomer, homo- or heterodimer (containing two subunits of CC similar size). Each subunit contains a covalently bound flavin. CC Enzymatically active as monomer (By similarity). CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane; Single-pass CC type IV membrane protein; Cytoplasmic side. CC -!- SIMILARITY: Belongs to the flavin monoamine oxidase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AL805907; CAM18994.1; -; Genomic_DNA. DR EMBL; AL831729; CAM18994.1; JOINED; Genomic_DNA. DR EMBL; AL831729; CAM26634.1; -; Genomic_DNA. DR EMBL; AL805907; CAM26634.1; JOINED; Genomic_DNA. DR EMBL; CH466584; EDL35717.1; -; Genomic_DNA. DR EMBL; BC029100; AAH29100.1; -; mRNA. DR EMBL; S78615; AAB34677.1; -; Genomic_DNA. DR EMBL; S78606; AAB34677.1; JOINED; Genomic_DNA. DR RefSeq; NP_776101.3; NM_173740.3. DR UniGene; Mm.21108; -. DR ProteinModelPortal; Q64133; -. DR SMR; Q64133; 11-520. DR BioGrid; 201307; 2. DR IntAct; Q64133; 1. DR MINT; MINT-4997361; -. DR BindingDB; Q64133; -. DR ChEMBL; CHEMBL3681; -. DR PhosphoSite; Q64133; -. DR PaxDb; Q64133; -. DR PRIDE; Q64133; -. DR Ensembl; ENSMUST00000026013; ENSMUSP00000026013; ENSMUSG00000025037. DR GeneID; 17161; -. DR KEGG; mmu:17161; -. DR UCSC; uc009ssa.2; mouse. DR CTD; 4128; -. DR MGI; MGI:96915; Maoa. DR eggNOG; COG1231; -. DR GeneTree; ENSGT00730000110903; -. DR HOGENOM; HOG000221615; -. DR HOVERGEN; HBG004255; -. DR InParanoid; B1AX52; -. DR KO; K00274; -. DR OMA; DAPWEAP; -. DR OrthoDB; EOG7K6PTP; -. DR TreeFam; TF313314; -. DR NextBio; 291438; -. DR PRO; PR:Q64133; -. DR ArrayExpress; Q64133; -. DR Bgee; Q64133; -. DR CleanEx; MM_MAOA; -. DR Genevestigator; Q64133; -. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW. DR GO; GO:0042420; P:dopamine catabolic process; IDA:MGI. DR GO; GO:0042135; P:neurotransmitter catabolic process; IEA:UniProtKB-KW. DR InterPro; IPR002937; Amino_oxidase. DR InterPro; IPR001613; Flavin_amine_oxidase. DR Pfam; PF01593; Amino_oxidase; 1. DR PRINTS; PR00757; AMINEOXDASEF. PE 1: Evidence at protein level; KW Acetylation; Catecholamine metabolism; Complete proteome; KW Direct protein sequencing; FAD; Flavoprotein; Membrane; Mitochondrion; KW Mitochondrion outer membrane; Neurotransmitter degradation; KW Oxidoreductase; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 526 Amine oxidase [flavin-containing] A. FT /FTId=PRO_0000099851. FT TOPO_DOM 1 497 Cytoplasmic (By similarity). FT TRANSMEM 498 518 Helical; Anchor for type IV membrane FT protein; (By similarity). FT TOPO_DOM 519 526 Mitochondrial intermembrane (By FT similarity). FT REGION 520 522 Interaction with membrane phospholipid FT headgroups (By similarity). FT SITE 335 335 Important for substrate specificity (By FT similarity). FT SITE 374 374 Important for catalytic activity (By FT similarity). FT MOD_RES 1 1 N-acetylmethionine (By similarity). FT MOD_RES 406 406 S-8alpha-FAD cysteine (By similarity). FT CONFLICT 83 83 E -> D (in Ref. 3; AAH29100). SQ SEQUENCE 526 AA; 59602 MW; 5375D1B0C4C5ACF9 CRC64; MTDLEKPSIT GHMFDVVVIG GGISGLAAAK LLSEYKINVL VLEARDRVGG RTYTVRNEHV KWVDVGGAYV GPTQNRILRL SKELGIETYK VNVNERLVQY VKGKTYPFRG AFPPVWNPLA YLDYNNLWRT MDDMGKEIPV DAPWQARHAE EWDKITMKDL IDKICWTKTA REFAYLFVNI NVTSEPHEVS ALWFLWYVRQ CGGTSRIFSV TNGGQERKFV GGSGQISEQI MVLLGDKVKL SSPVTYIDQT DDNIIIETLN HEHYECKYVI SAIPPVLTAK IHFKPELPPE RNQLIQRLPM GAVIKCMVYY KEAFWKKKDY CGCMIIEDEE APISITLDDT KPDGSMPAIM GFILARKAER LAKLHKDIRK RKICELYAKV LGSQEALSPV HYEEKNWCEE QYSGGCYTAY FPPGIMTLYG RVIRQPVGRI YFAGTETATQ WSGYMEGAVE AGERAAREVL NALGKVAKKD IWVQEPESKD VPALEITHTF LERNLPSVPG LLKITGFSTS VALLCFVLYK FKQPQS // ID AOFB_MOUSE Reviewed; 520 AA. AC Q8BW75; Q14CG9; Q8C0B2; DT 25-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 4. DT 19-MAR-2014, entry version 88. DE RecName: Full=Amine oxidase [flavin-containing] B; DE EC=1.4.3.4; DE AltName: Full=Monoamine oxidase type B; DE Short=MAO-B; GN Name=Maob; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Medulla oblongata, and Oviduct; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-52 AND LYS-248, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23576753; DOI=10.1073/pnas.1302961110; RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., RA Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.; RT "Label-free quantitative proteomics of the lysine acetylome in RT mitochondria identifies substrates of SIRT3 in metabolic pathways."; RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013). CC -!- FUNCTION: Catalyzes the oxidative deamination of biogenic and CC xenobiotic amines and has important functions in the metabolism of CC neuroactive and vasoactive amines in the central nervous system CC and peripheral tissues. MAOB preferentially degrades benzylamine CC and phenylethylamine (By similarity). CC -!- CATALYTIC ACTIVITY: RCH(2)NHR' + H(2)O + O(2) = RCHO + R'NH(2) + CC H(2)O(2). CC -!- COFACTOR: FAD (By similarity). CC -!- SUBUNIT: Monomer, homo- or heterodimer (containing two subunits of CC similar size). Each subunit contains a covalently bound flavin. CC Enzymatically active as monomer (By similarity). CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane; Single-pass CC type IV membrane protein; Cytoplasmic side (By similarity). CC -!- SIMILARITY: Belongs to the flavin monoamine oxidase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK031833; BAC27571.1; -; mRNA. DR EMBL; AK054050; BAC35634.1; -; mRNA. DR EMBL; AL732321; CAM16088.1; -; Genomic_DNA. DR EMBL; AL831729; CAM16088.1; JOINED; Genomic_DNA. DR EMBL; AL831729; CAM26633.1; -; Genomic_DNA. DR EMBL; AL732321; CAM26633.1; JOINED; Genomic_DNA. DR EMBL; CH466584; EDL35718.1; -; Genomic_DNA. DR EMBL; BC113182; AAI13183.1; -; mRNA. DR EMBL; BC113788; AAI13789.1; -; mRNA. DR RefSeq; NP_766366.2; NM_172778.2. DR UniGene; Mm.241656; -. DR ProteinModelPortal; Q8BW75; -. DR SMR; Q8BW75; 3-495. DR IntAct; Q8BW75; 2. DR MINT; MINT-1861050; -. DR BindingDB; Q8BW75; -. DR ChEMBL; CHEMBL3050; -. DR PhosphoSite; Q8BW75; -. DR PaxDb; Q8BW75; -. DR PRIDE; Q8BW75; -. DR Ensembl; ENSMUST00000040820; ENSMUSP00000040550; ENSMUSG00000040147. DR GeneID; 109731; -. DR KEGG; mmu:109731; -. DR UCSC; uc009ssb.2; mouse. DR CTD; 4129; -. DR MGI; MGI:96916; Maob. DR eggNOG; COG1231; -. DR GeneTree; ENSGT00730000110903; -. DR HOGENOM; HOG000221615; -. DR HOVERGEN; HBG004255; -. DR InParanoid; Q14CG9; -. DR KO; K00274; -. DR OMA; LHQRMPS; -. DR OrthoDB; EOG7K6PTP; -. DR TreeFam; TF313314; -. DR BRENDA; 1.4.3.4; 3474. DR NextBio; 362651; -. DR PRO; PR:Q8BW75; -. DR ArrayExpress; Q8BW75; -. DR Bgee; Q8BW75; -. DR CleanEx; MM_MAOB; -. DR Genevestigator; Q8BW75; -. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:MGI. DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:Ensembl. DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW. DR GO; GO:0014063; P:negative regulation of serotonin secretion; IEA:Ensembl. DR GO; GO:0045964; P:positive regulation of dopamine metabolic process; IEA:Ensembl. DR GO; GO:0010044; P:response to aluminum ion; IEA:Ensembl. DR GO; GO:0051412; P:response to corticosterone; IEA:Ensembl. DR GO; GO:0042493; P:response to drug; IEA:Ensembl. DR GO; GO:0045471; P:response to ethanol; IEA:Ensembl. DR GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl. DR GO; GO:0010269; P:response to selenium ion; IEA:Ensembl. DR GO; GO:0009636; P:response to toxic substance; IEA:Ensembl. DR InterPro; IPR002937; Amino_oxidase. DR InterPro; IPR001613; Flavin_amine_oxidase. DR Pfam; PF01593; Amino_oxidase; 1. DR PRINTS; PR00757; AMINEOXDASEF. PE 1: Evidence at protein level; KW Acetylation; Complete proteome; FAD; Flavoprotein; Membrane; KW Mitochondrion; Mitochondrion outer membrane; Oxidoreductase; KW Reference proteome; Transmembrane; Transmembrane helix. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 520 Amine oxidase [flavin-containing] B. FT /FTId=PRO_0000099860. FT TOPO_DOM 2 489 Cytoplasmic (By similarity). FT TRANSMEM 490 516 Helical; Anchor for type IV membrane FT protein; (By similarity). FT TOPO_DOM 517 520 Mitochondrial intermembrane (By FT similarity). FT COMPBIAS 36 52 Arg/Lys-rich (basic). FT SITE 156 156 Important for catalytic activity (By FT similarity). FT SITE 365 365 Important for catalytic activity (By FT similarity). FT SITE 382 382 Important for catalytic activity (By FT similarity). FT MOD_RES 2 2 N-acetylserine (By similarity). FT MOD_RES 52 52 N6-acetyllysine. FT MOD_RES 248 248 N6-acetyllysine. FT MOD_RES 397 397 S-8alpha-FAD cysteine (By similarity). FT CONFLICT 408 408 T -> S (in Ref. 1; BAC35634). FT CONFLICT 482 482 L -> M (in Ref. 1; BAC27571). SQ SEQUENCE 520 AA; 58558 MW; A5982EBBF5C4BD62 CRC64; MSNKSDVIVV GGGISGMAAA KLLHDCGLSV VVLEARDRVG GRTYTIRNKN VKYVDLGGSY VGPTQNRILR LAKELGLETY KVNEVERLIH FVKGKSYAFR GPFPPVWNPI TYLDNNNLWR TMDEMGQEIP SDAPWKAPLA EEWDYMTMKE LLDKICWTKS TKQIATLFVN LCVTAETHEV SALWFLWYVK QCGGTTRIIS TTNGGQERKF IGGSGQVSER IKDILGDRVK LERPVIHIDQ TGENVIVKTL NHEIYEAKYV ISAIPPALGM KIHYSPPLPM LRNQLISRVP LGSVIKCMVY YKEPFWRKKD FCGTMVIEGE EAPIAYTLDD TKPDGTYAAI MGFILAHKAR KLVRLTKEER LRKLCELYAK VLNSQEALQP VHYEEKNWCE EQYSGGCYTT YFPPGILTQY GRVLRQPVGK IFFAGTETAS HWSGYMEGAV EAGERAAREI LHAIGKIPED EIWQPEPESL DVPARPITST FLERHLPSVP GLLKLFGLTT ILSATALGFL AHKRGLFVHF // ID AOXD_MOUSE Reviewed; 1336 AA. AC Q3TYQ9; Q8VI17; DT 19-FEB-2014, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2005, sequence version 1. DT 19-MAR-2014, entry version 84. DE RecName: Full=Aldehyde oxidase 4; DE EC=1.2.3.1; DE AltName: Full=Aldehyde oxidase homolog 2; DE AltName: Full=Azaheterocycle hydroxylase 4; DE EC=1.17.3.-; DE AltName: Full=Retinal oxidase; GN Name=Aox4; Synonyms=Aoh2; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=129/Sv; RX PubMed=11562361; DOI=10.1074/jbc.M105744200; RA Terao M., Kurosaki M., Marini M., Vanoni M.A., Saltini G., Bonetto V., RA Bastone A., Federico C., Saccone S., Fanelli R., Salmona M., RA Garattini E.; RT "Purification of the aldehyde oxidase homolog 1 (AOH1) protein and RT cloning of the AOH1 and aldehyde oxidase homolog 2 (AOH2) genes. RT Identification of a novel molybdo-flavoprotein gene cluster on mouse RT chromosome 1."; RL J. Biol. Chem. 276:46347-46363(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP FUNCTION AS RETINAL OXIDASE, CATALYTIC ACTIVITY, KINETIC PARAMETERS, RP SUBSTRATE SPECIFICITY, TISSUE SPECIFICITY, INDUCTION, MASS RP SPECTROMETRY, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION. RX PubMed=18981221; DOI=10.1128/MCB.01385-08; RA Terao M., Kurosaki M., Barzago M.M., Fratelli M., Bagnati R., RA Bastone A., Giudice C., Scanziani E., Mancuso A., Tiveron C., RA Garattini E.; RT "Role of the molybdoflavoenzyme aldehyde oxidase homolog 2 in the RT biosynthesis of retinoic acid: generation and characterization of a RT knockout mouse."; RL Mol. Cell. Biol. 29:357-377(2009). RN [6] RP TISSUE SPECIFICITY, AND IDENTIFICATION OF PARALOGS. RX PubMed=23263164; DOI=10.1007/s00018-012-1229-5; RA Kurosaki M., Bolis M., Fratelli M., Barzago M.M., Pattini L., RA Perretta G., Terao M., Garattini E.; RT "Structure and evolution of vertebrate aldehyde oxidases: from gene RT duplication to gene suppression."; RL Cell. Mol. Life Sci. 70:1807-1830(2013). CC -!- FUNCTION: Aldehyde oxidase able to catalyze the oxidation of CC retinaldehyde into retinoate. Is responsible for the major all- CC trans-retinaldehyde-metabolizing activity in the Harderian gland, CC and contributes a significant amount of the same activity in the CC skin. Is devoid of pyridoxal-oxidizing activity, in contrast to CC the other aldehyde oxidases. Acts as a negative modulator of the CC epidermal trophism. May be able to oxidize a wide variety of CC aldehydes into their corresponding carboxylates and to hydroxylate CC azaheterocycles. CC -!- CATALYTIC ACTIVITY: An aldehyde + H(2)O + O(2) = a carboxylate + CC H(2)O(2). CC -!- CATALYTIC ACTIVITY: Retinal + O(2) + H(2)O = retinoate + H(2)O(2). CC -!- COFACTOR: Binds 2 2Fe-2S clusters per subunit (By similarity). CC -!- COFACTOR: Binds 1 FAD per subunit (By similarity). CC -!- COFACTOR: Binds 1 molybdenum-molybdopterin (Mo-MPT) cofactor per CC subunit (By similarity). CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=4.8 uM for all-trans-retinaldehyde (at 37 degrees Celsius and CC pH 7.4); CC Vmax=0.06 umol/min/mg enzyme with all-trans-retinaldehyde as CC substrate (at 37 degrees Celsius and pH 7.4); CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- TISSUE SPECIFICITY: Highly expressed in Harderian glands and CC sebaceous glands with detectable levels in the epidermis and other CC keratinized epithelia (at protein level). Detected in testis. The CC expression is 3 times greater in females than in males. CC -!- INDUCTION: Repressed by testosterone in Harderian glands. In skin, CC induced by UVB light. CC -!- DISRUPTION PHENOTYPE: Mice are viable, fertile and born at the CC expected Mendelian rate. However, they show a deficiency of CC retinoic acid synthesis in both the Harderian gland and skin. The CC Harderian gland's transcriptome of knockout mice demonstrates CC overall down-regulation of direct retinoid-dependent genes as well CC as perturbations in pathways controlling lipid homeostasis and CC cellular secretion, particularly in sexually immature animals. The CC skin is characterized by thickening of the epidermis in basal CC conditions and after UVB light exposure. CC -!- MISCELLANEOUS: AOX genes evolved from a xanthine oxidoreductase CC ancestral precursor via a series of gene duplication and CC suppression/deletion events. Different animal species contain a CC different complement of AOX genes encoding an equivalent number of CC AOX isoenzymes. In mammals, the two extremes are represented by CC certain rodents such as mice and rats, which are endowed with 4 CC AOX genes, and by humans, whose genome is characterized by a CC single active gene (PubMed:23263164). CC -!- SIMILARITY: Belongs to the xanthine dehydrogenase family. CC -!- SIMILARITY: Contains 1 2Fe-2S ferredoxin-type domain. CC -!- SIMILARITY: Contains 1 FAD-binding PCMH-type domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF321814; AAL38126.1; -; Genomic_DNA. DR EMBL; AF321780; AAL38126.1; JOINED; Genomic_DNA. DR EMBL; AF321781; AAL38126.1; JOINED; Genomic_DNA. DR EMBL; AF321782; AAL38126.1; JOINED; Genomic_DNA. DR EMBL; AF321783; AAL38126.1; JOINED; Genomic_DNA. DR EMBL; AF321784; AAL38126.1; JOINED; Genomic_DNA. DR EMBL; AF321785; AAL38126.1; JOINED; Genomic_DNA. DR EMBL; AF321786; AAL38126.1; JOINED; Genomic_DNA. DR EMBL; AF321787; AAL38126.1; JOINED; Genomic_DNA. DR EMBL; AF321788; AAL38126.1; JOINED; Genomic_DNA. DR EMBL; AF321789; AAL38126.1; JOINED; Genomic_DNA. DR EMBL; AF321790; AAL38126.1; JOINED; Genomic_DNA. DR EMBL; AF321791; AAL38126.1; JOINED; Genomic_DNA. DR EMBL; AF321792; AAL38126.1; JOINED; Genomic_DNA. DR EMBL; AF321793; AAL38126.1; JOINED; Genomic_DNA. DR EMBL; AF321794; AAL38126.1; JOINED; Genomic_DNA. DR EMBL; AF321795; AAL38126.1; JOINED; Genomic_DNA. DR EMBL; AF321796; AAL38126.1; JOINED; Genomic_DNA. DR EMBL; AF321797; AAL38126.1; JOINED; Genomic_DNA. DR EMBL; AF321798; AAL38126.1; JOINED; Genomic_DNA. DR EMBL; AF321799; AAL38126.1; JOINED; Genomic_DNA. DR EMBL; AF321800; AAL38126.1; JOINED; Genomic_DNA. DR EMBL; AF321801; AAL38126.1; JOINED; Genomic_DNA. DR EMBL; AF321802; AAL38126.1; JOINED; Genomic_DNA. DR EMBL; AF321803; AAL38126.1; JOINED; Genomic_DNA. DR EMBL; AF321804; AAL38126.1; JOINED; Genomic_DNA. DR EMBL; AF321805; AAL38126.1; JOINED; Genomic_DNA. DR EMBL; AF321806; AAL38126.1; JOINED; Genomic_DNA. DR EMBL; AF321807; AAL38126.1; JOINED; Genomic_DNA. DR EMBL; AF321808; AAL38126.1; JOINED; Genomic_DNA. DR EMBL; AF321809; AAL38126.1; JOINED; Genomic_DNA. DR EMBL; AF321810; AAL38126.1; JOINED; Genomic_DNA. DR EMBL; AF321811; AAL38126.1; JOINED; Genomic_DNA. DR EMBL; AF321812; AAL38126.1; JOINED; Genomic_DNA. DR EMBL; AF321813; AAL38126.1; JOINED; Genomic_DNA. DR EMBL; AK158427; BAE34503.1; -; mRNA. DR EMBL; AC025116; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC117975; AAI17976.1; -; mRNA. DR RefSeq; NP_076120.2; NM_023631.2. DR UniGene; Mm.244525; -. DR ProteinModelPortal; Q3TYQ9; -. DR SMR; Q3TYQ9; 7-168. DR STRING; 10090.ENSMUSP00000048929; -. DR PRIDE; Q3TYQ9; -. DR Ensembl; ENSMUST00000040442; ENSMUSP00000048929; ENSMUSG00000038242. DR GeneID; 71872; -. DR KEGG; mmu:71872; -. DR UCSC; uc007bbo.1; mouse. DR CTD; 71872; -. DR MGI; MGI:1919122; Aox4. DR GeneTree; ENSGT00390000003772; -. DR HOVERGEN; HBG004182; -. DR InParanoid; Q3TYQ9; -. DR KO; K00157; -. DR OMA; FNPEPLR; -. DR TreeFam; TF353036; -. DR ChiTaRS; Aox4; mouse. DR NextBio; 334806; -. DR ArrayExpress; Q3TYQ9; -. DR Bgee; Q8VI17; -. DR Genevestigator; Q3TYQ9; -. DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0004031; F:aldehyde oxidase activity; ISA:MGI. DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0030151; F:molybdenum ion binding; ISA:MGI. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR GO; GO:0008762; F:UDP-N-acetylmuramate dehydrogenase activity; IEA:InterPro. DR Gene3D; 1.10.150.120; -; 1. DR Gene3D; 3.10.20.30; -; 1. DR Gene3D; 3.30.365.10; -; 6. DR Gene3D; 3.30.43.10; -; 1. DR Gene3D; 3.30.465.10; -; 1. DR Gene3D; 3.90.1170.50; -; 1. DR InterPro; IPR002888; 2Fe-2S-bd. DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type. DR InterPro; IPR006058; 2Fe2S_fd_BS. DR InterPro; IPR000674; Ald_Oxase/Xan_DH_a/b. DR InterPro; IPR016208; Ald_Oxase/xanthine_DH. DR InterPro; IPR014313; Aldehyde_oxidase. DR InterPro; IPR008274; AldOxase/xan_DH_Mopterin-bd. DR InterPro; IPR012675; Beta-grasp_dom. DR InterPro; IPR005107; CO_DH_flav_C. DR InterPro; IPR016169; CO_DH_flavot_FAD-bd_sub2. DR InterPro; IPR016166; FAD-bd_2. DR InterPro; IPR016167; FAD-bd_2_sub1. DR InterPro; IPR002346; Mopterin_DH_FAD-bd. DR PANTHER; PTHR11908:SF10; PTHR11908:SF10; 1. DR Pfam; PF01315; Ald_Xan_dh_C; 1. DR Pfam; PF02738; Ald_Xan_dh_C2; 1. DR Pfam; PF03450; CO_deh_flav_C; 1. DR Pfam; PF00941; FAD_binding_5; 1. DR Pfam; PF00111; Fer2; 1. DR Pfam; PF01799; Fer2_2; 1. DR PIRSF; PIRSF000127; Xanthine_DH; 1. DR SMART; SM01008; Ald_Xan_dh_C; 1. DR SMART; SM01092; CO_deh_flav_C; 1. DR SUPFAM; SSF47741; SSF47741; 1. DR SUPFAM; SSF54292; SSF54292; 1. DR SUPFAM; SSF54665; SSF54665; 1. DR SUPFAM; SSF55447; SSF55447; 1. DR SUPFAM; SSF56003; SSF56003; 1. DR SUPFAM; SSF56176; SSF56176; 1. DR TIGRFAMs; TIGR02969; mam_aldehyde_ox; 1. DR PROSITE; PS00197; 2FE2S_FER_1; 1. DR PROSITE; PS51085; 2FE2S_FER_2; 1. DR PROSITE; PS51387; FAD_PCMH; 1. PE 1: Evidence at protein level; KW 2Fe-2S; Complete proteome; Cytoplasm; FAD; Flavoprotein; Iron; KW Iron-sulfur; Metal-binding; Molybdenum; Oxidoreductase; KW Reference proteome. FT CHAIN 1 1336 Aldehyde oxidase 4. FT /FTId=PRO_0000425250. FT DOMAIN 8 95 2Fe-2S ferredoxin-type. FT DOMAIN 237 423 FAD-binding PCMH-type. FT NP_BIND 265 272 FAD (By similarity). FT ACT_SITE 1267 1267 Proton acceptor; for azaheterocycle FT hydroxylase activity (By similarity). FT METAL 47 47 Iron-sulfur 1 (2Fe-2S) (By similarity). FT METAL 52 52 Iron-sulfur 1 (2Fe-2S) (By similarity). FT METAL 55 55 Iron-sulfur 1 (2Fe-2S) (By similarity). FT METAL 77 77 Iron-sulfur 1 (2Fe-2S) (By similarity). FT METAL 117 117 Iron-sulfur 2 (2Fe-2S) (By similarity). FT METAL 120 120 Iron-sulfur 2 (2Fe-2S) (By similarity). FT METAL 152 152 Iron-sulfur 2 (2Fe-2S) (By similarity). FT METAL 154 154 Iron-sulfur 2 (2Fe-2S) (By similarity). FT BINDING 116 116 Molybdopterin (By similarity). FT BINDING 355 355 FAD (By similarity). FT BINDING 359 359 FAD (By similarity). FT BINDING 368 368 FAD (By similarity). FT BINDING 413 413 FAD; via amide nitrogen (By similarity). FT BINDING 804 804 Molybdopterin; via amide nitrogen (By FT similarity). FT BINDING 1045 1045 Molybdopterin; via amide nitrogen (By FT similarity). FT BINDING 1201 1201 Molybdopterin (By similarity). FT CONFLICT 386 386 Missing (in Ref. 1; AAL38126). SQ SEQUENCE 1336 AA; 148279 MW; F12D7DA84A31A717 CRC64; MPSVSESDEL IFFVNGKKVI EKNPDPEKNL LFYTRKVLNL TGTKYSCGTG GCGACTVMVS RYNPKTRKIH HYPATACLVP ICWLHGAAIT TVEGVGSIKK RVHPVQERLA KCHGTQCGFC SPGMVMSIYT LLRNHPEPTP DQITEALGGN LCRCTGYRPI VESGKTFSQK STVCQMKGSG KCCMDPDEKC LESREKKMCT KLYNEDEFQP FDPSQEPIFP PELIRMAEDP NKRRLTFQGK RTTWIIPVTL NDLLELKASY PEAPLVMGNT TVGPGIKFND EFYPVFISPL GVPELNLMDT TNNGVTIGAG YSLAQLKDTL DFLVSEQPKE KTKTFHALQK HLRTLAGPQI RNMATLGGHT ASRPNFSDLN PILAAGNATI NVVSREGKDR QLPLNGPFLE KLPEADLKPE EVILSIFIPY TAQWQFVSGL RLAQRQENAF AIVNAGMSVE FEEGTNTIKD LKMFFGSVAP TVVSASQTCK QLIGRQWDDQ MLSDACQLVL QEIRIPPDAE GGMVEYRRTL IISLLFKFYL KVQRWLNEMD PQKFPDIPGK FVSALDDFPI ETPQGIQMFQ CVDPKQPQKD PVGHPIMHQS GIKHATGEAI FIDDMPPIDQ ELCLAVVTST RAHAKITSLD VSEALACPGV VDVITAEDVP GENDHNGEIL YAQSEVICVG QIICTVAADT YIHAKEAAKR VKIAYDDIEP TIITIEEALE HNSFLSPEKK IEQGNVDYAF KHVDQIVEGE IHVEGQEHFY METQTILAIP QTEDKEMVLH LGTQFPTHVQ EFVSAALNVP RSRIACHMKR AGGAFGGKVT KPALLGAVCA VAANKTGRPI RFILERSDDM LITAGRHPLL GKYKIGFMNN GEIRAADVEY YTNGGCTPDE SELVIEFVVL KSENTYHIPN FRCRGRACKT NLPSNTAFRG FGFPQATVVV EAYIAAVASK CNLLPEEVRE INMYKKTSKT AYKQTFNPEP LRRCWKECLE KSSFFARKKA AEEFNGNNYW KKRGLAVVPM KFSVAVPIAF YNQAAALVHI FLDGSVLLTH GGCELGQGLH TKMIQVASRE LNVPKSYVHF SETSTTTVPN SAFTAGSMGA DINGKAVQNA CQILMDRLRP IIRKNPKGKW EEWIKMAFEE SISLSATGYF KGYQTNMDWK KEEGDPYPYY VYGAACSEVE VDCLTGAHKL LRTDIFVDAA FSINPALDIG QVEGAFIQGM GFYTTEELKY SPKGVLYSRG PEDYKIPTIT EIPEEFYVTL VHSRNPIAIY SSKGLGEAGM FLGSSVLFAI YDAVTTARKE RGLSDIFPLN SPATPEVIRM ACTDQFTEMI PRDDPSTFTP WSIHVS // ID AOXC_MOUSE Reviewed; 1335 AA. AC G3X982; B2RSI5; Q8VI15; DT 19-FEB-2014, integrated into UniProtKB/Swiss-Prot. DT 16-NOV-2011, sequence version 1. DT 19-MAR-2014, entry version 21. DE RecName: Full=Aldehyde oxidase 3; DE EC=1.2.3.1; DE AltName: Full=Aldehyde oxidase homolog 1; DE AltName: Full=Azaheterocycle hydroxylase 3; DE EC=1.17.3.-; GN Name=Aox3; Synonyms=Aoh1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], IDENTIFICATION BY MASS RP SPECTROMETRY, FUNCTION AS OXIDASE, COFACTORS, ENZYME REGULATION, RP KINETIC PARAMETERS, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RC STRAIN=129/Sv; RX PubMed=11562361; DOI=10.1074/jbc.M105744200; RA Terao M., Kurosaki M., Marini M., Vanoni M.A., Saltini G., Bonetto V., RA Bastone A., Federico C., Saccone S., Fanelli R., Salmona M., RA Garattini E.; RT "Purification of the aldehyde oxidase homolog 1 (AOH1) protein and RT cloning of the AOH1 and aldehyde oxidase homolog 2 (AOH2) genes. RT Identification of a novel molybdo-flavoprotein gene cluster on mouse RT chromosome 1."; RL J. Biol. Chem. 276:46347-46363(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION. RC STRAIN=CD-1; TISSUE=Olfactory epithelium; RX PubMed=15383531; DOI=10.1074/jbc.M408734200; RA Kurosaki M., Terao M., Barzago M.M., Bastone A., Bernardinello D., RA Salmona M., Garattini E.; RT "The aldehyde oxidase gene cluster in mice and rats. Aldehyde oxidase RT homologue 3, a novel member of the molybdo-flavoenzyme family with RT selective expression in the olfactory mucosa."; RL J. Biol. Chem. 279:50482-50498(2004). RN [6] RP FUNCTION, TISSUE SPECIFICITY, AND INDUCTION BY TESTOSTERONE. RX PubMed=18981221; DOI=10.1128/MCB.01385-08; RA Terao M., Kurosaki M., Barzago M.M., Fratelli M., Bagnati R., RA Bastone A., Giudice C., Scanziani E., Mancuso A., Tiveron C., RA Garattini E.; RT "Role of the molybdoflavoenzyme aldehyde oxidase homolog 2 in the RT biosynthesis of retinoic acid: generation and characterization of a RT knockout mouse."; RL Mol. Cell. Biol. 29:357-377(2009). RN [7] RP CRYSTALLIZATION, FUNCTION AS OXIDASE, SUBSTRATE SPECIFICITY, KINETIC RP PARAMETERS, COFACTOR, AND HOMODIMER. RX PubMed=21705476; DOI=10.1124/dmd.111.040873; RA Mahro M., Coelho C., Trincao J., Rodrigues D., Terao M., Garattini E., RA Saggu M., Lendzian F., Hildebrandt P., Romao M.J., Leimkuhler S.; RT "Characterization and crystallization of mouse aldehyde oxidase 3: RT from mouse liver to Escherichia coli heterologous protein RT expression."; RL Drug Metab. Dispos. 39:1939-1945(2011). RN [8] RP IDENTIFICATION OF PARALOGS. RX PubMed=23263164; DOI=10.1007/s00018-012-1229-5; RA Kurosaki M., Bolis M., Fratelli M., Barzago M.M., Pattini L., RA Perretta G., Terao M., Garattini E.; RT "Structure and evolution of vertebrate aldehyde oxidases: from gene RT duplication to gene suppression."; RL Cell. Mol. Life Sci. 70:1807-1830(2013). RN [9] RP X-RAY CRYSTALLOGRAPHY (2.54 ANGSTROMS) IN COMPLEX WITH FE-S CLUSTERS; RP FAD AND MO-MPT, FUNCTION AS OXIDASE, SUBSTRATE SPECIFICITY, COFACTOR, RP KINETIC PARAMETERS, HOMODIMER, ENZYME REGULATION, REACTION MECHANISM, RP ACTIVE SITE, AND MUTAGENESIS OF ALA-807; TYR-885; LYS-889 AND RP GLU-1266. RX PubMed=23019336; DOI=10.1074/jbc.M112.390419; RA Coelho C., Mahro M., Trincao J., Carvalho A.T., Ramos M.J., Terao M., RA Garattini E., Leimkuhler S., Romao M.J.; RT "The first mammalian aldehyde oxidase crystal structure: insights into RT substrate specificity."; RL J. Biol. Chem. 287:40690-40702(2012). CC -!- FUNCTION: Oxidase with broad substrate specificity, oxidizing CC aromatic azaheterocycles, such as N1-methylnicotinamide and CC phthalazine, as well as aldehydes, such as benzaldehyde, retinal CC and pyridoxal. Plays a key role in the metabolism of xenobiotics CC and drugs containing aromatic azaheterocyclic substituents. Is CC probably involved in the regulation of reactive oxygen species CC homeostasis. May be a prominent source of superoxide generation CC via the one-electron reduction of molecular oxygen. Also may CC catalyze nitric oxide (NO) production via the reduction of nitrite CC to NO with NADH or aldehyde as electron donor. CC -!- CATALYTIC ACTIVITY: An aldehyde + H(2)O + O(2) = a carboxylate + CC H(2)O(2). CC -!- COFACTOR: Binds 2 2Fe-2S clusters per subunit. CC -!- COFACTOR: Binds 1 FAD per subunit. CC -!- COFACTOR: Binds 1 molybdenum-molybdopterin (Mo-MPT) cofactor per CC subunit. CC -!- ENZYME REGULATION: Inhibited by potassium cyanide, menadione, CC benzamidine, raloxifene and norharmane. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=2.3 uM for phthalazine (PubMed:11562361); CC KM=1.4 uM for phthalazine (at 37 degrees Celsius and pH 8) CC (PubMed:23019336); CC KM=2.5 uM for benzaldehyde (at 37 degrees Celsius and pH 8) CC (PubMed=23019336); CC KM=128.5 uM for N1-methylnicotinamide (at 37 degrees Celsius and CC pH 8) (PubMed:23019336); CC KM=32.3 uM for phenanthridine (at 37 degrees Celsius and pH 8) CC (PubMed:23019336); CC KM=13 uM for benzaldehyde (at 37 degrees Celsius and pH 7.4) CC (PubMed:21705476); CC KM=29 uM for butyraldehyde (at 37 degrees Celsius and pH 8) CC (PubMed:21705476); CC KM=173 uM for 2-OH-pyrimidine (at 37 degrees Celsius and pH 8) CC (PubMed:21705476); CC Note=kcat is 4 sec(-1) for phthalazine oxidation CC (PubMed:11562361). kcat is 130 min(-1) for benzaldehyde CC oxidation, 384 min(-1) for butyraldehyde oxidation and 1279 CC min(-1) for 2-OH-pyrimidine oxidation (PubMed=21705476). kcat is CC 41.1 min(-1) for phthalazine oxidation, 41.9 min(-1) for CC benzaldehyde oxidation, 14.7 min(-1) for N1-methylnicotinamide CC oxidation and 51.7 min(-1) for phenanthridine oxidation CC (PubMed:23019336); CC -!- SUBUNIT: Homodimer. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- TISSUE SPECIFICITY: Highly expressed in liver (at protein level). CC In liver, the expression is greater in males than females. CC -!- INDUCTION: Induced by testosterone. CC -!- MISCELLANEOUS: AOX genes evolved from a xanthine oxidoreductase CC ancestral precursor via a series of gene duplication and CC suppression/deletion events. Different animal species contain a CC different complement of AOX genes encoding an equivalent number of CC AOX isoenzymes. In mammals, the two extremes are represented by CC certain rodents such as mice and rats, which are endowed with 4 CC AOX genes, and by humans, whose genome is characterized by a CC single active gene (PubMed:23263164). CC -!- SIMILARITY: Belongs to the xanthine dehydrogenase family. CC -!- SIMILARITY: Contains 1 2Fe-2S ferredoxin-type domain. CC -!- SIMILARITY: Contains 1 FAD-binding PCMH-type domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF322178; AAL36596.1; -; Genomic_DNA. DR EMBL; AF322144; AAL36596.1; JOINED; Genomic_DNA. DR EMBL; AF322145; AAL36596.1; JOINED; Genomic_DNA. DR EMBL; AF322146; AAL36596.1; JOINED; Genomic_DNA. DR EMBL; AF322147; AAL36596.1; JOINED; Genomic_DNA. DR EMBL; AF322148; AAL36596.1; JOINED; Genomic_DNA. DR EMBL; AF322149; AAL36596.1; JOINED; Genomic_DNA. DR EMBL; AF322150; AAL36596.1; JOINED; Genomic_DNA. DR EMBL; AF322151; AAL36596.1; JOINED; Genomic_DNA. DR EMBL; AF322152; AAL36596.1; JOINED; Genomic_DNA. DR EMBL; AF322153; AAL36596.1; JOINED; Genomic_DNA. DR EMBL; AF322154; AAL36596.1; JOINED; Genomic_DNA. DR EMBL; AF322155; AAL36596.1; JOINED; Genomic_DNA. DR EMBL; AF322156; AAL36596.1; JOINED; Genomic_DNA. DR EMBL; AF322157; AAL36596.1; JOINED; Genomic_DNA. DR EMBL; AF322158; AAL36596.1; JOINED; Genomic_DNA. DR EMBL; AF322159; AAL36596.1; JOINED; Genomic_DNA. DR EMBL; AF322160; AAL36596.1; JOINED; Genomic_DNA. DR EMBL; AF322161; AAL36596.1; JOINED; Genomic_DNA. DR EMBL; AF322162; AAL36596.1; JOINED; Genomic_DNA. DR EMBL; AF322163; AAL36596.1; JOINED; Genomic_DNA. DR EMBL; AF322164; AAL36596.1; JOINED; Genomic_DNA. DR EMBL; AF322165; AAL36596.1; JOINED; Genomic_DNA. DR EMBL; AF322166; AAL36596.1; JOINED; Genomic_DNA. DR EMBL; AF322167; AAL36596.1; JOINED; Genomic_DNA. DR EMBL; AF322168; AAL36596.1; JOINED; Genomic_DNA. DR EMBL; AF322169; AAL36596.1; JOINED; Genomic_DNA. DR EMBL; AF322170; AAL36596.1; JOINED; Genomic_DNA. DR EMBL; AF322171; AAL36596.1; JOINED; Genomic_DNA. DR EMBL; AF322172; AAL36596.1; JOINED; Genomic_DNA. DR EMBL; AF322173; AAL36596.1; JOINED; Genomic_DNA. DR EMBL; AF322174; AAL36596.1; JOINED; Genomic_DNA. DR EMBL; AF322175; AAL36596.1; JOINED; Genomic_DNA. DR EMBL; AF322176; AAL36596.1; JOINED; Genomic_DNA. DR EMBL; AF322177; AAL36596.1; JOINED; Genomic_DNA. DR EMBL; AC025116; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH466548; EDL00068.1; -; Genomic_DNA. DR EMBL; BC138876; AAI38877.1; -; mRNA. DR RefSeq; NP_076106.2; NM_023617.2. DR UniGene; Mm.20108; -. DR PDB; 3ZYV; X-ray; 2.54 A; A/B/C/D=1-1335. DR PDBsum; 3ZYV; -. DR ProteinModelPortal; G3X982; -. DR SMR; G3X982; 7-167. DR MINT; MINT-1856330; -. DR PaxDb; B2RSI5; -. DR Ensembl; ENSMUST00000040999; ENSMUSP00000049391; ENSMUSG00000064294. DR GeneID; 71724; -. DR KEGG; mmu:71724; -. DR UCSC; uc007bbm.1; mouse. DR CTD; 71724; -. DR MGI; MGI:1918974; Aox3. DR eggNOG; COG4630; -. DR GeneTree; ENSGT00390000003772; -. DR HOVERGEN; HBG004182; -. DR InParanoid; B2RSI5; -. DR KO; K00157; -. DR OMA; PIVESAK; -. DR OrthoDB; EOG4H19TX; -. DR TreeFam; TF353036; -. DR NextBio; 334339; -. DR ArrayExpress; G3X982; -. DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0004031; F:aldehyde oxidase activity; IDA:MGI. DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0030151; F:molybdenum ion binding; IDA:MGI. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR GO; GO:0008762; F:UDP-N-acetylmuramate dehydrogenase activity; IEA:InterPro. DR Gene3D; 1.10.150.120; -; 1. DR Gene3D; 3.10.20.30; -; 1. DR Gene3D; 3.30.365.10; -; 6. DR Gene3D; 3.30.43.10; -; 1. DR Gene3D; 3.30.465.10; -; 1. DR Gene3D; 3.90.1170.50; -; 1. DR InterPro; IPR002888; 2Fe-2S-bd. DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type. DR InterPro; IPR006058; 2Fe2S_fd_BS. DR InterPro; IPR000674; Ald_Oxase/Xan_DH_a/b. DR InterPro; IPR016208; Ald_Oxase/xanthine_DH. DR InterPro; IPR014313; Aldehyde_oxidase. DR InterPro; IPR008274; AldOxase/xan_DH_Mopterin-bd. DR InterPro; IPR012675; Beta-grasp_dom. DR InterPro; IPR005107; CO_DH_flav_C. DR InterPro; IPR016169; CO_DH_flavot_FAD-bd_sub2. DR InterPro; IPR016166; FAD-bd_2. DR InterPro; IPR016167; FAD-bd_2_sub1. DR InterPro; IPR002346; Mopterin_DH_FAD-bd. DR PANTHER; PTHR11908:SF10; PTHR11908:SF10; 1. DR Pfam; PF01315; Ald_Xan_dh_C; 1. DR Pfam; PF02738; Ald_Xan_dh_C2; 1. DR Pfam; PF03450; CO_deh_flav_C; 1. DR Pfam; PF00941; FAD_binding_5; 1. DR Pfam; PF00111; Fer2; 1. DR Pfam; PF01799; Fer2_2; 1. DR PIRSF; PIRSF000127; Xanthine_DH; 1. DR SMART; SM01008; Ald_Xan_dh_C; 1. DR SMART; SM01092; CO_deh_flav_C; 1. DR SUPFAM; SSF47741; SSF47741; 1. DR SUPFAM; SSF54292; SSF54292; 1. DR SUPFAM; SSF54665; SSF54665; 1. DR SUPFAM; SSF55447; SSF55447; 1. DR SUPFAM; SSF56003; SSF56003; 1. DR SUPFAM; SSF56176; SSF56176; 1. DR TIGRFAMs; TIGR02969; mam_aldehyde_ox; 1. DR PROSITE; PS00197; 2FE2S_FER_1; 1. DR PROSITE; PS51085; 2FE2S_FER_2; 1. DR PROSITE; PS51387; FAD_PCMH; 1. PE 1: Evidence at protein level; KW 2Fe-2S; 3D-structure; Complete proteome; Cytoplasm; FAD; Flavoprotein; KW Iron; Iron-sulfur; Metal-binding; Molybdenum; Oxidoreductase; KW Reference proteome. FT CHAIN 1 1335 Aldehyde oxidase 3. FT /FTId=PRO_0000425247. FT DOMAIN 8 95 2Fe-2S ferredoxin-type. FT DOMAIN 236 421 FAD-binding PCMH-type. FT NP_BIND 264 271 FAD. FT ACT_SITE 1266 1266 Proton acceptor; for azaheterocycle FT hydroxylase activity (Probable). FT METAL 47 47 Iron-sulfur 1 (2Fe-2S). FT METAL 52 52 Iron-sulfur 1 (2Fe-2S). FT METAL 55 55 Iron-sulfur 1 (2Fe-2S). FT METAL 77 77 Iron-sulfur 1 (2Fe-2S). FT METAL 117 117 Iron-sulfur 2 (2Fe-2S). FT METAL 120 120 Iron-sulfur 2 (2Fe-2S). FT METAL 152 152 Iron-sulfur 2 (2Fe-2S). FT METAL 154 154 Iron-sulfur 2 (2Fe-2S). FT BINDING 116 116 Molybdopterin. FT BINDING 354 354 FAD. FT BINDING 358 358 FAD. FT BINDING 367 367 FAD. FT BINDING 411 411 FAD; via amide nitrogen. FT BINDING 802 802 Molybdopterin; via amide nitrogen. FT BINDING 1043 1043 Molybdopterin; via amide nitrogen. FT BINDING 1199 1199 Molybdopterin. FT MUTAGEN 807 807 A->V: No effect on kinetic constants with FT smaller substrates like benzaldehyde or FT phthalazine. Decreases substrate affinity FT and slightly increases catalytic FT efficiency for bulkier substrates like FT phenanthridine. FT MUTAGEN 885 885 Y->M: Slightly decreases substrate FT affinity but no effect on activity with FT smaller substrates like benzaldehyde or FT phthalazine. Increases catalytic FT efficiency with bulkier substrates like FT phenanthridine or more charged substrates FT like N1-methylnicotinamide. FT MUTAGEN 889 889 K->H: No effect on substrate affinity but FT decreases catalytic efficiency for FT smaller substrates like benzaldehyde or FT phthalazine. Increases substrate affinity FT and activity for bulkier substrates like FT phenanthridine. FT MUTAGEN 1266 1266 E->Q: Loss of activity with different N- FT heterocyclic compounds as substrates. 60% FT reduction of activity with benzaldehyde. FT CONFLICT 308 308 A -> T (in Ref. 1; AAL36596). FT CONFLICT 541 541 K -> R (in Ref. 4; AAI38877). SQ SEQUENCE 1335 AA; 146902 MW; 29683B03DD3E75E9 CRC64; MSPSKESDEL IFFVNGKKVT ERNADPEVNL LFYLRKVIRL TGTKYGCGGG DCGACTVMIS RYDPISKRIS HFSATACLVP ICSLHGAAVT TVEGIGSTKT RIHPVQERIA KGHGTQCGFC TPGMVMSIYT LLRNHPEPST EQIMETLGGN LCRCTGYRPI VESAKSFCPS STCCQMNGEG KCCLDEEKNE PERKNSVCTK LYEKKEFQPL DPTQELIFPP ELMRMAEESQ NTVLTFRGER TTWIAPGTLN DLLELKMKHP SAPLVIGNTY LGLHMKFTDV SYPIIISPAR ILELFVVTNT KQGLTLGAGL SLTQVKNVLS DVVSRLPKEK TQIYCALLKQ LKTLAGQQIR NVASLGGHII SRLPTSDLNP ILGIGNCILN VASTEGIQQI PLNDHFLAGV PDAILKPEQV LISVFVPRSS KWEFVSAFRQ APRQQNAFAT VNAGMKVVFK EDTNTITDLG ILYGGIGATV ISADKSCRQL IGRCWDEEML DDAGKMICEE VSLLMAAPGG MEEYRKTLAI SFLFMFYLDV LKQLKTRDPH KYPDISQKLL HILEDFPLTM PYGMQSFQDV DFQQPLQDPI GRPIMHQSGI KHATGEAVFC DDMSVLPGEL FLAVVTSSKS HAKIISLDAS EALASLGVVD VVTARDVPGD NGREEESLYA QDEVICVGQI VCAVAADSYA HAQQAAKKVK IVYQDIEPMI VTVQDALQYE SFIGPERKLE QGNVEEAFQC ADQILEGEVH LGGQEHFYME TQSVRVVPKG EDKEMDIYVS SQDAAFTQEM VARTLGIPKN RINCHVKRVG GAFGGKASKP GLLASVAAVA AQKTGRPIRF ILERRDDMLI TGGRHPLLGK YKIGFMNNGK IKAADIQLYI NGGCTPDDSE LVIEYALLKL ENAYKIPNLR VRGRVCKTNL PSNTAFRGFG FPQGAFVTET CMSAVAAKCR LPPEKVRELN MYRTIDRTIH NQEFDPTNLL QCWEACVENS SYYNRKKAVD EFNQQRFWKK RGIAIIPMKF SVGFPKTFYY QAAALVQIYT DGSVLVAHGG VELGQGINTK MIQVASRELK IPMSYIHLDE MSTVTVPNTV TTGASTGADV NGRAVQNACQ ILMKRLEPII KQNPSGTWEE WVKEAFVQSI SLSATGYFRG YQADMDWEKG EGDIFPYFVF GAACSEVEID CLTGAHKNIR TDIVMDGSFS INPAVDIGQI EGAFVQGLGL YTLEELKYSP EGVLYTRGPH QYKIASVTDI PEEFHVSLLT PTPNPKAIYS SKGLGEAGTF LGCSVFFAIA AAVAAAREER GLSPIWAINS PATAEVIRMA CEDQFTNLVP QTDSKCCKPW SIPVA // ID AOXA_MOUSE Reviewed; 1333 AA. AC O54754; Q9WU85; Q9Z2Z5; DT 15-MAY-2002, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1999, sequence version 2. DT 19-MAR-2014, entry version 123. DE RecName: Full=Aldehyde oxidase 1; DE EC=1.2.3.1; DE AltName: Full=Azaheterocycle hydroxylase 1; DE EC=1.17.3.-; DE AltName: Full=Retinal oxidase; GN Name=Aox1; Synonyms=Ao, Ro; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, INDUCTION, AND RP TISSUE SPECIFICITY. RC STRAIN=CD-1; TISSUE=Liver; RX PubMed=10377246; DOI=10.1042/0264-6021:3410071; RA Kurosaki M., Demontis S., Barzago M.M., Garattini E., Terao M.; RT "Molecular cloning of the cDNA coding for mouse aldehyde oxidase: RT tissue distribution and regulation in vivo by testosterone."; RL Biochem. J. 341:71-80(1999). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION AS RETINAL OXIDASE, CATALYTIC RP ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND HOMODIMER. RC STRAIN=C57BL/6 X CBA; TISSUE=Liver; RX PubMed=10190983; DOI=10.1006/abbi.1999.1129; RA Huang D.-Y., Furukawa A., Ichikawa Y.; RT "Molecular cloning of retinal oxidase/aldehyde oxidase cDNAs from RT rabbit and mouse livers and functional expression of recombinant mouse RT retinal oxidase cDNA in Escherichia coli."; RL Arch. Biochem. Biophys. 364:264-272(1999). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DEVELOPMENTAL STAGE. RC STRAIN=129/Sv; TISSUE=Thymus; RX PubMed=10673024; DOI=10.1016/S0167-4781(99)00174-8; RA Demontis S., Kurosaki M., Saccone S., Salvatore M., Garattini E., RA Terao M.; RT "The mouse aldehyde oxidase gene: molecular cloning, chromosomal RT mapping and functional characterization of the 5'-flanking region."; RL Biochim. Biophys. Acta 1489:207-222(1999). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] OF 561-746, AND TISSUE SPECIFICITY. RC STRAIN=C57BL/6J; TISSUE=Liver; RX PubMed=9243637; RA Bendotti C., Prosperini E., Kurosaki M., Garattini E., Terao M.; RT "Selective localization of mouse aldehyde oxidase mRNA in the choroid RT plexus and motor neurons."; RL NeuroReport 8:2343-2349(1997). RN [5] RP FUNCTION IN ADIPOGENESIS, DEVELOPMENTAL STAGE, AND INDUCTION. RX PubMed=18671973; DOI=10.1016/j.febslet.2008.07.034; RA Weigert J., Neumeier M., Bauer S., Mages W., Schnitzbauer A.A., RA Obed A., Groeschl B., Hartmann A., Schaeffler A., Aslanidis C., RA Schoelmerich J., Buechler C.; RT "Small-interference RNA-mediated knock-down of aldehyde oxidase 1 in RT 3T3-L1 cells impairs adipogenesis and adiponectin release."; RL FEBS Lett. 582:2965-2972(2008). RN [6] RP FUNCTION AS OXIDASE, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, RP HOMODIMER, COFACTORS, KINETIC PARAMETERS, REACTION MECHANISM, ACTIVE RP SITE, AND MUTAGENESIS OF VAL-806; MET-884 AND GLU-1265. RX PubMed=19401776; DOI=10.1371/journal.pone.0005348; RA Schumann S., Terao M., Garattini E., Saggu M., Lendzian F., RA Hildebrandt P., Leimkuhler S.; RT "Site directed mutagenesis of amino acid residues at the active site RT of mouse aldehyde oxidase AOX1."; RL PLoS ONE 4:E5348-E5348(2009). RN [7] RP TISSUE SPECIFICITY, AND IDENTIFICATION OF PARALOGS. RX PubMed=23263164; DOI=10.1007/s00018-012-1229-5; RA Kurosaki M., Bolis M., Fratelli M., Barzago M.M., Pattini L., RA Perretta G., Terao M., Garattini E.; RT "Structure and evolution of vertebrate aldehyde oxidases: from gene RT duplication to gene suppression."; RL Cell. Mol. Life Sci. 70:1807-1830(2013). RN [8] RP FUNCTION IN XENOBIOTIC METABOLISM, AND TISSUE SPECIFICITY. RX PubMed=23462233; DOI=10.1093/toxsci/kft066; RA Swenson T.L., Casida J.E.; RT "Aldehyde oxidase importance in vivo in xenobiotic metabolism: RT imidacloprid nitroreduction in mice."; RL Toxicol. Sci. 133:22-28(2013). CC -!- FUNCTION: Oxidase with broad substrate specificity, oxidizing CC aromatic azaheterocycles, such as N1-methylnicotinamide and N- CC methylphthalazinium, as well as aldehydes, such as benzaldehyde, CC retinal, pyridoxal, and vanillin. Plays a role in the metabolism CC of xenobiotics and drugs containing aromatic azaheterocyclic CC substituents. Participates in the bioactivation of prodrugs such CC as famciclovir, catalyzing the oxidation step from 6- CC deoxypenciclovir to penciclovir, which is a potent antiviral CC agent. Also plays a role in the reductive metabolism of the CC xenobiotic imidacloprid (IMI) via its nitroreduction to CC nitrosoguanidine (IMI-NNO) and aminoguanidine (IMI-NNH(2)). Is CC probably involved in the regulation of reactive oxygen species CC homeostasis. May be a prominent source of superoxide generation CC via the one-electron reduction of molecular oxygen. Also may CC catalyze nitric oxide (NO) production via the reduction of nitrite CC to NO with NADH or aldehyde as electron donor. May play a role in CC adipogenesis. Cannot use xanthine and hypoxanthine as substrate. CC -!- CATALYTIC ACTIVITY: An aldehyde + H(2)O + O(2) = a carboxylate + CC H(2)O(2). CC -!- CATALYTIC ACTIVITY: Retinal + O(2) + H(2)O = retinoate + H(2)O(2). CC -!- COFACTOR: Binds 2 2Fe-2S clusters per subunit. CC -!- COFACTOR: Binds 1 FAD per subunit. CC -!- COFACTOR: Binds 1 molybdenum-molybdopterin (Mo-MPT) cofactor per CC subunit. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=3.8 uM for retinal (at 37 degrees Celsius and pH 7.8) CC (PubMed:10190983); CC KM=97.7 uM for benzaldehyde (at 30 degrees Celsius and pH 7.5) CC (PubMed:19401776); CC KM=11.4 uM for phthalazine (at 30 degrees Celsius and pH 7.5) CC (PubMed:19401776); CC KM=55.8 uM for retinal (at 30 degrees Celsius and pH 7.5) CC (PubMed:19401776); CC KM=17.5 mM for acetaldehyde (at 30 degrees Celsius and pH 7.5) CC (PubMed:19401776); CC Vmax=807 nmol/min/mg enzyme with retinal as substrate (at 37 CC degrees Celsius and pH 7.8) (PubMed:10190983); CC Note=kcat is 317.6 min(-1) for benzaldehyde oxidation, 128.1 CC min(-1) for phthalazine oxidation, 49.5 min(-1) for retinal CC oxidation, and 519.9 min(-1) for acetaldehyde oxidation (at 30 CC degrees Celsius and pH 7.5) (PubMed:19401776). In CC PubMed:19401776, the measures are done with the recombinant CC protein, which is only 20% active, due to an incomplete CC saturation of the molybdenum cofactor with the sulfido ligand; CC -!- SUBUNIT: Homodimer. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- TISSUE SPECIFICITY: Highest expression in esophagus. Moderately CC low expression in lung, liver, heart, Harderian gland, olfactory CC mucosa, skin and testis. In brain, expression is very high in CC choroid plexus, high in hind brain and low in hippocampus and CC cerebellum. In spinal cord expression is strongest in anterior CC horns. Low expression detected in spleen and eye. AOX1 expression CC in the livers of mice is approximately seven times greater in CC males than females. CC -!- DEVELOPMENTAL STAGE: Expressed in adult liver but not in neonatal CC or embryonic liver. Not detected in preadipocytes but strongly CC induced in mature adipocytes. CC -!- INDUCTION: Repressed by pioglitazone, fenofibrate and PPARA CC agonists. Induced by testosterone. CC -!- MISCELLANEOUS: AOX genes evolved from a xanthine oxidoreductase CC ancestral precursor via a series of gene duplication and CC suppression/deletion events. Different animal species contain a CC different complement of AOX genes encoding an equivalent number of CC AOX isoenzymes. In mammals, the two extremes are represented by CC certain rodents such as mice and rats, which are endowed with 4 CC AOX genes, and by humans, whose genome is characterized by a CC single active gene (PubMed:23263164). CC -!- SIMILARITY: Belongs to the xanthine dehydrogenase family. CC -!- SIMILARITY: Contains 1 2Fe-2S ferredoxin-type domain. CC -!- SIMILARITY: Contains 1 FAD-binding PCMH-type domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF076216; AAC99382.1; -; mRNA. DR EMBL; AB017482; BAA36834.1; -; mRNA. DR EMBL; AF121945; AAD31763.1; -; Genomic_DNA. DR EMBL; AF121911; AAD31763.1; JOINED; Genomic_DNA. DR EMBL; AF121912; AAD31763.1; JOINED; Genomic_DNA. DR EMBL; AF121913; AAD31763.1; JOINED; Genomic_DNA. DR EMBL; AF121914; AAD31763.1; JOINED; Genomic_DNA. DR EMBL; AF121915; AAD31763.1; JOINED; Genomic_DNA. DR EMBL; AF121916; AAD31763.1; JOINED; Genomic_DNA. DR EMBL; AF121917; AAD31763.1; JOINED; Genomic_DNA. DR EMBL; AF121918; AAD31763.1; JOINED; Genomic_DNA. DR EMBL; AF121919; AAD31763.1; JOINED; Genomic_DNA. DR EMBL; AF121920; AAD31763.1; JOINED; Genomic_DNA. DR EMBL; AF121921; AAD31763.1; JOINED; Genomic_DNA. DR EMBL; AF121922; AAD31763.1; JOINED; Genomic_DNA. DR EMBL; AF121923; AAD31763.1; JOINED; Genomic_DNA. DR EMBL; AF121924; AAD31763.1; JOINED; Genomic_DNA. DR EMBL; AF121925; AAD31763.1; JOINED; Genomic_DNA. DR EMBL; AF121926; AAD31763.1; JOINED; Genomic_DNA. DR EMBL; AF121927; AAD31763.1; JOINED; Genomic_DNA. DR EMBL; AF121928; AAD31763.1; JOINED; Genomic_DNA. DR EMBL; AF121929; AAD31763.1; JOINED; Genomic_DNA. DR EMBL; AF121930; AAD31763.1; JOINED; Genomic_DNA. DR EMBL; AF121931; AAD31763.1; JOINED; Genomic_DNA. DR EMBL; AF121932; AAD31763.1; JOINED; Genomic_DNA. DR EMBL; AF121933; AAD31763.1; JOINED; Genomic_DNA. DR EMBL; AF121934; AAD31763.1; JOINED; Genomic_DNA. DR EMBL; AF121935; AAD31763.1; JOINED; Genomic_DNA. DR EMBL; AF121936; AAD31763.1; JOINED; Genomic_DNA. DR EMBL; AF121937; AAD31763.1; JOINED; Genomic_DNA. DR EMBL; AF121938; AAD31763.1; JOINED; Genomic_DNA. DR EMBL; AF121939; AAD31763.1; JOINED; Genomic_DNA. DR EMBL; AF121940; AAD31763.1; JOINED; Genomic_DNA. DR EMBL; AF121941; AAD31763.1; JOINED; Genomic_DNA. DR EMBL; AF121942; AAD31763.1; JOINED; Genomic_DNA. DR EMBL; AF121943; AAD31763.1; JOINED; Genomic_DNA. DR EMBL; AF121944; AAD31763.1; JOINED; Genomic_DNA. DR RefSeq; NP_033806.2; NM_009676.2. DR UniGene; Mm.26787; -. DR ProteinModelPortal; O54754; -. DR SMR; O54754; 4-535, 577-1315. DR IntAct; O54754; 2. DR MINT; MINT-1869370; -. DR BindingDB; O54754; -. DR ChEMBL; CHEMBL1641354; -. DR PhosphoSite; O54754; -. DR PaxDb; O54754; -. DR PRIDE; O54754; -. DR GeneID; 11761; -. DR KEGG; mmu:11761; -. DR CTD; 316; -. DR MGI; MGI:88035; Aox1. DR eggNOG; COG4630; -. DR HOGENOM; HOG000191197; -. DR HOVERGEN; HBG004182; -. DR InParanoid; O54754; -. DR KO; K00157; -. DR NextBio; 279515; -. DR PRO; PR:O54754; -. DR CleanEx; MM_AOX1; -. DR Genevestigator; O54754; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0004031; F:aldehyde oxidase activity; IDA:MGI. DR GO; GO:0009055; F:electron carrier activity; IDA:MGI. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR GO; GO:0008762; F:UDP-N-acetylmuramate dehydrogenase activity; IEA:InterPro. DR Gene3D; 1.10.150.120; -; 1. DR Gene3D; 3.10.20.30; -; 1. DR Gene3D; 3.30.365.10; -; 6. DR Gene3D; 3.30.43.10; -; 1. DR Gene3D; 3.30.465.10; -; 1. DR Gene3D; 3.90.1170.50; -; 1. DR InterPro; IPR002888; 2Fe-2S-bd. DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type. DR InterPro; IPR006058; 2Fe2S_fd_BS. DR InterPro; IPR000674; Ald_Oxase/Xan_DH_a/b. DR InterPro; IPR016208; Ald_Oxase/xanthine_DH. DR InterPro; IPR014313; Aldehyde_oxidase. DR InterPro; IPR008274; AldOxase/xan_DH_Mopterin-bd. DR InterPro; IPR012675; Beta-grasp_dom. DR InterPro; IPR005107; CO_DH_flav_C. DR InterPro; IPR016169; CO_DH_flavot_FAD-bd_sub2. DR InterPro; IPR016166; FAD-bd_2. DR InterPro; IPR016167; FAD-bd_2_sub1. DR InterPro; IPR002346; Mopterin_DH_FAD-bd. DR InterPro; IPR022407; OxRdtase_Mopterin_BS. DR PANTHER; PTHR11908:SF10; PTHR11908:SF10; 1. DR Pfam; PF01315; Ald_Xan_dh_C; 1. DR Pfam; PF02738; Ald_Xan_dh_C2; 1. DR Pfam; PF03450; CO_deh_flav_C; 1. DR Pfam; PF00941; FAD_binding_5; 1. DR Pfam; PF00111; Fer2; 1. DR Pfam; PF01799; Fer2_2; 1. DR PIRSF; PIRSF000127; Xanthine_DH; 1. DR SMART; SM01008; Ald_Xan_dh_C; 1. DR SMART; SM01092; CO_deh_flav_C; 1. DR SUPFAM; SSF47741; SSF47741; 1. DR SUPFAM; SSF54292; SSF54292; 1. DR SUPFAM; SSF54665; SSF54665; 1. DR SUPFAM; SSF55447; SSF55447; 1. DR SUPFAM; SSF56003; SSF56003; 1. DR SUPFAM; SSF56176; SSF56176; 1. DR TIGRFAMs; TIGR02969; mam_aldehyde_ox; 1. DR PROSITE; PS00197; 2FE2S_FER_1; 1. DR PROSITE; PS51085; 2FE2S_FER_2; 1. DR PROSITE; PS51387; FAD_PCMH; 1. DR PROSITE; PS00559; MOLYBDOPTERIN_EUK; 1. PE 1: Evidence at protein level; KW 2Fe-2S; Complete proteome; Cytoplasm; FAD; Flavoprotein; Iron; KW Iron-sulfur; Metal-binding; Molybdenum; Oxidoreductase; Polymorphism; KW Reference proteome. FT CHAIN 1 1333 Aldehyde oxidase 1. FT /FTId=PRO_0000166106. FT DOMAIN 4 91 2Fe-2S ferredoxin-type. FT DOMAIN 235 420 FAD-binding PCMH-type. FT NP_BIND 263 270 FAD (By similarity). FT ACT_SITE 1265 1265 Proton acceptor; for azaheterocycle FT hydroxylase activity (Probable). FT METAL 43 43 Iron-sulfur 1 (2Fe-2S) (By similarity). FT METAL 48 48 Iron-sulfur 1 (2Fe-2S) (By similarity). FT METAL 51 51 Iron-sulfur 1 (2Fe-2S) (By similarity). FT METAL 73 73 Iron-sulfur 1 (2Fe-2S) (By similarity). FT METAL 113 113 Iron-sulfur 2 (2Fe-2S) (By similarity). FT METAL 116 116 Iron-sulfur 2 (2Fe-2S) (By similarity). FT METAL 148 148 Iron-sulfur 2 (2Fe-2S) (By similarity). FT METAL 150 150 Iron-sulfur 2 (2Fe-2S) (By similarity). FT BINDING 112 112 Molybdopterin (By similarity). FT BINDING 353 353 FAD (By similarity). FT BINDING 357 357 FAD (By similarity). FT BINDING 366 366 FAD (By similarity). FT BINDING 410 410 FAD; via amide nitrogen (By similarity). FT BINDING 801 801 Molybdopterin; via amide nitrogen (By FT similarity). FT BINDING 1042 1042 Molybdopterin; via amide nitrogen (By FT similarity). FT BINDING 1198 1198 Molybdopterin (By similarity). FT VARIANT 109 109 H -> Q (in strain: 129/Sv). FT VARIANT 168 168 A -> G (in strain: C57BL/6 X CBA and 129/ FT Sv). FT VARIANT 449 449 R -> T (in strain: C57BL/6 X CBA). FT VARIANT 492 492 R -> A (in strain: C57BL/6 X CBA, FT requires 2 nucleotide substitutions). FT VARIANT 686 687 KQ -> NE (in strain: 129/Sv). FT VARIANT 857 857 E -> D (in strain: 129/Sv). FT VARIANT 983 983 E -> D (in strain: C57BL/6 X CBA). FT VARIANT 1169 1169 N -> D (in strain: C57BL/6 X CBA and 129/ FT Sv). FT VARIANT 1329 1329 C -> W (in strain: C57BL/6 X CBA and 129/ FT Sv). FT MUTAGEN 806 806 V->E: Decreases substrate affinity and FT activity on benzaldehyde, phthalazine and FT acetaldehyde, while increases affinity FT for more hydrophobic aldehydes like FT retinal. Abolishes catalytic activity; FT when associated with R-884. FT MUTAGEN 884 884 M->R: Abolishes catalytic activity on FT phthalazine and acetaldehyde. Decreases FT catalytic efficiency on benzaldehyde and FT retinal. Abolishes catalytic activity; FT when associated with E-806. FT MUTAGEN 1265 1265 E->Q: Abolishes catalytic activity. SQ SEQUENCE 1333 AA; 146678 MW; 320CF0A3742F6AC5 CRC64; MDPIQLLFYV NGQKVVEKNV DPEMMLLPYL RKNLRLTGTK YGCGGGGCGA CTVMISRYNP STKAIRHHPV NACLTPICSL HGTAVTTVEG LGNTRTRLHP IQERIAKCHG TQCGFCTPGM VMSMYALLRN HPEPTLDQLT DALGGNLCRC TGYRPIIDAC KTFCKASACC QSKENGVCCL DQEINGLAES QEEDKTSPEL FSEEEFLPLD PTQELIFPPE LMRIAEKQPP KTRVFYGERV TWISPVTLKE LVEAKFKYPQ APIVMGYTSV GPEVKFKGVF HPIIISPDRI EELGVISQAR DGLTLGAGLS LDQVKDILAD IVQKLPEEKT QTYRALLKHL RTLAGSQIRN MASLGGHIVS RHLDSDLNPL LAVGNCTLNL LSKDGERRIP LSEEFLRKCP EADLKPQEVL VSVNIPWSRK WEFVSAFRQA QRQQNALAIV NSGMRVLFRE GGGVIEELSI LYGGVGSTII SAKNSCQRLI GRPWNEGMLD TRCRLVLDEV TLAASAPGGK VEFKRTLIIS FLFKFYLEVS QGLKREDPGH SPSLAGNHES ALDDLHSKHP WRTLTHQNVD PAQLPQDPIG RPIMHLSGIK HATGEAIYCD DMPAVDRELF LTFVTSSRAH AKIVSIDLSE ALSLPGVVDI ITADHLQEAN TFGTETFLAT DEVHCVGHLV CAVIADSETR AKQAAKQVKV VYQDLAPLIL TIEEAIQHKS FFKSERKLEC GNVDEAFKIV DQILEGEIHI GGQEHFYMET QSMLVVPKGE DGEIDIYVST QFPKYIQDIV AATLKLSANK VMCHVRRVGG AFGGKVGKTS ILAAITAFAA SKHGRAVRCI LERGEDMLIT GGRHPYLGKY KAGFMNEGRI LALDVEHYCN GGCSLDESLW VIEMGLLKLD NAYKFPNLRC RGWACRTNLP SNTALRGFGF PQAGLVTEAC ITEVAIKCGL SPEQVRTINM YKHVDTTHYK QEFSAKALSE CWRECMAKCS YFERKAAIGK FNAENSWKKR GMAVIPLKFP VGIGSVAMGQ AAALVHIYLD GSALVSHGGI EMGQGVHTKM IQVVSRELRM PMSSVHLRGT STETVPNTNA SGGSVVADLN GLAVKDACQT LLKRLEPIIS KNPQGTWKDW AQTAFDQSIS LSAVGYFRGY ESNIDWEKGE GHPFEYFVFG AACSEVEINC LTGDHKNIRT NIVMDVGHSI NPALDIGQVE GAFIQGMGLY TIEELSYSPQ GTLYSRGPNQ YKIPAICDIP TEMHISFLPP SEHSNTLYSS KGLGESGVFL GCSVFFAIHD AVKAARQERG ISGPWKLNSP LTPEKIRMAC EDKFTKMIPR DEPGSYVPCN IPV // ID AOXB_MOUSE Reviewed; 1345 AA. AC Q5SGK3; B9EKC6; DT 19-FEB-2014, integrated into UniProtKB/Swiss-Prot. DT 04-JAN-2005, sequence version 2. DT 19-MAR-2014, entry version 90. DE RecName: Full=Aldehyde oxidase 2; DE EC=1.2.3.1; DE AltName: Full=Aldehyde oxidase homolog 3; DE AltName: Full=Azaheterocycle hydroxylase 2; DE EC=1.17.3.-; GN Name=Aox2; Synonyms=Aoh3, Aox3l1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION BY MASS SPECTROMETRY, RP FUNCTION AS OXIDASE, SUBSTRATE SPECIFICITY, TISSUE SPECIFICITY, AND RP SUBCELLULAR LOCATION. RC STRAIN=CD-1; TISSUE=Olfactory epithelium; RX PubMed=15383531; DOI=10.1074/jbc.M408734200; RA Kurosaki M., Terao M., Barzago M.M., Bastone A., Bernardinello D., RA Salmona M., Garattini E.; RT "The aldehyde oxidase gene cluster in mice and rats. Aldehyde oxidase RT homologue 3, a novel member of the molybdo-flavoenzyme family with RT selective expression in the olfactory mucosa."; RL J. Biol. Chem. 279:50482-50498(2004). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP TISSUE SPECIFICITY, AND IDENTIFICATION OF PARALOGS. RX PubMed=23263164; DOI=10.1007/s00018-012-1229-5; RA Kurosaki M., Bolis M., Fratelli M., Barzago M.M., Pattini L., RA Perretta G., Terao M., Garattini E.; RT "Structure and evolution of vertebrate aldehyde oxidases: from gene RT duplication to gene suppression."; RL Cell. Mol. Life Sci. 70:1807-1830(2013). CC -!- FUNCTION: Oxidase with broad substrate specificity, oxidizing CC aromatic azaheterocycles, such as phthalazine, as well as CC aldehydes, such as benzaldehyde and retinal. Cannot use CC hypoxanthine as substrate. CC -!- CATALYTIC ACTIVITY: An aldehyde + H(2)O + O(2) = a carboxylate + CC H(2)O(2). CC -!- COFACTOR: Binds 2 2Fe-2S clusters per subunit (By similarity). CC -!- COFACTOR: Binds 1 FAD per subunit (By similarity). CC -!- COFACTOR: Binds 1 molybdenum-molybdopterin (Mo-MPT) cofactor per CC subunit (By similarity). CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- TISSUE SPECIFICITY: Expressed in olfactory mucosa epithelium (at CC protein level). Detected in skin. CC -!- MISCELLANEOUS: AOX genes evolved from a xanthine oxidoreductase CC ancestral precursor via a series of gene duplication and CC suppression/deletion events. Different animal species contain a CC different complement of AOX genes encoding an equivalent number of CC AOX isoenzymes. In mammals, the two extremes are represented by CC certain rodents such as mice and rats, which are endowed with 4 CC AOX genes, and by humans, whose genome is characterized by a CC single active gene (PubMed:23263164). CC -!- SIMILARITY: Belongs to the xanthine dehydrogenase family. CC -!- SIMILARITY: Contains 1 2Fe-2S ferredoxin-type domain. CC -!- SIMILARITY: Contains 1 FAD-binding PCMH-type domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AY187018; AAO38750.2; -; mRNA. DR EMBL; AY665589; AAV68256.1; -; mRNA. DR EMBL; AC121091; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC163498; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC150826; AAI50827.1; -; mRNA. DR RefSeq; NP_001008419.1; NM_001008419.2. DR UniGene; Mm.414292; -. DR ProteinModelPortal; Q5SGK3; -. DR SMR; Q5SGK3; 8-168. DR STRING; 10090.ENSMUSP00000110006; -. DR PaxDb; B9EKC6; -. DR PRIDE; Q5SGK3; -. DR Ensembl; ENSMUST00000114366; ENSMUSP00000110006; ENSMUSG00000079554. DR GeneID; 213043; -. DR KEGG; mmu:213043; -. DR UCSC; uc007bbp.1; mouse. DR CTD; 213043; -. DR MGI; MGI:3529596; Aox2. DR eggNOG; COG4630; -. DR GeneTree; ENSGT00390000003772; -. DR HOGENOM; HOG000191197; -. DR HOVERGEN; HBG004182; -. DR InParanoid; Q5SGK3; -. DR KO; K00157; -. DR OMA; CYINGGC; -. DR OrthoDB; EOG7QRQSZ; -. DR TreeFam; TF353036; -. DR NextBio; 373826; -. DR Genevestigator; Q5SGK3; -. DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0004031; F:aldehyde oxidase activity; IEA:UniProtKB-EC. DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR GO; GO:0008762; F:UDP-N-acetylmuramate dehydrogenase activity; IEA:InterPro. DR Gene3D; 1.10.150.120; -; 1. DR Gene3D; 3.10.20.30; -; 1. DR Gene3D; 3.30.365.10; -; 6. DR Gene3D; 3.30.43.10; -; 1. DR Gene3D; 3.30.465.10; -; 1. DR Gene3D; 3.90.1170.50; -; 1. DR InterPro; IPR002888; 2Fe-2S-bd. DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type. DR InterPro; IPR006058; 2Fe2S_fd_BS. DR InterPro; IPR000674; Ald_Oxase/Xan_DH_a/b. DR InterPro; IPR016208; Ald_Oxase/xanthine_DH. DR InterPro; IPR014313; Aldehyde_oxidase. DR InterPro; IPR008274; AldOxase/xan_DH_Mopterin-bd. DR InterPro; IPR012675; Beta-grasp_dom. DR InterPro; IPR005107; CO_DH_flav_C. DR InterPro; IPR016169; CO_DH_flavot_FAD-bd_sub2. DR InterPro; IPR016166; FAD-bd_2. DR InterPro; IPR016167; FAD-bd_2_sub1. DR InterPro; IPR002346; Mopterin_DH_FAD-bd. DR PANTHER; PTHR11908:SF10; PTHR11908:SF10; 1. DR Pfam; PF01315; Ald_Xan_dh_C; 1. DR Pfam; PF02738; Ald_Xan_dh_C2; 1. DR Pfam; PF03450; CO_deh_flav_C; 1. DR Pfam; PF00941; FAD_binding_5; 1. DR Pfam; PF00111; Fer2; 1. DR Pfam; PF01799; Fer2_2; 1. DR PIRSF; PIRSF000127; Xanthine_DH; 1. DR SMART; SM01008; Ald_Xan_dh_C; 1. DR SMART; SM01092; CO_deh_flav_C; 1. DR SUPFAM; SSF47741; SSF47741; 1. DR SUPFAM; SSF54292; SSF54292; 1. DR SUPFAM; SSF54665; SSF54665; 1. DR SUPFAM; SSF55447; SSF55447; 1. DR SUPFAM; SSF56003; SSF56003; 1. DR SUPFAM; SSF56176; SSF56176; 1. DR TIGRFAMs; TIGR02969; mam_aldehyde_ox; 1. DR PROSITE; PS00197; 2FE2S_FER_1; 1. DR PROSITE; PS51085; 2FE2S_FER_2; 1. DR PROSITE; PS51387; FAD_PCMH; 1. PE 1: Evidence at protein level; KW 2Fe-2S; Complete proteome; Cytoplasm; FAD; Flavoprotein; Iron; KW Iron-sulfur; Metal-binding; Molybdenum; Oxidoreductase; KW Reference proteome. FT CHAIN 1 1345 Aldehyde oxidase 2. FT /FTId=PRO_0000425245. FT DOMAIN 9 96 2Fe-2S ferredoxin-type. FT DOMAIN 238 423 FAD-binding PCMH-type. FT NP_BIND 266 273 FAD (By similarity). FT ACT_SITE 1276 1276 Proton acceptor; for azaheterocycle FT hydroxylase activity (By similarity). FT METAL 48 48 Iron-sulfur 1 (2Fe-2S) (By similarity). FT METAL 53 53 Iron-sulfur 1 (2Fe-2S) (By similarity). FT METAL 56 56 Iron-sulfur 1 (2Fe-2S) (By similarity). FT METAL 78 78 Iron-sulfur 1 (2Fe-2S) (By similarity). FT METAL 118 118 Iron-sulfur 2 (2Fe-2S) (By similarity). FT METAL 121 121 Iron-sulfur 2 (2Fe-2S) (By similarity). FT METAL 153 153 Iron-sulfur 2 (2Fe-2S) (By similarity). FT METAL 155 155 Iron-sulfur 2 (2Fe-2S) (By similarity). FT BINDING 117 117 Molybdopterin (By similarity). FT BINDING 356 356 FAD (By similarity). FT BINDING 360 360 FAD (By similarity). FT BINDING 369 369 FAD (By similarity). FT BINDING 413 413 FAD; via amide nitrogen (By similarity). FT BINDING 812 812 Molybdopterin; via amide nitrogen (By FT similarity). FT BINDING 1053 1053 Molybdopterin; via amide nitrogen (By FT similarity). FT BINDING 1209 1209 Molybdopterin (By similarity). FT CONFLICT 202 202 K -> E (in Ref. 3; AAI50827). SQ SEQUENCE 1345 AA; 147913 MW; 6D3FA441A3F6F92C CRC64; MPCPAQISDD LEFFVNGRKV TEKNVDPEVT LLAFLRKNLC LTGTKDACGT GGCGACTVMV SQHDPVCKKT RHFSVMACLV PLCSLHGAAV TTVEGVGSIK TRLHPVQERI AKSHGTQCGF CTPGMVMSIY TLLRNHPQPS EEQLMEALGG NLCRCTGYRP ILESGRTFCM EPDGCPQKGT GQCCLDQKES DSSGSKSDIC TKLFVKDEFQ PLDPTQELIF PPELLRMAEN PEKQTLTFYG ERITWIAPGT LQELLVLKAK YPEAPLISGN TALGPAMKSQ GHFYPVLLSP ARIPDLRMVT KTSGGLTIGA CCSLAQVKDI LAESISELPQ EKTQTYRALL KHLRSLAGQQ IRNMASLGGH VISRHCYSDL NPILSVGNTT LNLLSEEGPR QIPLSGHFLA GLASADLKPE EILGSVYIPH SQKREFVSAF RQAQCHQNAL PDVNAGMRVL FREGTDVIEE LSIAYGGVGP TTVSAQRSCQ QLLGRRWNAL MLDEACRLLL DEVSLPGSAL GGKVEFRRTL IVSLFFKFYL EVLQELKADQ KLPPESTDSQ RYPEIADRFL SSLGDFQVTL PRGVQTYQRV DSHQPLQDPV GRPIMHLSGL KHATGEAVFC DDIPRVDKEL FMALVTSTRA HARIISIDSS EVLDLPGVVD VITAEDIPGN NGEEDDKLLA VDKVLCVGQV ICAVVAETDV QAKRATEKIK ITYEDLKPVI FTIEDAIKHN SFLCPEKKLE QGNIEEAFEN VDQVAEGTVH VGGQEHFYME TQRVLVIPKT EDKELDMYVS TQDPAHVQKT VSSTLNIPIS RITCHVKRVG GGFGGKVGRP AVFGAIAAVG AVKTGHPIRL VLDREDDMLI TGGRHPLFAK YKVGFMNSGR IKALDIECYI NGGCTLDDSE LVTEFLVLKL ENAYKIRNLR LRGRACMTNL PSNTAFRGFG FPQGALVTES CITAVAAKCG LPPEKIREKN MYKTVDKTIY KQAFNPDPLI RCWNECLDKS SFHIRRTRVD EFNKKSYWKK RGIAIVPMKF SVGFAATSYH QAAALVHIYT DGSVLVAHGG NELGQGIHTK MLQVASRELK IPLSYLHICE TSTTTVPNTI ATAASVGADV NGRAVQNACQ ILLKRLEPVI KKNPEGTWRD WIEAAFEKRI SLSATGYFRG YKAFMDWEKG EGDPFPYYVY GAACSEVEID CLTGAHKKIR TDIVMDACCS LNPAIDIGQI EGAFIQGMGL YTTEELLYSP EGVLYSRSPD KYKIPTVTDV PEQFNVSLLP SSQTPLTLYS SKGLGESGMF LGSSVFFAIV DAVAAARRQR DIAEDFTVKS PATPEWVRMA CADRFTDMIP RDDPKTFKPW SIPIA // ID AOC3_MOUSE Reviewed; 765 AA. AC O70423; A2A4I7; Q66JM4; Q9R055; DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 19-MAR-2014, entry version 122. DE RecName: Full=Membrane primary amine oxidase; DE EC=1.4.3.21; DE AltName: Full=Copper amine oxidase; DE AltName: Full=Semicarbazide-sensitive amine oxidase; DE Short=SSAO; DE AltName: Full=Vascular adhesion protein 1; DE Short=VAP-1; GN Name=Aoc3; Synonyms=Vap1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1). RC STRAIN=129/SvJ, and BALB/c; RX PubMed=9743358; RA Bono P., Salmi M., Smith D.J., Leppanen I., Horelli-Kuitunen N., RA Palotie A., Jalkanen S.; RT "Isolation, structural characterization, and chromosomal mapping of RT the mouse vascular adhesion protein-1 gene and promoter."; RL J. Immunol. 161:2953-2960(1998). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=10092636; DOI=10.1074/jbc.274.14.9515; RA Moldes M., Feve B., Pairault J.; RT "Molecular cloning of a major mRNA species in murine 3T3 adipocyte RT lineage. differentiation-dependent expression, regulation, and RT identification as semicarbazide-sensitive amine oxidase."; RL J. Biol. Chem. 274:9515-9523(1999). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC STRAIN=C57BL/6; TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: Cell adhesion protein that participates in lymphocyte CC recirculation by mediating the binding of lymphocytes to CC peripheral lymph node vascular endothelial cells in an L-selectin- CC independent fashion. Has a monoamine oxidase activity. May play a CC role in adipogenesis (By similarity). CC -!- CATALYTIC ACTIVITY: RCH(2)NH(2) + H(2)O + O(2) = RCHO + NH(3) + CC H(2)O(2). CC -!- COFACTOR: Binds 1 copper ion per subunit (By similarity). CC -!- COFACTOR: Binds 2 calcium ions per subunit (By similarity). CC -!- COFACTOR: Contains 1 topaquinone per subunit (By similarity). CC -!- SUBUNIT: Homodimer; disulfide-linked. Forms a heterodimer with CC AOC2 (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane CC protein (By similarity). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=O70423-1; Sequence=Displayed; CC Name=2; CC IsoId=O70423-2; Sequence=VSP_016604; CC Note=No experimental confirmation available; CC -!- PTM: Topaquinone (TPQ) is generated by copper-dependent CC autoxidation of a specific tyrosyl residue. CC -!- PTM: N- and O-glycosylated (By similarity). CC -!- SIMILARITY: Belongs to the copper/topaquinone oxidase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF054831; AAC23747.1; -; mRNA. DR EMBL; AF078705; AAC35839.1; -; Genomic_DNA. DR EMBL; AF115411; AAD09199.1; -; mRNA. DR EMBL; AL590969; CAM19551.1; -; Genomic_DNA. DR EMBL; BC080857; AAH80857.1; -; mRNA. DR RefSeq; NP_033805.1; NM_009675.2. DR UniGene; Mm.67281; -. DR ProteinModelPortal; O70423; -. DR SMR; O70423; 58-761. DR BioGrid; 198116; 1. DR IntAct; O70423; 3. DR MINT; MINT-4087892; -. DR STRING; 10090.ENSMUSP00000099394; -. DR ChEMBL; CHEMBL4727; -. DR PaxDb; O70423; -. DR PRIDE; O70423; -. DR Ensembl; ENSMUST00000103105; ENSMUSP00000099394; ENSMUSG00000019326. [O70423-1] DR GeneID; 11754; -. DR KEGG; mmu:11754; -. DR UCSC; uc007lop.2; mouse. [O70423-1] DR CTD; 8639; -. DR MGI; MGI:1306797; Aoc3. DR eggNOG; COG3733; -. DR GeneTree; ENSGT00510000046461; -. DR HOGENOM; HOG000233919; -. DR HOVERGEN; HBG004164; -. DR InParanoid; A2A4I7; -. DR KO; K00276; -. DR OMA; SWERYQL; -. DR OrthoDB; EOG7353W8; -. DR TreeFam; TF314750; -. DR NextBio; 279503; -. DR PRO; PR:O70423; -. DR ArrayExpress; O70423; -. DR Bgee; O70423; -. DR CleanEx; MM_AOC3; -. DR Genevestigator; O70423; -. DR GO; GO:0009986; C:cell surface; ISS:UniProtKB. DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl. DR GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB. DR GO; GO:0005902; C:microvillus; IEA:Ensembl. DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB. DR GO; GO:0052595; F:aliphatic-amine oxidase activity; IEA:UniProtKB-EC. DR GO; GO:0052594; F:aminoacetone:oxygen oxidoreductase(deaminating) activity; IEA:UniProtKB-EC. DR GO; GO:0005509; F:calcium ion binding; IEA:Ensembl. DR GO; GO:0005261; F:cation channel activity; IEA:Ensembl. DR GO; GO:0005507; F:copper ion binding; IEA:InterPro. DR GO; GO:0052596; F:phenethylamine:oxygen oxidoreductase (deaminating) activity; IEA:UniProtKB-EC. DR GO; GO:0008131; F:primary amine oxidase activity; ISS:UniProtKB. DR GO; GO:0048038; F:quinone binding; ISS:UniProtKB. DR GO; GO:0052593; F:tryptamine:oxygen oxidoreductase (deaminating) activity; IEA:UniProtKB-EC. DR GO; GO:0009308; P:amine metabolic process; ISS:UniProtKB. DR GO; GO:0006812; P:cation transport; IEA:GOC. DR GO; GO:0007155; P:cell adhesion; ISS:UniProtKB. DR GO; GO:0034220; P:ion transmembrane transport; IEA:GOC. DR GO; GO:0046677; P:response to antibiotic; IEA:Ensembl. DR Gene3D; 2.70.98.20; -; 1. DR Gene3D; 3.10.450.40; -; 2. DR InterPro; IPR000269; Cu_amine_oxidase. DR InterPro; IPR015798; Cu_amine_oxidase_C. DR InterPro; IPR016182; Cu_amine_oxidase_N-reg. DR InterPro; IPR015800; Cu_amine_oxidase_N2. DR InterPro; IPR015801; Cu_amine_oxidase_N2/3. DR InterPro; IPR015802; Cu_amine_oxidase_N3. DR PANTHER; PTHR10638; PTHR10638; 1. DR Pfam; PF01179; Cu_amine_oxid; 1. DR Pfam; PF02727; Cu_amine_oxidN2; 1. DR Pfam; PF02728; Cu_amine_oxidN3; 1. DR PRINTS; PR00766; CUDAOXIDASE. DR SUPFAM; SSF49998; SSF49998; 1. DR SUPFAM; SSF54416; SSF54416; 2. DR PROSITE; PS01164; COPPER_AMINE_OXID_1; 1. DR PROSITE; PS01165; COPPER_AMINE_OXID_2; 1. PE 2: Evidence at transcript level; KW Alternative splicing; Calcium; Cell adhesion; Complete proteome; KW Copper; Disulfide bond; Glycoprotein; Membrane; Metal-binding; KW Oxidoreductase; Reference proteome; Signal-anchor; TPQ; Transmembrane; KW Transmembrane helix. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 765 Membrane primary amine oxidase. FT /FTId=PRO_0000064103. FT TOPO_DOM 2 6 Cytoplasmic (Potential). FT TRANSMEM 7 27 Helical; Signal-anchor for type II FT membrane protein; (Potential). FT TOPO_DOM 28 765 Extracellular (Potential). FT ACT_SITE 386 386 Proton acceptor (By similarity). FT ACT_SITE 471 471 Schiff-base intermediate with substrate; FT via topaquinone (By similarity). FT METAL 520 520 Copper (By similarity). FT METAL 522 522 Copper (By similarity). FT METAL 529 529 Calcium 1 (By similarity). FT METAL 530 530 Calcium 1; via carbonyl oxygen (By FT similarity). FT METAL 531 531 Calcium 1 (By similarity). FT METAL 572 572 Calcium 2 (By similarity). FT METAL 638 638 Calcium 2 (By similarity). FT METAL 663 663 Calcium 2; via carbonyl oxygen (By FT similarity). FT METAL 665 665 Calcium 2 (By similarity). FT METAL 667 667 Calcium 2 (By similarity). FT METAL 673 673 Calcium 1 (By similarity). FT METAL 674 674 Calcium 1; via carbonyl oxygen (By FT similarity). FT METAL 684 684 Copper (By similarity). FT MOD_RES 471 471 2',4',5'-topaquinone (By similarity). FT CARBOHYD 137 137 N-linked (GlcNAc...) (Potential). FT CARBOHYD 212 212 O-linked (GalNAc...) (By similarity). FT CARBOHYD 232 232 N-linked (GlcNAc...) (Potential). FT CARBOHYD 294 294 N-linked (GlcNAc...) (Potential). FT CARBOHYD 592 592 N-linked (GlcNAc...) (Potential). FT CARBOHYD 659 659 N-linked (GlcNAc...) (Potential). FT CARBOHYD 666 666 N-linked (GlcNAc...) (Potential). FT DISULFID 198 199 By similarity. FT DISULFID 734 741 By similarity. FT DISULFID 748 748 Interchain (By similarity). FT VAR_SEQ 630 765 Missing (in isoform 2). FT /FTId=VSP_016604. FT CONFLICT 659 659 N -> D (in Ref. 2; AAD09199). SQ SEQUENCE 765 AA; 84534 MW; 7489ED67D3DBB44D CRC64; MTQKTTLVLL ALAVITIFAL VCVLLAGRSG DGGGLSQPLH CPSVLPSVQP RTHPSQSQPF ADLSPEELTA VMSFLTKHLG PGLVDAAQAR PSDNCVFSVE LQLPAKAAAL AHLDRGGPPP VREALAIIFF GGQPKPNVSE LVVGPLPHPS YMRDVTVERH GGPLPYYRRP VLDREYQDIE EMIFHRELPQ ASGLLHHCCF YKHQGQNLLT MTTAPRGLQS GDRATWFGLY YNLSGAGFYP HPIGLELLID HKALDPALWT IQKVFYQGRY YESLTQLEDQ FEAGLVNVVL VPNNGTGGSW SLKSSVPPGP APPLQFHPQG PRFSVQGSQV SSSLWAFSFG LGAFSGPRIF DIRFQGERVA YEISVQEAIA LYGGNSPASM STCYVDGSFG IGKYSTPLIR GVDCPYLATY VDWHFLLESQ APKTLRDAFC VFEQNQGLPL RRHHSDFYSH YFGGVVGTVL VVRSVSTLLN YDYIWDMVFH PNGAIEVKFH ATGYISSAFF FGAGEKFGNR VGAHTLGTVH THSAHFKVDL DVAGLKNWAW AEDMAFVPTI VPWQPEYQMQ RLQVTRKLLE TEEEAAFPLG GATPRYLYLA SNHSNKWGHR RGYRIQILSF AGKPLPQESP IEKAFTWGRY HLAVTQRKEE EPSSSSIFNQ NDPWTPTVNF TDFISNETIA GEDLVAWVTA GFLHIPHAED IPNTVTAGNS VGFFLRPYNF FDEDPSFHSA DSIYFREGQD ATACEVNPLA CLSQTATCAP EIPAFSHGGF AYRDN // ID ARK72_MOUSE Reviewed; 367 AA. AC Q8CG76; A2AMV3; Q3UPU2; Q8CG77; Q8JZQ8; Q9D157; DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 3. DT 19-MAR-2014, entry version 105. DE RecName: Full=Aflatoxin B1 aldehyde reductase member 2; DE EC=1.1.1.n11; DE AltName: Full=Succinic semialdehyde reductase; DE Short=SSA reductase; GN Name=Akr7a2; Synonyms=Afar, Akr7a5; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Eye; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 5-367. RC STRAIN=FVB/N; TISSUE=Liver; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] OF 25-367. RC STRAIN=BALB/c; RX PubMed=12879023; DOI=10.1038/sj.onc.1206684; RA Praml C., Savelyeva L., Schwab M.; RT "Aflatoxin B1 aldehyde reductase (AFAR) genes cluster at 1p35-1p36.1 RT in a region frequently altered in human tumour cells."; RL Oncogene 22:4765-4773(2003). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 30-367, AND TISSUE SPECIFICITY. RC STRAIN=CD-1; TISSUE=Liver; RX PubMed=12123834; DOI=10.1016/S0014-5793(02)02982-4; RA Hinshelwood A., McGarvie G., Ellis E.; RT "Characterisation of a novel mouse liver aldo-keto reductase AKR7A5."; RL FEBS Lett. 523:213-218(2002). RN [6] RP SEQUENCE REVISION TO 127 AND 162. RA Ellis E.M., Hinshelwood A., McGarvie G.; RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases. RN [7] RP GENE STRUCTURE. RX PubMed=12071861; DOI=10.1042/BJ20020342; RA Kelly V.P., Sherratt P.J., Crouch D.H., Hayes J.D.; RT "Novel homodimeric and heterodimeric rat gamma-hydroxybutyrate RT synthases that associate with the Golgi apparatus define a distinct RT subclass of aldo-keto reductase 7 family proteins."; RL Biochem. J. 366:847-861(2002). RN [8] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=17242355; DOI=10.1073/pnas.0609836104; RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; RT "Large-scale phosphorylation analysis of mouse liver."; RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). RN [9] RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-244, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., RA Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). RN [10] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-136, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23576753; DOI=10.1073/pnas.1302961110; RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., RA Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.; RT "Label-free quantitative proteomics of the lysine acetylome in RT mitochondria identifies substrates of SIRT3 in metabolic pathways."; RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013). RN [11] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 30-367 IN COMPLEX WITH NADP RP AND THE INHIBITOR TARTRATE, ENZYME REGULATION, CATALYTIC ACTIVITY, RP BIOPHYSICOCHEMICAL PROPERTIES, FUNCTION, AND SUBUNIT. RX PubMed=16460003; DOI=10.1021/bi051610k; RA Zhu X., Lapthorn A.J., Ellis E.M.; RT "Crystal structure of mouse succinic semialdehyde reductase AKR7A5: RT structural basis for substrate specificity."; RL Biochemistry 45:1562-1570(2006). CC -!- FUNCTION: Catalyzes the NADPH-dependent reduction of succinic CC semialdehyde to gamma-hydroxybutyrate. May have an important role CC in producing the neuromodulator gamma-hydroxybutyrate (GHB). Has CC broad substrate specificity. Can reduce the dialdehyde protein- CC binding form of aflatoxin B1 (AFB1) to the non-binding AFB1 CC dialcohol. May be involved in protection of liver against the CC toxic and carcinogenic effects of AFB1, a potent hepatocarcinogen CC (By similarity). CC -!- CATALYTIC ACTIVITY: 4-hydroxybutanoate + NADP(+) = succinate CC semialdehyde + NADPH. CC -!- ENZYME REGULATION: Inhibited by citrate, succinate and tartrate. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=19.8 uM for succinic semialdehyde; CC -!- SUBUNIT: Homodimer. CC -!- SUBCELLULAR LOCATION: Golgi apparatus (By similarity). Cytoplasm CC (By similarity). CC -!- TISSUE SPECIFICITY: Expressed in liver, kidney, testis and brain CC with low levels in skeletal muscle, spleen, heart and lung. CC -!- SIMILARITY: Belongs to the aldo/keto reductase family. Aldo/keto CC reductase 2 subfamily. CC -!- SEQUENCE CAUTION: CC Sequence=AAH31857.1; Type=Erroneous initiation; CC Sequence=CAC81077.1; Type=Erroneous initiation; CC Sequence=CAC81078.1; Type=Erroneous initiation; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK143203; BAE25302.1; -; mRNA. DR EMBL; AL807811; CAM18543.1; -; Genomic_DNA. DR EMBL; BC031857; AAH31857.1; ALT_INIT; mRNA. DR EMBL; AJ271800; CAC81077.1; ALT_INIT; mRNA. DR EMBL; AJ271801; CAC81078.1; ALT_INIT; mRNA. DR EMBL; AF525358; AAO38437.2; -; mRNA. DR EMBL; BK000393; DAA00087.1; -; mRNA. DR RefSeq; NP_079613.3; NM_025337.3. DR UniGene; Mm.482154; -. DR PDB; 2C91; X-ray; 2.30 A; A/B/C/D/E/F/G/H/I/J=30-367. DR PDBsum; 2C91; -. DR ProteinModelPortal; Q8CG76; -. DR SMR; Q8CG76; 43-367. DR IntAct; Q8CG76; 3. DR MINT; MINT-1869477; -. DR PhosphoSite; Q8CG76; -. DR REPRODUCTION-2DPAGE; Q8CG76; -. DR PaxDb; Q8CG76; -. DR PRIDE; Q8CG76; -. DR Ensembl; ENSMUST00000073787; ENSMUSP00000073459; ENSMUSG00000028743. DR GeneID; 110198; -. DR KEGG; mmu:110198; -. DR UCSC; uc008vmc.2; mouse. DR CTD; 110198; -. DR MGI; MGI:107796; Akr7a5. DR eggNOG; COG0667; -. DR GeneTree; ENSGT00550000074567; -. DR HOGENOM; HOG000250286; -. DR HOVERGEN; HBG050576; -. DR InParanoid; A2AMV3; -. DR KO; K15303; -. DR OMA; CTVKIAT; -. DR OrthoDB; EOG77127F; -. DR TreeFam; TF329173; -. DR SABIO-RK; Q8CG76; -. DR EvolutionaryTrace; Q8CG76; -. DR NextBio; 363519; -. DR PRO; PR:Q8CG76; -. DR Bgee; Q8CG76; -. DR Genevestigator; Q8CG76; -. DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR GO; GO:0004032; F:alditol:NADP+ 1-oxidoreductase activity; IEA:Ensembl. DR Gene3D; 3.20.20.100; -; 1. DR InterPro; IPR001395; Aldo/ket_red. DR InterPro; IPR023210; NADP_OxRdtase_dom. DR PANTHER; PTHR11732; PTHR11732; 1. DR Pfam; PF00248; Aldo_ket_red; 1. DR SUPFAM; SSF51430; SSF51430; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Complete proteome; Cytoplasm; KW Golgi apparatus; NADP; Oxidoreductase; Reference proteome. FT CHAIN 1 367 Aflatoxin B1 aldehyde reductase member 2. FT /FTId=PRO_0000070376. FT NP_BIND 179 180 NADP. FT NP_BIND 234 244 NADP. FT NP_BIND 326 334 NADP. FT ACT_SITE 85 85 Proton donor. FT BINDING 80 80 NADP. FT BINDING 149 149 Substrate. FT BINDING 205 205 NADP. FT BINDING 258 258 NADP. FT BINDING 268 268 Substrate. FT BINDING 271 271 Substrate. FT BINDING 367 367 Substrate. FT SITE 113 113 Lowers pKa of active site Tyr (By FT similarity). FT MOD_RES 136 136 N6-acetyllysine. FT MOD_RES 244 244 N6-succinyllysine. FT CONFLICT 5 5 A -> G (in Ref. 1; BAE25302). FT CONFLICT 9 9 V -> G (in Ref. 1; BAE25302). FT CONFLICT 12 12 A -> V (in Ref. 1; BAE25302). FT CONFLICT 17 17 A -> G (in Ref. 1; BAE25302). FT CONFLICT 127 127 I -> V (in Ref. 3; AAH31857 and 4; FT CAC81078). FT CONFLICT 162 162 R -> C (in Ref. 5; AAO38437). FT CONFLICT 354 354 A -> G (in Ref. 3; AAH31857). FT STRAND 47 51 FT TURN 56 58 FT HELIX 61 73 FT STRAND 78 80 FT HELIX 85 88 FT HELIX 89 95 FT STRAND 109 114 FT TURN 117 120 FT HELIX 124 137 FT STRAND 143 148 FT HELIX 157 169 FT STRAND 172 180 FT HELIX 183 196 FT STRAND 201 207 FT HELIX 214 216 FT HELIX 219 226 FT STRAND 229 233 FT HELIX 237 242 FT HELIX 247 250 FT TURN 251 253 FT STRAND 260 262 FT HELIX 265 272 FT HELIX 275 292 FT HELIX 293 295 FT HELIX 299 309 FT HELIX 315 317 FT STRAND 320 323 FT HELIX 328 337 FT HELIX 345 358 FT HELIX 359 361 SQ SEQUENCE 367 AA; 40612 MW; 1123BD7028D3FBDF CRC64; MLRAASRAVG RAAVRSAQRS GTSVGRPLAM SRPPPPRAAS GAPLRPATVL GTMEMGRRMD ASASAASVRA FLERGHSELD TAFMYCDGQS ENILGGLGLG LGSGDCTVKI ATKANPWEGK SLKPDSIRSQ LETSLKRLQC PRVDLFYLHA PDHSTPVEET LRACHQLHQE GKFVELGLSN YASWEVAEIC TLCKSNGWIL PTVYQGMYNA TTRQVEAELL PCLRHFGLRF YAYNPLAGGL LTGKYKYEDK DGKQPVGRFF GNNWAETYRN RFWKEHHFEA IALVEKALQT TYGTNAPRMT SAALRWMYHH SQLQGTRGDA VILGMSSLEQ LEQNLAATEE GPLEPAVVEA FDQAWNMVAH ECPNYFR // ID ASPD_MOUSE Reviewed; 287 AA. AC Q9DCQ2; Q8VCQ0; DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 19-MAR-2014, entry version 94. DE RecName: Full=Putative L-aspartate dehydrogenase; DE EC=1.4.1.21; DE AltName: Full=Aspartate dehydrogenase domain-containing protein; GN Name=Aspdh; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Kidney; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Liver; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP PROTEIN SEQUENCE OF 13-20, AND MASS SPECTROMETRY. RC STRAIN=OF1; TISSUE=Hippocampus; RA Lubec G., Sunyer B., Chen W.-Q.; RL Submitted (JAN-2009) to UniProtKB. CC -!- FUNCTION: Specifically catalyzes the NAD or NADP-dependent CC dehydrogenation of L-aspartate to iminoaspartate (By similarity). CC -!- CATALYTIC ACTIVITY: L-aspartate + H(2)O + NAD(P)(+) = oxaloacetate CC + NH(3) + NAD(P)H. CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; CC iminoaspartate from L-aspartate (dehydrogenase route): step 1/1. CC -!- MISCELLANEOUS: The iminoaspartate product is unstable in aqueous CC solution and can decompose to oxaloacetate and ammonia (By CC similarity). CC -!- SIMILARITY: Belongs to the L-aspartate dehydrogenase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK002587; BAB22209.1; -; mRNA. DR EMBL; BC019451; AAH19451.1; -; mRNA. DR RefSeq; NP_080966.1; NM_026690.1. DR UniGene; Mm.88478; -. DR ProteinModelPortal; Q9DCQ2; -. DR SMR; Q9DCQ2; 10-275. DR IntAct; Q9DCQ2; 3. DR MINT; MINT-1856535; -. DR PhosphoSite; Q9DCQ2; -. DR PaxDb; Q9DCQ2; -. DR PRIDE; Q9DCQ2; -. DR Ensembl; ENSMUST00000035929; ENSMUSP00000039202; ENSMUSG00000038704. DR GeneID; 68352; -. DR KEGG; mmu:68352; -. DR UCSC; uc009gpk.1; mouse. DR CTD; 554235; -. DR MGI; MGI:1915602; Aspdh. DR eggNOG; COG1712; -. DR GeneTree; ENSGT00390000004452; -. DR HOGENOM; HOG000007399; -. DR HOVERGEN; HBG062283; -. DR InParanoid; Q9DCQ2; -. DR OMA; LELVFVW; -. DR OrthoDB; EOG773XH5; -. DR TreeFam; TF315092; -. DR UniPathway; UPA00253; UER00456. DR NextBio; 327053; -. DR PRO; PR:Q9DCQ2; -. DR ArrayExpress; Q9DCQ2; -. DR Bgee; Q9DCQ2; -. DR CleanEx; MM_0610012D14RIK; -. DR Genevestigator; Q9DCQ2; -. DR GO; GO:0033735; F:aspartate dehydrogenase activity; IEA:UniProtKB-EC. DR GO; GO:0050661; F:NADP binding; IEA:InterPro. DR GO; GO:0009435; P:NAD biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0006742; P:NADP catabolic process; IEA:InterPro. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR005106; Asp/hSer_DH_NAD-bd. DR InterPro; IPR002811; Asp_DH. DR InterPro; IPR011182; Asp_DH_NAD_syn. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Pfam; PF01958; DUF108; 1. DR Pfam; PF03447; NAD_binding_3; 1. DR PIRSF; PIRSF005227; Asp_dh_NAD_syn; 1. PE 1: Evidence at protein level; KW Complete proteome; Direct protein sequencing; NAD; NADP; KW Oxidoreductase; Pyridine nucleotide biosynthesis; Reference proteome. FT CHAIN 1 287 Putative L-aspartate dehydrogenase. FT /FTId=PRO_0000144901. FT BINDING 131 131 NAD; via amide nitrogen (By similarity). FT BINDING 196 196 NAD (By similarity). FT CONFLICT 117 117 A -> V (in Ref. 2; AAH19451). FT CONFLICT 245 245 A -> S (in Ref. 2; AAH19451). SQ SEQUENCE 287 AA; 30270 MW; 889D164D943B88DD CRC64; MATSTLPQVP YKVGVVGYGR LGQSLVSRLL AQGSELGLEL VFVWNRDPGR MAGSVPPALQ LQDLTALEER HPDLVVEVAH PKIIHESGAQ ILRHANLLVG SPSALADQTT EQQLLEASKR WGHTVFVARG ALWGSEDISR LDAAGGLQSL RVTMATHPDG FRLEGPLAAA HSSGPRTVLY EGPVRGLCPL APRNSNTMAA AALAAPSLGF DRVIGVLVAD LSLTDMHVVD VELLGPPGPS GRSFAVHTHR ENPAQPGAVT GSATVTAFWH SLLGCCQLTS RPGIHLC // ID ASPH1_MOUSE Reviewed; 360 AA. AC Q2TA57; DT 18-MAY-2010, integrated into UniProtKB/Swiss-Prot. DT 18-MAY-2010, sequence version 2. DT 19-MAR-2014, entry version 57. DE RecName: Full=Aspartate beta-hydroxylase domain-containing protein 1; DE EC=1.14.11.-; GN Name=Asphd1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane CC protein (Potential). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q2TA57-1; Sequence=Displayed; CC Name=2; CC IsoId=Q2TA57-2; Sequence=VSP_039171; CC -!- SIMILARITY: Belongs to the aspartyl/asparaginyl beta-hydroxylase CC family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AC122863; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC111101; AAI11102.1; -; mRNA. DR RefSeq; NP_001034734.1; NM_001039645.1. DR RefSeq; XP_006507801.1; XM_006507738.1. DR UniGene; Mm.444143; -. DR ProteinModelPortal; Q2TA57; -. DR SMR; Q2TA57; 158-355. DR STRING; 10090.ENSMUSP00000101947; -. DR PaxDb; Q2TA57; -. DR PRIDE; Q2TA57; -. DR Ensembl; ENSMUST00000052937; ENSMUSP00000049848; ENSMUSG00000046378. [Q2TA57-2] DR Ensembl; ENSMUST00000106339; ENSMUSP00000101946; ENSMUSG00000046378. [Q2TA57-2] DR Ensembl; ENSMUST00000106340; ENSMUSP00000101947; ENSMUSG00000046378. [Q2TA57-1] DR GeneID; 233879; -. DR KEGG; mmu:233879; -. DR UCSC; uc009jtn.1; mouse. [Q2TA57-1] DR UCSC; uc009jto.1; mouse. [Q2TA57-2] DR CTD; 253982; -. DR MGI; MGI:2685014; Asphd1. DR eggNOG; NOG315282; -. DR GeneTree; ENSGT00530000063281; -. DR HOGENOM; HOG000233597; -. DR InParanoid; Q2TA57; -. DR OMA; WGLEDAP; -. DR OrthoDB; EOG7JMGDJ; -. DR NextBio; 381911; -. DR PRO; PR:Q2TA57; -. DR Bgee; Q2TA57; -. DR Genevestigator; Q2TA57; -. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW. DR GO; GO:0018193; P:peptidyl-amino acid modification; IEA:InterPro. DR Gene3D; 2.60.120.330; -; 1. DR InterPro; IPR007803; Asp_Arg_Pro-Hydrxlase. DR InterPro; IPR027443; IPNS-like. DR Pfam; PF05118; Asp_Arg_Hydrox; 1. PE 2: Evidence at transcript level; KW Alternative splicing; Complete proteome; Dioxygenase; Membrane; KW Oxidoreductase; Reference proteome; Signal-anchor; Transmembrane; KW Transmembrane helix. FT CHAIN 1 360 Aspartate beta-hydroxylase domain- FT containing protein 1. FT /FTId=PRO_0000394142. FT TOPO_DOM 1 45 Cytoplasmic (Potential). FT TRANSMEM 46 68 Helical; (Potential). FT TOPO_DOM 69 360 Lumenal (Potential). FT COMPBIAS 80 158 Gly-rich. FT VAR_SEQ 1 251 Missing (in isoform 2). FT /FTId=VSP_039171. SQ SEQUENCE 360 AA; 38266 MW; 2239BB3186C7D23B CRC64; MWKGGNQEAV IEGSGGELGV PGSWGLQDAA CHLARASLPI MFPWPLPLGS SALTMLLGAL TSLFLWYCYR LGSQDMQALG TGSRAGGVSG MPDVCSQTGP RGLGDSGEGP RAEGLVSRRL RAYARRYSWA GMGRVRRAAQ GGSGLTGGAG VMGIQRPGLL FLPDLPSSPF VPRDAQRHDV ELLQSSFPAI LRDFGAVSWD FSGTTPLPRG WSPPLAPGCY QLLLYQAGRC QPSNCRRCPG AYRALRGLRS FMSANTFGNA GFSVLLPGAR LEGRCGPTNA RVRCHLGLKI PPGCELVVGG EPQCWAEGHC LLVDDSFLHT VAHNGSPEDG PRVVFIVDLW HPNVAGAERQ ALDFVFAPDP // ID ASPH2_MOUSE Reviewed; 343 AA. AC Q80VP9; Q9CUZ2; DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2003, sequence version 1. DT 19-FEB-2014, entry version 71. DE RecName: Full=Aspartate beta-hydroxylase domain-containing protein 2; DE EC=1.14.11.-; GN Name=Asphd2; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Olfactory epithelium; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 168-343. RC STRAIN=C57BL/6J; TISSUE=Hippocampus; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane CC protein (Potential). CC -!- SIMILARITY: Belongs to the aspartyl/asparaginyl beta-hydroxylase CC family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BC046606; AAH46606.1; -; mRNA. DR EMBL; AK013495; BAB28881.1; -; mRNA. DR RefSeq; NP_082662.1; NM_028386.1. DR UniGene; Mm.151745; -. DR ProteinModelPortal; Q80VP9; -. DR SMR; Q80VP9; 162-338. DR STRING; 10090.ENSMUSP00000031291; -. DR PhosphoSite; Q80VP9; -. DR PaxDb; Q80VP9; -. DR PRIDE; Q80VP9; -. DR Ensembl; ENSMUST00000031291; ENSMUSP00000031291; ENSMUSG00000029348. DR GeneID; 72898; -. DR KEGG; mmu:72898; -. DR UCSC; uc008yth.2; mouse. DR CTD; 57168; -. DR MGI; MGI:1920148; Asphd2. DR eggNOG; COG3555; -. DR GeneTree; ENSGT00530000063281; -. DR HOGENOM; HOG000233597; -. DR HOVERGEN; HBG079419; -. DR InParanoid; Q80VP9; -. DR OMA; EWVTFYL; -. DR OrthoDB; EOG7JMGDJ; -. DR TreeFam; TF312799; -. DR NextBio; 337107; -. DR PRO; PR:Q80VP9; -. DR Bgee; Q80VP9; -. DR CleanEx; MM_ASPHD2; -. DR Genevestigator; Q80VP9; -. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW. DR GO; GO:0018193; P:peptidyl-amino acid modification; IEA:InterPro. DR Gene3D; 2.60.120.330; -; 1. DR InterPro; IPR007803; Asp_Arg_Pro-Hydrxlase. DR InterPro; IPR027443; IPNS-like. DR Pfam; PF05118; Asp_Arg_Hydrox; 1. PE 2: Evidence at transcript level; KW Complete proteome; Dioxygenase; Glycoprotein; Membrane; KW Oxidoreductase; Reference proteome; Signal-anchor; Transmembrane; KW Transmembrane helix. FT CHAIN 1 343 Aspartate beta-hydroxylase domain- FT containing protein 2. FT /FTId=PRO_0000254163. FT TOPO_DOM 1 31 Cytoplasmic (Potential). FT TRANSMEM 32 52 Helical; (Potential). FT TOPO_DOM 53 343 Lumenal (Potential). FT CARBOHYD 77 77 N-linked (GlcNAc...) (Potential). FT CARBOHYD 185 185 N-linked (GlcNAc...) (Potential). SQ SEQUENCE 343 AA; 38731 MW; 34284066FD6E76B2 CRC64; MWLEWLVAWS WSLDGLRDCI ATGIQSVRDC DGTAVITVAC LLILFVWYCY HVGREQPRPH VSVNSLLQGV DANGLQNGSM YCQSPECARC THHEGLNQKL YHNLQEYAKR YSWSGMGRIH KGIREQGRYL SSQPSIQKPE VFFLPDLPTT PYFSRDAQKH DVELLERNFQ AILCEFETLY KAFSNCSLPQ GWKVNSTPSG EWFTFDFVSQ GVCVPRNCRK CPRTYRLLGS LRTCIGNNVF GNACISVLSP GTVITEHYGP TNIRIRCHLG LKTPNGCELV VGGEPQCWAE GRCLLFDDSF LHTAFHEGSA EDGPRVVFMV DLWHPNVAAA ERQALDFIFA PGR // ID ASPH_MOUSE Reviewed; 741 AA. AC Q8BSY0; Q9EPA6; DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 19-MAR-2014, entry version 100. DE RecName: Full=Aspartyl/asparaginyl beta-hydroxylase; DE EC=1.14.11.16; DE AltName: Full=Aspartate beta-hydroxylase; DE Short=ASP beta-hydroxylase; DE AltName: Full=Peptide-aspartate beta-dioxygenase; GN Name=Asph; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=BALB/c; TISSUE=Liver; RX PubMed=10956665; DOI=10.1074/jbc.M006753200; RA Dinchuk J.E., Henderson N.L., Burn T.C., Huber R., Ho S.P., Link J., RA O'Neil K.T., Focht R.J., Scully M.S., Hollis J.M., Hollis G.F., RA Friedman P.A.; RT "Aspartyl beta -hydroxylase (Asph) and an evolutionarily conserved RT isoform of Asph missing the catalytic domain share exons with RT junctin."; RL J. Biol. Chem. 275:39543-39554(2000). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). CC -!- FUNCTION: Specifically hydroxylates an Asp or Asn residue in CC certain epidermal growth factor-like (EGF) domains of a number of CC proteins. CC -!- CATALYTIC ACTIVITY: Peptide L-aspartate + 2-oxoglutarate + O(2) = CC peptide 3-hydroxy-L-aspartate + succinate + CO(2). CC -!- COFACTOR: Iron (By similarity). CC -!- SUBUNIT: Monomer (By similarity). CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass CC type II membrane protein (By similarity). CC -!- PTM: Might be processed to the 56 kDa (AA 274-757) or 52 kDa (AA CC 315-757) forms in the lumen of the endoplasmic reticulum (By CC similarity). CC -!- SIMILARITY: Belongs to the aspartyl/asparaginyl beta-hydroxylase CC family. CC -!- SIMILARITY: Contains 5 TPR repeats. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF289486; AAG40808.1; -; mRNA. DR EMBL; AF289487; AAG40809.1; -; mRNA. DR EMBL; AK030293; BAC26882.1; -; mRNA. DR RefSeq; NP_001171321.1; NM_001177850.1. DR RefSeq; NP_001171323.1; NM_001177852.1. DR RefSeq; NP_001171324.1; NM_001177853.1. DR RefSeq; NP_001171325.1; NM_001177854.1. DR RefSeq; NP_001171326.1; NM_001177855.1. DR RefSeq; NP_075553.2; NM_023066.3. DR UniGene; Mm.222206; -. DR UniGene; Mm.412008; -. DR ProteinModelPortal; Q8BSY0; -. DR SMR; Q8BSY0; 328-376, 405-522, 545-741. DR BioGrid; 211167; 2. DR IntAct; Q8BSY0; 4. DR MINT; MINT-4112262; -. DR PhosphoSite; Q8BSY0; -. DR PaxDb; Q8BSY0; -. DR PRIDE; Q8BSY0; -. DR DNASU; 65973; -. DR Ensembl; ENSMUST00000078139; ENSMUSP00000077273; ENSMUSG00000028207. DR GeneID; 65973; -. DR KEGG; mmu:65973; -. DR UCSC; uc008ryf.2; mouse. DR CTD; 444; -. DR MGI; MGI:1914186; Asph. DR eggNOG; COG3555; -. DR GeneTree; ENSGT00530000063281; -. DR HOGENOM; HOG000231625; -. DR HOVERGEN; HBG004290; -. DR InParanoid; Q8BSY0; -. DR KO; K00476; -. DR OMA; RNENACK; -. DR OrthoDB; EOG715Q44; -. DR TreeFam; TF312799; -. DR NextBio; 320434; -. DR PRO; PR:Q8BSY0; -. DR ArrayExpress; Q8BSY0; -. DR Bgee; Q8BSY0; -. DR CleanEx; MM_ASPH; -. DR Genevestigator; Q8BSY0; -. DR GO; GO:0032541; C:cortical endoplasmic reticulum; IEA:Ensembl. DR GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL. DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IEA:Ensembl. DR GO; GO:0016021; C:integral component of membrane; ISS:MGI. DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl. DR GO; GO:0004597; F:peptide-aspartate beta-dioxygenase activity; ISS:MGI. DR GO; GO:0097202; P:activation of cysteine-type endopeptidase activity; IEA:Ensembl. DR GO; GO:0032237; P:activation of store-operated calcium channel activity; IEA:Ensembl. DR GO; GO:0070588; P:calcium ion transmembrane transport; IEA:Ensembl. DR GO; GO:0071277; P:cellular response to calcium ion; IEA:Ensembl. DR GO; GO:0060325; P:face morphogenesis; IMP:MGI. DR GO; GO:0035108; P:limb morphogenesis; IMP:MGI. DR GO; GO:0008285; P:negative regulation of cell proliferation; IGI:MGI. DR GO; GO:0060021; P:palate development; IMP:MGI. DR GO; GO:0007389; P:pattern specification process; IMP:MGI. DR GO; GO:0042264; P:peptidyl-aspartic acid hydroxylation; IDA:MGI. DR GO; GO:0010524; P:positive regulation of calcium ion transport into cytosol; IEA:Ensembl. DR GO; GO:0090316; P:positive regulation of intracellular protein transport; IEA:Ensembl. DR GO; GO:0045862; P:positive regulation of proteolysis; IEA:Ensembl. DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IEA:Ensembl. DR GO; GO:0031585; P:regulation of inositol 1,4,5-trisphosphate-sensitive calcium-release channel activity; IEA:Ensembl. DR GO; GO:1901879; P:regulation of protein depolymerization; IDA:BHF-UCL. DR GO; GO:0031647; P:regulation of protein stability; IDA:BHF-UCL. DR GO; GO:0033198; P:response to ATP; IEA:Ensembl. DR Gene3D; 1.25.40.10; -; 1. DR Gene3D; 2.60.120.330; -; 1. DR InterPro; IPR007943; Asp-B-hydro/Triadin_dom. DR InterPro; IPR007803; Asp_Arg_Pro-Hydrxlase. DR InterPro; IPR027443; IPNS-like. DR InterPro; IPR013026; TPR-contain_dom. DR InterPro; IPR011990; TPR-like_helical. DR InterPro; IPR013105; TPR_2. DR InterPro; IPR019734; TPR_repeat. DR Pfam; PF05279; Asp-B-Hydro_N; 1. DR Pfam; PF05118; Asp_Arg_Hydrox; 1. DR Pfam; PF07719; TPR_2; 1. DR PROSITE; PS50005; TPR; 2. DR PROSITE; PS50293; TPR_REGION; 1. PE 2: Evidence at transcript level; KW Complete proteome; Dioxygenase; Endoplasmic reticulum; Glycoprotein; KW Iron; Membrane; Oxidoreductase; Reference proteome; Repeat; KW Signal-anchor; TPR repeat; Transmembrane; Transmembrane helix. FT CHAIN 1 741 Aspartyl/asparaginyl beta-hydroxylase. FT /FTId=PRO_0000254161. FT TOPO_DOM 1 62 Cytoplasmic (Potential). FT TRANSMEM 63 83 Helical; Signal-anchor for type II FT membrane protein; (Potential). FT TOPO_DOM 84 741 Lumenal (Potential). FT REPEAT 324 357 TPR 1. FT REPEAT 365 398 TPR 2. FT REPEAT 437 470 TPR 3. FT REPEAT 472 504 TPR 4. FT REPEAT 508 540 TPR 5. FT COMPBIAS 9 61 Gly-rich. FT COMPBIAS 14 38 Ser-rich. FT COMPBIAS 310 315 Poly-Lys. FT CARBOHYD 453 453 N-linked (GlcNAc...) (Potential). FT CARBOHYD 689 689 N-linked (GlcNAc...) (Potential). FT CONFLICT 131 132 Missing (in Ref. 1; AAG40808/AAG40809). FT CONFLICT 279 279 A -> E (in Ref. 1; AAG40808/AAG40809). SQ SEQUENCE 741 AA; 83042 MW; 0660A6A5E34418C8 CRC64; MAPRKNAKGG GGNSSSSGSG SGSGSGSPST GSSGSSSSPG ARREAKHGGH KNGRRGGISG GSFFTWFMVI ALLGVWTSVA VVWFDLVDYE EVLGKLGVYD ADGDGDFDVD DAKVLLGLKE RSPSERTFPP EEEAETHAEL EEQAPEGADI QNVEDEVKEQ IQSLLQESVH TDHDLEADGL AGEPQPEVED FLTVTDSDDR FEDLEPGTVH EEIEDTYHVE DTASQNHPND MEEMTNEQEN SDPSEAVTDA GVLLPHAEEV RHQDYDEPVY EPSEHEGVAI SDNTIDDSSI ISEEINVASV EEQQDTPPVK KKKPKLLNKF DKTIKAELDA AEKLRKRGKI EEAVNAFEEL VRKYPQSPRA RYGKAQCEDD LAEKQRSNEV LRRAIETYQE AADLPDAPTD LVKLSLKRRS ERQQFLGHMR GSLLTLQRLV QLFPSDTTLK NDLGVGYLLL GDNDSAKKVY EEVLNVTPND GFAKVHYGFI LKAQNKISES IPYLKEGIES GDPGTDDGRF YFHLGDAMQR VGNKEAYKWY ELGHKRGHFA SVWQRSLYNV NGLKAQPWWT PRETGYTELV KSLERNWKLI RDEGLMVMDK AKGLFLPEDE NLREKGDWSQ FTLWQQGRKN ENACKGAPKT CALLEKFSET TGCRRGQIKY SIMHPGTHVW PHTGPTNCRL RMHLGLVIPK EGCKIRCANE TRTWEEGKVL IFDDSFEHEV WQDASSFRLI FIVDVWHPEL TPQQRRSLPA I // ID BCDO1_MOUSE Reviewed; 566 AA. AC Q9JJS6; Q6K1L5; Q8C6N5; Q9ERN9; DT 10-OCT-2003, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2001, sequence version 2. DT 19-MAR-2014, entry version 97. DE RecName: Full=Beta,beta-carotene 15,15'-monooxygenase; DE EC=1.14.99.36; DE AltName: Full=Beta-carotene dioxygenase 1; GN Name=Bcmo1; Synonyms=Bcdo, Bcdo1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=C57BL/6; TISSUE=Kidney; RX PubMed=11237856; DOI=10.1042/0264-6021:3540521; RA Wyss A., Wirtz G.M., Woggon W.D., Brugger R., Wyss M., Friedlein A., RA Riss G., Bachmann H., Hunziker W.; RT "Expression pattern and localization of beta,beta-carotene 15,15'- RT dioxygenase in different tissues."; RL Biochem. J. 354:521-529(2001). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=C57BL/6; TISSUE=Kidney; RX PubMed=11401432; DOI=10.1006/geno.2000.6476; RA Yan W., Jang G.-F., Haeseleer F., Esumi N., Chang J., Kerrigan M., RA Campochiaro M., Campochiaro P., Palczewski K., Zack D.J.; RT "Cloning and characterization of a human beta,beta-carotene-15,15- RT prime dioxygenase that is highly expressed in the retinal pigment RT epithelium."; RL Genomics 72:193-202(2001). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL RP PROPERTIES, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE. RC STRAIN=C57BL/6; RX PubMed=11092891; DOI=10.1074/jbc.M009030200; RA Redmond T.M., Gentleman S., Duncan T., Yu S., Wiggert B., Gantt E., RA Cunningham F.X. Jr.; RT "Identification, expression, and substrate specificity of a mammalian RT beta-carotene 15,15'-dioxygenase."; RL J. Biol. Chem. 276:6560-6565(2001). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=129/Sv; RX PubMed=12759335; DOI=10.1096/fj.02-0690fje; RA Boulanger A., McLemore P., Copeland N.G., Gilbert D.J., Jenkins N.A., RA Yu S.S., Gentleman S., Redmond T.M.; RT "Identification of beta-carotene 15,15'-monooxygenase as a peroxisome RT proliferator-activated receptor target gene."; RL FASEB J. 17:1304-1306(2003). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 29-483. RC STRAIN=C57BL/6J; TISSUE=Oviduct; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). CC -!- FUNCTION: Symmetrically cleaves beta-carotene into two molecules CC of retinal. The reaction proceeds in three stages, epoxidation of CC the 15,15'-double bond, hydration of the double bond leading to CC ring opening, and oxidative cleavage of the diol formed. CC -!- CATALYTIC ACTIVITY: Beta-carotene + O(2) = 2 all-trans-retinal. CC -!- COFACTOR: Binds 1 Fe(2+) ion per subunit (By similarity). CC -!- PATHWAY: Cofactor metabolism; retinol metabolism. CC -!- TISSUE SPECIFICITY: Expressed in liver, kidney, small intestine CC and testis. CC -!- DEVELOPMENTAL STAGE: Abundantly expressed at embryonic day 7 with CC lower levels at embryonic days 11, 13 and 15. CC -!- SIMILARITY: Belongs to the carotenoid oxygenase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJ278064; CAB92531.2; -; mRNA. DR EMBL; AF271298; AAG33982.1; -; mRNA. DR EMBL; AF294899; AAG15381.1; -; mRNA. DR EMBL; AY114302; AAM76677.1; -; Genomic_DNA. DR EMBL; AY114294; AAM76677.1; JOINED; Genomic_DNA. DR EMBL; AY114295; AAM76677.1; JOINED; Genomic_DNA. DR EMBL; AY114296; AAM76677.1; JOINED; Genomic_DNA. DR EMBL; AY114297; AAM76677.1; JOINED; Genomic_DNA. DR EMBL; AY114298; AAM76677.1; JOINED; Genomic_DNA. DR EMBL; AY114299; AAM76677.1; JOINED; Genomic_DNA. DR EMBL; AY114300; AAM76677.1; JOINED; Genomic_DNA. DR EMBL; AY114301; AAM76677.1; JOINED; Genomic_DNA. DR EMBL; AK054171; BAC35679.1; -; mRNA. DR RefSeq; NP_067461.2; NM_021486.3. DR UniGene; Mm.174133; -. DR ProteinModelPortal; Q9JJS6; -. DR SMR; Q9JJS6; 10-517. DR STRING; 10090.ENSMUSP00000034308; -. DR PhosphoSite; Q9JJS6; -. DR PRIDE; Q9JJS6; -. DR Ensembl; ENSMUST00000034308; ENSMUSP00000034308; ENSMUSG00000031845. DR GeneID; 63857; -. DR KEGG; mmu:63857; -. DR UCSC; uc009now.2; mouse. DR CTD; 53630; -. DR MGI; MGI:1926923; Bcmo1. DR eggNOG; COG3670; -. DR GeneTree; ENSGT00500000044783; -. DR HOGENOM; HOG000232156; -. DR HOVERGEN; HBG050679; -. DR InParanoid; Q9JJS6; -. DR KO; K00515; -. DR OMA; SWASCMA; -. DR OrthoDB; EOG7353WB; -. DR TreeFam; TF314019; -. DR BRENDA; 1.14.99.36; 3474. DR SABIO-RK; Q9JJS6; -. DR UniPathway; UPA00912; -. DR NextBio; 319783; -. DR PRO; PR:Q9JJS6; -. DR ArrayExpress; Q9JJS6; -. DR Bgee; Q9JJS6; -. DR CleanEx; MM_BCMO1; -. DR Genevestigator; Q9JJS6; -. DR GO; GO:0003834; F:beta-carotene 15,15'-monooxygenase activity; IDA:UniProtKB. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW. DR GO; GO:0001523; P:retinoid metabolic process; IDA:UniProtKB. DR GO; GO:0042572; P:retinol metabolic process; IEA:UniProtKB-UniPathway. DR InterPro; IPR004294; Carotenoid_Oase. DR PANTHER; PTHR10543; PTHR10543; 1. DR Pfam; PF03055; RPE65; 1. PE 1: Evidence at protein level; KW Complete proteome; Iron; Metal-binding; Monooxygenase; Oxidoreductase; KW Reference proteome. FT CHAIN 1 566 Beta,beta-carotene 15,15'-monooxygenase. FT /FTId=PRO_0000143934. FT METAL 172 172 Iron; catalytic (By similarity). FT METAL 237 237 Iron; catalytic (By similarity). FT METAL 308 308 Iron; catalytic (By similarity). FT METAL 514 514 Iron; catalytic (By similarity). FT CONFLICT 409 409 I -> T (in Ref. 2; AAG15381). SQ SEQUENCE 566 AA; 63864 MW; 1B4367815247A8D2 CRC64; MEIIFGQNKK EQLEPVQAKV TGSIPAWLQG TLLRNGPGMH TVGESKYNHW FDGLALLHSF SIRDGEVFYR SKYLQSDTYI ANIEANRIVV SEFGTMAYPD PCKNIFSKAF SYLSHTIPDF TDNCLINIMK CGEDFYATTE TNYIRKIDPQ TLETLEKVDY RKYVAVNLAT SHPHYDEAGN VLNMGTSVVD KGRTKYVIFK IPATVPDSKK KGKSPVKHAE VFCSISSRSL LSPSYYHSFG VTENYVVFLE QPFKLDILKM ATAYMRGVSW ASCMSFDRED KTYIHIIDQR TRKPVPTKFY TDPMVVFHHV NAYEEDGCVL FDVIAYEDSS LYQLFYLANL NKDFEEKSRL TSVPTLRRFA VPLHVDKDAE VGSNLVKVSS TTATALKEKD GHVYCQPEVL YEGLELPRIN YAYNGKPYRY IFAAEVQWSP VPTKILKYDI LTKSSLKWSE ESCWPAEPLF VPTPGAKDED DGVILSAIVS TDPQKLPFLL ILDAKSFTEL ARASVDADMH LDLHGLFIPD ADWNAVKQTP AETQEVENSD HPTDPTAPEL SHSENDFTAG HGGSSL // ID BCDO2_MOUSE Reviewed; 532 AA. AC Q99NF1; DT 10-OCT-2003, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 19-MAR-2014, entry version 85. DE RecName: Full=Beta,beta-carotene 9',10'-oxygenase; DE EC=1.13.11.71; DE AltName: Full=B-diox-II; DE AltName: Full=Beta-carotene dioxygenase 2; GN Name=Bco2; Synonyms=Bcdo2; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND CATALYTIC ACTIVITY. RC TISSUE=Liver; RX PubMed=11278918; DOI=10.1074/jbc.M011510200; RA Kiefer C., Hessel S., Lampert J.M., Vogt K., Lederer M.O., RA Breithaupt D.E., von Lintig J.; RT "Identification and characterization of a mammalian enzyme catalyzing RT the asymmetric oxidative cleavage of provitamin A."; RL J. Biol. Chem. 276:14110-14116(2001). RN [2] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=21106934; DOI=10.1096/fj.10-173906; RA Amengual J., Lobo G.P., Golczak M., Li H.N., Klimova T., Hoppel C.L., RA Wyss A., Palczewski K., von Lintig J.; RT "A mitochondrial enzyme degrades carotenoids and protects against RT oxidative stress."; RL FASEB J. 25:948-959(2011). CC -!- FUNCTION: Asymmetrically cleaves beta-carotene at the 9',10' CC double bond resulting in the formation of beta-apo-10'-carotenal CC and beta-ionone. Besides beta-carotene, lycopene is also CC oxidatively cleaved. The apocarotenals formed by this enzyme may CC be the precursors for the biosynthesis of retinoic acid or exert CC unknown physiological effects. CC -!- CATALYTIC ACTIVITY: All-trans-beta-carotene + O(2) = all-trans- CC 10'-apo-beta-carotenal + beta-ionone. CC -!- COFACTOR: Binds 1 Fe(2+) ion per subunit (By similarity). CC -!- SUBCELLULAR LOCATION: Mitochondrion. CC -!- SIMILARITY: Belongs to the carotenoid oxygenase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJ290392; CAC28026.1; -; mRNA. DR RefSeq; NP_573480.1; NM_133217.3. DR RefSeq; XP_006510107.1; XM_006510044.1. DR RefSeq; XP_006510108.1; XM_006510045.1. DR RefSeq; XP_006510109.1; XM_006510046.1. DR UniGene; Mm.390149; -. DR ProteinModelPortal; Q99NF1; -. DR SMR; Q99NF1; 14-529. DR PhosphoSite; Q99NF1; -. DR PaxDb; Q99NF1; -. DR PRIDE; Q99NF1; -. DR Ensembl; ENSMUST00000119103; ENSMUSP00000112727; ENSMUSG00000032066. DR GeneID; 170752; -. DR KEGG; mmu:170752; -. DR UCSC; uc009pjq.1; mouse. DR CTD; 83875; -. DR MGI; MGI:2177469; Bco2. DR eggNOG; COG3670; -. DR GeneTree; ENSGT00500000044783; -. DR HOGENOM; HOG000232156; -. DR HOVERGEN; HBG050679; -. DR InParanoid; Q99NF1; -. DR KO; K10252; -. DR OMA; ISDGISW; -. DR OrthoDB; EOG7353WB; -. DR TreeFam; TF314019; -. DR NextBio; 370330; -. DR PRO; PR:Q99NF1; -. DR ArrayExpress; Q99NF1; -. DR Bgee; Q99NF1; -. DR Genevestigator; Q99NF1; -. DR GO; GO:0005739; C:mitochondrion; IDA:BHF-UCL. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0016702; F:oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen; IDA:UniProtKB. DR GO; GO:0016121; P:carotene catabolic process; IDA:BHF-UCL. DR GO; GO:0016116; P:carotenoid metabolic process; IMP:BHF-UCL. DR GO; GO:0051881; P:regulation of mitochondrial membrane potential; IMP:BHF-UCL. DR GO; GO:2000377; P:regulation of reactive oxygen species metabolic process; IMP:BHF-UCL. DR GO; GO:0042574; P:retinal metabolic process; NAS:UniProtKB. DR GO; GO:0042573; P:retinoic acid metabolic process; NAS:UniProtKB. DR InterPro; IPR004294; Carotenoid_Oase. DR PANTHER; PTHR10543; PTHR10543; 1. DR Pfam; PF03055; RPE65; 1. PE 1: Evidence at protein level; KW Complete proteome; Dioxygenase; Iron; Metal-binding; Mitochondrion; KW Oxidoreductase; Reference proteome. FT CHAIN 1 532 Beta,beta-carotene 9',10'-oxygenase. FT /FTId=PRO_0000143939. FT METAL 179 179 Iron; catalytic (By similarity). FT METAL 239 239 Iron; catalytic (By similarity). FT METAL 310 310 Iron; catalytic (By similarity). FT METAL 526 526 Iron; catalytic (By similarity). SQ SEQUENCE 532 AA; 60142 MW; 7461AD5A53FE86A3 CRC64; MLGPKQSLPC IAPLLTTAEE TLSAVSARVR GHIPEWLNGY LLRVGPGKFE FGKDRYNHWF DGMALLHQFR MERGTVTYKS KFLQSDTYKA NSAGGRIVIS EFGTLALPDP CKSIFERFMS RFEPPTMTDN TNVNFVQYKG DYYMSTETNF MNKVDIEMLE RTEKVDWSKF IAVNGATAHP HYDPDGTAYN MGNSYGPRGS CYNIIRVPPK KKEPGETIHG AQVLCSIAST EKMKPSYYHS FGMTKNYIIF VEQPVKMKLW KIITSKIRGK PFADGISWEP QYNTRFHVVD KHTGQLLPGM YYSMPFLTYH QINAFEDQGC IVIDLCCQDD GRSLDLYQLQ NLRKAGEGLD QVYELKAKSF PRRFVLPLDV SVDAAEGKNL SPLSYSSASA VKQGDGEIWC SPENLHHEDL EEEGGIEFPQ INYGRFNGKK YSFFYGCGFR HLVGDSLIKV DVTNKTLRVW REEGFYPSEP VFVPVPGADE EDSGVILSVV ITPNQSESNF LLVLDAKSFT ELGRAEVPVQ MPYGFHGTFV PI // ID BDH2_MOUSE Reviewed; 245 AA. AC Q8JZV9; DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2002, sequence version 1. DT 19-FEB-2014, entry version 91. DE RecName: Full=3-hydroxybutyrate dehydrogenase type 2; DE EC=1.1.1.-; DE EC=1.1.1.30; DE AltName: Full=Dehydrogenase/reductase SDR family member 6; DE AltName: Full=R-beta-hydroxybutyrate dehydrogenase; GN Name=Bdh2; Synonyms=Dhrs6; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Kidney; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [2] RP FUNCTION, PATHWAY, TISSUE SPECIFICITY, AND MUTAGENESIS OF TYR-147. RX PubMed=20550936; DOI=10.1016/j.cell.2010.04.040; RA Devireddy L.R., Hart D.O., Goetz D.H., Green M.R.; RT "A mammalian siderophore synthesized by an enzyme with a bacterial RT homolog involved in enterobactin production."; RL Cell 141:1006-1017(2010). CC -!- FUNCTION: Dehydrogenase that mediates the formation of 2,5- CC dihydroxybenzoic acid (2,5-DHBA), a siderophore that shares CC structural similarities with bacterial enterobactin and associates CC with LCN2, thereby playing a key role in iron homeostasis and CC transport. Also acts as a 3-hydroxybutyrate dehydrogenase. CC -!- CATALYTIC ACTIVITY: (R)-3-hydroxybutanoate + NAD(+) = acetoacetate CC + NADH. CC -!- PATHWAY: Siderophore biosynthesis. CC -!- SUBUNIT: Homotetramer (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- TISSUE SPECIFICITY: Widely expressed. CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases CC (SDR) family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BC036998; AAH36998.1; -; mRNA. DR RefSeq; NP_081484.1; NM_027208.2. DR UniGene; Mm.45121; -. DR ProteinModelPortal; Q8JZV9; -. DR SMR; Q8JZV9; 1-245. DR STRING; 10090.ENSMUSP00000112683; -. DR PhosphoSite; Q8JZV9; -. DR PaxDb; Q8JZV9; -. DR PRIDE; Q8JZV9; -. DR Ensembl; ENSMUST00000029817; ENSMUSP00000029817; ENSMUSG00000028167. DR Ensembl; ENSMUST00000120397; ENSMUSP00000112683; ENSMUSG00000028167. DR GeneID; 69772; -. DR KEGG; mmu:69772; -. DR UCSC; uc008rla.2; mouse. DR CTD; 56898; -. DR MGI; MGI:1917022; Bdh2. DR eggNOG; COG1028; -. DR GeneTree; ENSGT00710000106273; -. DR HOVERGEN; HBG002145; -. DR InParanoid; Q8JZV9; -. DR KO; K00019; -. DR OrthoDB; EOG7W154W; -. DR TreeFam; TF328795; -. DR NextBio; 330302; -. DR PRO; PR:Q8JZV9; -. DR ArrayExpress; Q8JZV9; -. DR Bgee; Q8JZV9; -. DR CleanEx; MM_BDH2; -. DR Genevestigator; Q8JZV9; -. DR GO; GO:0005737; C:cytoplasm; ISS:HGNC. DR GO; GO:0003858; F:3-hydroxybutyrate dehydrogenase activity; ISS:HGNC. DR GO; GO:0051287; F:NAD binding; ISS:HGNC. DR GO; GO:0016628; F:oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor; IMP:UniProtKB. DR GO; GO:0006635; P:fatty acid beta-oxidation; ISS:HGNC. DR GO; GO:0042168; P:heme metabolic process; ISS:UniProtKB. DR GO; GO:0055072; P:iron ion homeostasis; IMP:UniProtKB. DR GO; GO:0019290; P:siderophore biosynthetic process; IMP:UniProtKB. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR002198; DH_sc/Rdtase_SDR. DR InterPro; IPR002347; Glc/ribitol_DH. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR020904; Sc_DH/Rdtase_CS. DR PRINTS; PR00081; GDHRDH. DR PRINTS; PR00080; SDRFAMILY. DR PROSITE; PS00061; ADH_SHORT; 1. PE 1: Evidence at protein level; KW Complete proteome; Cytoplasm; NAD; Oxidoreductase; Reference proteome. FT CHAIN 1 245 3-hydroxybutyrate dehydrogenase type 2. FT /FTId=PRO_0000042581. FT NP_BIND 10 37 NAD (By similarity). FT NP_BIND 180 184 NAD (By similarity). FT ACT_SITE 147 147 Proton acceptor. FT BINDING 58 58 NAD (By similarity). FT BINDING 144 144 Substrate (By similarity). FT BINDING 151 151 NAD (By similarity). FT BINDING 188 188 Substrate (By similarity). FT BINDING 205 205 Substrate (By similarity). FT MUTAGEN 147 147 Y->F: Loss of function. SQ SEQUENCE 245 AA; 26753 MW; 343A25B1F56B9CCF CRC64; MGRLDGKVIV LTAAAQGIGR ASALAFAREG AKVIATDINE SKLQELESYR GIQTRVLDVT KKRQIDQFAS EIERIDVLFN VAGFVHHGTI LDCEEKDWDF SMNLNVRSMF LMIKAFLPKM LAQKSGNIIN MSSVASSIKG VENRCVYSAT KAAVIGLTKS VAADFIQQGI RCNCVCPGTV DTPSLQERIQ ARDNPKEALK TFLNRQKTGR FASAEEVALL CVYLASDESA YVTGNPVIID GGWSL // ID BDH_MOUSE Reviewed; 343 AA. AC Q80XN0; Q3UJS9; Q3UL45; Q8BK53; Q8R0C8; DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 2. DT 19-MAR-2014, entry version 103. DE RecName: Full=D-beta-hydroxybutyrate dehydrogenase, mitochondrial; DE Short=BDH; DE EC=1.1.1.30; DE AltName: Full=3-hydroxybutyrate dehydrogenase; DE Flags: Precursor; GN Name=Bdh1; Synonyms=Bdh; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J, and DBA/2; TISSUE=Testis, and Thymus; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Kidney, and Liver; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP PROTEIN SEQUENCE OF 224-252, AND MASS SPECTROMETRY. RC STRAIN=C57BL/6; TISSUE=Brain; RA Lubec G., Kang S.U.; RL Submitted (APR-2007) to UniProtKB. RN [4] RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-103 AND LYS-259, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., RA Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). RN [5] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-73; LYS-97; LYS-103; RP LYS-132; LYS-177; LYS-212; LYS-258; LYS-259 AND LYS-280, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23576753; DOI=10.1073/pnas.1302961110; RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., RA Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.; RT "Label-free quantitative proteomics of the lysine acetylome in RT mitochondria identifies substrates of SIRT3 in metabolic pathways."; RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013). CC -!- CATALYTIC ACTIVITY: (R)-3-hydroxybutanoate + NAD(+) = acetoacetate CC + NADH. CC -!- ENZYME REGULATION: Requires phosphatidylcholine as an allosteric CC activator for enzymatic activity (By similarity). CC -!- SUBUNIT: Homotetramer (By similarity). CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix (By similarity). CC -!- PTM: Acetylation of Lys-132 is observed in liver mitochondria from CC fasted mice but not from fed mice. CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases CC (SDR) family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK076718; BAC36453.1; -; mRNA. DR EMBL; AK137955; BAE23523.1; -; mRNA. DR EMBL; AK145711; BAE26605.1; -; mRNA. DR EMBL; AK146321; BAE27076.1; -; mRNA. DR EMBL; BC027063; AAH27063.1; -; mRNA. DR EMBL; BC043683; AAH43683.1; -; mRNA. DR EMBL; BC096457; AAH96457.1; -; mRNA. DR RefSeq; NP_001116155.1; NM_001122683.1. DR RefSeq; NP_780386.3; NM_175177.4. DR UniGene; Mm.293470; -. DR ProteinModelPortal; Q80XN0; -. DR SMR; Q80XN0; 54-334. DR IntAct; Q80XN0; 6. DR MINT; MINT-1861188; -. DR PhosphoSite; Q80XN0; -. DR PaxDb; Q80XN0; -. DR PRIDE; Q80XN0; -. DR Ensembl; ENSMUST00000089759; ENSMUSP00000087192; ENSMUSG00000046598. DR Ensembl; ENSMUST00000115226; ENSMUSP00000110881; ENSMUSG00000046598. DR Ensembl; ENSMUST00000115227; ENSMUSP00000110882; ENSMUSG00000046598. DR GeneID; 71911; -. DR KEGG; mmu:71911; -. DR UCSC; uc007yxi.2; mouse. DR CTD; 622; -. DR MGI; MGI:1919161; Bdh1. DR eggNOG; COG1028; -. DR GeneTree; ENSGT00650000093222; -. DR HOVERGEN; HBG005482; -. DR InParanoid; Q3UL45; -. DR KO; K00019; -. DR OrthoDB; EOG7FXZZX; -. DR TreeFam; TF325617; -. DR ChiTaRS; BDH1; mouse. DR NextBio; 334926; -. DR PRO; PR:Q80XN0; -. DR ArrayExpress; Q80XN0; -. DR Bgee; Q80XN0; -. DR CleanEx; MM_BDH1; -. DR Genevestigator; Q80XN0; -. DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:MGI. DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell. DR GO; GO:0005634; C:nucleus; IEA:Ensembl. DR GO; GO:0003858; F:3-hydroxybutyrate dehydrogenase activity; IEA:UniProtKB-EC. DR GO; GO:0005543; F:phospholipid binding; IEA:Ensembl. DR GO; GO:0060612; P:adipose tissue development; IEA:Ensembl. DR GO; GO:0007420; P:brain development; IEA:Ensembl. DR GO; GO:0001889; P:liver development; IEA:Ensembl. DR GO; GO:0046686; P:response to cadmium ion; IEA:Ensembl. DR GO; GO:0051412; P:response to corticosterone; IEA:Ensembl. DR GO; GO:0042493; P:response to drug; IEA:Ensembl. DR GO; GO:0032355; P:response to estradiol; IEA:Ensembl. DR GO; GO:0045471; P:response to ethanol; IEA:Ensembl. DR GO; GO:0060416; P:response to growth hormone; IEA:Ensembl. DR GO; GO:0032868; P:response to insulin; IEA:Ensembl. DR GO; GO:0007584; P:response to nutrient; IEA:Ensembl. DR GO; GO:0042594; P:response to starvation; IEA:Ensembl. DR GO; GO:0009636; P:response to toxic substance; IEA:Ensembl. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR002198; DH_sc/Rdtase_SDR. DR InterPro; IPR002347; Glc/ribitol_DH. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR020904; Sc_DH/Rdtase_CS. DR Pfam; PF00106; adh_short; 1. DR PRINTS; PR00081; GDHRDH. DR PRINTS; PR00080; SDRFAMILY. DR PROSITE; PS00061; ADH_SHORT; 1. PE 1: Evidence at protein level; KW Acetylation; Allosteric enzyme; Complete proteome; KW Direct protein sequencing; Mitochondrion; NAD; Oxidoreductase; KW Reference proteome; Transit peptide. FT TRANSIT 1 46 Mitochondrion (By similarity). FT CHAIN 47 343 D-beta-hydroxybutyrate dehydrogenase, FT mitochondrial. FT /FTId=PRO_0000031961. FT NP_BIND 60 84 NAD (By similarity). FT ACT_SITE 209 209 Proton acceptor (By similarity). FT BINDING 196 196 Substrate (By similarity). FT MOD_RES 73 73 N6-acetyllysine. FT MOD_RES 97 97 N6-acetyllysine. FT MOD_RES 103 103 N6-acetyllysine; alternate. FT MOD_RES 103 103 N6-succinyllysine; alternate. FT MOD_RES 132 132 N6-acetyllysine. FT MOD_RES 177 177 N6-acetyllysine. FT MOD_RES 212 212 N6-acetyllysine. FT MOD_RES 258 258 N6-acetyllysine. FT MOD_RES 259 259 N6-acetyllysine; alternate. FT MOD_RES 259 259 N6-succinyllysine; alternate. FT MOD_RES 280 280 N6-acetyllysine. FT CONFLICT 152 152 E -> G (in Ref. 1; BAC36453). FT CONFLICT 215 215 I -> V (in Ref. 1; BAC36453/BAE23523/ FT BAE26605). SQ SEQUENCE 343 AA; 38299 MW; B72B0550713EDB7F CRC64; MLAARLSRPL SQLPGKALSV RDRENGTRHT LLFYPASFSP DTRRTYASQA DAASGKAILI TGCDSGFGFS LAKHLHSKGF LVFAGCLMKD KGDAGVKELD SLKSDRLRTI QLNVCNSEEV EKAVETIRSG LKDPEKGMWG LVNNAGISTF GEVEFTSMET YKEVAEVNLW GTVRTTKSFL PLLRRAKGRV VNISSMLGRM ANPARSPYCI TKFGIEAFSD CLRYEMHPLG VKVSVVEPGN FIAATSLYSP ERIQAIAKKM WDDLPEVVRK DYGRKYFDEK IAKMETYCNS GSTDTSSVIN AVTHALTAAT PYTRYHPMDY YWWLRMQIMT HFPGAISDKI YIH // ID BIEA_MOUSE Reviewed; 295 AA. AC Q9CY64; Q3T9C6; Q80WR6; Q9DD21; DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 19-MAR-2014, entry version 97. DE RecName: Full=Biliverdin reductase A; DE Short=BVR A; DE EC=1.3.1.24; DE AltName: Full=Biliverdin-IX alpha-reductase; DE Flags: Precursor; GN Name=Blvra; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J, and NOD; TISSUE=Embryonic liver, Kidney, and Spleen; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: Reduces the gamma-methene bridge of the open CC tetrapyrrole, biliverdin IX alpha, to bilirubin with the CC concomitant oxidation of a NADH or NADPH cofactor (By similarity). CC -!- CATALYTIC ACTIVITY: Bilirubin + NAD(P)(+) = biliverdin + NAD(P)H. CC -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity). CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoheme CC degradation. CC -!- SUBUNIT: Monomer (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- MISCELLANEOUS: Uses the reactants NADH or NADPH depending on the CC pH; NADH is used at the acidic pH range (6-6.9) and NADPH at the CC alkaline range (8.5-8.7). NADPH, however, is the probable reactant CC in biological systems (By similarity). CC -!- SIMILARITY: Belongs to the Gfo/Idh/MocA family. Biliverdin CC reductase subfamily. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK002231; BAB21950.1; -; mRNA. DR EMBL; AK010847; BAB27219.1; -; mRNA. DR EMBL; AK172620; BAE43098.1; -; mRNA. DR EMBL; BC052146; AAH52146.1; -; mRNA. DR RefSeq; NP_080954.4; NM_026678.4. DR RefSeq; XP_006498634.1; XM_006498571.1. DR RefSeq; XP_006498635.1; XM_006498572.1. DR UniGene; Mm.22028; -. DR ProteinModelPortal; Q9CY64; -. DR SMR; Q9CY64; 8-291. DR IntAct; Q9CY64; 2. DR MINT; MINT-1854695; -. DR PhosphoSite; Q9CY64; -. DR PaxDb; Q9CY64; -. DR PRIDE; Q9CY64; -. DR Ensembl; ENSMUST00000002064; ENSMUSP00000002064; ENSMUSG00000001999. DR GeneID; 109778; -. DR KEGG; mmu:109778; -. DR UCSC; uc008meq.1; mouse. DR CTD; 644; -. DR MGI; MGI:88170; Blvra. DR eggNOG; NOG114525; -. DR GeneTree; ENSGT00390000011072; -. DR HOGENOM; HOG000231884; -. DR HOVERGEN; HBG003218; -. DR InParanoid; Q9CY64; -. DR KO; K00214; -. DR OMA; KRILHCL; -. DR OrthoDB; EOG78WKS5; -. DR TreeFam; TF342889; -. DR UniPathway; UPA00684; -. DR NextBio; 362743; -. DR PRO; PR:Q9CY64; -. DR ArrayExpress; Q9CY64; -. DR Bgee; Q9CY64; -. DR CleanEx; MM_BLVRA; -. DR Genevestigator; Q9CY64; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004074; F:biliverdin reductase activity; IDA:MGI. DR GO; GO:0000166; F:nucleotide binding; ISO:MGI. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042167; P:heme catabolic process; ISO:MGI. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR017094; Biliverdin_Rdtase_A. DR InterPro; IPR015249; Biliverdin_Rdtase_cat. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR000683; Oxidoreductase_N. DR Pfam; PF09166; Biliv-reduc_cat; 1. DR Pfam; PF01408; GFO_IDH_MocA; 1. DR PIRSF; PIRSF037032; Biliverdin_reductase_A; 1. DR ProDom; PD040165; Biliverdin_Rdtase_cat; 1. PE 2: Evidence at transcript level; KW Acetylation; Complete proteome; Cytoplasm; Metal-binding; NAD; NADP; KW Oxidoreductase; Phosphoprotein; Reference proteome; Zinc. FT PROPEP 1 2 By similarity. FT /FTId=PRO_0000010854. FT CHAIN 3 295 Biliverdin reductase A. FT /FTId=PRO_0000010855. FT NP_BIND 15 20 NAD or NADP (By similarity). FT NP_BIND 76 79 NAD or NADP (By similarity). FT COMPBIAS 11 16 Poly-Val. FT METAL 279 279 Zinc (Potential). FT METAL 280 280 Zinc (Potential). FT METAL 291 291 Zinc (Potential). FT METAL 292 292 Zinc (Potential). FT BINDING 97 97 NAD or NADP; via carbonyl oxygen (By FT similarity). FT MOD_RES 173 173 Phosphothreonine (By similarity). FT MOD_RES 177 177 Phosphoserine (By similarity). FT MOD_RES 229 229 Phosphoserine (By similarity). FT MOD_RES 247 247 N6-acetyllysine (By similarity). FT MOD_RES 252 252 N6-acetyllysine (By similarity). FT CONFLICT 27 27 L -> S (in Ref. 2; AAH52146). FT CONFLICT 295 295 Q -> QWGGSFRYL (in Ref. 1; BAB21950). SQ SEQUENCE 295 AA; 33525 MW; F2E1682BD77032A4 CRC64; MSTEPKRKFG VVVVGVGRAG SVRIRDLKDP HSSAFLNLIG YVSRRELGSL DNVRQISLED ALRSQEVDVA YICTESSSHE DYIRQFLQAG KHVLVEYPMA LSFAAAQELW ELAAQKGRVL HEEHIELLME EFEFLKREVA GKELLKGSLR FTASPLEEEK FGFPAFSGIS RLTWLVSLFG ELSLISATME NRKEDQYMKM TVQLETQNKS PLSWIEEKGP GLKRNRHISI HFKSGSLEEV PNVGVNKNIF LKDQDIFIQK LLGQVSAEDL AAEKKRILHC LELASDIQRL CHRKQ // ID BLVRB_MOUSE Reviewed; 206 AA. AC Q923D2; DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 19-FEB-2014, entry version 90. DE RecName: Full=Flavin reductase (NADPH); DE Short=FR; DE EC=1.5.1.30; DE AltName: Full=Biliverdin reductase B; DE Short=BVR-B; DE EC=1.3.1.24; DE AltName: Full=Biliverdin-IX beta-reductase; DE AltName: Full=NADPH-dependent diaphorase; DE AltName: Full=NADPH-flavin reductase; DE Short=FLR; GN Name=Blvrb; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Czech II, and FVB/N; TISSUE=Mammary tumor; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: Broad specificity oxidoreductase that catalyzes the CC NADPH-dependent reduction of a variety of flavins, such as CC riboflavin, FAD or FMN, biliverdins, methemoglobin and PQQ CC (pyrroloquinoline quinone). Contributes to heme catabolism and CC metabolizes linear tetrapyrroles. Can also reduce the complexed CC Fe(3+) iron to Fe(2+) in the presence of FMN and NADPH. In the CC liver, converts biliverdin to bilirubin (By similarity). CC -!- CATALYTIC ACTIVITY: Reduced riboflavin + NADP(+) = riboflavin + CC NADPH. CC -!- CATALYTIC ACTIVITY: Bilirubin + NAD(P)(+) = biliverdin + NAD(P)H. CC -!- SUBUNIT: Monomer (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BC006617; AAH06617.1; -; mRNA. DR EMBL; BC027279; AAH27279.1; -; mRNA. DR RefSeq; NP_659172.1; NM_144923.3. DR UniGene; Mm.24021; -. DR ProteinModelPortal; Q923D2; -. DR SMR; Q923D2; 1-205. DR IntAct; Q923D2; 2. DR MINT; MINT-1868915; -. DR PhosphoSite; Q923D2; -. DR PaxDb; Q923D2; -. DR PRIDE; Q923D2; -. DR Ensembl; ENSMUST00000037399; ENSMUSP00000043092; ENSMUSG00000040466. DR GeneID; 233016; -. DR KEGG; mmu:233016; -. DR UCSC; uc009fwd.1; mouse. DR CTD; 645; -. DR MGI; MGI:2385271; Blvrb. DR eggNOG; NOG75634; -. DR GeneTree; ENSGT00390000014810; -. DR HOGENOM; HOG000262432; -. DR HOVERGEN; HBG050695; -. DR KO; K05901; -. DR OrthoDB; EOG7966J5; -. DR TreeFam; TF324063; -. DR NextBio; 381462; -. DR PRO; PR:Q923D2; -. DR ArrayExpress; Q923D2; -. DR Bgee; Q923D2; -. DR CleanEx; MM_BLVRB; -. DR Genevestigator; Q923D2; -. DR GO; GO:0005829; C:cytosol; ISS:UniProtKB. DR GO; GO:0005634; C:nucleus; IEA:Ensembl. DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl. DR GO; GO:0004074; F:biliverdin reductase activity; ISS:UniProtKB. DR GO; GO:0042602; F:riboflavin reductase (NADPH) activity; ISS:UniProtKB. DR GO; GO:0042167; P:heme catabolic process; ISS:UniProtKB. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR016040; NAD(P)-bd_dom. PE 2: Evidence at transcript level; KW Complete proteome; Cytoplasm; NADP; Oxidoreductase; KW Reference proteome. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 206 Flavin reductase (NADPH). FT /FTId=PRO_0000064949. FT NP_BIND 10 15 NADP (By similarity). FT NP_BIND 54 55 NADP (By similarity). FT NP_BIND 75 78 NADP (By similarity). FT BINDING 35 35 NADP (By similarity). FT BINDING 132 132 NADP (By similarity). FT BINDING 153 153 Substrate (By similarity). FT BINDING 154 154 NADP; via amide nitrogen (By similarity). SQ SEQUENCE 206 AA; 22197 MW; EDAEE91F5F39F629 CRC64; MTVKKIAIFG ATGRTGLTTL AQAVQAGYEV TVLVRDSSRL PSEGPQPAHV VVGDVRQAAD VDKTVAGQEA VIVLLGTGND LSPTTVMSEG TRNIVTAMKA HGVDKVVACT SAFLLWDPTK VPPRLQDVTD DHIRMHKILQ ESGLKYVAVM PPHIGDQPLT GAYTVTLDGR GPSRVISKHD LGHFMLRCLT TNEYDGHTTY PSHQYD // ID BODG_MOUSE Reviewed; 387 AA. AC Q924Y0; DT 20-JUN-2002, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 19-MAR-2014, entry version 92. DE RecName: Full=Gamma-butyrobetaine dioxygenase; DE EC=1.14.11.1; DE AltName: Full=Gamma-butyrobetaine hydroxylase; DE Short=Gamma-BBH; DE AltName: Full=Gamma-butyrobetaine,2-oxoglutarate dioxygenase; GN Name=Bbox1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=FVB/N; RA Vaz F.M., Ofman R., Wanders R.J.A.; RT "Identification of mouse gamma-butyrobetaine hydroxylase cDNA."; RL Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Liver; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: Catalyzes the formation of L-carnitine from gamma- CC butyrobetaine (By similarity). CC -!- CATALYTIC ACTIVITY: 4-trimethylammoniobutanoate + 2-oxoglutarate + CC O(2) = 3-hydroxy-4-trimethylammoniobutanoate + succinate + CO(2). CC -!- COFACTOR: Binds 1 Fe(2+) ion per subunit (By similarity). CC -!- COFACTOR: Ascorbate (By similarity). CC -!- PATHWAY: Amine and polyamine biosynthesis; carnitine biosynthesis. CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the gamma-BBH/TMLD family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AY033514; AAK54388.1; -; mRNA. DR EMBL; BC019406; AAH19406.1; -; mRNA. DR RefSeq; NP_569719.1; NM_130452.1. DR RefSeq; XP_006498885.1; XM_006498822.1. DR RefSeq; XP_006498886.1; XM_006498823.1. DR UniGene; Mm.27335; -. DR ProteinModelPortal; Q924Y0; -. DR SMR; Q924Y0; 1-385. DR IntAct; Q924Y0; 1. DR MINT; MINT-1856133; -. DR STRING; 10090.ENSMUSP00000046302; -. DR PhosphoSite; Q924Y0; -. DR PaxDb; Q924Y0; -. DR PRIDE; Q924Y0; -. DR DNASU; 170442; -. DR Ensembl; ENSMUST00000046233; ENSMUSP00000046302; ENSMUSG00000041660. DR GeneID; 170442; -. DR KEGG; mmu:170442; -. DR UCSC; uc008lmu.1; mouse. DR CTD; 8424; -. DR MGI; MGI:1891372; Bbox1. DR eggNOG; COG2175; -. DR GeneTree; ENSGT00530000063582; -. DR HOGENOM; HOG000231427; -. DR HOVERGEN; HBG031125; -. DR InParanoid; Q924Y0; -. DR KO; K00471; -. DR OMA; CAIQKAE; -. DR OrthoDB; EOG7XPZ5P; -. DR TreeFam; TF313805; -. DR UniPathway; UPA00118; -. DR NextBio; 370087; -. DR PRO; PR:Q924Y0; -. DR ArrayExpress; Q924Y0; -. DR Bgee; Q924Y0; -. DR Genevestigator; Q924Y0; -. DR GO; GO:0015629; C:actin cytoskeleton; IEA:Ensembl. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR GO; GO:0008336; F:gamma-butyrobetaine dioxygenase activity; ISS:UniProtKB. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB. DR GO; GO:0045329; P:carnitine biosynthetic process; ISS:UniProtKB. DR InterPro; IPR012775; 2-oxoglut_dOase. DR InterPro; IPR010376; DUF971. DR InterPro; IPR003819; Taurine_dOase. DR Pfam; PF06155; DUF971; 1. DR Pfam; PF02668; TauD; 1. DR TIGRFAMs; TIGR02409; carnitine_bodg; 1. PE 2: Evidence at transcript level; KW Carnitine biosynthesis; Complete proteome; Cytoplasm; Dioxygenase; KW Iron; Metal-binding; Oxidoreductase; Reference proteome; Zinc. FT CHAIN 1 387 Gamma-butyrobetaine dioxygenase. FT /FTId=PRO_0000207086. FT METAL 38 38 Zinc (By similarity). FT METAL 40 40 Zinc (By similarity). FT METAL 43 43 Zinc (By similarity). FT METAL 82 82 Zinc (By similarity). FT METAL 202 202 Iron; catalytic (By similarity). FT METAL 204 204 Iron; catalytic (By similarity). FT METAL 347 347 Iron; catalytic (By similarity). SQ SEQUENCE 387 AA; 44699 MW; 9F17F5F9CAE052BE CRC64; MHCAILKAEA VDGAHLMQIF WHDGAESLYP AVWLRDNCQC SDCYLHSAKA RKLLLEALDV NIRIDDLTFD RKKVYITWPN DHYSEFEANW LKKRCFSQQA RARLQGELFL PECQYWGSEL QLPTLNFEDV LNDDDHAYKW LSSLKKVGIV RLTGAADKRG EIIKLGKRIG FLYLTFYGHT WQVQDKIDAN NVAYTTGKLS FHTDYPALHH PPGVQLLHCI KQTVTGGDSE IVDGFNVCQK LKEKNPQAFH ILSSTFVDFT DIGVDYCDFS VQSKHKIIEL DDKGQVVRVN FNNATRDTVF DVPIERVQPF YAALKEFVDL MNSKEYKYTF KMNPGDVITF DNWRLLHGRR SYEAGTEISR HLEGAYADWD VVMSRLRILR QRVTNGN // ID C11B2_MOUSE Reviewed; 500 AA. AC P15539; Q14AB5; Q64661; DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 3. DT 22-JAN-2014, entry version 124. DE RecName: Full=Cytochrome P450 11B2, mitochondrial; DE AltName: Full=Aldosterone synthase; DE AltName: Full=CYPXIB2; DE AltName: Full=Cytochrome P450C11; DE AltName: Full=Steroid 11-beta-hydroxylase; DE EC=1.14.15.4; DE EC=1.14.15.5; DE Flags: Precursor; GN Name=Cyp11b2; Synonyms=Cyp11b-2; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=1686470; RA Domalik L.J., Chaplin D.D., Kirkman M.S., Wu R.C., Liu W., RA Howard T.A., Seldin M.F., Parker K.L.; RT "Different isozymes of mouse 11 beta-hydroxylase produce RT mineralocorticoids and glucocorticoids."; RL Mol. Endocrinol. 5:1853-1861(1991). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-42. RX PubMed=2783417; RA Mouw A.R., Rice D.A., Meade J.C., Chua S.C., White P.C., RA Schimmer B.P., Parker K.L.; RT "Structural and functional analysis of the promoter region of the gene RT encoding mouse steroid 11 beta-hydroxylase."; RL J. Biol. Chem. 264:1305-1309(1989). CC -!- FUNCTION: Forms corticosterone from 11-deoxycorticosterone. CC -!- CATALYTIC ACTIVITY: A steroid + reduced adrenodoxin + O(2) = an CC 11-beta-hydroxysteroid + oxidized adrenodoxin + H(2)O. CC -!- CATALYTIC ACTIVITY: Corticosterone + reduced adrenodoxin + O(2) = CC 18-hydroxycorticosterone + oxidized adrenodoxin + H(2)O. CC -!- COFACTOR: Heme group (By similarity). CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane. CC -!- SIMILARITY: Belongs to the cytochrome P450 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; S85260; AAB21517.2; -; Genomic_DNA. DR EMBL; BC116908; AAI16909.1; -; mRNA. DR EMBL; BC119321; AAI19322.1; -; mRNA. DR EMBL; J04451; AAA50299.1; -; Genomic_DNA. DR PIR; A41552; A41552. DR RefSeq; NP_034121.3; NM_009991.3. DR UniGene; Mm.377079; -. DR ProteinModelPortal; P15539; -. DR SMR; P15539; 34-499. DR STRING; 10090.ENSMUSP00000023253; -. DR PRIDE; P15539; -. DR GeneID; 13072; -. DR KEGG; mmu:13072; -. DR CTD; 1585; -. DR MGI; MGI:88584; Cyp11b2. DR eggNOG; COG2124; -. DR HOGENOM; HOG000013161; -. DR HOVERGEN; HBG051098; -. DR InParanoid; Q14AB5; -. DR KO; K00497; -. DR NextBio; 283008; -. DR PRO; PR:P15539; -. DR ArrayExpress; P15539; -. DR Bgee; P15539; -. DR Genevestigator; P15539; -. DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR GO; GO:0047783; F:corticosterone 18-monooxygenase activity; IEA:UniProtKB-EC. DR GO; GO:0020037; F:heme binding; ISS:UniProtKB. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0004507; F:steroid 11-beta-monooxygenase activity; IDA:MGI. DR GO; GO:0032342; P:aldosterone biosynthetic process; IDA:MGI. DR GO; GO:0042756; P:drinking behavior; IMP:MGI. DR GO; GO:0050801; P:ion homeostasis; IMP:MGI. DR GO; GO:0002017; P:regulation of blood volume by renal aldosterone; IMP:MGI. DR GO; GO:0001991; P:regulation of systemic arterial blood pressure by circulatory renin-angiotensin; IMP:MGI. DR Gene3D; 1.10.630.10; -; 1. DR InterPro; IPR001128; Cyt_P450. DR InterPro; IPR017972; Cyt_P450_CS. DR InterPro; IPR002399; Cyt_P450_mitochondrial. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00408; MITP450. DR PRINTS; PR00385; P450. DR SUPFAM; SSF48264; SSF48264; 1. DR PROSITE; PS00086; CYTOCHROME_P450; 1. PE 2: Evidence at transcript level; KW Complete proteome; Heme; Iron; Membrane; Metal-binding; Mitochondrion; KW Monooxygenase; Oxidoreductase; Reference proteome; Steroidogenesis; KW Transit peptide. FT TRANSIT 1 24 Mitochondrion. FT CHAIN 25 500 Cytochrome P450 11B2, mitochondrial. FT /FTId=PRO_0000003600. FT METAL 447 447 Iron (heme axial ligand) (By similarity). FT CONFLICT 491 491 S -> E (in Ref. 1; AAB21517). SQ SEQUENCE 500 AA; 57373 MW; DCAFFF3EF2663195 CRC64; MALRVTADVW LARPWQCLHR TRALGTTATL APKTLQPFEA IPQYSRNKWL KMIQILREQG QENLHLEMHQ VFRELGPIFR HSVGKTQIVS VMLPEDAEKL HQVESMLPRR MHLEPWVAHR ELRGLRRGVF LLNGPEWRLN RLRLNRNVLS PKAVQKFVPM VDMVARDFLE TLKEKVLQNA RGSLTMDVQQ SLFNYTIEAS NFALFGERLG LLGHDLSPGS LKFIHALHSM FKSTSQLLFL PKSLTRWTST RVWKEHFDAW DVISEYANRC IWKVHQELRL GSSQTYSGIV AELISQGSLP LDAIKANSME LTAGSVDTTA IPLVMTLFEL ARNPDVQKAL RQESLAAEAS IAANPQKAMS DLPLLRAALK ETLRLYPVGG FLERILSSDL VLQNYHVPAG TLVLLYLYSM GRNPAVFPRP ERYMPQRWLE RKRSFQHLAF GFGVRQCLGR RLAEVEMMLL LHHILKTFQV ETLRQEDVQM AYRFVLMPSS SPVLTFRPVS // ID C1TC_MOUSE Reviewed; 935 AA. AC Q922D8; Q8R013; DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 4. DT 19-FEB-2014, entry version 104. DE RecName: Full=C-1-tetrahydrofolate synthase, cytoplasmic; DE Short=C1-THF synthase; DE Includes: DE RecName: Full=Methylenetetrahydrofolate dehydrogenase; DE EC=1.5.1.5; DE Includes: DE RecName: Full=Methenyltetrahydrofolate cyclohydrolase; DE EC=3.5.4.9; DE Includes: DE RecName: Full=Formyltetrahydrofolate synthetase; DE EC=6.3.4.3; DE Contains: DE RecName: Full=C-1-tetrahydrofolate synthase, cytoplasmic, N-terminally processed; GN Name=Mthfd1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. RC STRAIN=129/SvJ; RX PubMed=12061812; DOI=10.1016/S0003-9861(02)00203-5; RA Patel H., Christensen K.E., Mejia N., MacKenzie R.E.; RT "Mammalian mitochondrial methylenetetrahydrofolate dehydrogenase- RT cyclohydrolase derived from a trifunctional methylenetetrahydrofolate RT dehydrogenase-cyclohydrolase-synthetase."; RL Arch. Biochem. Biophys. 403:145-148(2002). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=NOD; TISSUE=Thymus; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP PROTEIN SEQUENCE OF 2-17; 27-56; 59-66; 75-83; 123-134; 138-173; RP 176-198; 205-223; 251-262; 314-324; 330-352; 355-362; 371-402; RP 464-473; 488-495; 505-517; 521-532; 543-553; 658-679; 687-702; RP 706-733; 747-772; 776-784; 805-819; 833-848 AND 855-889, AND MASS RP SPECTROMETRY. RC STRAIN=OF1; TISSUE=Hippocampus; RA Lubec G., Sunyer B., Chen W.-Q.; RL Submitted (JAN-2009) to UniProtKB. RN [5] RP DISRUPTION PHENOTYPE. RX PubMed=15611115; DOI=10.1074/jbc.M409380200; RA Christensen K.E., Patel H., Kuzmanov U., Mejia N.R., MacKenzie R.E.; RT "Disruption of the mthfd1 gene reveals a monofunctional 10- RT formyltetrahydrofolate synthetase in mammalian mitochondria."; RL J. Biol. Chem. 280:7597-7602(2005). CC -!- CATALYTIC ACTIVITY: 5,10-methylenetetrahydrofolate + NADP(+) = CC 5,10-methenyltetrahydrofolate + NADPH. CC -!- CATALYTIC ACTIVITY: 5,10-methenyltetrahydrofolate + H(2)O = 10- CC formyltetrahydrofolate. CC -!- CATALYTIC ACTIVITY: ATP + formate + tetrahydrofolate = ADP + CC phosphate + 10-formyltetrahydrofolate. CC -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion. CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- DOMAIN: This trifunctional enzyme consists of two major domains: CC an N-terminal part containing the methylene-THF dehydrogenase and CC cyclohydrolase activities and a larger C-terminal part containing CC formyl-THF synthetase activity. CC -!- DISRUPTION PHENOTYPE: Knockout mice have revealed Mthfd1l as a CC monofunctional enzyme having only formyltetrahydrofolate CC synthetase activity and lacking methenyl-THF dehydrogenase and CC cyclohydrolase activities. CC -!- SIMILARITY: In the N-terminal section; belongs to the CC tetrahydrofolate dehydrogenase/cyclohydrolase family. CC -!- SIMILARITY: In the C-terminal section; belongs to the formate-- CC tetrahydrofolate ligase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF364579; AAL99692.1; -; mRNA. DR EMBL; AF364591; AAL99693.1; -; Genomic_DNA. DR EMBL; AF364580; AAL99693.1; JOINED; Genomic_DNA. DR EMBL; AF364581; AAL99693.1; JOINED; Genomic_DNA. DR EMBL; AF364582; AAL99693.1; JOINED; Genomic_DNA. DR EMBL; AF364583; AAL99693.1; JOINED; Genomic_DNA. DR EMBL; AF364584; AAL99693.1; JOINED; Genomic_DNA. DR EMBL; AF364585; AAL99693.1; JOINED; Genomic_DNA. DR EMBL; AF364586; AAL99693.1; JOINED; Genomic_DNA. DR EMBL; AF364587; AAL99693.1; JOINED; Genomic_DNA. DR EMBL; AF364588; AAL99693.1; JOINED; Genomic_DNA. DR EMBL; AF364589; AAL99693.1; JOINED; Genomic_DNA. DR EMBL; AF364590; AAL99693.1; JOINED; Genomic_DNA. DR EMBL; AK088700; BAC40513.1; -; mRNA. DR EMBL; BC008523; AAH08523.1; -; mRNA. DR RefSeq; NP_620084.2; NM_138745.2. DR UniGene; Mm.29584; -. DR ProteinModelPortal; Q922D8; -. DR SMR; Q922D8; 2-296, 316-935. DR IntAct; Q922D8; 5. DR MINT; MINT-1856310; -. DR ChEMBL; CHEMBL3137; -. DR PhosphoSite; Q922D8; -. DR REPRODUCTION-2DPAGE; Q922D8; -. DR PaxDb; Q922D8; -. DR PRIDE; Q922D8; -. DR Ensembl; ENSMUST00000021443; ENSMUSP00000021443; ENSMUSG00000021048. DR GeneID; 108156; -. DR KEGG; mmu:108156; -. DR UCSC; uc007nxz.2; mouse. DR CTD; 4522; -. DR MGI; MGI:1342005; Mthfd1. DR eggNOG; COG0190; -. DR GeneTree; ENSGT00730000110859; -. DR HOVERGEN; HBG004916; -. DR InParanoid; Q8R013; -. DR KO; K00288; -. DR OMA; RIFHERT; -. DR OrthoDB; EOG76T9QN; -. DR TreeFam; TF300623; -. DR UniPathway; UPA00193; -. DR ChiTaRS; MTHFD1; mouse. DR NextBio; 360186; -. DR PRO; PR:Q922D8; -. DR ArrayExpress; Q922D8; -. DR Bgee; Q922D8; -. DR Genevestigator; Q922D8; -. DR GO; GO:0005829; C:cytosol; IBA:RefGenome. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004329; F:formate-tetrahydrofolate ligase activity; IBA:RefGenome. DR GO; GO:0004477; F:methenyltetrahydrofolate cyclohydrolase activity; IBA:RefGenome. DR GO; GO:0004488; F:methylenetetrahydrofolate dehydrogenase (NADP+) activity; IBA:RefGenome. DR GO; GO:0009396; P:folic acid-containing compound biosynthetic process; IEA:InterPro. DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0006730; P:one-carbon metabolic process; IBA:RefGenome. DR GO; GO:0006164; P:purine nucleotide biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0035999; P:tetrahydrofolate interconversion; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.720; -; 1. DR HAMAP; MF_01543; FTHFS; 1. DR HAMAP; MF_01576; THF_DHG_CYH; 1. DR InterPro; IPR000559; Formate_THF_ligase. DR InterPro; IPR020628; Formate_THF_ligase_CS. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR000672; THF_DH/CycHdrlase. DR InterPro; IPR020630; THF_DH/CycHdrlase_cat_dom. DR InterPro; IPR020867; THF_DH/CycHdrlase_CS. DR InterPro; IPR020631; THF_DH/CycHdrlase_NAD-bd_dom. DR Pfam; PF01268; FTHFS; 1. DR Pfam; PF00763; THF_DHG_CYH; 1. DR Pfam; PF02882; THF_DHG_CYH_C; 1. DR PRINTS; PR00085; THFDHDRGNASE. DR SUPFAM; SSF52540; SSF52540; 2. DR PROSITE; PS00721; FTHFS_1; 1. DR PROSITE; PS00722; FTHFS_2; 1. DR PROSITE; PS00766; THF_DHG_CYH_1; 1. DR PROSITE; PS00767; THF_DHG_CYH_2; 1. PE 1: Evidence at protein level; KW Acetylation; Amino-acid biosynthesis; ATP-binding; Complete proteome; KW Cytoplasm; Direct protein sequencing; Histidine biosynthesis; KW Hydrolase; Ligase; Methionine biosynthesis; Multifunctional enzyme; KW NADP; Nucleotide-binding; One-carbon metabolism; Oxidoreductase; KW Purine biosynthesis; Reference proteome. FT CHAIN 1 935 C-1-tetrahydrofolate synthase, FT cytoplasmic. FT /FTId=PRO_0000199322. FT INIT_MET 1 1 Removed; alternate (By similarity). FT CHAIN 2 935 C-1-tetrahydrofolate synthase, FT cytoplasmic, N-terminally processed. FT /FTId=PRO_0000423281. FT NP_BIND 172 174 NADP (By similarity). FT NP_BIND 380 387 ATP (By similarity). FT REGION 1 305 Methylenetetrahydrofolate dehydrogenase FT and cyclohydrolase. FT REGION 52 56 Substrate binding (By similarity). FT REGION 99 101 Substrate binding (By similarity). FT REGION 272 276 Substrate binding (By similarity). FT REGION 306 935 Formyltetrahydrofolate synthetase. FT BINDING 197 197 NADP (By similarity). FT MOD_RES 1 1 N-acetylmethionine (By similarity). FT CONFLICT 365 365 H -> Y (in Ref. 3; AAH08523). FT CONFLICT 610 610 A -> T (in Ref. 3; AAH08523). SQ SEQUENCE 935 AA; 101200 MW; 0EB92D58C78DDEB5 CRC64; MAPAGILNGK LVSAQIRDRL KNQVTRMQEQ VPGFTPGLAI LQVGDRDDSN LYINVKLKAA EEIGIKATHI KLPRTSTESE VLKYVISLNE DASVHGFIVQ LPLDSENSIN TEAVINAIAP EKDVDGLTSV SAGKLARGDL NDCFIPCTPK GCLELIKEAG VQIAGRHAVV VGRSKIVGAP MHDLLLWNNA TVTTCHSKTA NLDKEVNKGD ILVVATGQPE MVKGEWIKPG AVVIDCGINY VPDDTKPNGR KVVGDVAYDE AKERASFITP VPGGVGPMTV AMLMQSTVES AQRFLQKFKP GKWTIQYNKL NLKTPVPSDI AISRSCKPKL IGNLAREIGL LTEEVELYGE TKAKVLLSAL DRLKHQPDGK YVVVTGITPT PLGEGKSTTT IGLVQALGAH LRQNVFACVR QPSQGPTFGI KGGAAGGGYS QVIPMEEFNL HLTGDIHAIT AANNLVAAAI DARIFHELTQ TDKALFNRLV PSVNGIRKFS DIQIRRLRRL GIEKTDPTTL TDDEINRFAR LDIDPETITW QRVLDTNDRF LRKITIGQSP TEKGHTRTAQ FDISVASEIM AVLALTSSLE DMRERLGRMV VASSKKGEPI SCEDLGVSGA LTVLMKDAIK PNLMQTLEGT PVFVHAGPFA NIAHGNSSII ADRIALKLVG PEGFVVTEAG FGADIGMEKF FNIKCRYSGL QPHVVVLVAT VRALKMHGGG PTVTAGLPLP KAYTEEDLDL VEKGFSNLRK QIENARMFGV PVVVAVNVFK TDTDAELDLV SRLSREHGAF DAVKCTHWAE GGQGALALAQ AVQRASQAPS SFQLLYDLKL SIEDKIRIIA QRIYGADDIE LLPEAQNKAE IYTKQGFGNL PICMAKTHLS LSHNPEQKGV PTGFVLPIRD IRASVGAGFL YPLVGTMSTM PGLPTRPCFY DIDLDPETEQ VNGLF // ID CATA_MOUSE Reviewed; 527 AA. AC P24270; Q3TXQ6; DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 4. DT 19-MAR-2014, entry version 133. DE RecName: Full=Catalase; DE EC=1.11.1.6; GN Name=Cat; Synonyms=Cas-1, Cas1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=C3H/CS(A); TISSUE=Kidney, and Liver; RX PubMed=2268310; DOI=10.1016/S0006-291X(05)80891-5; RA Shaffer J.B., Preston K.E.; RT "Molecular analysis of an acatalasemic mouse mutant."; RL Biochem. Biophys. Res. Commun. 173:1043-1050(1990). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=C3H/CS(A), and C3H/HeJ; TISSUE=Liver; RX PubMed=2395665; DOI=10.1093/nar/18.16.4941; RA Shaffer J.B., Preston K.E., Shepard B.A.; RT "Nucleotide and deduced amino acid sequences of mouse catalase: RT molecular analysis of a low activity mutant."; RL Nucleic Acids Res. 18:4941-4941(1990). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=BALB/c; TISSUE=Liver; RX PubMed=8088826; DOI=10.1006/geno.1994.1273; RA Reimer D.L., Bailley J., Singh S.M.; RT "Complete cDNA and 5' genomic sequences and multilevel regulation of RT the mouse catalase gene."; RL Genomics 21:325-336(1994). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Amnion, and Bone marrow; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Kidney; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [8] RP PROTEIN SEQUENCE OF 2-12; 221-232; 287-300; 306-314 AND 468-475, RP CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, AND MASS RP SPECTROMETRY. RC STRAIN=C57BL/6J; TISSUE=Skeletal muscle; RA Kanor S., Quadroni M., Bienvenut W.V.; RL Submitted (MAR-2006) to UniProtKB. RN [9] RP PROTEIN SEQUENCE OF 48-66, AND MASS SPECTROMETRY. RC STRAIN=OF1; TISSUE=Hippocampus; RA Lubec G., Sunyer B., Chen W.-Q.; RL Submitted (JAN-2009) to UniProtKB. RN [10] RP NUCLEOTIDE SEQUENCE [MRNA] OF 503-527. RX PubMed=3654595; RA Shaffer J.B., Sutton R.B., Bewley G.C.; RT "Isolation of a cDNA clone for murine catalase and analysis of an RT acatalasemic mutant."; RL J. Biol. Chem. 262:12908-12911(1987). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-417 AND SER-434, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=17242355; DOI=10.1073/pnas.0609836104; RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; RT "Large-scale phosphorylation analysis of mouse liver."; RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). RN [12] RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2 AND LYS-449, SUCCINYLATION RP [LARGE SCALE ANALYSIS] AT LYS-13; LYS-221; LYS-306; LYS-430; LYS-449; RP LYS-480 AND LYS-522, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE RP SCALE ANALYSIS]. RC TISSUE=Embryonic fibroblast, and Liver; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., RA Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). RN [13] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-233; LYS-306; LYS-430; RP LYS-449; LYS-480 AND LYS-499, AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23576753; DOI=10.1073/pnas.1302961110; RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., RA Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.; RT "Label-free quantitative proteomics of the lysine acetylome in RT mitochondria identifies substrates of SIRT3 in metabolic pathways."; RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013). CC -!- FUNCTION: Occurs in almost all aerobically respiring organisms and CC serves to protect cells from the toxic effects of hydrogen CC peroxide. Promotes growth of cells. CC -!- CATALYTIC ACTIVITY: 2 H(2)O(2) = O(2) + 2 H(2)O. CC -!- COFACTOR: Heme group. CC -!- COFACTOR: NADP. CC -!- SUBUNIT: Homotetramer. CC -!- SUBCELLULAR LOCATION: Peroxisome. CC -!- SIMILARITY: Belongs to the catalase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M62897; AAA37373.1; -; mRNA. DR EMBL; X52108; CAA36342.1; -; mRNA. DR EMBL; L25069; AAA66054.1; -; mRNA. DR EMBL; AK150893; BAE29939.1; -; mRNA. DR EMBL; AK159152; BAE34859.1; -; mRNA. DR EMBL; AK159885; BAE35454.1; -; mRNA. DR EMBL; AK159891; BAE35458.1; -; mRNA. DR EMBL; AK169069; BAE40856.1; -; mRNA. DR EMBL; AL773505; CAM17512.1; -; Genomic_DNA. DR EMBL; CH466519; EDL27697.1; -; Genomic_DNA. DR EMBL; BC013447; AAH13447.1; -; mRNA. DR EMBL; M29394; AAA37371.1; -; mRNA. DR PIR; A36695; A36695. DR RefSeq; NP_033934.2; NM_009804.2. DR UniGene; Mm.4215; -. DR ProteinModelPortal; P24270; -. DR SMR; P24270; 4-501. DR IntAct; P24270; 3. DR MINT; MINT-1859622; -. DR PhosphoSite; P24270; -. DR SWISS-2DPAGE; P24270; -. DR PaxDb; P24270; -. DR PRIDE; P24270; -. DR Ensembl; ENSMUST00000028610; ENSMUSP00000028610; ENSMUSG00000027187. DR GeneID; 12359; -. DR KEGG; mmu:12359; -. DR UCSC; uc008liw.2; mouse. DR CTD; 847; -. DR MGI; MGI:88271; Cat. DR eggNOG; COG0753; -. DR GeneTree; ENSGT00390000018100; -. DR HOGENOM; HOG000087852; -. DR HOVERGEN; HBG003986; -. DR InParanoid; Q3TXQ6; -. DR KO; K03781; -. DR OMA; LYTQINA; -. DR OrthoDB; EOG7V7660; -. DR TreeFam; TF300540; -. DR ChiTaRS; CAT; mouse. DR NextBio; 281024; -. DR PRO; PR:P24270; -. DR ArrayExpress; P24270; -. DR Bgee; P24270; -. DR CleanEx; MM_CAT; -. DR Genevestigator; P24270; -. DR GO; GO:0005829; C:cytosol; IEA:Ensembl. DR GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl. DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl. DR GO; GO:0005764; C:lysosome; IEA:Ensembl. DR GO; GO:0005758; C:mitochondrial intermembrane space; IEA:Ensembl. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR GO; GO:0005778; C:peroxisomal membrane; IDA:MGI. DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl. DR GO; GO:0004046; F:aminoacylase activity; IMP:MGI. DR GO; GO:0004096; F:catalase activity; IDA:MGI. DR GO; GO:0020037; F:heme binding; IEA:Ensembl. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0050661; F:NADP binding; IEA:Ensembl. DR GO; GO:0009060; P:aerobic respiration; IMP:MGI. DR GO; GO:0071363; P:cellular response to growth factor stimulus; IEA:Ensembl. DR GO; GO:0008203; P:cholesterol metabolic process; IMP:MGI. DR GO; GO:0020027; P:hemoglobin metabolic process; IMP:MGI. DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IDA:MGI. DR GO; GO:0001822; P:kidney development; IEA:Ensembl. DR GO; GO:0042697; P:menopause; IEA:Ensembl. DR GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl. DR GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; IDA:MGI. DR GO; GO:0051781; P:positive regulation of cell division; IEA:UniProtKB-KW. DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IDA:MGI. DR GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IDA:MGI. DR GO; GO:0051289; P:protein homotetramerization; IEA:Ensembl. DR GO; GO:0055093; P:response to hyperoxia; IEA:Ensembl. DR GO; GO:0001666; P:response to hypoxia; IEA:Ensembl. DR GO; GO:0033197; P:response to vitamin E; IEA:Ensembl. DR GO; GO:0006641; P:triglyceride metabolic process; IMP:MGI. DR GO; GO:0001657; P:ureteric bud development; IEA:Ensembl. DR GO; GO:0009650; P:UV protection; IEA:Ensembl. DR Gene3D; 2.40.180.10; -; 1. DR InterPro; IPR018028; Catalase. DR InterPro; IPR020835; Catalase-like_dom. DR InterPro; IPR024708; Catalase_AS. DR InterPro; IPR024711; Catalase_clade1/3. DR InterPro; IPR011614; Catalase_core. DR InterPro; IPR002226; Catalase_haem_BS. DR InterPro; IPR010582; Catalase_immune_responsive. DR PANTHER; PTHR11465; PTHR11465; 1. DR Pfam; PF00199; Catalase; 1. DR Pfam; PF06628; Catalase-rel; 1. DR PIRSF; PIRSF038928; Catalase_clade1-3; 1. DR PRINTS; PR00067; CATALASE. DR SMART; SM01060; Catalase; 1. DR SUPFAM; SSF56634; SSF56634; 1. DR PROSITE; PS00437; CATALASE_1; 1. DR PROSITE; PS00438; CATALASE_2; 1. DR PROSITE; PS51402; CATALASE_3; 1. PE 1: Evidence at protein level; KW Acetylation; Complete proteome; Direct protein sequencing; Heme; KW Hydrogen peroxide; Iron; Metal-binding; Mitogen; NADP; Oxidoreductase; KW Peroxidase; Peroxisome; Phosphoprotein; Reference proteome. FT INIT_MET 1 1 Removed. FT CHAIN 2 527 Catalase. FT /FTId=PRO_0000084902. FT ACT_SITE 75 75 By similarity. FT ACT_SITE 148 148 By similarity. FT METAL 358 358 Iron (heme axial ligand) (By similarity). FT MOD_RES 2 2 N-acetylserine. FT MOD_RES 13 13 N6-succinyllysine. FT MOD_RES 221 221 N6-succinyllysine. FT MOD_RES 233 233 N6-acetyllysine. FT MOD_RES 306 306 N6-acetyllysine; alternate. FT MOD_RES 306 306 N6-succinyllysine; alternate. FT MOD_RES 417 417 Phosphoserine. FT MOD_RES 430 430 N6-acetyllysine; alternate. FT MOD_RES 430 430 N6-succinyllysine; alternate. FT MOD_RES 434 434 Phosphoserine. FT MOD_RES 449 449 N6-acetyllysine; alternate. FT MOD_RES 449 449 N6-succinyllysine; alternate. FT MOD_RES 480 480 N6-acetyllysine; alternate. FT MOD_RES 480 480 N6-succinyllysine; alternate. FT MOD_RES 499 499 N6-acetyllysine. FT MOD_RES 522 522 N6-succinyllysine. FT MUTAGEN 11 11 Q->H: Acatalasemia. FT CONFLICT 97 97 A -> G (in Ref. 3; AAA66054). FT CONFLICT 117 117 T -> A (in Ref. 1; AAA37373, 2; CAA36342, FT 3; AAA66054 and 4; AAH13447). FT CONFLICT 316 316 L -> V (in Ref. 3; AAA66054). FT CONFLICT 350 350 M -> K (in Ref. 3; AAA66054). SQ SEQUENCE 527 AA; 59795 MW; 4D86F3C9D1A3DF9E CRC64; MSDSRDPASD QMKQWKEQRA SQRPDVLTTG GGNPIGDKLN IMTAGSRGPL LVQDVVFTDE MAHFDRERIP ERVVHAKGAG AFGYFEVTHD ITRYSKAKVF EHIGKRTPIA VRFSTVTGES GSADTVRDPR GFAVKFYTED GNWDLVGNNT PIFFIRDAIL FPSFIHSQKR NPQTHLKDPD MVWDFWSLRP ESLHQVSFLF SDRGIPDGHR HMNGYGSHTF KLVNADGEAV YCKFHYKTDQ GIKNLPVGEA GRLAQEDPDY GLRDLFNAIA NGNYPSWTFY IQVMTFKEAE TFPFNPFDLT KVWPHKDYPL IPVGKLVLNK NPVNYFAEVE QMAFDPSNMP PGIEPSPDKM LQGRLFAYPD THRHRLGPNY LQIPVNCPYR ARVANYQRDG PMCMHDNQGG APNYYPNSFS APEQQRSALE HSVQCAVDVK RFNSANEDNV TQVRTFYTKV LNEEERKRLC ENIAGHLKDA QLFIQKKAVK NFTDVHPDYG ARIQALLDKY NAEKPKNAIH TYTQAGSHMA AKGKANL // ID CBR1_MOUSE Reviewed; 277 AA. AC P48758; Q91X28; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 17-APR-2007, sequence version 3. DT 19-FEB-2014, entry version 107. DE RecName: Full=Carbonyl reductase [NADPH] 1; DE EC=1.1.1.184; DE AltName: Full=15-hydroxyprostaglandin dehydrogenase [NADP(+)]; DE EC=1.1.1.197; DE AltName: Full=NADPH-dependent carbonyl reductase 1; DE AltName: Full=Prostaglandin 9-ketoreductase; DE AltName: Full=Prostaglandin-E(2) 9-reductase; DE EC=1.1.1.189; GN Name=Cbr1; Synonyms=Cbr; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=CBA/CJ; TISSUE=Cerebellum; RX PubMed=8661038; DOI=10.1006/geno.1996.0255; RA Wei J., Dlouhy S.R., Hara A., Ghetti B., Hodes M.E.; RT "Cloning a cDNA for carbonyl reductase (Cbr) from mouse cerebellum: RT murine genes that express cbr map to chromosomes 16 and 11."; RL Genomics 34:147-148(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Colon; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP PROTEIN SEQUENCE OF 59-71; 80-96 AND 221-232, AND MASS SPECTROMETRY. RC STRAIN=OF1; TISSUE=Hippocampus; RA Lubec G., Klug S., Sunyer B., Chen W.-Q.; RL Submitted (JAN-2009) to UniProtKB. CC -!- FUNCTION: NADPH-dependent reductase with broad substrate CC specificity. Catalyzes the reduction of a wide variety of carbonyl CC compounds including quinones, prostaglandins, menadione, plus CC various xenobiotics. Catalyzes the reduction of the antitumor CC anthracyclines doxorubicin and daunorubicin to the cardiotoxic CC compounds doxorubicinol and daunorubicinol. Can convert CC prostaglandin E2 to prostaglandin F2-alpha. Can bind glutathione, CC which explains its higher affinity for glutathione-conjugated CC substrates. Catalyzes the reduction of S-nitrosoglutathione (By CC similarity). CC -!- CATALYTIC ACTIVITY: R-CHOH-R' + NADP(+) = R-CO-R' + NADPH. CC -!- CATALYTIC ACTIVITY: (5Z,13E)-(15S)-9-alpha,11-alpha,15- CC trihydroxyprosta-5,13-dienoate + NADP(+) = (5Z,13E)-(15S)-11- CC alpha,15-dihydroxy-9-oxoprosta-5,13-dienoate + NADPH. CC -!- CATALYTIC ACTIVITY: (13E)-(15S)-11-alpha,15-dihydroxy-9-oxoprost- CC 13-enoate + NADP(+) = (13E)-11-alpha-hydroxy-9,15-dioxoprost-13- CC enoate + NADPH. CC -!- SUBUNIT: Monomer (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases CC (SDR) family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U31966; AAB19006.1; -; mRNA. DR EMBL; BC012714; AAH12714.1; -; mRNA. DR RefSeq; NP_031646.2; NM_007620.2. DR UniGene; Mm.26940; -. DR ProteinModelPortal; P48758; -. DR SMR; P48758; 7-277. DR BioGrid; 198531; 1. DR IntAct; P48758; 4. DR MINT; MINT-1869255; -. DR PhosphoSite; P48758; -. DR REPRODUCTION-2DPAGE; P48758; -. DR PaxDb; P48758; -. DR PRIDE; P48758; -. DR Ensembl; ENSMUST00000039659; ENSMUSP00000049394; ENSMUSG00000051483. DR GeneID; 12408; -. DR KEGG; mmu:12408; -. DR UCSC; uc007zzr.1; mouse. DR CTD; 873; -. DR MGI; MGI:88284; Cbr1. DR eggNOG; COG1028; -. DR GeneTree; ENSGT00510000046499; -. DR HOVERGEN; HBG001909; -. DR InParanoid; P48758; -. DR KO; K00079; -. DR OMA; VIGVIRV; -. DR OrthoDB; EOG7PGDR4; -. DR TreeFam; TF329359; -. DR SABIO-RK; P48758; -. DR NextBio; 281186; -. DR PRO; PR:P48758; -. DR ArrayExpress; P48758; -. DR Bgee; P48758; -. DR CleanEx; MM_CBR1; -. DR Genevestigator; P48758; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0047021; F:15-hydroxyprostaglandin dehydrogenase (NADP+) activity; IEA:UniProtKB-EC. DR GO; GO:0004090; F:carbonyl reductase (NADPH) activity; ISS:UniProtKB. DR GO; GO:0050221; F:prostaglandin-E2 9-reductase activity; IEA:UniProtKB-EC. DR GO; GO:0017144; P:drug metabolic process; ISS:UniProtKB. DR GO; GO:0042373; P:vitamin K metabolic process; ISS:UniProtKB. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR002198; DH_sc/Rdtase_SDR. DR InterPro; IPR002347; Glc/ribitol_DH. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR020904; Sc_DH/Rdtase_CS. DR Pfam; PF00106; adh_short; 1. DR PRINTS; PR00081; GDHRDH. DR PRINTS; PR00080; SDRFAMILY. DR PROSITE; PS00061; ADH_SHORT; 1. PE 1: Evidence at protein level; KW Acetylation; Complete proteome; Cytoplasm; Direct protein sequencing; KW NADP; Oxidoreductase; Reference proteome. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 277 Carbonyl reductase [NADPH] 1. FT /FTId=PRO_0000054603. FT NP_BIND 10 34 NADP (By similarity). FT NP_BIND 63 64 NADP (By similarity). FT NP_BIND 194 198 NADP (By similarity). FT NP_BIND 231 233 NADP (By similarity). FT REGION 95 97 Glutathione binding (By similarity). FT REGION 193 194 Glutathione binding (By similarity). FT ACT_SITE 194 194 Proton acceptor (By similarity). FT BINDING 90 90 NADP; via carbonyl oxygen (By FT similarity). FT BINDING 106 106 Glutathione (By similarity). FT BINDING 140 140 Substrate (By similarity). FT MOD_RES 2 2 N-acetylserine (By similarity). FT CONFLICT 90 90 N -> K (in Ref. 1; AAB19006). FT CONFLICT 112 112 K -> E (in Ref. 1; AAB19006). FT CONFLICT 218 218 G -> E (in Ref. 1; AAB19006). SQ SEQUENCE 277 AA; 30641 MW; 6053423B6D5F82B7 CRC64; MSSSRPVALV TGANKGIGFA ITRDLCRKFS GDVVLAARDE ERGQTAVQKL QAEGLSPRFH QLDIDNPQSI RALRDFLLKE YGGLDVLVNN AGIAFKVNDD TPFHIQAEVT MKTNFFGTRD VCKELLPLIK PQGRVVNVSS MVSLRALKNC RLELQQKFRS ETITEEELVG LMNKFVEDTK KGVHAEEGWP NSAYGVTKIG VTVLSRILAR KLNEQRRGDK ILLNACCPGW VRTDMAGPKA TKSPEEGAET PVYLALLPPD AEGPHGQFVQ DKKVEPW // ID CBR2_MOUSE Reviewed; 244 AA. AC P08074; DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1988, sequence version 1. DT 19-FEB-2014, entry version 124. DE RecName: Full=Carbonyl reductase [NADPH] 2; DE EC=1.1.1.184; DE AltName: Full=Adipocyte protein P27; DE Short=AP27; DE AltName: Full=Lung carbonyl reductase; DE Short=LCR; DE AltName: Full=NADPH-dependent carbonyl reductase 2; GN Name=Cbr2; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=CH3; RX PubMed=2455724; DOI=10.1083/jcb.107.1.279; RA Navre M., Ringold G.M.; RT "A growth factor-repressible gene associated with protein kinase C- RT mediated inhibition of adipocyte differentiation."; RL J. Cell Biol. 107:279-286(1988). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND FUNCTION. RX PubMed=7705352; DOI=10.1111/j.1432-1033.1995.tb20274.x; RA Nakanishi M., Deyashiki Y., Ohshima K., Hara A.; RT "Cloning, expression and tissue distribution of mouse tetrameric RT carbonyl reductase. Identity with an adipocyte 27-kDa protein."; RL Eur. J. Biochem. 228:381-387(1995). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Colon; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP SUBCELLULAR LOCATION. RX PubMed=8040004; DOI=10.1007/BF00157764; RA Matsuura K., Bunai Y., Ohya I., Hara A., Nakanishi M., Sawada H.; RT "Ultrastructural localization of carbonyl reductase in mouse lung."; RL Histochem. J. 26:311-316(1994). RN [5] RP MUTAGENESIS OF THR-38, AND COENZYME SPECIFICITY. RX PubMed=8999926; DOI=10.1074/jbc.272.4.2218; RA Nakanishi M., Matsuura K., Kaibe H., Tanaka N., Nonaka T., Mitsui Y., RA Hara A.; RT "Switch of coenzyme specificity of mouse lung carbonyl reductase by RT substitution of threonine 38 with aspartic acid."; RL J. Biol. Chem. 272:2218-2222(1997). RN [6] RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH NADPH. RX PubMed=8805511; DOI=10.1016/S0969-2126(96)00007-X; RA Tanaka N., Nonaka T., Nakanishi M., Deyashiki Y., Hara A., Mitsui Y.; RT "Crystal structure of the ternary complex of mouse lung carbonyl RT reductase at 1.8-A resolution: the structural origin of coenzyme RT specificity in the short-chain dehydrogenase/reductase family."; RL Structure 4:33-45(1996). CC -!- FUNCTION: May function in the pulmonary metabolism of endogenous CC carbonyl compounds, such as aliphatic aldehydes and ketones CC derived from lipid peroxidation, 3-ketosteroids and fatty CC aldehydes, as well as in xenobiotic metabolism. CC -!- CATALYTIC ACTIVITY: R-CHOH-R' + NADP(+) = R-CO-R' + NADPH. CC -!- SUBUNIT: Homotetramer. CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix. CC -!- TISSUE SPECIFICITY: Lung (ciliated cells, non-ciliated bronchiolar CC cells and type-II alveolar pneumocytes). Low expression in adipose CC tissue > testis = heart > kidney = spleen > brain = liver. CC -!- INDUCTION: By glucocorticoids. Activated by fatty acids. CC -!- MISCELLANEOUS: Uses both NADP and NAD as substrates. Has a strong CC preference for NADP. CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases CC (SDR) family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; D26123; BAA05120.1; -; mRNA. DR EMBL; X07411; CAA30309.1; -; mRNA. DR EMBL; BC010758; AAH10758.1; -; mRNA. DR PIR; S03382; A28053. DR RefSeq; NP_031647.1; NM_007621.2. DR UniGene; Mm.21454; -. DR PDB; 1CYD; X-ray; 1.80 A; A/B/C/D=1-244. DR PDBsum; 1CYD; -. DR ProteinModelPortal; P08074; -. DR SMR; P08074; 3-244. DR IntAct; P08074; 1. DR MINT; MINT-4090057; -. DR PhosphoSite; P08074; -. DR PaxDb; P08074; -. DR PRIDE; P08074; -. DR Ensembl; ENSMUST00000026148; ENSMUSP00000026148; ENSMUSG00000025150. DR GeneID; 12409; -. DR KEGG; mmu:12409; -. DR UCSC; uc007muj.2; mouse. DR CTD; 12409; -. DR MGI; MGI:107200; Cbr2. DR eggNOG; COG1028; -. DR HOVERGEN; HBG105069; -. DR InParanoid; P08074; -. DR KO; K00081; -. DR OMA; KGAMTML; -. DR OrthoDB; EOG74TX0K; -. DR TreeFam; TF313841; -. DR SABIO-RK; P08074; -. DR EvolutionaryTrace; P08074; -. DR NextBio; 281190; -. DR PRO; PR:P08074; -. DR ArrayExpress; P08074; -. DR Bgee; P08074; -. DR CleanEx; MM_CBR2; -. DR Genevestigator; P08074; -. DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR GO; GO:0004090; F:carbonyl reductase (NADPH) activity; IDA:MGI. DR GO; GO:0043621; F:protein self-association; IDA:MGI. DR GO; GO:0006116; P:NADH oxidation; TAS:MGI. DR GO; GO:0051262; P:protein tetramerization; IDA:MGI. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR002198; DH_sc/Rdtase_SDR. DR InterPro; IPR002347; Glc/ribitol_DH. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR020904; Sc_DH/Rdtase_CS. DR Pfam; PF00106; adh_short; 1. DR PRINTS; PR00081; GDHRDH. DR PRINTS; PR00080; SDRFAMILY. DR PROSITE; PS00061; ADH_SHORT; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Direct protein sequencing; KW Mitochondrion; NAD; NADP; Oxidoreductase; Reference proteome. FT CHAIN 1 244 Carbonyl reductase [NADPH] 2. FT /FTId=PRO_0000054547. FT NP_BIND 11 39 NADP. FT ACT_SITE 149 149 Proton acceptor. FT BINDING 136 136 Substrate. FT MUTAGEN 38 38 T->R: Converts the coenzyme specificity FT from NADP to NAD. FT STRAND 9 14 FT HELIX 18 29 FT STRAND 33 39 FT HELIX 41 50 FT STRAND 55 58 FT HELIX 64 71 FT STRAND 78 82 FT HELIX 92 94 FT HELIX 97 107 FT HELIX 109 125 FT STRAND 129 134 FT HELIX 137 139 FT HELIX 147 167 FT HELIX 168 170 FT STRAND 172 179 FT HELIX 185 190 FT HELIX 194 203 FT HELIX 212 223 FT HELIX 225 227 FT STRAND 232 238 FT HELIX 241 243 SQ SEQUENCE 244 AA; 25958 MW; 4FA14C5722DD231E CRC64; MKLNFSGLRA LVTGAGKGIG RDTVKALHAS GAKVVAVTRT NSDLVSLAKE CPGIEPVCVD LGDWDATEKA LGGIGPVDLL VNNAALVIMQ PFLEVTKEAF DRSFSVNLRS VFQVSQMVAR DMINRGVPGS IVNVSSMVAH VTFPNLITYS STKGAMTMLT KAMAMELGPH KIRVNSVNPT VVLTDMGKKV SADPEFARKL KERHPLRKFA EVEDVVNSIL FLLSDRSAST SGGGILVDAG YLAS // ID CBR3_MOUSE Reviewed; 277 AA. AC Q8K354; DT 22-FEB-2012, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2002, sequence version 1. DT 19-FEB-2014, entry version 95. DE RecName: Full=Carbonyl reductase [NADPH] 3; DE EC=1.1.1.184; DE AltName: Full=NADPH-dependent carbonyl reductase 3; GN Name=Cbr3; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Tongue; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J, Czech II, and FVB/N-3; RC TISSUE=Lung, Mammary gland, and Mammary tumor; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Has low NADPH-dependent oxidoreductase activity towards CC 4-benzoylpyridine and menadione (in vitro) (By similarity). CC -!- CATALYTIC ACTIVITY: R-CHOH-R' + NADP(+) = R-CO-R' + NADPH. CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases CC (SDR) family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK028150; BAC25778.1; -; mRNA. DR EMBL; AC154449; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH466602; EDL03763.1; -; Genomic_DNA. DR EMBL; BC028763; AAH28763.1; -; mRNA. DR EMBL; BC087735; AAH87735.1; -; mRNA. DR EMBL; BC096658; AAH96658.1; -; mRNA. DR RefSeq; NP_766635.1; NM_173047.3. DR UniGene; Mm.4512; -. DR ProteinModelPortal; Q8K354; -. DR SMR; Q8K354; 5-277. DR IntAct; Q8K354; 1. DR MINT; MINT-4117620; -. DR STRING; 10090.ENSMUSP00000047712; -. DR PhosphoSite; Q8K354; -. DR PaxDb; Q8K354; -. DR PRIDE; Q8K354; -. DR Ensembl; ENSMUST00000039620; ENSMUSP00000047712; ENSMUSG00000022947. DR GeneID; 109857; -. DR KEGG; mmu:109857; -. DR UCSC; uc007zzs.2; mouse. DR CTD; 874; -. DR MGI; MGI:1309992; Cbr3. DR eggNOG; COG1028; -. DR GeneTree; ENSGT00510000046499; -. DR HOVERGEN; HBG001909; -. DR InParanoid; Q8K354; -. DR KO; K00084; -. DR OMA; TEPHGQL; -. DR OrthoDB; EOG7PGDR4; -. DR TreeFam; TF329359; -. DR NextBio; 362899; -. DR PRO; PR:Q8K354; -. DR Bgee; Q8K354; -. DR Genevestigator; Q8K354; -. DR GO; GO:0005829; C:cytosol; IEA:Ensembl. DR GO; GO:0005634; C:nucleus; IEA:Ensembl. DR GO; GO:0000253; F:3-keto sterol reductase activity; IEA:Ensembl. DR GO; GO:0004090; F:carbonyl reductase (NADPH) activity; IEA:UniProtKB-EC. DR GO; GO:0070402; F:NADPH binding; IEA:Ensembl. DR GO; GO:0042376; P:phylloquinone catabolic process; IEA:Ensembl. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR002198; DH_sc/Rdtase_SDR. DR InterPro; IPR002347; Glc/ribitol_DH. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR020904; Sc_DH/Rdtase_CS. DR Pfam; PF00106; adh_short; 1. DR PRINTS; PR00081; GDHRDH. DR PRINTS; PR00080; SDRFAMILY. DR PROSITE; PS00061; ADH_SHORT; 1. PE 2: Evidence at transcript level; KW Complete proteome; Cytoplasm; NADP; Oxidoreductase; KW Reference proteome. FT CHAIN 1 277 Carbonyl reductase [NADPH] 3. FT /FTId=PRO_0000415806. FT NP_BIND 10 34 NADP (By similarity). FT NP_BIND 38 42 NADP (By similarity). FT NP_BIND 63 64 NADP (By similarity). FT NP_BIND 194 198 NADP (By similarity). FT ACT_SITE 194 194 Proton acceptor (By similarity). FT BINDING 90 90 NADP; via carbonyl oxygen (By FT similarity). FT BINDING 140 140 Substrate (By similarity). SQ SEQUENCE 277 AA; 30953 MW; EC6009AB9C83FACF CRC64; MSSCSRVALV TGANKGIGFA ITRDLCRKFS GDVVLTARDE ARGRAAVQQL QAEGLSPRFH QLDIDDPQSI RALRDFLRKE YGGLNVLVNN AGIAFRMDDP TPFDIQAEVT LKTNFFATRN VCTELLPIMK PHGRVVNISS LQGLKALENC REDLQEKFRC DTLTEVDLVD LMKKFVEDTK NEVHEREGWP DSAYGVSKLG VTVLTRILAR QLDEKRKADR ILLNACCPGW VKTDMARDQG SRTVEEGAET PVYLALLPPD ATEPHGQLVR DKVVQTW // ID CBR4_MOUSE Reviewed; 236 AA. AC Q91VT4; Q3UBY4; Q8BXV1; DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 26-FEB-2008, sequence version 2. DT 19-MAR-2014, entry version 89. DE RecName: Full=Carbonyl reductase family member 4; DE EC=1.-.-.-; DE AltName: Full=3-oxoacyl-[acyl-carrier-protein] reductase; DE EC=1.1.1.-; DE AltName: Full=Quinone reductase CBR4; GN Name=Cbr4; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Bone marrow macrophage, and Cerebellum; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=129; TISSUE=Mammary tumor; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-40; LYS-96 AND LYS-194, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23576753; DOI=10.1073/pnas.1302961110; RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., RA Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.; RT "Label-free quantitative proteomics of the lysine acetylome in RT mitochondria identifies substrates of SIRT3 in metabolic pathways."; RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013). CC -!- FUNCTION: The heteroteramer with HSD17B8 has NADH-dependent 3- CC ketoacyl-acyl carrier protein reductase activity. May play a role CC in biosynthesis of fatty acids in mitochondria. The homotetramer CC may act as NADPH-dependent quinone reductase. Has broad substrate CC specificity and reduces 9,10-phenanthrenequinone, 1,4-benzoquinone CC and various other o-quinones and p-quinones (in vitro) (By CC similarity). CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis. CC -!- SUBUNIT: Homotetramer. Heterotetramer with HSD17B8; contains two CC molecules of HSD17B8 and CBR4 (By similarity). CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix (By similarity). CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases CC (SDR) family. CC -!- SEQUENCE CAUTION: CC Sequence=BAC31519.1; Type=Erroneous initiation; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK043313; BAC31519.1; ALT_INIT; mRNA. DR EMBL; AK150763; BAE29830.1; -; mRNA. DR EMBL; BC009118; AAH09118.1; -; mRNA. DR RefSeq; NP_663570.2; NM_145595.2. DR UniGene; Mm.29059; -. DR ProteinModelPortal; Q91VT4; -. DR SMR; Q91VT4; 2-231. DR IntAct; Q91VT4; 2. DR MINT; MINT-4121071; -. DR PaxDb; Q91VT4; -. DR PRIDE; Q91VT4; -. DR DNASU; 234309; -. DR Ensembl; ENSMUST00000034058; ENSMUSP00000034058; ENSMUSG00000031641. DR GeneID; 234309; -. DR KEGG; mmu:234309; -. DR UCSC; uc009lub.2; mouse. DR CTD; 84869; -. DR MGI; MGI:2384567; Cbr4. DR eggNOG; COG1028; -. DR GeneTree; ENSGT00710000106273; -. DR HOVERGEN; HBG002145; -. DR InParanoid; Q91VT4; -. DR KO; K11539; -. DR OMA; KEMANVD; -. DR OrthoDB; EOG70KGQM; -. DR TreeFam; TF354265; -. DR UniPathway; UPA00094; -. DR NextBio; 382085; -. DR PRO; PR:Q91VT4; -. DR ArrayExpress; Q91VT4; -. DR Bgee; Q91VT4; -. DR CleanEx; MM_CBR4; -. DR Genevestigator; Q91VT4; -. DR GO; GO:0005759; C:mitochondrial matrix; ISS:UniProtKB. DR GO; GO:0003955; F:NAD(P)H dehydrogenase (quinone) activity; IEA:Ensembl. DR GO; GO:0070402; F:NADPH binding; ISS:UniProtKB. DR GO; GO:0008753; F:NADPH dehydrogenase (quinone) activity; ISS:UniProtKB. DR GO; GO:0048038; F:quinone binding; ISS:UniProtKB. DR GO; GO:0044597; P:daunorubicin metabolic process; IEA:Ensembl. DR GO; GO:0044598; P:doxorubicin metabolic process; IEA:Ensembl. DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0051289; P:protein homotetramerization; IEA:Ensembl. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR002198; DH_sc/Rdtase_SDR. DR InterPro; IPR002347; Glc/ribitol_DH. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR020904; Sc_DH/Rdtase_CS. DR Pfam; PF00106; adh_short; 1. DR PRINTS; PR00081; GDHRDH. DR PRINTS; PR00080; SDRFAMILY. DR PROSITE; PS00061; ADH_SHORT; 1. PE 1: Evidence at protein level; KW Acetylation; Complete proteome; Fatty acid biosynthesis; KW Fatty acid metabolism; Lipid biosynthesis; Lipid metabolism; KW Mitochondrion; NAD; NADP; Oxidoreductase; Reference proteome. FT CHAIN 1 236 Carbonyl reductase family member 4. FT /FTId=PRO_0000319879. FT NP_BIND 7 31 NAD or NADP (By similarity). FT ACT_SITE 147 147 Proton acceptor (By similarity). FT BINDING 134 134 Substrate (By similarity). FT MOD_RES 1 1 N-acetylmethionine (By similarity). FT MOD_RES 40 40 N6-acetyllysine. FT MOD_RES 96 96 N6-acetyllysine. FT MOD_RES 194 194 N6-acetyllysine. FT CONFLICT 89 89 D -> G (in Ref. 2; AAH09118). SQ SEQUENCE 236 AA; 25415 MW; 546F400177DDC7F1 CRC64; MDKVCAVFGG SRGIGRAVAQ LMAQKGYRLA IVSRNLEVAK VTAGELGGNH LAFRCDVAKE QDVQSTFQEM EKHLGPVNFL VNAAGINRDS LLVRTKTEDM ISQLHTNLLG SMLTCKAAMK TMIQQGGSIV NVGSIIGLKG NVGQSAYSAT KGGLVGFSRS LAKEVARKKI RVNVVAPGFI RTDMTRHLKE EHFKKNIPLG RFGETLEVAH AVVFLLESPY ITGHVLIVDG GLQLTV // ID CDO1_MOUSE Reviewed; 200 AA. AC P60334; Q3UED8; DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot. DT 16-FEB-2004, sequence version 1. DT 19-MAR-2014, entry version 92. DE RecName: Full=Cysteine dioxygenase type 1; DE EC=1.13.11.20; DE AltName: Full=Cysteine dioxygenase type I; DE Short=CDO; DE Short=CDO-I; GN Name=Cdo1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY. RX PubMed=11602353; DOI=10.1016/S0378-1119(01)00691-6; RA Hirschberger L.L., Daval S., Stover P.J., Stipanuk M.H.; RT "Murine cysteine dioxygenase gene: structural organization, tissue- RT specific expression and promoter identification."; RL Gene 277:153-161(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Liver; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Liver; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) IN COMPLEX WITH NICKEL IONS, RP CROSS-LINK, AND SUBUNIT. RX PubMed=16492780; DOI=10.1073/pnas.0509262103; RA McCoy J.G., Bailey L.J., Bitto E., Bingman C.A., Aceti D.J., Fox B.G., RA Phillips G.N. Jr.; RT "Structure and mechanism of mouse cysteine dioxygenase."; RL Proc. Natl. Acad. Sci. U.S.A. 103:3084-3089(2006). CC -!- CATALYTIC ACTIVITY: L-cysteine + O(2) = 3-sulfinoalanine. CC -!- COFACTOR: Binds 1 iron ion per subunit. Nickel and zinc to a CC lesser extent. CC -!- PATHWAY: Organosulfur biosynthesis; taurine biosynthesis; CC hypotaurine from L-cysteine: step 1/2. CC -!- SUBUNIT: Monomer. CC -!- TISSUE SPECIFICITY: Highest expression in liver. Also expressed in CC kidney, lung, brain and small intestine. CC -!- PTM: The thioether cross-link between Cys-93 and Tyr-157 plays a CC structural role through stabilizing the Fe(2+) ion, and prevents CC the production of highly damaging free hydroxyl radicals by CC holding the oxygen radical via hydroxyl hydrogen. CC -!- SIMILARITY: Belongs to the cysteine dioxygenase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF355472; AAK53364.1; -; Genomic_DNA. DR EMBL; AF355469; AAK53364.1; JOINED; Genomic_DNA. DR EMBL; AF355470; AAK53364.1; JOINED; Genomic_DNA. DR EMBL; AF355471; AAK53364.1; JOINED; Genomic_DNA. DR EMBL; AK004249; BAB23236.1; -; mRNA. DR EMBL; AK149582; BAE28973.1; -; mRNA. DR EMBL; BC013638; AAH13638.1; -; mRNA. DR RefSeq; NP_149026.1; NM_033037.3. DR UniGene; Mm.241056; -. DR PDB; 2ATF; X-ray; 1.75 A; A=2-200. DR PDB; 2Q4S; X-ray; 1.75 A; A=2-200. DR PDBsum; 2ATF; -. DR PDBsum; 2Q4S; -. DR ProteinModelPortal; P60334; -. DR SMR; P60334; 5-190. DR STRING; 10090.ENSMUSP00000046517; -. DR PhosphoSite; P60334; -. DR REPRODUCTION-2DPAGE; P60334; -. DR PaxDb; P60334; -. DR PRIDE; P60334; -. DR DNASU; 12583; -. DR Ensembl; ENSMUST00000035804; ENSMUSP00000046517; ENSMUSG00000033022. DR GeneID; 12583; -. DR KEGG; mmu:12583; -. DR UCSC; uc008evt.1; mouse. DR CTD; 1036; -. DR MGI; MGI:105925; Cdo1. DR eggNOG; NOG126313; -. DR GeneTree; ENSGT00390000018226; -. DR HOGENOM; HOG000177818; -. DR HOVERGEN; HBG004469; -. DR InParanoid; P60334; -. DR KO; K00456; -. DR OMA; KMTFWSK; -. DR OrthoDB; EOG77M8PK; -. DR TreeFam; TF105636; -. DR Reactome; REACT_188576; Developmental Biology. DR UniPathway; UPA00012; UER00537. DR EvolutionaryTrace; P60334; -. DR NextBio; 281718; -. DR PRO; PR:P60334; -. DR Bgee; P60334; -. DR CleanEx; MM_CDO1; -. DR Genevestigator; P60334; -. DR GO; GO:0005829; C:cytosol; IDA:MGI. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0017172; F:cysteine dioxygenase activity; TAS:MGI. DR GO; GO:0008198; F:ferrous iron binding; IEA:Ensembl. DR GO; GO:0019452; P:L-cysteine catabolic process to taurine; TAS:MGI. DR GO; GO:0007595; P:lactation; IEA:Ensembl. DR GO; GO:0043200; P:response to amino acid; IEA:Ensembl. DR GO; GO:0051591; P:response to cAMP; IEA:Ensembl. DR GO; GO:0045471; P:response to ethanol; IEA:Ensembl. DR GO; GO:0033762; P:response to glucagon; IEA:Ensembl. DR GO; GO:0051384; P:response to glucocorticoid; IEA:Ensembl. DR GO; GO:0042412; P:taurine biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 2.60.120.10; -; 1. DR InterPro; IPR010300; Cys_dOase_I. DR InterPro; IPR014710; RmlC-like_jellyroll. DR InterPro; IPR011051; RmlC_Cupin. DR Pfam; PF05995; CDO_I; 1. DR SUPFAM; SSF51182; SSF51182; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Dioxygenase; Iron; Metal-binding; KW Oxidoreductase; Reference proteome; Thioether bond. FT CHAIN 1 200 Cysteine dioxygenase type 1. FT /FTId=PRO_0000206607. FT METAL 86 86 Iron; catalytic. FT METAL 88 88 Iron; catalytic. FT METAL 140 140 Iron; catalytic. FT CROSSLNK 93 157 3'-(S-cysteinyl)-tyrosine (Cys-Tyr). FT HELIX 12 22 FT STRAND 24 27 FT HELIX 30 39 FT HELIX 44 47 FT HELIX 48 50 FT STRAND 55 57 FT STRAND 59 64 FT HELIX 66 68 FT STRAND 71 77 FT STRAND 92 100 FT STRAND 102 107 FT STRAND 112 114 FT STRAND 121 125 FT STRAND 130 133 FT TURN 135 137 FT STRAND 139 143 FT STRAND 151 159 FT STRAND 162 167 FT TURN 169 171 FT STRAND 174 178 FT STRAND 182 184 SQ SEQUENCE 200 AA; 23026 MW; 118F1A3326B340F9 CRC64; MERTELLKPR TLADLIRILH ELFAGDEVNV EEVQAVLEAY ESNPAEWALY AKFDQYRYTR NLVDQGNGKF NLMILCWGEG HGSSIHDHTD SHCFLKLLQG NLKETLFDWP DKKSNEMIKK SERTLRENQC AYINDSIGLH RVENVSHTEP AVSLHLYSPP FDTCHAFDQR TGHKNKVTMT FHSKFGIRTP FTTSGSLENN // ID CERU_MOUSE Reviewed; 1061 AA. AC Q61147; Q6P5C8; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 04-DEC-2007, sequence version 2. DT 19-MAR-2014, entry version 110. DE RecName: Full=Ceruloplasmin; DE EC=1.16.3.1; DE AltName: Full=Ferroxidase; DE Flags: Precursor; GN Name=Cp; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY. RX PubMed=8690795; DOI=10.1172/JCI118768; RA Klomp L.W.J., Farhangrazi Z.S., Dugan L.L., Gitlin J.D.; RT "Ceruloplasmin gene expression in the murine central nervous system."; RL J. Clin. Invest. 98:207-215(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6; TISSUE=Eye; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-138 AND ASN-757. RC STRAIN=C57BL/6; TISSUE=Plasma; RX PubMed=16944957; DOI=10.1021/pr060186m; RA Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J., RA Gevaert K.; RT "Proteome-wide characterization of N-glycosylation events by diagonal RT chromatography."; RL J. Proteome Res. 5:2438-2447(2006). RN [4] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-138 AND ASN-757. RC STRAIN=C57BL/6; TISSUE=Plasma; RX PubMed=17330941; DOI=10.1021/pr0604559; RA Bernhard O.K., Kapp E.A., Simpson R.J.; RT "Enhanced analysis of the mouse plasma proteome using cysteine- RT containing tryptic glycopeptides."; RL J. Proteome Res. 6:987-995(2007). CC -!- FUNCTION: Ceruloplasmin is a blue, copper-binding (6-7 atoms per CC molecule) glycoprotein. It has ferroxidase activity oxidizing CC Fe(2+) to Fe(3+) without releasing radical oxygen species. It is CC involved in iron transport across the cell membrane. Provides CC Cu(2+) ions for the ascorbate-mediated deaminase degradation of CC the heparan sulfate chains of GPC1. May also play a role in fetal CC lung development or pulmonary antioxidant defense (By similarity). CC -!- CATALYTIC ACTIVITY: 4 Fe(2+) + 4 H(+) + O(2) = 4 Fe(3+) + 2 H(2)O. CC -!- COFACTOR: Binds 6 copper ions per monomer (By similarity). CC -!- SUBCELLULAR LOCATION: Secreted. Note=Colocalizes with GCP1 in CC secretory intracellular compartments (By similarity). CC -!- TISSUE SPECIFICITY: Expressed in many tissues, including liver, CC eye and brain. CC -!- SIMILARITY: Belongs to the multicopper oxidase family. CC -!- SIMILARITY: Contains 3 F5/8 type A domains. CC -!- SIMILARITY: Contains 6 plastocyanin-like domains. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U49430; AAB07996.1; -; mRNA. DR EMBL; BC062957; AAH62957.1; -; mRNA. DR RefSeq; NP_001263177.1; NM_001276248.1. DR RefSeq; NP_031778.2; NM_007752.3. DR UniGene; Mm.13787; -. DR ProteinModelPortal; Q61147; -. DR IntAct; Q61147; 6. DR MINT; MINT-4090622; -. DR PhosphoSite; Q61147; -. DR PaxDb; Q61147; -. DR PRIDE; Q61147; -. DR Ensembl; ENSMUST00000091309; ENSMUSP00000088857; ENSMUSG00000003617. DR GeneID; 12870; -. DR KEGG; mmu:12870; -. DR UCSC; uc008orz.1; mouse. DR CTD; 1356; -. DR MGI; MGI:88476; Cp. DR eggNOG; NOG276067; -. DR GeneTree; ENSGT00550000074552; -. DR HOGENOM; HOG000231499; -. DR HOVERGEN; HBG003674; -. DR KO; K13624; -. DR OrthoDB; EOG7V49XN; -. DR TreeFam; TF329807; -. DR ChiTaRS; CP; mouse. DR NextBio; 282456; -. DR PRO; PR:Q61147; -. DR ArrayExpress; Q61147; -. DR Bgee; Q61147; -. DR CleanEx; MM_CP; -. DR Genevestigator; Q61147; -. DR GO; GO:0005615; C:extracellular space; IDA:MGI. DR GO; GO:0005507; F:copper ion binding; IDA:MGI. DR GO; GO:0004322; F:ferroxidase activity; IDA:MGI. DR GO; GO:0006879; P:cellular iron ion homeostasis; IEA:InterPro. DR GO; GO:0006825; P:copper ion transport; IEA:UniProtKB-KW. DR Gene3D; 2.60.40.420; -; 6. DR InterPro; IPR027150; CP. DR InterPro; IPR001117; Cu-oxidase. DR InterPro; IPR011706; Cu-oxidase_2. DR InterPro; IPR011707; Cu-oxidase_3. DR InterPro; IPR002355; Cu_oxidase_Cu_BS. DR InterPro; IPR008972; Cupredoxin. DR PANTHER; PTHR10127:SF89; PTHR10127:SF89; 1. DR Pfam; PF00394; Cu-oxidase; 1. DR Pfam; PF07731; Cu-oxidase_2; 1. DR Pfam; PF07732; Cu-oxidase_3; 3. DR SUPFAM; SSF49503; SSF49503; 6. DR PROSITE; PS00079; MULTICOPPER_OXIDASE1; 3. DR PROSITE; PS00080; MULTICOPPER_OXIDASE2; 1. PE 1: Evidence at protein level; KW Complete proteome; Copper; Copper transport; Disulfide bond; KW Glycoprotein; Ion transport; Metal-binding; Oxidoreductase; KW Reference proteome; Repeat; Secreted; Signal; Transport. FT SIGNAL 1 19 By similarity. FT CHAIN 20 1061 Ceruloplasmin. FT /FTId=PRO_0000002913. FT DOMAIN 20 356 F5/8 type A 1. FT DOMAIN 20 199 Plastocyanin-like 1. FT DOMAIN 208 356 Plastocyanin-like 2. FT DOMAIN 369 713 F5/8 type A 2. FT DOMAIN 369 555 Plastocyanin-like 3. FT DOMAIN 565 713 Plastocyanin-like 4. FT DOMAIN 725 1056 F5/8 type A 3. FT DOMAIN 725 895 Plastocyanin-like 5. FT DOMAIN 903 1056 Plastocyanin-like 6. FT METAL 120 120 Copper 1; type 2 (By similarity). FT METAL 122 122 Copper 2; type 3 (By similarity). FT METAL 179 179 Copper 2; type 3 (By similarity). FT METAL 181 181 Copper 3; type 3 (By similarity). FT METAL 294 294 Copper 4; type 1 (By similarity). FT METAL 337 337 Copper 4; type 1 (By similarity). FT METAL 342 342 Copper 4; type 1 (By similarity). FT METAL 651 651 Copper 5; type 1 (By similarity). FT METAL 694 694 Copper 5; type 1 (By similarity). FT METAL 699 699 Copper 5; type 1 (By similarity). FT METAL 704 704 Copper 5; type 1 (By similarity). FT METAL 989 989 Copper 6; type 1 (By similarity). FT METAL 992 992 Copper 1; type 2 (By similarity). FT METAL 994 994 Copper 3; type 3 (By similarity). FT METAL 1034 1034 Copper 3; type 3 (By similarity). FT METAL 1035 1035 Copper 6; type 1 (By similarity). FT METAL 1036 1036 Copper 2; type 3 (By similarity). FT METAL 1040 1040 Copper 6; type 1 (By similarity). FT METAL 1045 1045 Copper 6; type 1 (By similarity). FT CARBOHYD 138 138 N-linked (GlcNAc...). FT CARBOHYD 226 226 N-linked (GlcNAc...) (Potential). FT CARBOHYD 396 396 N-linked (GlcNAc...) (Potential). FT CARBOHYD 583 583 N-linked (GlcNAc...) (Potential). FT CARBOHYD 757 757 N-linked (GlcNAc...). FT CARBOHYD 921 921 N-linked (GlcNAc...) (Potential). FT DISULFID 173 199 By similarity. FT DISULFID 275 356 By similarity. FT DISULFID 529 555 By similarity. FT DISULFID 632 713 By similarity. FT DISULFID 869 895 By similarity. FT CONFLICT 354 354 R -> Q (in Ref. 1; AAB07996). FT CONFLICT 361 362 PE -> SK (in Ref. 1; AAB07996). FT CONFLICT 366 368 QDR -> RGK (in Ref. 1; AAB07996). FT CONFLICT 389 389 T -> I (in Ref. 1; AAB07996). FT CONFLICT 394 396 GEN -> EEK (in Ref. 1; AAB07996). FT CONFLICT 400 401 LE -> SG (in Ref. 1; AAB07996). FT CONFLICT 405 405 R -> G (in Ref. 1; AAB07996). FT CONFLICT 437 437 Q -> E (in Ref. 1; AAB07996). FT CONFLICT 471 471 P -> H (in Ref. 1; AAB07996). FT CONFLICT 495 495 R -> A (in Ref. 1; AAB07996). FT CONFLICT 537 537 G -> A (in Ref. 1; AAB07996). FT CONFLICT 597 597 T -> H (in Ref. 1; AAB07996). FT CONFLICT 627 630 PGLN -> SWPH (in Ref. 1; AAB07996). FT CONFLICT 662 662 S -> C (in Ref. 1; AAB07996). FT CONFLICT 666 666 R -> E (in Ref. 1; AAB07996). FT CONFLICT 732 732 A -> D (in Ref. 1; AAB07996). FT CONFLICT 796 796 E -> EE (in Ref. 1; AAB07996). FT CONFLICT 850 850 R -> A (in Ref. 1; AAB07996). FT CONFLICT 979 979 V -> L (in Ref. 1; AAB07996). SQ SEQUENCE 1061 AA; 121151 MW; 16A2DAEA4F483886 CRC64; MKFLLLSTFI FLYSSLALAR DKHYFIGITE AVWDYASGTE EKKLISVDTE QSNFYLQNGP DRIGRKYKKA LYFEYTDGTF SKTIDKPAWL GFLGPVIKAE VEDKVYVHLK NLASRIYTFH AHGVTYTKEY EGAVYPDNTT DFQRADDKVL PGQQYVYVLH ANEPSPGEGD SNCVTRIYHS HVDAPKDIAS GLIGPLILCK KGSLYKEKEK NIDQEFVLMF SVVDENLSWY LEDNIKTFCS EPEKVDKDNE DFQESNRMYS INGYTFGSLP GLSMCAADRV KWYLFGMGNE VDVHSAFFHG QALTSRNYQT DIINLFPATL IDAYMVAQNP GVWMLSCQNL NHLKAGLQAF FQVRDCNKPS PEDNIQDRHV RHYYIAAEEV IWNYAPSGTD IFTGENLTAL ESDSRVFFEQ GATRIGGSYK KMAYREYTDG SFTNRKQRGP DEEHLGILGP VIWAEVGDTI KVTFHNKGQH PLSIQPMGVS FTAENEGTYY GPPGRSSQQA ASHVAPKETF TYEWTVPKEM GPTYADPVCL SKMYYSGVDP TKDIFTGLIG PMKICKKGSL LADGRQKDVD KEFYLFPTVF DENESLLLDD NIRMFTTAPD QVDKEDEDFQ ESNKMHSMNG FMYGNQPGLN MCLGESIVWY LFSAGNEADV HGIYFSGNTY LSKGERRDTA NLFPHKSLTL LMNPDTKGTF DVECLTTDHY TGGMKQKYTV NQCQRQFEDF TVYLGERTYY VAAVEVEWDY SPSRAWEKEL HHLQEQNVSN VFLDKEEFFI GSKYKKVVYR QFTDSSFREQ VKRRAEDEHL GILGPPIHAN VGDKVKVVFK NMATRPYSIH AHGVKTESST VVPTLPGEVR TYTWQIPERS GAGREDSACI PWAYYSTVDR VKDLYSGLIG PLIVCRKSYV KVFSPKKKME FFLLFLVFDE NESWYLDDNI KTYSEHPEKV NKDNEEFLES NKMHAINGKM FGNLQGLTMH VKDEVNWYVM GMGNEIDLHT VHFHGHSFQY KHRGVYSSDV FDLFPGTYQT LEMFPQTPGT WLLHCHVTDH VHAGMATTYT VLPVEQETKS G // ID CH25H_MOUSE Reviewed; 298 AA. AC Q9Z0F5; Q3TUM6; Q8CHQ2; DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1999, sequence version 1. DT 19-FEB-2014, entry version 89. DE RecName: Full=Cholesterol 25-hydroxylase; DE EC=1.14.99.38; DE AltName: Full=Cholesterol 25-monooxygenase; DE Short=m25OH; GN Name=Ch25h; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, ENZYME ACTIVITY, RP COFACTOR, SUBCELLULAR LOCATION, GLYCOSYLATION, TISSUE SPECIFICITY, AND RP MUTAGENESIS OF 242-HIS-HIS-243. RC STRAIN=129/SvEv, and C57BL/6; RX PubMed=9852097; DOI=10.1074/jbc.273.51.34316; RA Lund E.G., Kerr T.A., Sakai J., Li W.-P., Russell D.W.; RT "cDNA cloning of mouse and human cholesterol 25-hydroxylases, RT polytopic membrane proteins that synthesize a potent oxysterol RT regulator of lipid metabolism."; RL J. Biol. Chem. 273:34316-34327(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Adipose tissue, and Bone marrow; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Mammary tumor; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP DISRUPTION PHENOTYPE. RX PubMed=12543708; DOI=10.1146/annurev.biochem.72.121801.161712; RA Russell D.W.; RT "The enzymes, regulation, and genetics of bile acid synthesis."; RL Annu. Rev. Biochem. 72:137-174(2003). CC -!- FUNCTION: Catalyzes the formation of 25-hydroxycholesterol from CC cholesterol, leading to repress cholesterol biosynthetic enzymes. CC May play an important role in regulating lipid metabolism by CC synthesizing a corepressor that blocks sterol regulatory element CC binding protein (SREBP) processing. In testis, production of 25- CC hydroxycholesterol by macrophages may play a role in Leydig cell CC differentiation. CC -!- CATALYTIC ACTIVITY: Cholesterol + AH(2) + O(2) = 25- CC hydroxycholesterol + A + H(2)O. CC -!- COFACTOR: Iron. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass CC membrane protein. CC -!- TISSUE SPECIFICITY: Widely expressed at low level and at higher CC level in the lung. Weakly expressed in the heart, lung and kidney. CC -!- PTM: N-glycosylated. CC -!- DISRUPTION PHENOTYPE: Mice do not display any apparent alteration CC in bile acid synthesis and cholesterol metabolism. CC -!- SIMILARITY: Belongs to the sterol desaturase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF059211; AAC97480.1; -; Genomic_DNA. DR EMBL; AF059213; AAC97482.1; -; mRNA. DR EMBL; AK140360; BAE24352.1; -; mRNA. DR EMBL; AK152770; BAE31482.1; -; mRNA. DR EMBL; AK160657; BAE35945.1; -; mRNA. DR EMBL; BC039919; AAH39919.1; -; mRNA. DR RefSeq; NP_034020.1; NM_009890.1. DR UniGene; Mm.30824; -. DR PRIDE; Q9Z0F5; -. DR Ensembl; ENSMUST00000050562; ENSMUSP00000049683; ENSMUSG00000050370. DR GeneID; 12642; -. DR KEGG; mmu:12642; -. DR UCSC; uc008hgj.1; mouse. DR CTD; 9023; -. DR MGI; MGI:1333869; Ch25h. DR eggNOG; COG3000; -. DR GeneTree; ENSGT00530000063017; -. DR HOGENOM; HOG000015767; -. DR HOVERGEN; HBG080944; -. DR InParanoid; Q9Z0F5; -. DR KO; K10223; -. DR OMA; WHVLHHK; -. DR OrthoDB; EOG7288S0; -. DR TreeFam; TF353265; -. DR BRENDA; 1.14.99.38; 3474. DR NextBio; 281840; -. DR PRO; PR:Q9Z0F5; -. DR Bgee; Q9Z0F5; -. DR CleanEx; MM_CH25H; -. DR Genevestigator; Q9Z0F5; -. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0001567; F:cholesterol 25-hydroxylase activity; IEA:UniProtKB-EC. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0008395; F:steroid hydroxylase activity; IDA:MGI. DR GO; GO:0008203; P:cholesterol metabolic process; IDA:MGI. DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro. DR GO; GO:0016126; P:sterol biosynthetic process; IEA:UniProtKB-KW. DR InterPro; IPR006694; Fatty_acid_hydroxylase. DR Pfam; PF04116; FA_hydroxylase; 1. PE 1: Evidence at protein level; KW Complete proteome; Endoplasmic reticulum; Glycoprotein; Iron; KW Lipid biosynthesis; Lipid metabolism; Membrane; Metal-binding; KW Monooxygenase; Oxidoreductase; Reference proteome; KW Steroid biosynthesis; Steroid metabolism; Sterol biosynthesis; KW Sterol metabolism; Transmembrane; Transmembrane helix. FT CHAIN 1 298 Cholesterol 25-hydroxylase. FT /FTId=PRO_0000226802. FT TRANSMEM 38 58 Helical; (Potential). FT TRANSMEM 88 108 Helical; (Potential). FT TRANSMEM 124 144 Helical; (Potential). FT MOTIF 142 146 Histidine box-1. FT MOTIF 157 161 Histidine box-2. FT MOTIF 238 244 Histidine box-3. FT CARBOHYD 5 5 N-linked (GlcNAc...) (Potential). FT CARBOHYD 163 163 N-linked (GlcNAc...) (Potential). FT MUTAGEN 242 243 HH->EE: Loss of function. FT CONFLICT 122 122 V -> A (in Ref. 3; AAH39919). FT CONFLICT 199 199 T -> S (in Ref. 2; BAE35945). FT CONFLICT 282 282 N -> D (in Ref. 3; AAH39919). SQ SEQUENCE 298 AA; 34672 MW; BBCE4A97A20284C6 CRC64; MGCYNGSELQ DLGCSSQLLL QPLWDTIRTR EAFTRSPIFP VTFSIITYVG FCLPFVVLDV LYPWVPILRR YKIHPDFSPS VKQLLPCLGL TLYQHLVFVF PVTLLHWVRS PALLPQEAPE LVQLLSHVLI CLLLFDTEIF AWHLLHHKVP WLYRTFHKVH HQNSSSFALA TQYMSFWELL SLTFFDVLNV AVLRCHPLTI FTFHVINIWL SVEDHSGYDF PWSTHRLVPF GWYGGVAHHD MHHSQFNCNF APYFTHWDKM LGTLRSAPLP ESLCACGERC VNSRERCAVH LIQKKKQT // ID CHDH_MOUSE Reviewed; 596 AA. AC Q8BJ64; Q3TPY4; Q8CHT7; DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 19-MAR-2014, entry version 100. DE RecName: Full=Choline dehydrogenase, mitochondrial; DE Short=CDH; DE Short=CHD; DE EC=1.1.99.1; DE Flags: Precursor; GN Name=Chdh; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Thymus; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE. RX PubMed=20371614; DOI=10.1096/fj.09-153718; RA Johnson A.R., Craciunescu C.N., Guo Z., Teng Y.W., Thresher R.J., RA Blusztajn J.K., Zeisel S.H.; RT "Deletion of murine choline dehydrogenase results in diminished sperm RT motility."; RL FASEB J. 24:2752-2761(2010). RN [4] RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-438; LYS-486 AND LYS-498, RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., RA Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). RN [5] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-486; LYS-498 AND LYS-582, RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23576753; DOI=10.1073/pnas.1302961110; RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., RA Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.; RT "Label-free quantitative proteomics of the lysine acetylome in RT mitochondria identifies substrates of SIRT3 in metabolic pathways."; RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013). CC -!- CATALYTIC ACTIVITY: Choline + acceptor = betaine aldehyde + CC reduced acceptor. CC -!- COFACTOR: FAD (By similarity). CC -!- PATHWAY: Amine and polyamine biosynthesis; betaine biosynthesis CC via choline pathway; betaine aldehyde from choline (cytochrome c CC reductase route): step 1/1. CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane. CC -!- PTM: Acetylation of Lys-498 is observed in liver mitochondria from CC fasted mice but not from fed mice. CC -!- DISRUPTION PHENOTYPE: Decreased testicular betaine and increased CC choline and phosphatidylcholine concentrations. Only one of eleven CC males was able to reproduce, impaired fertility was due to CC diminished sperm motility. CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK030900; BAC27176.1; -; mRNA. DR EMBL; AK164042; BAE37601.1; -; mRNA. DR EMBL; BC039186; AAH39186.1; -; mRNA. DR RefSeq; NP_001129712.1; NM_001136240.1. DR RefSeq; NP_758468.2; NM_172264.2. DR RefSeq; NP_780552.1; NM_175343.5. DR UniGene; Mm.259916; -. DR ProteinModelPortal; Q8BJ64; -. DR SMR; Q8BJ64; 43-573. DR IntAct; Q8BJ64; 2. DR MINT; MINT-1843656; -. DR PhosphoSite; Q8BJ64; -. DR PaxDb; Q8BJ64; -. DR PRIDE; Q8BJ64; -. DR Ensembl; ENSMUST00000067620; ENSMUSP00000065542; ENSMUSG00000015970. DR Ensembl; ENSMUST00000118917; ENSMUSP00000112916; ENSMUSG00000015970. DR GeneID; 218865; -. DR KEGG; mmu:218865; -. DR UCSC; uc007sup.2; mouse. DR CTD; 55349; -. DR MGI; MGI:1860776; Chdh. DR eggNOG; COG2303; -. DR GeneTree; ENSGT00530000063260; -. DR HOGENOM; HOG000139600; -. DR HOVERGEN; HBG023639; -. DR InParanoid; Q8BJ64; -. DR KO; K00108; -. DR OMA; DMSAGSK; -. DR OrthoDB; EOG7DFXBR; -. DR TreeFam; TF313911; -. DR UniPathway; UPA00529; UER00385. DR NextBio; 376465; -. DR PRO; PR:Q8BJ64; -. DR Bgee; Q8BJ64; -. DR CleanEx; MM_CHDH; -. DR Genevestigator; Q8BJ64; -. DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:MGI. DR GO; GO:0008812; F:choline dehydrogenase activity; IEA:UniProtKB-EC. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. DR GO; GO:0019285; P:glycine betaine biosynthetic process from choline; IEA:UniProtKB-UniPathway. DR InterPro; IPR011533; Choline_dehydrogenase. DR InterPro; IPR012132; GMC_OxRdtase. DR InterPro; IPR000172; GMC_OxRdtase_N. DR InterPro; IPR007867; GMC_OxRtase_C. DR Pfam; PF05199; GMC_oxred_C; 1. DR Pfam; PF00732; GMC_oxred_N; 1. DR PIRSF; PIRSF000137; Alcohol_oxidase; 1. DR TIGRFAMs; TIGR01810; betA; 1. DR PROSITE; PS00623; GMC_OXRED_1; 1. DR PROSITE; PS00624; GMC_OXRED_2; 1. PE 1: Evidence at protein level; KW Acetylation; Complete proteome; FAD; Flavoprotein; Membrane; KW Mitochondrion; Mitochondrion inner membrane; Oxidoreductase; KW Reference proteome; Transit peptide. FT TRANSIT 1 34 Mitochondrion (By similarity). FT CHAIN 35 596 Choline dehydrogenase, mitochondrial. FT /FTId=PRO_0000012330. FT NP_BIND 44 73 FAD (By similarity). FT ACT_SITE 513 513 By similarity. FT MOD_RES 438 438 N6-succinyllysine. FT MOD_RES 486 486 N6-acetyllysine; alternate. FT MOD_RES 486 486 N6-succinyllysine; alternate. FT MOD_RES 498 498 N6-acetyllysine; alternate. FT MOD_RES 498 498 N6-succinyllysine; alternate. FT MOD_RES 582 582 N6-acetyllysine. FT CONFLICT 4 4 V -> A (in Ref. 2; AAH39186). FT CONFLICT 12 12 W -> C (in Ref. 2; AAH39186). FT CONFLICT 24 24 Q -> R (in Ref. 2; AAH39186). FT CONFLICT 212 212 G -> A (in Ref. 1; BAE37601). SQ SEQUENCE 596 AA; 66415 MW; D31F19A0E0DB9587 CRC64; MWQVLRGWRK GWQSPRGALA WAVQGQPCPP CSRAVASVGK DEYTFVVVGA GSAGCVLASR LTEDPNHRVL LLEAGPKDLL MGSKRLQWKI HMPAALVSNL CDDKYNWYYH TEPQPGMDSR VLYWPRGRVW GGSSSLNAMV YIRGHAEDYN RWHREGAEGW DYAHCLPYFR KAQRHELGAN MYRGGDGPLH VSRGKTNHPL HQAFLQAARQ AGYPFTEDMN GFQQEGFGWM DMTVHQGKRW STACAYLHPV LSRPNLRAEV QTLVSRVLFE GTRAVGVEYI KDGQRHKAYV SREVILSGGA INSPQLLMLS GVGNADDLRK LDIPVVCHLP GVGQNLQDHL EVYVQQACTQ PITLHSAQKP LRKVCIGLEW LWSYTGDGAT AHLETGGFIR SRPGVPHPDI QFHFLPSQVI DHGRKPTQQE AYQVHVGTMR ATSVGWLKLR SANPRDHPVI HPNYLSTETD VEDFRQCVRL SREIFAQEAL APFRGKELQP GSHVQSDKEI DAFVRAKADS AYHPSCTCKM GRSSDPTAVV DAQTKVIGVE NLRVVDASIM PSVVSGNLNA PTVMIAEKAA DIIKGHPALE DKNVPVYKPQ TLDTQR // ID CMAH_MOUSE Reviewed; 577 AA. AC Q61419; Q7TMR9; Q8JZM9; DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 19-MAR-2014, entry version 109. DE RecName: Full=Cytidine monophosphate-N-acetylneuraminic acid hydroxylase; DE Short=CMP-N-acetylneuraminic acid hydroxylase; DE EC=1.14.18.2; DE AltName: Full=CMP-N-acetylneuraminate monooxygenase; DE AltName: Full=CMP-Neu5Ac hydroxylase; DE AltName: Full=CMP-NeuAc hydroxylase; DE Flags: Precursor; GN Name=Cmah; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 5-33; RP 504-524 AND 543-561, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RC STRAIN=BALB/c; TISSUE=Liver; RX PubMed=7608218; DOI=10.1074/jbc.270.27.16458; RA Kawano T., Koyama S., Takematsu H., Kozutsumi Y., Kawasaki H., RA Kawashima S., Kawasaki T., Suzuki A.; RT "Molecular cloning of cytidine monophospho-N-acetylneuraminic acid RT hydroxylase."; RL J. Biol. Chem. 270:16458-16463(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1). RC STRAIN=BALB/c; TISSUE=Liver; RA Koyama S., Takematsu H., Takasaki-Nishigaki M., Kawasaki T., RA Suzuki A., Kozutsumi Y.; RT "Isolation and analysis of the mouse gene encoding CMP-N- RT acetylneuraminic acid hydroxylase."; RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC STRAIN=C57BL/6NCr; TISSUE=Hematopoietic stem cell; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=8132639; RA Kawano T., Kozutsumi Y., Kawasaki T., Suzuki A.; RT "Biosynthesis of N-glycolylneuraminic acid-containing glycoconjugates. RT Purification and characterization of the key enzyme of the cytidine RT monophospho-N-acetylneuraminic acid hydroxylation system."; RL J. Biol. Chem. 269:9024-9029(1994). RN [6] RP ALTERNATIVE SPLICING, AND SUBCELLULAR LOCATION. RX PubMed=8781965; DOI=10.1007/BF00731467; RA Koyama S., Yamaji T., Takematsu H., Kawano T., Kozutsumi Y., RA Suzuki A., Kawasaki T.; RT "A naturally occurring 46-amino acid deletion of cytidine monophospho- RT N-acetylneuraminic acid hydroxylase leads to a change in the RT intracellular distribution of the protein."; RL Glycoconj. J. 13:353-358(1996). RN [7] RP FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE. RX PubMed=22692205; DOI=10.1074/jbc.M112.363549; RA Bergfeld A.K., Pearce O.M., Diaz S.L., Pham T., Varki A.; RT "Metabolism of vertebrate amino sugars with N-glycolyl groups: RT elucidating the intracellular fate of the non-human sialic acid N- RT glycolylneuraminic acid."; RL J. Biol. Chem. 287:28865-28881(2012). CC -!- FUNCTION: Catalyzes the conversion of CMP-N-acetylneuraminic acid CC (CMP-Neu5Ac) into its hydroxylated derivative CMP-N- CC glycolylneuraminic acid (CMP-Neu5Gc), a sialic acid abundantly CC expressed at the surface of many cells, except in brain. CC -!- CATALYTIC ACTIVITY: CMP-N-acetylneuraminate + 2 ferrocytochrome b5 CC + O(2) + 2 H(+) = CMP-N-glycoloylneuraminate + 2 ferricytochrome CC b5 + H(2)O. CC -!- COFACTOR: Binds 1 2Fe-2S cluster per subunit (Probable). CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=5 uM for CMP-NeuAc; CC -!- PATHWAY: Amino-sugar metabolism; N-acetylneuraminate metabolism. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SUBCELLULAR LOCATION: Isoform 2: Endoplasmic reticulum (Probable). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q61419-1; Sequence=Displayed; CC Name=2; CC IsoId=Q61419-2; Sequence=VSP_013769; CC Note=Inactive; CC -!- TISSUE SPECIFICITY: Expressed in all tissues tested, except in CC brain. CC -!- DISRUPTION PHENOTYPE: Mice do not synthesize N-glycolylneuraminic CC acid (Neu5Gc). CC -!- SIMILARITY: Belongs to the CMP-Neu5Ac hydroxylase family. CC -!- SIMILARITY: Contains 1 Rieske domain. CC -!- SEQUENCE CAUTION: CC Sequence=BAB91361.1; Type=Erroneous initiation; CC Sequence=BAB91362.1; Type=Erroneous initiation; CC Sequence=BAB91553.1; Type=Erroneous initiation; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; D21826; BAA04850.1; -; mRNA. DR EMBL; AB061276; BAB91361.1; ALT_INIT; mRNA. DR EMBL; AB061277; BAB91362.1; ALT_INIT; mRNA. DR EMBL; AB061346; BAB91553.1; ALT_INIT; Genomic_DNA. DR EMBL; AL589744; CAI26039.1; -; Genomic_DNA. DR EMBL; BC055079; AAH55079.1; -; mRNA. DR PIR; A57469; A57469. DR RefSeq; NP_001104580.1; NM_001111110.2. DR RefSeq; NP_001271448.1; NM_001284519.1. DR RefSeq; NP_001271449.1; NM_001284520.1. DR RefSeq; NP_031743.3; NM_007717.5. DR RefSeq; XP_006516601.1; XM_006516538.1. DR RefSeq; XP_006516602.1; XM_006516539.1. DR UniGene; Mm.8396; -. DR ProteinModelPortal; Q61419; -. DR SMR; Q61419; 19-95. DR STRING; 10090.ENSMUSP00000106021; -. DR PhosphoSite; Q61419; -. DR PaxDb; Q61419; -. DR PRIDE; Q61419; -. DR Ensembl; ENSMUST00000050859; ENSMUSP00000061045; ENSMUSG00000016756. [Q61419-1] DR Ensembl; ENSMUST00000110391; ENSMUSP00000106021; ENSMUSG00000016756. [Q61419-1] DR Ensembl; ENSMUST00000167746; ENSMUSP00000129007; ENSMUSG00000016756. [Q61419-1] DR GeneID; 12763; -. DR KEGG; mmu:12763; -. DR UCSC; uc007pvq.2; mouse. [Q61419-1] DR UCSC; uc011yxn.1; mouse. [Q61419-2] DR CTD; 12763; -. DR MGI; MGI:103227; Cmah. DR eggNOG; NOG74230; -. DR GeneTree; ENSGT00390000010830; -. DR HOGENOM; HOG000111807; -. DR HOVERGEN; HBG051000; -. DR InParanoid; Q61419; -. DR KO; K08080; -. DR OMA; PSREHPY; -. DR OrthoDB; EOG71P29R; -. DR TreeFam; TF331273; -. DR BioCyc; MetaCyc:MONOMER-14525; -. DR SABIO-RK; Q61419; -. DR UniPathway; UPA00628; -. DR NextBio; 282114; -. DR PRO; PR:Q61419; -. DR Bgee; Q61419; -. DR Genevestigator; Q61419; -. DR GO; GO:0005737; C:cytoplasm; IDA:MGI. DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell. DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0030338; F:CMP-N-acetylneuraminate monooxygenase activity; IMP:UniProtKB. DR GO; GO:0016787; F:hydrolase activity; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0046381; P:CMP-N-acetylneuraminate metabolic process; IDA:MGI. DR GO; GO:0006054; P:N-acetylneuraminate metabolic process; IEA:UniProtKB-UniPathway. DR Gene3D; 2.102.10.10; -; 1. DR Gene3D; 3.60.15.10; -; 2. DR InterPro; IPR001279; Beta-lactamas-like. DR InterPro; IPR027033; Cnh. DR InterPro; IPR017941; Rieske_2Fe-2S. DR PANTHER; PTHR15032:SF2; PTHR15032:SF2; 1. DR Pfam; PF00355; Rieske; 1. DR SUPFAM; SSF50022; SSF50022; 1. DR PROSITE; PS51296; RIESKE; 1. PE 1: Evidence at protein level; KW 2Fe-2S; Alternative splicing; Complete proteome; Cytoplasm; KW Direct protein sequencing; Electron transport; Endoplasmic reticulum; KW Iron; Iron-sulfur; Metal-binding; Oxidoreductase; Reference proteome; KW Transport. FT PROPEP 1 4 Probable. FT /FTId=PRO_0000030699. FT CHAIN 5 577 Cytidine monophosphate-N-acetylneuraminic FT acid hydroxylase. FT /FTId=PRO_0000030700. FT DOMAIN 14 112 Rieske. FT METAL 54 54 Iron-sulfur (2Fe-2S) (By similarity). FT METAL 56 56 Iron-sulfur (2Fe-2S); via pros nitrogen FT (By similarity). FT METAL 75 75 Iron-sulfur (2Fe-2S) (By similarity). FT METAL 78 78 Iron-sulfur (2Fe-2S); via pros nitrogen FT (By similarity). FT VAR_SEQ 279 324 Missing (in isoform 2). FT /FTId=VSP_013769. FT CONFLICT 515 515 I -> T (in Ref. 4; AAH55079). SQ SEQUENCE 577 AA; 66936 MW; 6808ECC75E4F6B78 CRC64; MMDRKQTAET LLTLSPAEVA NLKEGINFFR NKTTGKEYIL YKEKDHLKAC KNLCKHQGGL FMKDIEDLDG RSVKCTKHNW KLDVSTMKYI NPPGSFCQDE LVIEMDENNG LSLVELNPPN PWDSDPRSPE ELAFGEVQIT YLTHACMDLK LGDKRMVFDP WLIGPAFARG WWLLHEPPSD WLERLCKADL IYISHMHSDH LSYPTLKQLS QRRPDIPIYV GDTERPVFWN LDQSGVGLTN INVVPFGIWQ QVDKSLRFMI LMDGVHPEMD TCIIVEYKGH KILNTVDCTR PNGGRLPEKV ALMMSDFAGG ASGFPMTFSG GKFTEEWKAQ FIKAERRKLL NYKAQLVKDL QPRIYCPFAG YFVESHPSDK YIKETNTKND PNQLNNLIRK NSDVVTWTPR PGAVLDLGRM LKDPTDSKGI VEPPEGTKIY KDSWDFGPYL EILNSAVRDE IFCHSSWIKE YFTWAGFKNY NLVVRMIETD EDFSPFPGGY DYLVDFLDLS FPKERPSREH PYEEIHSRVD VIRYVVKNGL LWDDLYIGFQ TRLLRDPDIY HHLFWNHFQI KLPLTPPNWK SFLMHCD // ID COQ6_MOUSE Reviewed; 476 AA. AC Q8R1S0; Q3TJM2; Q80V13; Q8BJY5; DT 28-NOV-2002, integrated into UniProtKB/Swiss-Prot. DT 05-SEP-2012, sequence version 3. DT 19-MAR-2014, entry version 93. DE RecName: Full=Ubiquinone biosynthesis monooxygenase COQ6; DE EC=1.14.13.-; DE AltName: Full=Coenzyme Q10 monooxygenase 6; GN Name=Coq6; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Forelimb, Placenta, and Stomach; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Czech II, and FVB/N; TISSUE=Brain, Liver, and Mammary tumor; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE. RX PubMed=21540551; DOI=10.1172/JCI45693; RA Heeringa S.F., Chernin G., Chaki M., Zhou W., Sloan A.J., Ji Z., RA Xie L.X., Salviati L., Hurd T.W., Vega-Warner V., Killen P.D., RA Raphael Y., Ashraf S., Ovunc B., Schoeb D.S., McLaughlin H.M., RA Airik R., Vlangos C.N., Gbadegesin R., Hinkes B., Saisawat P., RA Trevisson E., Doimo M., Casarin A., Pertegato V., Giorgi G., RA Prokisch H., Rotig A., Nurnberg G., Becker C., Wang S., Ozaltin F., RA Topaloglu R., Bakkaloglu A., Bakkaloglu S.A., Muller D., Beissert A., RA Mir S., Berdeli A., Varpizen S., Zenker M., Matejas V., RA Santos-Ocana C., Navas P., Kusakabe T., Kispert A., Akman S., RA Soliman N.A., Krick S., Mundel P., Reiser J., Nurnberg P., RA Clarke C.F., Wiggins R.C., Faul C., Hildebrandt F.; RT "COQ6 mutations in human patients produce nephrotic syndrome with RT sensorineural deafness."; RL J. Clin. Invest. 121:2013-2024(2011). RN [6] RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-219, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic fibroblast; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., RA Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). CC -!- COFACTOR: FAD (Potential). CC -!- PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis. CC -!- SUBUNIT: Interacts with ADCK4 and COQ7 (By similarity). CC -!- SUBCELLULAR LOCATION: Golgi apparatus. Cell projection (By CC similarity). Note=Localizes to podocyte cell processes (By CC similarity). CC -!- TISSUE SPECIFICITY: Expressed in the kidney, in podocytes. CC -!- DEVELOPMENTAL STAGE: At 12.5 dpc, expressed in the metanephric CC mesenchyme. At 16.5 dpc, expressed in the condensing metanephric CC mesenchyme surrounding the ureter tips. At 18.5 dpc, expressed in CC whole kidney. CC -!- SIMILARITY: Belongs to the UbiH/COQ6 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK077863; BAC37039.1; -; mRNA. DR EMBL; AK131889; BAE20853.1; -; mRNA. DR EMBL; AK167380; BAE39473.1; -; mRNA. DR EMBL; AC120402; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH466590; EDL02790.1; -; Genomic_DNA. DR EMBL; BC024135; AAH24135.1; -; mRNA. DR EMBL; BC051055; AAH51055.1; -; mRNA. DR EMBL; BC132168; AAI32169.1; -; mRNA. DR EMBL; BC132170; AAI32171.1; -; mRNA. DR RefSeq; NP_766170.2; NM_172582.3. DR RefSeq; XP_006515762.1; XM_006515699.1. DR UniGene; Mm.280062; -. DR ProteinModelPortal; Q8R1S0; -. DR SMR; Q8R1S0; 43-443. DR IntAct; Q8R1S0; 1. DR MINT; MINT-4111022; -. DR STRING; 10090.ENSMUSP00000105905; -. DR PhosphoSite; Q8R1S0; -. DR PaxDb; Q8R1S0; -. DR PRIDE; Q8R1S0; -. DR Ensembl; ENSMUST00000021661; ENSMUSP00000021661; ENSMUSG00000021235. DR Ensembl; ENSMUST00000110276; ENSMUSP00000105905; ENSMUSG00000021235. DR GeneID; 217707; -. DR KEGG; mmu:217707; -. DR UCSC; uc007ofb.2; mouse. DR CTD; 51004; -. DR MGI; MGI:1924408; Coq6. DR eggNOG; COG0654; -. DR GeneTree; ENSGT00390000015152; -. DR HOVERGEN; HBG029533; -. DR InParanoid; Q8R1S0; -. DR KO; K06126; -. DR OMA; DMRLGLC; -. DR OrthoDB; EOG7H793X; -. DR TreeFam; TF105772; -. DR UniPathway; UPA00232; -. DR NextBio; 375980; -. DR PRO; PR:Q8R1S0; -. DR ArrayExpress; Q8R1S0; -. DR Bgee; Q8R1S0; -. DR CleanEx; MM_COQ6; -. DR Genevestigator; Q8R1S0; -. DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-SubCell. DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. DR GO; GO:0016709; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen; IEA:InterPro. DR GO; GO:0006744; P:ubiquinone biosynthetic process; IEA:UniProtKB-UniPathway. DR InterPro; IPR002938; mOase_FAD-bd. DR InterPro; IPR003042; Rng_hydrolase-like. DR InterPro; IPR018168; Ubi_Hdrlase_CS. DR InterPro; IPR010971; Ubi_Hdrxlases. DR InterPro; IPR000689; UbQ_biosynth_mOase. DR Pfam; PF01494; FAD_binding_3; 2. DR PRINTS; PR00420; RNGMNOXGNASE. DR TIGRFAMs; TIGR01989; COQ6; 1. DR TIGRFAMs; TIGR01988; Ubi-OHases; 1. DR PROSITE; PS01304; UBIH; 1. PE 1: Evidence at protein level; KW Cell projection; Complete proteome; FAD; Flavoprotein; KW Golgi apparatus; Monooxygenase; Oxidoreductase; Reference proteome; KW Ubiquinone biosynthesis. FT CHAIN 1 476 Ubiquinone biosynthesis monooxygenase FT COQ6. FT /FTId=PRO_0000207584. FT MOD_RES 219 219 N6-succinyllysine. FT CONFLICT 33 33 Q -> R (in Ref. 4; AAH51055). FT CONFLICT 441 441 L -> I (in Ref. 1; BAC37039). SQ SEQUENCE 476 AA; 51393 MW; B431032EFE97D9E5 CRC64; MAARIGSMAG LLCVRWWSSA QLAARGGPLV ASQRWAGSSA DTVYDVVVSG GGLVGSAMAC ALGHDIHFHD KKILLLEAGP KKALEKLSET YSNRVSSISP GSTTLLSSFG AWDHICNMRC KAFRRMQVWD SCSEALIMFD RDNLDDMGYI VENDVIMYAL TKQLEAVADR VKVLYESKAV GYSWPGAFSM ADSSPWVHIT LGDGSTLQTK LLIGADGHKS GVRQAAGIQN VSWKYDQSAV VATLHLSEAT ENNVAWQRFL PSGPIALLPL SDTLSSLVWS TSHEHAAELV SMDEEEFVDA INSAFWSDVH HTDFVDSASA MVRHAVALLK PTKVSARQLP PSIAKVDAKS RALFPLGLGH AAEYVRPRVA LIGDAAHRIH PLAGQGVNMG FGDISSLVHH LSTAAFNGKD LGSMSHLTGY ETDRQRHNTA LLAATDLLKR LYSTSATPLV LLRTWGLQAT NAVSPLKEQI MAFASK // ID COX1_MOUSE Reviewed; 514 AA. AC P00397; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 21-JUL-1986, sequence version 1. DT 19-MAR-2014, entry version 105. DE RecName: Full=Cytochrome c oxidase subunit 1; DE EC=1.9.3.1; DE AltName: Full=Cytochrome c oxidase polypeptide I; GN Name=Mtco1; Synonyms=COI, mt-Co1; OS Mus musculus (Mouse). OG Mitochondrion. OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=7332926; DOI=10.1016/0092-8674(81)90300-7; RA Bibb M.J., van Etten R.A., Wright C.T., Walberg M.W., Clayton D.A.; RT "Sequence and gene organization of mouse mitochondrial DNA."; RL Cell 26:167-180(1981). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=C57BL/6; TISSUE=Spleen; RX PubMed=8617953; RA Morse M.C., Bleau G., Dabhi V.M., Hetu F., Drobetsky E.A., RA Lindahl K.F., Perreault C.; RT "The COI mitochondrial gene encodes a minor histocompatibility antigen RT presented by H2-M3."; RL J. Immunol. 156:3301-3307(1996). CC -!- FUNCTION: Cytochrome c oxidase is the component of the respiratory CC chain that catalyzes the reduction of oxygen to water. Subunits 1- CC 3 form the functional core of the enzyme complex. CO I is the CC catalytic subunit of the enzyme. Electrons originating in CC cytochrome c are transferred via the copper A center of subunit 2 CC and heme A of subunit 1 to the bimetallic center formed by heme A3 CC and copper B. CC -!- CATALYTIC ACTIVITY: 4 ferrocytochrome c + O(2) + 4 H(+) = 4 CC ferricytochrome c + 2 H(2)O. CC -!- PATHWAY: Energy metabolism; oxidative phosphorylation. CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass CC membrane protein. CC -!- SIMILARITY: Belongs to the heme-copper respiratory oxidase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; J01420; AAB48646.1; -; Genomic_DNA. DR EMBL; V00711; CAA24082.1; -; Genomic_DNA. DR EMBL; U39315; AAA85227.1; -; Genomic_DNA. DR PIR; A00465; ODMS1. DR ProteinModelPortal; P00397; -. DR SMR; P00397; 2-514. DR PaxDb; P00397; -. DR PRIDE; P00397; -. DR MGI; MGI:102504; mt-Co1. DR eggNOG; COG0843; -. DR HOGENOM; HOG000085274; -. DR HOVERGEN; HBG003841; -. DR InParanoid; P00397; -. DR UniPathway; UPA00705; -. DR NextBio; 35563454; -. DR PRO; PR:P00397; -. DR Genevestigator; P00397; -. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell. DR GO; GO:0045277; C:respiratory chain complex IV; ISS:UniProtKB. DR GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:UniProtKB-EC. DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0009060; P:aerobic respiration; IEA:InterPro. DR GO; GO:1902600; P:hydrogen ion transmembrane transport; ISS:GOC. DR GO; GO:0006119; P:oxidative phosphorylation; IEA:UniProtKB-UniPathway. DR Gene3D; 1.20.210.10; -; 1. DR InterPro; IPR000883; Cyt_c_Oxase_su1. DR InterPro; IPR023615; Cyt_c_Oxase_su1_BS. DR InterPro; IPR023616; Cyt_c_Oxase_su1_dom. DR PANTHER; PTHR10422; PTHR10422; 1. DR Pfam; PF00115; COX1; 1. DR PRINTS; PR01165; CYCOXIDASEI. DR SUPFAM; SSF81442; SSF81442; 1. DR PROSITE; PS50855; COX1; 1. DR PROSITE; PS00077; COX1_CUB; 1. PE 3: Inferred from homology; KW Complete proteome; Copper; Electron transport; Heme; Iron; Membrane; KW Metal-binding; Mitochondrion; Mitochondrion inner membrane; KW Oxidoreductase; Reference proteome; Respiratory chain; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1 514 Cytochrome c oxidase subunit 1. FT /FTId=PRO_0000183363. FT TRANSMEM 17 37 Helical; (Potential). FT TRANSMEM 56 76 Helical; (Potential). FT TRANSMEM 102 122 Helical; (Potential). FT TRANSMEM 145 165 Helical; (Potential). FT TRANSMEM 183 203 Helical; (Potential). FT TRANSMEM 234 254 Helical; (Potential). FT TRANSMEM 268 288 Helical; (Potential). FT TRANSMEM 310 330 Helical; (Potential). FT TRANSMEM 338 358 Helical; (Potential). FT TRANSMEM 380 400 Helical; (Potential). FT TRANSMEM 414 434 Helical; (Potential). FT TRANSMEM 456 476 Helical; (Potential). FT METAL 61 61 Iron (heme A axial ligand) (Probable). FT METAL 240 240 Copper B (Probable). FT METAL 244 244 Copper B (Probable). FT METAL 290 290 Copper B (Probable). FT METAL 291 291 Copper B (Probable). FT METAL 376 376 Iron (heme A3 axial ligand) (Probable). FT METAL 378 378 Iron (heme A axial ligand) (Probable). FT CROSSLNK 240 244 1'-histidyl-3'-tyrosine (His-Tyr) (By FT similarity). SQ SEQUENCE 514 AA; 56862 MW; 5C0174D7BA2F6BD3 CRC64; MFINRWLFST NHKDIGTLYL LFGAWAGMVG TALSILIRAE LGQPGALLGD DQIYNVIVTA HAFVMIFFMV MPMMIGGFGN WLVPLMIGAP DMAFPRMNNM SFWLLPPSFL LLLASSMVEA GAGTGWTVYP PLAGNPVHAG ASVDLTIFSL HLAGVSSILG AINFITTIIN MKPPAMTQYQ TPLFVWSVLI TAVLLLLSLP VLAAGITMLL TDRNLNTTFF DPAGGGDPIL YQHLFWFFGH PEVYILILPG FGIISHVVTY YSGKKEPFGY MGMVWAMMSI GFLGFIVWAH HMFTVGLDVD TRACFTSATM IIAIPTGVKV FSWLATLHGG NIKWSPAMLW ALGFIFLFTV GGLTGIVLSN SSLDIVLHDT YYVVAHFHYV LSMGAVFAIM AGFVHWFPLF SGFTLDDTWA KAHFAIMFVG VNMTFFPQHF LGLSGMPRRY SDYPDAYTTW NTVSSMGSFI SLTAVLIMIF MIWEAFASKR EVMSVSYAST NLEWLHGCPP PYHTFEEPTY VKVK // ID CP11A_MOUSE Reviewed; 526 AA. AC Q9QZ82; DT 04-MAY-2001, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 19-FEB-2014, entry version 106. DE RecName: Full=Cholesterol side-chain cleavage enzyme, mitochondrial; DE EC=1.14.15.6; DE AltName: Full=CYPXIA1; DE AltName: Full=Cholesterol desmolase; DE AltName: Full=Cytochrome P450 11A1; DE AltName: Full=Cytochrome P450(scc); DE Flags: Precursor; GN Name=Cyp11a1; Synonyms=Cyp11a; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=C57BL/6; RA Tanaka M., Hennebold J.H., Adashi E.Y.; RL Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the side-chain cleavage reaction of CC cholesterol to pregnenolone (By similarity). CC -!- CATALYTIC ACTIVITY: Cholesterol + 6 reduced adrenodoxin + 3 O(2) = CC pregnenolone + 4-methylpentanal + 6 oxidized adrenodoxin + 4 CC H(2)O. CC -!- COFACTOR: Heme group (By similarity). CC -!- PATHWAY: Lipid metabolism; C21-steroid hormone metabolism. CC -!- SUBUNIT: Interacts with FDX1/adrenodoxin (By similarity). CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane. CC -!- SIMILARITY: Belongs to the cytochrome P450 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF195119; AAF03897.1; -; mRNA. DR RefSeq; NP_062753.3; NM_019779.3. DR UniGene; Mm.302865; -. DR ProteinModelPortal; Q9QZ82; -. DR SMR; Q9QZ82; 41-510. DR PhosphoSite; Q9QZ82; -. DR PaxDb; Q9QZ82; -. DR PRIDE; Q9QZ82; -. DR Ensembl; ENSMUST00000034874; ENSMUSP00000034874; ENSMUSG00000032323. DR GeneID; 13070; -. DR KEGG; mmu:13070; -. DR UCSC; uc009pwa.1; mouse. DR CTD; 1583; -. DR MGI; MGI:88582; Cyp11a1. DR eggNOG; COG2124; -. DR GeneTree; ENSGT00550000074304; -. DR HOGENOM; HOG000013161; -. DR HOVERGEN; HBG051098; -. DR InParanoid; Q9QZ82; -. DR KO; K00498; -. DR OMA; YQRPIGV; -. DR OrthoDB; EOG7MKW5S; -. DR TreeFam; TF105094; -. DR UniPathway; UPA00229; -. DR NextBio; 283004; -. DR PRO; PR:Q9QZ82; -. DR Bgee; Q9QZ82; -. DR Genevestigator; Q9QZ82; -. DR GO; GO:0030061; C:mitochondrial crista; IEA:Ensembl. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR GO; GO:0043204; C:perikaryon; IEA:Ensembl. DR GO; GO:0015485; F:cholesterol binding; IEA:Ensembl. DR GO; GO:0008386; F:cholesterol monooxygenase (side-chain-cleaving) activity; IDA:MGI. DR GO; GO:0020037; F:heme binding; ISS:UniProtKB. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0018879; P:biphenyl metabolic process; IEA:Ensembl. DR GO; GO:0006700; P:C21-steroid hormone biosynthetic process; IDA:MGI. DR GO; GO:0071236; P:cellular response to antibiotic; IEA:Ensembl. DR GO; GO:0071276; P:cellular response to cadmium ion; IEA:Ensembl. DR GO; GO:0071320; P:cellular response to cAMP; IEA:Ensembl. DR GO; GO:0044344; P:cellular response to fibroblast growth factor stimulus; IEA:Ensembl. DR GO; GO:0071372; P:cellular response to follicle-stimulating hormone stimulus; IEA:Ensembl. DR GO; GO:0071347; P:cellular response to interleukin-1; IEA:Ensembl. DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IEA:Ensembl. DR GO; GO:0071375; P:cellular response to peptide hormone stimulus; IEA:Ensembl. DR GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IEA:Ensembl. DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IEA:Ensembl. DR GO; GO:0021549; P:cerebellum development; IEA:Ensembl. DR GO; GO:0008203; P:cholesterol metabolic process; ISS:UniProtKB. DR GO; GO:0018894; P:dibenzo-p-dioxin metabolic process; IEA:Ensembl. DR GO; GO:0006703; P:estrogen biosynthetic process; IEA:Ensembl. DR GO; GO:0050756; P:fractalkine metabolic process; IEA:Ensembl. DR GO; GO:0060014; P:granulosa cell differentiation; IEA:Ensembl. DR GO; GO:0021766; P:hippocampus development; IEA:Ensembl. DR GO; GO:0033327; P:Leydig cell differentiation; IEA:Ensembl. DR GO; GO:0060135; P:maternal process involved in female pregnancy; IEA:Ensembl. DR GO; GO:0007617; P:mating behavior; IEA:Ensembl. DR GO; GO:0018958; P:phenol-containing compound metabolic process; IEA:Ensembl. DR GO; GO:0018963; P:phthalate metabolic process; IEA:Ensembl. DR GO; GO:0006701; P:progesterone biosynthetic process; IEA:Ensembl. DR GO; GO:0001101; P:response to acid; IEA:Ensembl. DR GO; GO:0043279; P:response to alkaloid; IEA:Ensembl. DR GO; GO:0051412; P:response to corticosterone; IEA:Ensembl. DR GO; GO:0042493; P:response to drug; IEA:Ensembl. DR GO; GO:0060992; P:response to fungicide; IEA:Ensembl. DR GO; GO:0010332; P:response to gamma radiation; IEA:Ensembl. DR GO; GO:0033595; P:response to genistein; IEA:Ensembl. DR GO; GO:0042542; P:response to hydrogen peroxide; IEA:Ensembl. DR GO; GO:0017085; P:response to insecticide; IEA:Ensembl. DR GO; GO:0033591; P:response to L-ascorbic acid; IEA:Ensembl. DR GO; GO:0009651; P:response to salt stress; IEA:Ensembl. DR GO; GO:0033197; P:response to vitamin E; IEA:Ensembl. DR GO; GO:0014037; P:Schwann cell differentiation; IEA:Ensembl. DR GO; GO:0061370; P:testosterone biosynthetic process; IEA:Ensembl. DR Gene3D; 1.10.630.10; -; 1. DR InterPro; IPR001128; Cyt_P450. DR InterPro; IPR017972; Cyt_P450_CS. DR InterPro; IPR002401; Cyt_P450_E_grp-I. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00463; EP450I. DR PRINTS; PR00385; P450. DR SUPFAM; SSF48264; SSF48264; 1. DR PROSITE; PS00086; CYTOCHROME_P450; 1. PE 2: Evidence at transcript level; KW Cholesterol metabolism; Complete proteome; Heme; Iron; KW Lipid metabolism; Membrane; Metal-binding; Mitochondrion; KW Monooxygenase; Oxidoreductase; Reference proteome; Steroid metabolism; KW Steroidogenesis; Sterol metabolism; Transit peptide. FT TRANSIT 1 36 Mitochondrion (By similarity). FT CHAIN 37 526 Cholesterol side-chain cleavage enzyme, FT mitochondrial. FT /FTId=PRO_0000003587. FT METAL 458 458 Iron (heme axial ligand) (By similarity). SQ SEQUENCE 526 AA; 60315 MW; E5029738EE4ECB71 CRC64; MLAKGLSLRS VLVKGCQPFL SPTWQGPVLS TGKGAGTSTS SPRSFNEIPS PGDNGWLNLY HFWRESGTQK IHYHQMQSFQ KYGPIYREKL GTLESVYIVD PKDASILFSC EGPNPERFLV PPWVAYHQYY QRPIGVLFKS SDAWKKDRIV LNQEVMAPGA IKNFVPLLEG VAQDFIKVLH RRIKQQNSGN FSGVISDDLF RFSFESISSV IFGERMGMLE EIVDPEAQRF INAVYQMFHT SVPMLNLPPD FFRLLRTKTW KDHAAAWDVI FNKADEYTQN FYWDLRQKRD FSQYPGVLYS LLGGNKLPFK NIQANITEML AGGVDTTSMT LQWNLYEMAH NLKVQEMLRA EVLAARRQAQ GDMAKMVQLV PLLKASIKET LRLHPISVTL QRYTVNDLVL RNYKIPAKTL VQVASFAMGR DPGFFPNPNK FDPTRWLEKS QNTTHFRYLG FGWGVRQCLG RRIAELEMTI LLINLLENFR IEVQNLRDVG TKFSLILMPE NPILFNFQPL KQDLGPAVTR KDNTVN // ID CP17A_MOUSE Reviewed; 507 AA. AC P27786; DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1992, sequence version 1. DT 19-FEB-2014, entry version 116. DE RecName: Full=Steroid 17-alpha-hydroxylase/17,20 lyase; DE EC=1.14.99.9; DE EC=4.1.2.30; DE AltName: Full=17-alpha-hydroxyprogesterone aldolase; DE AltName: Full=CYPXVII; DE AltName: Full=Cytochrome P450 17A1; DE AltName: Full=Cytochrome P450-C17; DE Short=Cytochrome P450c17; GN Name=Cyp17a1; Synonyms=Cyp17; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=1840559; DOI=10.1016/0888-7543(91)90511-C; RA Youngblood G.L., Sartorius C., Taylor B.A., Payne A.H.; RT "Isolation, characterization, and chromosomal mapping of mouse P450 17 RT alpha-hydroxylase/C17-20 lyase."; RL Genomics 10:270-275(1991). CC -!- FUNCTION: Conversion of pregnenolone and progesterone to their 17- CC alpha-hydroxylated products and subsequently to CC dehydroepiandrosterone (DHEA) and androstenedione. Catalyzes both CC the 17-alpha-hydroxylation and the 17,20-lyase reaction. Involved CC in sexual development during fetal life and at puberty. CC -!- CATALYTIC ACTIVITY: A C(21)-steroid + (reduced NADPH--hemoprotein CC reductase) + O(2) = a 17-alpha-hydroxy-C(21)-steroid + (oxidized CC NADPH--hemoprotein reductase) + H(2)O. CC -!- CATALYTIC ACTIVITY: 17-alpha-hydroxyprogesterone = androst-4-ene- CC 3,17-dione + acetaldehyde. CC -!- COFACTOR: Heme group (By similarity). CC -!- ENZYME REGULATION: Regulated predominantly by intracellular cAMP CC levels. CC -!- PATHWAY: Lipid metabolism; steroid biosynthesis. CC -!- SUBCELLULAR LOCATION: Membrane (Potential). CC -!- SIMILARITY: Belongs to the cytochrome P450 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M64863; AAA39877.1; -; mRNA. DR PIR; A39072; A39072. DR RefSeq; NP_031835.3; NM_007809.3. DR UniGene; Mm.1262; -. DR ProteinModelPortal; P27786; -. DR SMR; P27786; 34-502. DR PhosphoSite; P27786; -. DR PaxDb; P27786; -. DR PRIDE; P27786; -. DR Ensembl; ENSMUST00000026012; ENSMUSP00000026012; ENSMUSG00000003555. DR GeneID; 13074; -. DR KEGG; mmu:13074; -. DR UCSC; uc008hua.2; mouse. DR CTD; 1586; -. DR MGI; MGI:88586; Cyp17a1. DR eggNOG; COG2124; -. DR HOGENOM; HOG000036991; -. DR HOVERGEN; HBG106944; -. DR InParanoid; P27786; -. DR KO; K00512; -. DR OMA; ILAYFFW; -. DR OrthoDB; EOG7RBZ85; -. DR TreeFam; TF105095; -. DR UniPathway; UPA00062; -. DR NextBio; 283012; -. DR PRO; PR:P27786; -. DR ArrayExpress; P27786; -. DR Bgee; P27786; -. DR Genevestigator; P27786; -. DR GO; GO:0030424; C:axon; IDA:MGI. DR GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR GO; GO:0043025; C:neuronal cell body; IDA:MGI. DR GO; GO:0047442; F:17-alpha-hydroxyprogesterone aldolase activity; IEA:UniProtKB-EC. DR GO; GO:0020037; F:heme binding; ISS:UniProtKB. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0004508; F:steroid 17-alpha-monooxygenase activity; IDA:MGI. DR GO; GO:0030325; P:adrenal gland development; IEA:Ensembl. DR GO; GO:0018879; P:biphenyl metabolic process; IEA:Ensembl. DR GO; GO:0071236; P:cellular response to antibiotic; IEA:Ensembl. DR GO; GO:0071371; P:cellular response to gonadotropin stimulus; IEA:Ensembl. DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IEA:Ensembl. DR GO; GO:0018894; P:dibenzo-p-dioxin metabolic process; IEA:Ensembl. DR GO; GO:0006704; P:glucocorticoid biosynthetic process; IDA:MGI. DR GO; GO:0021766; P:hippocampus development; IEA:Ensembl. DR GO; GO:0042446; P:hormone biosynthetic process; ISS:UniProtKB. DR GO; GO:0033327; P:Leydig cell differentiation; IEA:Ensembl. DR GO; GO:0030728; P:ovulation; IEA:Ensembl. DR GO; GO:0018958; P:phenol-containing compound metabolic process; IEA:Ensembl. DR GO; GO:0018963; P:phthalate metabolic process; IEA:Ensembl. DR GO; GO:0090031; P:positive regulation of steroid hormone biosynthetic process; IEA:Ensembl. DR GO; GO:0042448; P:progesterone metabolic process; ISS:UniProtKB. DR GO; GO:0010034; P:response to acetate; IEA:Ensembl. DR GO; GO:0051591; P:response to cAMP; IEA:Ensembl. DR GO; GO:0034097; P:response to cytokine; IEA:Ensembl. DR GO; GO:0042493; P:response to drug; IEA:Ensembl. DR GO; GO:0060992; P:response to fungicide; IEA:Ensembl. DR GO; GO:0009635; P:response to herbicide; IEA:Ensembl. DR GO; GO:0017085; P:response to insecticide; IEA:Ensembl. DR GO; GO:0010212; P:response to ionizing radiation; IEA:Ensembl. DR GO; GO:0051597; P:response to methylmercury; IEA:Ensembl. DR GO; GO:0031667; P:response to nutrient levels; IEA:Ensembl. DR GO; GO:0032526; P:response to retinoic acid; IEA:Ensembl. DR GO; GO:0048545; P:response to steroid hormone; IEA:Ensembl. DR Gene3D; 1.10.630.10; -; 1. DR InterPro; IPR001128; Cyt_P450. DR InterPro; IPR017972; Cyt_P450_CS. DR InterPro; IPR002401; Cyt_P450_E_grp-I. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00463; EP450I. DR PRINTS; PR00385; P450. DR SUPFAM; SSF48264; SSF48264; 1. DR PROSITE; PS00086; CYTOCHROME_P450; 1. PE 2: Evidence at transcript level; KW Complete proteome; Heme; Iron; Lyase; Membrane; Metal-binding; KW Monooxygenase; Oxidoreductase; Reference proteome; Steroidogenesis. FT CHAIN 1 507 Steroid 17-alpha-hydroxylase/17,20 lyase. FT /FTId=PRO_0000051935. FT METAL 441 441 Iron (heme axial ligand) (By similarity). SQ SEQUENCE 507 AA; 57638 MW; C0916193356EFEBD CRC64; MWELVGLLLL ILAYFFWPKS KTPNAKFPRS LPFLPLVGSL PFLPRRGHMH ANFFKLQEKY GPIYSLRLGT TTAVIVGHYQ LAREVLVKKG KEFSGRPQMV TLGLLSDQGK GVAFADSSSS WQLHRKLVFS TFSLFRDDQK LEKMICQEAN SLCDLILTYD GESRDLSTLI FKSVINIICT ICFNISFENK DPILTTIQTF TEGIVDVLGH SDLVDIFPWL KIFPNKNLEM IKEHTKIREK TLVEMFEKCK EKFNSESLSS LTDILIQAKM NAENNNTGEG QDPSVFSDKH ILVTVGDIFG AGIETTSSVL NWILAFLVHN PEVKRKIQKE IDQYVGFSRT PSFNDRTHLL MLEATIREVL RIRPVAPLLI PHKANIDSSI GEFAIPKDTH VIINLWALHH DKNEWDQPDR FMPERFLDPT GSHLITPTPS YLPFGAGPRS CIGEALARQE LFIFMALLLQ RFDFDVSDDK QLPCLVGDPK VVFLIDPFKV KITVRQAWKD AQVEVST // ID CP19A_MOUSE Reviewed; 503 AA. AC P28649; DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-1992, sequence version 1. DT 19-MAR-2014, entry version 108. DE RecName: Full=Aromatase; DE EC=1.14.14.14; DE AltName: Full=CYPXIX; DE AltName: Full=Cytochrome P-450AROM; DE AltName: Full=Cytochrome P450 19A1; DE AltName: Full=Estrogen synthase; GN Name=Cyp19a1; Synonyms=Arom, Cyp19; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Ovary; RX PubMed=1897929; DOI=10.1016/0003-9861(91)90354-L; RA Terashima M., Toda K., Kawamoto T., Kuribayashi I., Ogawa Y., RA Maeda T., Shizuta Y.; RT "Isolation of a full-length cDNA encoding mouse aromatase P450."; RL Arch. Biochem. Biophys. 285:231-237(1991). CC -!- FUNCTION: Catalyzes the formation of aromatic C18 estrogens from CC C19 androgens. CC -!- CATALYTIC ACTIVITY: Testosterone + 3 O(2) + 3 reduced CC flavoproteins = 17-beta-estradiol + formate + 4 H(2)O + 3 oxidized CC flavoproteins. CC -!- CATALYTIC ACTIVITY: Androst-4-ene-3,17-dione + 3 O(2) + 3 reduced CC flavoproteins = estrone + formate + 4 H(2)O + 3 oxidized CC flavoproteins. CC -!- COFACTOR: Heme group (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein. CC -!- SIMILARITY: Belongs to the cytochrome P450 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; D00659; BAA00551.1; -; mRNA. DR PIR; S13912; S13912. DR RefSeq; NP_031836.1; NM_007810.3. DR RefSeq; XP_006510868.1; XM_006510805.1. DR RefSeq; XP_006510869.1; XM_006510806.1. DR RefSeq; XP_006510870.1; XM_006510807.1. DR UniGene; Mm.478781; -. DR UniGene; Mm.5199; -. DR ProteinModelPortal; P28649; -. DR SMR; P28649; 45-496. DR STRING; 10090.ENSMUSP00000034811; -. DR PhosphoSite; P28649; -. DR PRIDE; P28649; -. DR Ensembl; ENSMUST00000034811; ENSMUSP00000034811; ENSMUSG00000032274. DR GeneID; 13075; -. DR KEGG; mmu:13075; -. DR UCSC; uc009pmu.1; mouse. DR CTD; 1588; -. DR MGI; MGI:88587; Cyp19a1. DR eggNOG; COG2124; -. DR HOGENOM; HOG000111912; -. DR HOVERGEN; HBG050750; -. DR InParanoid; P28649; -. DR KO; K07434; -. DR OMA; MRRIMLD; -. DR OrthoDB; EOG7D85W5; -. DR TreeFam; TF352039; -. DR NextBio; 283016; -. DR PRO; PR:P28649; -. DR ArrayExpress; P28649; -. DR Bgee; P28649; -. DR Genevestigator; P28649; -. DR GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell. DR GO; GO:0070330; F:aromatase activity; ISS:UniProtKB. DR GO; GO:0020037; F:heme binding; ISS:UniProtKB. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0008209; P:androgen metabolic process; IMP:MGI. DR GO; GO:0060736; P:prostate gland growth; IMP:MGI. DR Gene3D; 1.10.630.10; -; 1. DR InterPro; IPR001128; Cyt_P450. DR InterPro; IPR017972; Cyt_P450_CS. DR InterPro; IPR002401; Cyt_P450_E_grp-I. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00463; EP450I. DR PRINTS; PR00385; P450. DR SUPFAM; SSF48264; SSF48264; 1. DR PROSITE; PS00086; CYTOCHROME_P450; 1. PE 2: Evidence at transcript level; KW Complete proteome; Heme; Iron; Membrane; Metal-binding; Monooxygenase; KW Oxidoreductase; Reference proteome. FT CHAIN 1 503 Aromatase. FT /FTId=PRO_0000051957. FT METAL 437 437 Iron (heme axial ligand) (By similarity). FT BINDING 309 309 Substrate (By similarity). FT BINDING 374 374 Substrate; via amide nitrogen (By FT similarity). SQ SEQUENCE 503 AA; 58015 MW; 737400389D1AEFF1 CRC64; MFLEMLNPMQ YNVTIMVPET VTVSAMPLLL IMGLLLLIWN CESSSSIPGP GYCLGIGPLI SHGRFLWMGI GSACNYYNKM YGEFMRVWIS GEETLIISKS SSMFHVMKHS HYISRFGSKR GLQCIGMHEN GIIFNNNPSL WRTIRPFFMK ALTGPGLVRM VEVCVESIKQ HLDRLGEVTD TSGYVDVLTL MRHIMLDTSN MLFLGIPLDE SAIVKKIQGY FNAWQALLIK PNIFFKISWL YRKYERSVKD LKDEIAVLVE KKRHKVSTAE KLEDCMDFAT DLIFAERRGD LTKENVNQCI LEMLIAAPDT MSVTLYFMLL LVAEYPEVEA AILKEIHTVV GDRDIKIEDI QNLKVVENFI NESMRYQPVV DLVMRRALED DVIDGYPVKK GTNIILNIGR MHRLEYFPKP NEFTLENFEK NVPYRYFQPF GFGPRGCAGK YIAMVMMKVV LVTLLRRFQV KTLQKRCIEN IPKKNDLSLH PNEDRHLVEI IFSPRNSDKY LQQ // ID CP1A1_MOUSE Reviewed; 524 AA. AC P00184; Q61455; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 2. DT 19-MAR-2014, entry version 135. DE RecName: Full=Cytochrome P450 1A1; DE EC=1.14.14.1; DE AltName: Full=CYPIA1; DE AltName: Full=Cytochrome P450-P1; GN Name=Cyp1a1; Synonyms=Cyp1a-1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. RC STRAIN=C57BL/6; TISSUE=Liver; RX PubMed=6547952; RA Kimura S., Gonzalez F.J., Nebert D.W.; RT "The murine Ah locus. Comparison of the complete cytochrome P1-450 and RT P3-450 cDNA nucleotide and amino acid sequences."; RL J. Biol. Chem. 259:10705-10713(1984). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=3988744; RA Gonzalez F.J., Kimura S., Nebert D.W.; RT "Comparison of the flanking regions and introns of the mouse 2,3,7,8- RT tetrachlorodibenzo-p-dioxin-inducible cytochrome P1-450 and P3-450 RT genes."; RL J. Biol. Chem. 260:5040-5049(1985). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=C57BL/6; RX PubMed=3308449; RA Kimura S., Smith H.H., Hankinson O., Nebert D.W.; RT "Analysis of two benzo[a]pyrene-resistant mutants of the mouse RT hepatoma Hepa-1 P(1)450 gene via cDNA expression in yeast."; RL EMBO J. 6:1929-1933(1987). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=6548461; DOI=10.1016/0378-1119(84)90057-X; RA Gonzalez F.J., McKenzie P.I., Kimura S., Nebert D.W.; RT "Isolation and characterization of full-length mouse cDNA and genomic RT clones of 3-methylcholanthrene-inducible cytochrome P1-450 and P3- RT 450."; RL Gene 29:281-292(1984). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Liver; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [6] RP PROTEIN SEQUENCE OF 2-25. RC STRAIN=C57BL/6; RX PubMed=3718958; DOI=10.1021/bi00357a015; RA Cheng K.C., Park S.S., Krutzsch H.C., Grantham P.H., Gelboin H.V., RA Friedman F.K.; RT "Amino-terminal sequence and structure of monoclonal antibody RT immunopurified cytochromes P-450."; RL Biochemistry 25:2397-2402(1986). RN [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 280-321. RX PubMed=2425809; DOI=10.1016/0006-2952(86)90577-0; RA Peterson T.C., Gonzalez F.J., Nebert D.W.; RT "Methylation differences in the murine P-1-450 and P-3-450 genes in RT wild-type and mutant hepatoma cell culture."; RL Biochem. Pharmacol. 35:2107-2114(1986). CC -!- FUNCTION: Cytochromes P450 are a group of heme-thiolate CC monooxygenases. In liver microsomes, this enzyme is involved in an CC NADPH-dependent electron transport pathway. It oxidizes a variety CC of structurally unrelated compounds, including steroids, fatty CC acids, and xenobiotics. CC -!- CATALYTIC ACTIVITY: RH + reduced flavoprotein + O(2) = ROH + CC oxidized flavoprotein + H(2)O. CC -!- COFACTOR: Heme group (By similarity). CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral CC membrane protein. Microsome membrane; Peripheral membrane protein. CC -!- INDUCTION: By 3-methylcholanthrene (3MC). CC -!- SIMILARITY: Belongs to the cytochrome P450 family. CC -!- SEQUENCE CAUTION: CC Sequence=AAA37506.1; Type=Erroneous initiation; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; Y00071; CAA68277.1; -; mRNA. DR EMBL; X01681; CAA25836.1; -; Genomic_DNA. DR EMBL; K02588; AAA37506.1; ALT_INIT; mRNA. DR EMBL; M10021; AAA37507.1; -; Genomic_DNA. DR EMBL; AK005000; BAB23734.1; -; mRNA. DR EMBL; M25623; AAA39868.1; -; Genomic_DNA. DR PIR; A23923; O4MSM1. DR RefSeq; NP_001129531.1; NM_001136059.2. DR RefSeq; NP_034122.1; NM_009992.4. DR RefSeq; XP_006510873.1; XM_006510810.1. DR UniGene; Mm.14089; -. DR ProteinModelPortal; P00184; -. DR SMR; P00184; 40-516. DR ChEMBL; CHEMBL6171; -. DR PhosphoSite; P00184; -. DR PaxDb; P00184; -. DR PRIDE; P00184; -. DR Ensembl; ENSMUST00000034865; ENSMUSP00000034865; ENSMUSG00000032315. DR GeneID; 13076; -. DR KEGG; mmu:13076; -. DR UCSC; uc009pvn.3; mouse. DR CTD; 1543; -. DR MGI; MGI:88588; Cyp1a1. DR eggNOG; COG2124; -. DR HOGENOM; HOG000036991; -. DR HOVERGEN; HBG106944; -. DR InParanoid; P00184; -. DR KO; K07408; -. DR OrthoDB; EOG7RBZ85; -. DR TreeFam; TF105095; -. DR NextBio; 283020; -. DR PRO; PR:P00184; -. DR ArrayExpress; P00184; -. DR Bgee; P00184; -. DR Genevestigator; P00184; -. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl. DR GO; GO:0070330; F:aromatase activity; IEA:UniProtKB-EC. DR GO; GO:0032451; F:demethylase activity; IEA:Ensembl. DR GO; GO:0016711; F:flavonoid 3'-monooxygenase activity; IEA:Ensembl. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0016679; F:oxidoreductase activity, acting on diphenols and related substances as donors; IEA:Ensembl. DR GO; GO:0016712; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen; IDA:MGI. DR GO; GO:0008395; F:steroid hydroxylase activity; IEA:Ensembl. DR GO; GO:0070576; F:vitamin D 24-hydroxylase activity; IEA:Ensembl. DR GO; GO:0042904; P:9-cis-retinoic acid biosynthetic process; IEA:Ensembl. DR GO; GO:0007568; P:aging; IEA:Ensembl. DR GO; GO:0009308; P:amine metabolic process; IMP:MGI. DR GO; GO:0043010; P:camera-type eye development; IEA:Ensembl. DR GO; GO:0008283; P:cell proliferation; IEA:Ensembl. DR GO; GO:0009804; P:coumarin metabolic process; IEA:Ensembl. DR GO; GO:0048565; P:digestive tract development; IEA:Ensembl. DR GO; GO:0017144; P:drug metabolic process; IEA:Ensembl. DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IEA:Ensembl. DR GO; GO:0009812; P:flavonoid metabolic process; IEA:Ensembl. DR GO; GO:0070365; P:hepatocyte differentiation; IEA:Ensembl. DR GO; GO:0046483; P:heterocycle metabolic process; IMP:MGI. DR GO; GO:0050665; P:hydrogen peroxide biosynthetic process; IMP:MGI. DR GO; GO:0017143; P:insecticide metabolic process; IEA:Ensembl. DR GO; GO:0060137; P:maternal process involved in parturition; IEA:Ensembl. DR GO; GO:0006778; P:porphyrin-containing compound metabolic process; IEA:Ensembl. DR GO; GO:1900087; P:positive regulation of G1/S transition of mitotic cell cycle; IEA:Ensembl. DR GO; GO:0046677; P:response to antibiotic; IEA:Ensembl. DR GO; GO:0046685; P:response to arsenic-containing substance; IEA:Ensembl. DR GO; GO:0042493; P:response to drug; IEA:Ensembl. DR GO; GO:0032094; P:response to food; IEA:Ensembl. DR GO; GO:0009635; P:response to herbicide; IEA:Ensembl. DR GO; GO:0055093; P:response to hyperoxia; IEA:Ensembl. DR GO; GO:0001666; P:response to hypoxia; IEA:Ensembl. DR GO; GO:0010041; P:response to iron(III) ion; IEA:Ensembl. DR GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl. DR GO; GO:0009624; P:response to nematode; IEA:Ensembl. DR GO; GO:0014070; P:response to organic cyclic compound; IEA:Ensembl. DR GO; GO:0009636; P:response to toxic substance; IMP:MGI. DR GO; GO:0009615; P:response to virus; IEA:Ensembl. DR GO; GO:0033189; P:response to vitamin A; IEA:Ensembl. DR GO; GO:0009611; P:response to wounding; IEA:Ensembl. DR GO; GO:0009404; P:toxin metabolic process; IMP:MGI. DR Gene3D; 1.10.630.10; -; 1. DR InterPro; IPR001128; Cyt_P450. DR InterPro; IPR017972; Cyt_P450_CS. DR InterPro; IPR002401; Cyt_P450_E_grp-I. DR InterPro; IPR008066; Cyt_P450_E_grp-I_CYP1. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00463; EP450I. DR PRINTS; PR01683; EP450ICYP1A. DR PRINTS; PR00385; P450. DR SUPFAM; SSF48264; SSF48264; 1. DR PROSITE; PS00086; CYTOCHROME_P450; 1. PE 1: Evidence at protein level; KW Complete proteome; Direct protein sequencing; Endoplasmic reticulum; KW Heme; Iron; Membrane; Metal-binding; Microsome; Monooxygenase; KW Oxidoreductase; Reference proteome. FT CHAIN 1 524 Cytochrome P450 1A1. FT /FTId=PRO_0000051631. FT METAL 461 461 Iron (heme axial ligand) (By similarity). FT BINDING 228 228 Substrate (By similarity). SQ SEQUENCE 524 AA; 59230 MW; E31D9E9CBA7B2B02 CRC64; MPSMYGLPAF VSATELLLAV TVFCLGFWVV RATRTWVPKG LKTPPGPWGL PFIGHMLTVG KNPHLSLTRL SQQYGDVLQI RIGSTPVVVL SGLNTIKQAL VRQGDDFKGR PDLYSFTLIT NGKSMTFNPD SGPVWAARRR LAQNALKSFS IASDPTSASS CYLEEHVSKE ANYLVSKLQK VMAEVGHFDP YKYLVVSVAN VICAICFGQR YDHDDQELLS IVNLSNEFGE VTGSGYPADF IPVLRYLPNS SLDAFKDLND KFYSFMKKLI KEHYRTFEKG HIRDITDSLI EHCQDRKLDE NANVQLSDDK VITIVLDLFG AGFDTVTTAI SWSLMYLVTN PRVQRKIQEE LDTVIGRDRQ PRLSDRPQLP YLEAFILETF RHSSFVPFTI PHSTTRDTSL NGFYIPKGCC VFVNQWQVNH DRELWGDPNE FRPERFLTPS GTLDKRLSEK VTLFGLGKRK CIGETIGRSE VFLFLAILLQ QIEFKVSPGE KVDMTPTYGL TLKHARCEHF QVQMRSSGPQ HLQA // ID CP1A2_MOUSE Reviewed; 513 AA. AC P00186; Q9QWJ4; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 21-JUL-1986, sequence version 1. DT 19-FEB-2014, entry version 134. DE RecName: Full=Cytochrome P450 1A2; DE EC=1.14.14.1; DE AltName: Full=CYPIA2; DE AltName: Full=Cytochrome P450-P2; DE AltName: Full=Cytochrome P450-P3; GN Name=Cyp1a2; Synonyms=Cyp1a-2; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (P3). RC STRAIN=C57BL/6N; RX PubMed=6547952; RA Kimura S., Gonzalez F.J., Nebert D.W.; RT "The murine Ah locus. Comparison of the complete cytochrome P1-450 and RT P3-450 cDNA nucleotide and amino acid sequences."; RL J. Biol. Chem. 259:10705-10713(1984). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (P3). RC STRAIN=C57BL/6N; RX PubMed=6324134; DOI=10.1093/nar/12.6.2917; RA Kimura S., Gonzalez F.J., Nebert D.W.; RT "Mouse cytochrome P3-450: complete cDNA and amino acid sequence."; RL Nucleic Acids Res. 12:2917-2928(1984). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (P3). RX PubMed=3988744; RA Gonzalez F.J., Kimura S., Nebert D.W.; RT "Comparison of the flanking regions and introns of the mouse 2,3,7,8- RT tetrachlorodibenzo-p-dioxin-inducible cytochrome P1-450 and P3-450 RT genes."; RL J. Biol. Chem. 260:5040-5049(1985). RN [4] RP ERRATUM. RA Gonzalez F.J., Kimura S., Nebert D.W.; RL J. Biol. Chem. 260:11884-11889(1985). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (P3). RX PubMed=6548461; DOI=10.1016/0378-1119(84)90057-X; RA Gonzalez F.J., McKenzie P.I., Kimura S., Nebert D.W.; RT "Isolation and characterization of full-length mouse cDNA and genomic RT clones of 3-methylcholanthrene-inducible cytochrome P1-450 and P3- RT 450."; RL Gene 29:281-292(1984). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] (P2). RC STRAIN=DBA/2N; TISSUE=Liver; RX PubMed=3755821; DOI=10.1093/nar/14.16.6765; RA Kimura S., Nebert D.W.; RT "cDNA and complete amino acid sequence of mouse P2(450): allelic RT variant of mouse P3(450) gene."; RL Nucleic Acids Res. 14:6765-6766(1986). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (P3). RC TISSUE=Liver; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [8] RP PROTEIN SEQUENCE OF 2-26. RC STRAIN=DBA/2; RX PubMed=3718958; DOI=10.1021/bi00357a015; RA Cheng K.C., Park S.S., Krutzsch H.C., Grantham P.H., Gelboin H.V., RA Friedman F.K.; RT "Amino-terminal sequence and structure of monoclonal antibody RT immunopurified cytochromes P-450."; RL Biochemistry 25:2397-2402(1986). RN [9] RP NUCLEOTIDE SEQUENCE [MRNA] OF 277-315. RX PubMed=2425809; DOI=10.1016/0006-2952(86)90577-0; RA Peterson T.C., Gonzalez F.J., Nebert D.W.; RT "Methylation differences in the murine P-1-450 and P-3-450 genes in RT wild-type and mutant hepatoma cell culture."; RL Biochem. Pharmacol. 35:2107-2114(1986). CC -!- FUNCTION: Cytochromes P450 are a group of heme-thiolate CC monooxygenases. In liver microsomes, this enzyme is involved in an CC NADPH-dependent electron transport pathway. It oxidizes a variety CC of structurally unrelated compounds, including steroids, fatty CC acids, and xenobiotics. Most active in catalyzing 2-hydroxylation CC (By similarity). CC -!- CATALYTIC ACTIVITY: RH + reduced flavoprotein + O(2) = ROH + CC oxidized flavoprotein + H(2)O. CC -!- COFACTOR: Heme group (By similarity). CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral CC membrane protein. Microsome membrane; Peripheral membrane protein. CC -!- INDUCTION: By 3-methylcholanthrene (3MC). CC -!- SIMILARITY: Belongs to the cytochrome P450 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X01682; CAA25837.1; -; Genomic_DNA. DR EMBL; X00479; CAA25156.1; -; mRNA. DR EMBL; X04283; CAA27832.1; -; mRNA. DR EMBL; K02589; AAA37509.1; ALT_SEQ; mRNA. DR EMBL; M10022; AAA37508.1; -; Genomic_DNA. DR EMBL; BC018298; AAH18298.1; -; mRNA. DR EMBL; BC054827; AAH54827.1; -; mRNA. DR PIR; B92495; O4MSM3. DR RefSeq; NP_034123.1; NM_009993.3. DR UniGene; Mm.15537; -. DR ProteinModelPortal; P00186; -. DR SMR; P00186; 33-512. DR IntAct; P00186; 2. DR MINT; MINT-1870125; -. DR ChEMBL; CHEMBL1671611; -. DR PhosphoSite; P00186; -. DR PaxDb; P00186; -. DR PRIDE; P00186; -. DR Ensembl; ENSMUST00000034860; ENSMUSP00000034860; ENSMUSG00000032310. DR GeneID; 13077; -. DR KEGG; mmu:13077; -. DR UCSC; uc009pvm.1; mouse. DR CTD; 1544; -. DR MGI; MGI:88589; Cyp1a2. DR eggNOG; COG2124; -. DR GeneTree; ENSGT00720000108651; -. DR HOGENOM; HOG000036991; -. DR HOVERGEN; HBG106944; -. DR InParanoid; P00186; -. DR KO; K07409; -. DR OMA; VSKEANH; -. DR OrthoDB; EOG7RBZ85; -. DR TreeFam; TF105095; -. DR NextBio; 283024; -. DR PRO; PR:P00186; -. DR ArrayExpress; P00186; -. DR Bgee; P00186; -. DR Genevestigator; P00186; -. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0070330; F:aromatase activity; IEA:UniProtKB-EC. DR GO; GO:0034875; F:caffeine oxidase activity; IEA:Ensembl. DR GO; GO:0032451; F:demethylase activity; IEA:Ensembl. DR GO; GO:0020037; F:heme binding; ISS:UniProtKB. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0016712; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen; IDA:MGI. DR GO; GO:0009820; P:alkaloid metabolic process; IEA:Ensembl. DR GO; GO:0045333; P:cellular respiration; IMP:MGI. DR GO; GO:0071276; P:cellular response to cadmium ion; IDA:MGI. DR GO; GO:0018894; P:dibenzo-p-dioxin metabolic process; IMP:MGI. DR GO; GO:0017144; P:drug metabolic process; IMP:MGI. DR GO; GO:0042738; P:exogenous drug catabolic process; IEA:Ensembl. DR GO; GO:0050665; P:hydrogen peroxide biosynthetic process; IMP:MGI. DR GO; GO:0030324; P:lung development; IMP:MGI. DR GO; GO:0032787; P:monocarboxylic acid metabolic process; IEA:Ensembl. DR GO; GO:0016098; P:monoterpenoid metabolic process; IEA:Ensembl. DR GO; GO:0071615; P:oxidative deethylation; IEA:Ensembl. DR GO; GO:0070989; P:oxidative demethylation; IEA:Ensembl. DR GO; GO:0006778; P:porphyrin-containing compound metabolic process; IMP:MGI. DR GO; GO:0009791; P:post-embryonic development; IMP:MGI. DR GO; GO:0010468; P:regulation of gene expression; IMP:MGI. DR GO; GO:0032355; P:response to estradiol; IEA:Ensembl. DR GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl. DR GO; GO:0006706; P:steroid catabolic process; IEA:Ensembl. DR GO; GO:0009403; P:toxin biosynthetic process; IEA:Ensembl. DR GO; GO:0009404; P:toxin metabolic process; IMP:MGI. DR Gene3D; 1.10.630.10; -; 1. DR InterPro; IPR001128; Cyt_P450. DR InterPro; IPR017972; Cyt_P450_CS. DR InterPro; IPR002401; Cyt_P450_E_grp-I. DR InterPro; IPR008066; Cyt_P450_E_grp-I_CYP1. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00463; EP450I. DR PRINTS; PR01683; EP450ICYP1A. DR PRINTS; PR00385; P450. DR SUPFAM; SSF48264; SSF48264; 1. DR PROSITE; PS00086; CYTOCHROME_P450; 1. PE 1: Evidence at protein level; KW Complete proteome; Direct protein sequencing; Endoplasmic reticulum; KW Heme; Iron; Membrane; Metal-binding; Microsome; Monooxygenase; KW Oxidoreductase; Polymorphism; Reference proteome. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 513 Cytochrome P450 1A2. FT /FTId=PRO_0000051654. FT METAL 456 456 Iron (heme axial ligand). FT BINDING 225 225 Substrate (By similarity). FT VARIANT 384 384 I -> M (in P2). SQ SEQUENCE 513 AA; 58184 MW; DC2D7D976B126E3B CRC64; MAFSQYISLA PELLLATAIF CLVFWMVRAS RTQVPKGLKN PPGPWGLPFI GHMLTVGKNP HLSLTRLSQQ YGDVLQIRIG STPVVVLSGL NTIKQALVRQ GDDFKGRPDL YSFTLITNGK SMTFNPDSGP VWAARRRLAQ DALKSFSIAS DPTSASSCYL EEHVSKEANH LVSKLQKAMA EVGHFEPVSQ VVESVANVIG AMCFGKNFPR KSEEMLNIVN NSKDFVENVT SGNAVDFFPV LRYLPNPALK RFKTFNDNFV LFLQKTVQEH YQDFNKNSIQ DITSALFKHS ENYKDNGGLI PEEKIVNIVN DIFGAGFDTV TTAITWSILL LVTWPNVQRK IHEELDTVVG RDRQPRLSDR PQLPYLEAFI LEIYRYTSFV PFTIPHSTTR DTSLNGFHIP KERCIYINQW QVNHDEKQWK DPFVFRPERF LTNNNSAIDK TQSEKVMLFG LGKRRCIGEI PAKWEVFLFL AILLQHLEFS VPPGVKVDLT PNYGLTMKPG TCEHVQAWPR FSK // ID CP1B1_MOUSE Reviewed; 543 AA. AC Q64429; Q3UVA8; Q60593; Q64461; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 3. DT 19-FEB-2014, entry version 117. DE RecName: Full=Cytochrome P450 1B1; DE EC=1.14.14.1; DE AltName: Full=CYPIB1; DE AltName: Full=Cytochrome P450CMEF; DE Short=Cytochrome P450EF; GN Name=Cyp1b1; Synonyms=Cyp1-b1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=C3H; RX PubMed=7772257; DOI=10.1089/dna.1994.13.763; RA Shen Z., Liu J., Wells R.L., Elkind M.M.; RT "cDNA cloning, sequence analysis, and induction by aryl hydrocarbons RT of a murine cytochrome P450 gene, Cyp1b1."; RL DNA Cell Biol. 13:763-769(1994). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=C3H; RX PubMed=8195121; RA Savas U., Bhattacharyya K.K., Christou M., Alexander D.L., RA Jefcoate C.R.; RT "Mouse cytochrome P-450EF, representative of a new 1B subfamily of RT cytochrome P-450s. Cloning, sequence determination, and tissue RT expression."; RL J. Biol. Chem. 269:14905-14911(1994). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Bone; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 361-466. RX PubMed=7505439; DOI=10.1073/pnas.90.24.11483; RA Shen Z., Wells R.L., Liu J., Elkind M.M.; RT "Identification of a cytochrome P450 gene by reverse transcription-PCR RT using degenerate primers containing inosine."; RL Proc. Natl. Acad. Sci. U.S.A. 90:11483-11487(1993). CC -!- FUNCTION: Cytochromes P450 are a group of heme-thiolate CC monooxygenases. In liver microsomes, this enzyme is involved in an CC NADPH-dependent electron transport pathway. It oxidizes a variety CC of structurally unrelated compounds, including steroids, fatty CC acids, and xenobiotics. CC -!- CATALYTIC ACTIVITY: RH + reduced flavoprotein + O(2) = ROH + CC oxidized flavoprotein + H(2)O. CC -!- COFACTOR: Heme group (By similarity). CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral CC membrane protein. Microsome membrane; Peripheral membrane protein. CC -!- INDUCTION: By polycyclic aromatic hydrocarbons (PAH) and 2,3,7,8- CC tetrachlorodibenzo-p-dioxin (TCDD). CC -!- SIMILARITY: Belongs to the cytochrome P450 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U03283; AAC52141.1; -; mRNA. DR EMBL; X78445; CAA55205.1; -; mRNA. DR EMBL; AK137461; BAE23362.1; -; mRNA. DR EMBL; CH466537; EDL38490.1; -; Genomic_DNA. DR EMBL; U02479; AAC52131.1; -; mRNA. DR PIR; A53790; A53790. DR RefSeq; NP_034124.1; NM_009994.1. DR UniGene; Mm.214016; -. DR ProteinModelPortal; Q64429; -. DR SMR; Q64429; 68-530. DR PhosphoSite; Q64429; -. DR PaxDb; Q64429; -. DR PRIDE; Q64429; -. DR Ensembl; ENSMUST00000024894; ENSMUSP00000024894; ENSMUSG00000024087. DR GeneID; 13078; -. DR KEGG; mmu:13078; -. DR UCSC; uc008dqc.1; mouse. DR CTD; 1545; -. DR MGI; MGI:88590; Cyp1b1. DR eggNOG; COG2124; -. DR GeneTree; ENSGT00720000108651; -. DR HOGENOM; HOG000036991; -. DR HOVERGEN; HBG106944; -. DR InParanoid; Q3UVA8; -. DR KO; K07410; -. DR OMA; NEPSKMS; -. DR OrthoDB; EOG7RBZ85; -. DR TreeFam; TF105095; -. DR NextBio; 283028; -. DR PRO; PR:Q64429; -. DR ArrayExpress; Q64429; -. DR Bgee; Q64429; -. DR Genevestigator; Q64429; -. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0070330; F:aromatase activity; IEA:UniProtKB-EC. DR GO; GO:0020037; F:heme binding; ISS:UniProtKB. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0016712; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen; IDA:MGI. DR GO; GO:0001525; P:angiogenesis; IMP:MGI. DR GO; GO:0006725; P:cellular aromatic compound metabolic process; IDA:MGI. DR GO; GO:0043542; P:endothelial cell migration; IMP:MGI. DR GO; GO:0071603; P:endothelial cell-cell adhesion; IMP:MGI. DR GO; GO:0009636; P:response to toxic substance; IMP:MGI. DR GO; GO:0061298; P:retina vasculature development in camera-type eye; IMP:MGI. DR GO; GO:0008202; P:steroid metabolic process; ISS:UniProtKB. DR GO; GO:0009404; P:toxin metabolic process; IMP:MGI. DR GO; GO:0006805; P:xenobiotic metabolic process; ISS:UniProtKB. DR Gene3D; 1.10.630.10; -; 1. DR InterPro; IPR001128; Cyt_P450. DR InterPro; IPR017972; Cyt_P450_CS. DR InterPro; IPR002401; Cyt_P450_E_grp-I. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00463; EP450I. DR PRINTS; PR00385; P450. DR SUPFAM; SSF48264; SSF48264; 1. DR PROSITE; PS00086; CYTOCHROME_P450; 1. PE 2: Evidence at transcript level; KW Complete proteome; Endoplasmic reticulum; Heme; Iron; Membrane; KW Metal-binding; Microsome; Monooxygenase; Oxidoreductase; KW Reference proteome. FT CHAIN 1 543 Cytochrome P450 1B1. FT /FTId=PRO_0000051661. FT METAL 470 470 Iron (heme axial ligand) (By similarity). FT CONFLICT 195 195 Q -> P (in Ref. 2; CAA55205). FT CONFLICT 307 307 A -> D (in Ref. 2; CAA55205). FT CONFLICT 328 328 F -> G (in Ref. 2; CAA55205). FT CONFLICT 457 457 A -> T (in Ref. 2; CAA55205). FT CONFLICT 516 516 F -> V (in Ref. 2; CAA55205). SQ SEQUENCE 543 AA; 60537 MW; 7C89B4312CB5BC4A CRC64; MATSLSADSP QQLSSLSTQQ TTLLLLFSVL AAVHLGQWLL RQWQRKPWSS PPGPFPWPLI GNAAAVGQAS HLYFARLARR YGDVFQIRLG SCPVVVLNGE SAIHQALVQQ GSIFADRPPF ASFRVVSGGR SLAFGHYSEH WKTQRRSAYS TMRAFSTRHP RSRGLLEGHA LAEARELVAV LVRRCAGGAF LDPTQPVIVA VANVMSAVCF GCRYNHDDAE FLELLSHNEE FGRTVGAGSL VDVLPWLQLF PNPVRTTFRK FEQLNRNFSN FVLDKFLRHR ESLVPGAAPR DMTDAFILSA EKKASGAPGD DSSGLDLEDV PATITDIFGA SQDTLSTALL WLLILFTRYP DVQARVQAEL DQVVGRDRLP CMSDQPNLPY VMAFLYESMR FSSFLPVTIP HATTANTFVL GYYIPKNTVV FVNQWSVNHD PAKWPNPEDF DPARFLDKDG FINKALASSV MIFSVGKRRC IGEELSKMLL FLFISILAHQ CNFKANQNES SNMSFSYGLT IKPKSFRIHV SLRESMELLD NAVKKLQTEE GCK // ID CP237_MOUSE Reviewed; 490 AA. AC P56654; E9QKN4; DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 2. DT 19-FEB-2014, entry version 107. DE RecName: Full=Cytochrome P450 2C37; DE EC=1.14.14.1; DE AltName: Full=CYPIIC37; GN Name=Cyp2c37; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=CD-1; RX PubMed=9721182; DOI=10.1006/abbi.1998.0806; RA Luo G., Zeldin D.C., Blaisdell J.A., Hodgson E., Goldstein J.A.; RT "Cloning and expression of murine CYP2Cs and their ability to RT metabolize arachidonic acid."; RL Arch. Biochem. Biophys. 357:45-57(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Liver; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: Metabolizes arachidonic acid to produce 12- CC hydroxyeicosatetraenoic acid (HETE). CC -!- CATALYTIC ACTIVITY: RH + reduced flavoprotein + O(2) = ROH + CC oxidized flavoprotein + H(2)O. CC -!- COFACTOR: Heme group (By similarity). CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral CC membrane protein. Microsome membrane; Peripheral membrane protein. CC -!- TISSUE SPECIFICITY: Liver. CC -!- INDUCTION: P450 can be induced to high levels in liver and other CC tissues by various foreign compounds, including drugs, pesticides, CC and carcinogens. CC -!- SIMILARITY: Belongs to the cytochrome P450 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF047542; AAD13719.1; -; mRNA. DR EMBL; AC148014; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC057912; AAH57912.1; -; mRNA. DR RefSeq; NP_034131.2; NM_010001.2. DR UniGene; Mm.38963; -. DR ProteinModelPortal; P56654; -. DR SMR; P56654; 30-489. DR IntAct; P56654; 2. DR MINT; MINT-1863877; -. DR STRING; 10090.ENSMUSP00000045362; -. DR PhosphoSite; P56654; -. DR PaxDb; P56654; -. DR PRIDE; P56654; -. DR Ensembl; ENSMUST00000049178; ENSMUSP00000045362; ENSMUSG00000042248. DR GeneID; 13096; -. DR KEGG; mmu:13096; -. DR UCSC; uc008hkf.2; mouse. DR CTD; 13096; -. DR MGI; MGI:1306806; Cyp2c37. DR eggNOG; COG2124; -. DR GeneTree; ENSGT00680000099783; -. DR HOGENOM; HOG000036992; -. DR HOVERGEN; HBG015789; -. DR InParanoid; P56654; -. DR KO; K07413; -. DR OrthoDB; EOG7RBZ85; -. DR TreeFam; TF352043; -. DR ChiTaRS; Cyp2c37; mouse. DR NextBio; 283078; -. DR PRO; PR:P56654; -. DR Bgee; P56654; -. DR Genevestigator; P56654; -. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0070330; F:aromatase activity; IEA:UniProtKB-EC. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR Gene3D; 1.10.630.10; -; 1. DR InterPro; IPR001128; Cyt_P450. DR InterPro; IPR017972; Cyt_P450_CS. DR InterPro; IPR002401; Cyt_P450_E_grp-I. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00463; EP450I. DR PRINTS; PR00385; P450. DR SUPFAM; SSF48264; SSF48264; 1. DR PROSITE; PS00086; CYTOCHROME_P450; 1. PE 2: Evidence at transcript level; KW Complete proteome; Endoplasmic reticulum; Heme; Iron; Membrane; KW Metal-binding; Microsome; Monooxygenase; Oxidoreductase; KW Reference proteome. FT CHAIN 1 490 Cytochrome P450 2C37. FT /FTId=PRO_0000051720. FT METAL 435 435 Iron (heme axial ligand) (By similarity). FT CONFLICT 239 239 S -> C (in Ref. 1; AAD13719 and 3; FT AAH57912). FT CONFLICT 310 310 I -> L (in Ref. 1; AAD13719 and 3; FT AAH57912). FT CONFLICT 325 325 E -> K (in Ref. 1; AAD13719 and 3; FT AAH57912). FT CONFLICT 372 372 S -> C (in Ref. 1; AAD13719 and 3; FT AAH57912). FT CONFLICT 406 406 K -> V (in Ref. 1; AAD13719 and 3; FT AAH57912). FT CONFLICT 415 415 E -> G (in Ref. 1; AAD13719 and 3; FT AAH57912). FT CONFLICT 426 426 I -> M (in Ref. 1; AAD13719 and 3; FT AAH57912). FT CONFLICT 455 455 N -> S (in Ref. 1; AAD13719 and 3; FT AAH57912). FT CONFLICT 477 477 A -> G (in Ref. 1; AAD13719 and 3; FT AAH57912). SQ SEQUENCE 490 AA; 55606 MW; 9623AACA4B5E5DBD CRC64; MDPILVLVLT LSCLFLLSLW RQSSERGKLP PGPTPLPIIG NILQIDVKDI CQSFTNLSKV YGPVYTLYLG RKPTVVLHGY EAVKEALVDH GEEFAGRGRF PVFDKATNGM GLAFSKGNVW KNTRRFSLMT LRNLGMGKRS IEDRVQEEAR CLVEELRKTN GSPCDPTFIL GCAPCNVICS IIFQDRFDYK DRDFLNLMEK LNEITKILSS PWLQICNTYP ALLDYCPGSH KQFFKNYASI KNFLLEKIKE HEESLDVTIP RDFIDYFLIN GGQEDGNQPL QNRLEHLAIT VTDLFSAGTE TTSTTLRYAI LLLLKYPHVT AKVQEEIEHV IGKHRSPCMQ DRSRMPYTDA MIHEVQRFID LIPNSLPHEV TSDIKFRNYF IPKGTTVITS LSSVLHDSTE FPNPEKFDPG HFLDENGKFK KSDYFIPFST GKRICAGEGL ARMELFLFLT SILQNFNLKP LVHPKDIDVT PMLIGLASVP PAFQLCFIPS // ID CP239_MOUSE Reviewed; 490 AA. AC P56656; B9EIA6; G5E854; DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot. DT 03-OCT-2012, sequence version 2. DT 19-FEB-2014, entry version 95. DE RecName: Full=Cytochrome P450 2C39; DE EC=1.14.14.1; DE AltName: Full=CYPIIC39; GN Name=Cyp2c39; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=CD-1; RX PubMed=9721182; DOI=10.1006/abbi.1998.0806; RA Luo G., Zeldin D.C., Blaisdell J.A., Hodgson E., Goldstein J.A.; RT "Cloning and expression of murine CYP2Cs and their ability to RT metabolize arachidonic acid."; RL Arch. Biochem. Biophys. 357:45-57(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: Metabolizes arachidonic acid to produce 14,15-cis- CC epoxyeicosatrienoic acid (EET). CC -!- CATALYTIC ACTIVITY: RH + reduced flavoprotein + O(2) = ROH + CC oxidized flavoprotein + H(2)O. CC -!- COFACTOR: Heme group (By similarity). CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral CC membrane protein. Microsome membrane; Peripheral membrane protein. CC -!- TISSUE SPECIFICITY: Liver. CC -!- INDUCTION: P450 can be induced to high levels in liver and other CC tissues by various foreign compounds, including drugs, pesticides, CC and carcinogens. CC -!- SIMILARITY: Belongs to the cytochrome P450 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF047726; AAD13721.1; -; mRNA. DR EMBL; AC117790; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC139233; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH466534; EDL41819.1; -; Genomic_DNA. DR EMBL; BC139290; AAI39291.1; -; mRNA. DR EMBL; BC139291; AAI39292.1; -; mRNA. DR RefSeq; NP_034133.2; NM_010003.2. DR UniGene; Mm.42101; -. DR ProteinModelPortal; P56656; -. DR SMR; P56656; 30-489. DR IntAct; P56656; 2. DR MINT; MINT-1865726; -. DR PhosphoSite; P56656; -. DR PaxDb; P56656; -. DR PRIDE; P56656; -. DR Ensembl; ENSMUST00000025968; ENSMUSP00000025968; ENSMUSG00000025003. DR GeneID; 13098; -. DR KEGG; mmu:13098; -. DR UCSC; uc008hkb.2; mouse. DR CTD; 13098; -. DR MGI; MGI:1306818; Cyp2c39. DR eggNOG; COG2124; -. DR GeneTree; ENSGT00680000099783; -. DR HOVERGEN; HBG015789; -. DR InParanoid; P56656; -. DR KO; K07413; -. DR OMA; SHENLAC; -. DR OrthoDB; EOG7RBZ85; -. DR TreeFam; TF352043; -. DR SABIO-RK; P56656; -. DR NextBio; 283086; -. DR PRO; PR:P56656; -. DR Genevestigator; P56656; -. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0070330; F:aromatase activity; IEA:UniProtKB-EC. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR Gene3D; 1.10.630.10; -; 1. DR InterPro; IPR001128; Cyt_P450. DR InterPro; IPR017972; Cyt_P450_CS. DR InterPro; IPR002401; Cyt_P450_E_grp-I. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00463; EP450I. DR PRINTS; PR00385; P450. DR SUPFAM; SSF48264; SSF48264; 1. DR PROSITE; PS00086; CYTOCHROME_P450; 1. PE 2: Evidence at transcript level; KW Complete proteome; Endoplasmic reticulum; Heme; Iron; Membrane; KW Metal-binding; Microsome; Monooxygenase; Oxidoreductase; KW Reference proteome. FT CHAIN 1 490 Cytochrome P450 2C39. FT /FTId=PRO_0000051722. FT METAL 435 435 Iron (heme axial ligand) (By similarity). FT CONFLICT 47 47 I -> M (in Ref. 1; AAD13721 and 4; FT AAI39291/AAI39292). FT CONFLICT 50 50 V -> F (in Ref. 1; AAD13721 and 4; FT AAI39291/AAI39292). FT CONFLICT 460 460 S -> P (in Ref. 1; AAD13721 and 4; FT AAI39291/AAI39292). SQ SEQUENCE 490 AA; 55827 MW; EE583A2B53CFC410 CRC64; MDLVTFLVLT LSSLILLSLW RQSCGRGSLP PGPTPFPIIG NFLQIDIKNV SQSLTNFSKA YGPVFTLYLG SRPTVVLHGY EAVKEALIDH GEEFSDRGSI PMVEKINNGL GIVFSNGNRW KEIRRFTLTT LRNLGMGKRN IEDRVQEEAQ CLVEELRKTK GSPCDPTFIL SCAPCNVICS IIFQDRFDYK DKDFLMLMEK LNENVKILSS PWLQVCNNFP LLIDYCPGSH HKVLKNVKYI RSYLLEKIKE HQESLDVTNP RDFIDYYLIK QKQANHIQQA EFSLENLACT INNLFAAGTE TTSTTLRYAL LLLMKYPDVT AKVQEEIDHV IGRHRSPCMQ DRNHMPYTDA MIHEVQRFIN LVPNNIPRAV TCDIKFRNYL IPKGTTVVTS LTSVLHDSKE FPNPELFDPG HFLDANGNFK KSDHFMPFSA GKRVCAGEGL ARMELFLFLT TILQNFKLKS LVHPKDIDMI PFVNGLIALP PHYQVCIIPR // ID CP240_MOUSE Reviewed; 491 AA. AC P56657; B2RTP3; DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 2. DT 22-JAN-2014, entry version 101. DE RecName: Full=Cytochrome P450 2C40; DE EC=1.14.14.1; DE AltName: Full=CYPIIC40; GN Name=Cyp2c40; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=CD-1; RX PubMed=9721182; DOI=10.1006/abbi.1998.0806; RA Luo G., Zeldin D.C., Blaisdell J.A., Hodgson E., Goldstein J.A.; RT "Cloning and expression of murine CYP2Cs and their ability to RT metabolize arachidonic acid."; RL Arch. Biochem. Biophys. 357:45-57(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: Metabolizes arachidonic acid to produce an unidentified CC metabolite that coelutes with 16-,17-, and 18- CC hydroxyeicosatetraenoic acid (HETE). CC -!- CATALYTIC ACTIVITY: RH + reduced flavoprotein + O(2) = ROH + CC oxidized flavoprotein + H(2)O. CC -!- COFACTOR: Heme group (By similarity). CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral CC membrane protein. Microsome membrane; Peripheral membrane protein. CC -!- TISSUE SPECIFICITY: Liver, brain, kidney, and intestine, with CC trace amounts in lung and heart. CC -!- INDUCTION: P450 can be induced to high levels in liver and other CC tissues by various foreign compounds, including drugs, pesticides, CC and carcinogens. CC -!- SIMILARITY: Belongs to the cytochrome P450 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF047727; AAD13722.1; -; mRNA. DR EMBL; BC139471; AAI39472.1; -; mRNA. DR EMBL; BC139472; AAI39473.1; -; mRNA. DR RefSeq; NP_034134.2; NM_010004.2. DR UniGene; Mm.353875; -. DR ProteinModelPortal; P56657; -. DR SMR; P56657; 30-490. DR IntAct; P56657; 2. DR MINT; MINT-1863844; -. DR STRING; 10090.ENSMUSP00000025969; -. DR PhosphoSite; P56657; -. DR PaxDb; P56657; -. DR PRIDE; P56657; -. DR GeneID; 13099; -. DR KEGG; mmu:13099; -. DR CTD; 13099; -. DR MGI; MGI:1306815; Cyp2c40. DR eggNOG; COG2124; -. DR HOGENOM; HOG000036992; -. DR HOVERGEN; HBG015789; -. DR InParanoid; B2RTP3; -. DR KO; K07413; -. DR NextBio; 283090; -. DR PRO; PR:P56657; -. DR ArrayExpress; P56657; -. DR Bgee; P56657; -. DR Genevestigator; P56657; -. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0070330; F:aromatase activity; IEA:UniProtKB-EC. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR Gene3D; 1.10.630.10; -; 1. DR InterPro; IPR001128; Cyt_P450. DR InterPro; IPR017972; Cyt_P450_CS. DR InterPro; IPR002401; Cyt_P450_E_grp-I. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00463; EP450I. DR PRINTS; PR00385; P450. DR SUPFAM; SSF48264; SSF48264; 1. DR PROSITE; PS00086; CYTOCHROME_P450; 1. PE 2: Evidence at transcript level; KW Complete proteome; Endoplasmic reticulum; Heme; Iron; Membrane; KW Metal-binding; Microsome; Monooxygenase; Oxidoreductase; KW Reference proteome. FT CHAIN 1 491 Cytochrome P450 2C40. FT /FTId=PRO_0000051723. FT METAL 435 435 Iron (heme axial ligand) (By similarity). FT CONFLICT 382 382 P -> L (in Ref. 1; AAD13722). SQ SEQUENCE 491 AA; 55763 MW; 2F4CCEC2F219EA4F CRC64; MDPFVVLVLC LSFLLVLSLW RQRSARGNLP PGPTPLPIIG NYHLIDMKDI GQCLTNFSKT YGPVFTLYFG SQPIVVLHGY EAIKEALIDH GEEFSGRGRI PVFDKVSTGK GIGFSHGNVW KATRVFTVNT LRNLGMGKRT IENKVQEEAQ WLMKELKKTN GSPCDPQFII GCAPCNVICS IVFQNRFDYK DKDFLSLIGK VNECTEILSS PGCQIFNAVP ILIDYCPGSH NKLFKNHTWI KSYLLGKIKE HEESLDVTNP RDFIDYFLIQ RRQKNGIEHM DYTIEHLATL VTDLVFGGTE TLSSTMRFAL LLLMKHTHIT AKVQEEIDNV IGRHRSPCMQ DRNHMPYTNA MVHEVQRYID LGPNGVVHEV TCDTKFRNYF IPKGTQVMTS LTSVLHDSTE FPNPEVFDPG HFLDDNGNFK KSDYFVPFSA GKRICVGESL ARMELFLFLT TILQNFKLKP LVDPKDIDMT PKHSGFSKIP PNFQMCFIPV E // ID CP21A_MOUSE Reviewed; 487 AA. AC P03940; A0JP50; O88304; Q64510; Q9QX14; DT 23-OCT-1986, integrated into UniProtKB/Swiss-Prot. DT 26-APR-2005, sequence version 3. DT 19-FEB-2014, entry version 123. DE RecName: Full=Steroid 21-hydroxylase; DE EC=1.14.99.10; DE AltName: Full=21-OHase; DE AltName: Full=Cytochrome P-450c21; DE AltName: Full=Cytochrome P450 21; DE AltName: Full=Cytochrome P450 XXI; DE AltName: Full=Cytochrome P450-C21; GN Name=Cyp21; Synonyms=Cyp21a-1, Cyp21a1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=3491986; DOI=10.1073/pnas.83.24.9601; RA Chaplin D.D., Galbraith L.J., Seidman J.G., White P.C., Parker K.L.; RT "Nucleotide sequence analysis of murine 21-hydroxylase genes: RT mutations affecting gene expression."; RL Proc. Natl. Acad. Sci. U.S.A. 83:9601-9605(1986). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=B10.WR; RX PubMed=1918990; RA Zepf N.E., Ogata R.T.; RT "The murine Slp gene: additional evidence that sex-limited protein has RT no biological function."; RL J. Immunol. 147:2756-2763(1991). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=C57BL/6 X CBA; RA Matsumoto K., Ikuta T.; RT "Mus musculus 5' truncated pseudogene of tenascin-X, steroid 21- RT hydroxylase (Cyp21), and sex-limited protein (Slp) genes, partial cds RT and complete sequences."; RL Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=129; RX PubMed=14656967; DOI=10.1101/gr.1736803; RA Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S., RA Campbell R.D., Hood L.; RT "Analysis of the gene-dense major histocompatibility complex class III RT region and its comparison to mouse."; RL Genome Res. 13:2621-2636(2003). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 399-487. RX PubMed=3874401; DOI=10.1073/pnas.82.13.4453; RA Amor M., Tosi M., Duponchel C., Steinmetz M., Meo T.; RT "Liver mRNA probes disclose two cytochrome P-450 genes duplicated in RT tandem with the complement C4 loci of the mouse H-2S region."; RL Proc. Natl. Acad. Sci. U.S.A. 82:4453-4457(1985). CC -!- FUNCTION: Specifically catalyzes the 21-hydroxylation of steroids. CC Required for the adrenal synthesis of mineralocorticoids and CC glucocorticoids. CC -!- CATALYTIC ACTIVITY: A C(21) steroid + (reduced NADPH--hemoprotein CC reductase) + O(2) = a 21-hydroxy-C(21)-steroid + (oxidized NADPH-- CC hemoprotein reductase) + H(2)O. CC -!- COFACTOR: Heme group (By similarity). CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral CC membrane protein. Microsome membrane; Peripheral membrane protein. CC -!- DOMAIN: The leucine-rich hydrophobic amino acid N-terminal region CC probably helps to anchor the protein to the microsomal membrane. CC -!- SIMILARITY: Belongs to the cytochrome P450 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M15009; AAA37114.1; -; Genomic_DNA. DR EMBL; M64933; AAA40118.1; -; Genomic_DNA. DR EMBL; AB015623; BAA31153.1; -; Genomic_DNA. DR EMBL; AF049850; AAC05278.1; -; Genomic_DNA. DR EMBL; BC127167; AAI27168.1; -; mRNA. DR PIR; A26660; A26660. DR PIR; S54785; S54785. DR RefSeq; NP_034125.2; NM_009995.2. DR UniGene; Mm.440407; -. DR ProteinModelPortal; P03940; -. DR SMR; P03940; 29-475. DR STRING; 10090.ENSMUSP00000025223; -. DR PhosphoSite; P03940; -. DR PRIDE; P03940; -. DR Ensembl; ENSMUST00000025223; ENSMUSP00000025223; ENSMUSG00000024365. DR GeneID; 13079; -. DR KEGG; mmu:13079; -. DR UCSC; uc008cdo.2; mouse. DR CTD; 13079; -. DR MGI; MGI:88591; Cyp21a1. DR eggNOG; COG2124; -. DR GeneTree; ENSGT00720000108419; -. DR HOVERGEN; HBG106944; -. DR InParanoid; A0JP50; -. DR KO; K00513; -. DR OrthoDB; EOG7BCNBG; -. DR TreeFam; TF105095; -. DR NextBio; 283032; -. DR PRO; PR:P03940; -. DR ArrayExpress; P03940; -. DR Bgee; P03940; -. DR Genevestigator; P03940; -. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0004509; F:steroid 21-monooxygenase activity; IEA:UniProtKB-EC. DR GO; GO:0005496; F:steroid binding; IEA:UniProtKB-KW. DR GO; GO:0006694; P:steroid biosynthetic process; IEA:UniProtKB-KW. DR Gene3D; 1.10.630.10; -; 1. DR InterPro; IPR001128; Cyt_P450. DR InterPro; IPR017972; Cyt_P450_CS. DR InterPro; IPR002401; Cyt_P450_E_grp-I. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00463; EP450I. DR PRINTS; PR00385; P450. DR SUPFAM; SSF48264; SSF48264; 1. DR PROSITE; PS00086; CYTOCHROME_P450; 1. PE 2: Evidence at transcript level; KW Complete proteome; Endoplasmic reticulum; Heme; Iron; Lipid-binding; KW Membrane; Metal-binding; Microsome; Monooxygenase; Oxidoreductase; KW Reference proteome; Steroid-binding; Steroidogenesis. FT CHAIN 1 487 Steroid 21-hydroxylase. FT /FTId=PRO_0000051977. FT REGION 334 350 Steroid-binding (By similarity). FT METAL 420 420 Iron (heme axial ligand). FT CONFLICT 31 32 PP -> LR (in Ref. 1; AAA37114). FT CONFLICT 66 66 M -> L (in Ref. 1; AAA37114). FT CONFLICT 218 218 L -> F (in Ref. 3; BAA31153). FT CONFLICT 238 238 Q -> R (in Ref. 3; BAA31153 and 4; FT AAC05278). FT CONFLICT 241 241 D -> E (in Ref. 1; AAA37114). FT CONFLICT 314 314 E -> A (in Ref. 1; AAA37114). SQ SEQUENCE 487 AA; 55328 MW; CAD32B606004449F CRC64; MLLPGLLLLL LLLAGTRWLW GQWKLRKLHL PPLAPGFLHF LQPNLPIYLL GLTQKLGPIY RIRLGMQDVV VLNSNRTIEE ALIQKWVDFA GRPHMLNGKM DLDLSLGDYS LMWKAHKKLS RSALMLGMRD SMEPLIEQLT QEFCERMRAQ AGTPVAIHKE FSFLTCSIIS CLTFGDKDST LVQTLHDCVQ DLLQAWNHWS IQILTIIPLL RFLPNPGLQK LKQIQESRDH IVKQQLKQHK DSLVAGQWKD MIDYMLQGVE KQRDGKDEER LHEGHVHMSV VDLFIGGTET TATTLSWAVA FLLHHPEIQK RLQEELDLKL GPGSQLLYRN RMQLPLLMAT IAEVLRLRPV VPLALPHRAT RASSISGYDI PKDMVIIPNI QGANLDEMVW ELPSKFWPDR FLEPGKNPRT PSFGCGARVC LGEPLARLEL FVVLARLLQA FTLLPPPDGT LPSLQPQPYA GINLPIPPFQ VRLQPRNLAP QDQGERP // ID CP254_MOUSE Reviewed; 490 AA. AC Q6XVG2; DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 19-FEB-2014, entry version 78. DE RecName: Full=Cytochrome P450 2C54; DE EC=1.14.14.1; DE AltName: Full=CYPIIC54; GN Name=Cyp2c54; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE RP SPECIFICITY. RC STRAIN=C57BL/6; TISSUE=Liver; RX PubMed=15102943; DOI=10.1124/mol.65.5.1148; RA Wang H., Zhao Y., Bradbury J.A., Graves J.P., Foley J., RA Blaisdell J.A., Goldstein J.A., Zeldin D.C.; RT "Cloning, expression, and characterization of three new mouse RT cytochrome p450 enzymes and partial characterization of their fatty RT acid oxidation activities."; RL Mol. Pharmacol. 65:1148-1158(2004). CC -!- FUNCTION: Metabolizes arachidonic acid mainly to 12- CC hydroxyeicosatetraenoic acid (HETE). CC -!- CATALYTIC ACTIVITY: RH + reduced flavoprotein + O(2) = ROH + CC oxidized flavoprotein + H(2)O. CC -!- COFACTOR: Heme group (By similarity). CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral CC membrane protein. Microsome membrane; Peripheral membrane protein. CC -!- TISSUE SPECIFICITY: Expressed in liver. CC -!- INDUCTION: P450 can be induced to high levels in liver and other CC tissues by various foreign compounds, including drugs, pesticides, CC and carcinogens. CC -!- SIMILARITY: Belongs to the cytochrome P450 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AY206874; AAO52737.1; -; mRNA. DR RefSeq; NP_996260.1; NM_206537.2. DR UniGene; Mm.379575; -. DR ProteinModelPortal; Q6XVG2; -. DR SMR; Q6XVG2; 27-489. DR MINT; MINT-1862953; -. DR STRING; 10090.ENSMUSP00000048284; -. DR PhosphoSite; Q6XVG2; -. DR PaxDb; Q6XVG2; -. DR PRIDE; Q6XVG2; -. DR DNASU; 404195; -. DR Ensembl; ENSMUST00000048959; ENSMUSP00000048284; ENSMUSG00000067225. DR GeneID; 404195; -. DR KEGG; mmu:404195; -. DR UCSC; uc012bln.1; mouse. DR CTD; 404195; -. DR MGI; MGI:3642960; Cyp2c54. DR eggNOG; COG2124; -. DR GeneTree; ENSGT00680000099783; -. DR HOGENOM; HOG000036992; -. DR HOVERGEN; HBG015789; -. DR InParanoid; Q6XVG2; -. DR KO; K07413; -. DR OrthoDB; EOG7RBZ85; -. DR TreeFam; TF352043; -. DR NextBio; 406406; -. DR PRO; PR:Q6XVG2; -. DR Bgee; Q6XVG2; -. DR Genevestigator; Q6XVG2; -. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0070330; F:aromatase activity; IEA:UniProtKB-EC. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR Gene3D; 1.10.630.10; -; 1. DR InterPro; IPR001128; Cyt_P450. DR InterPro; IPR017972; Cyt_P450_CS. DR InterPro; IPR002401; Cyt_P450_E_grp-I. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00463; EP450I. DR PRINTS; PR00385; P450. DR SUPFAM; SSF48264; SSF48264; 1. DR PROSITE; PS00086; CYTOCHROME_P450; 1. PE 2: Evidence at transcript level; KW Complete proteome; Endoplasmic reticulum; Heme; Iron; Membrane; KW Metal-binding; Microsome; Monooxygenase; Oxidoreductase; KW Reference proteome. FT CHAIN 1 490 Cytochrome P450 2C54. FT /FTId=PRO_0000282958. FT METAL 435 435 Iron (heme axial ligand) (By similarity). SQ SEQUENCE 490 AA; 55858 MW; C226BBBB734DE29D CRC64; MDPILVLVLT LSCLFLLSLW RQSYERGKLP PGPTPLPIIG NILQIDVKDI CQSFTNLSRV YGPVYTLYLG RKPTVVLHGY EAVKEALVDH GDVFAGRGRL PVFDKATNGM GIGFSNGSVW KNTRHFSLMT LRNLGMGKRS IEDRVQEEAR CLVEELRKTN GSPCDPTFIL GCAPCNVICS IIFQDRFDYK DRDFLNLLEK LDEISKILST PWLQVCNTFP ALLDYCPGSH NQFFKNYAYI KNFLLEKIRE HKESLDVTIP RDFIDYFLIK GAQEDDNHPL KNNFEHLAIT VTDLFIGGTE SMSTTLRYAL LLLLKYPHVT AKVQEEIEHV IGKHRRPCMQ DRSHMPYTNA MIHEVQRFID LVPNNLPHEV TCDIKFRNYF IPKGTTVITS LSSVLRDSKE FPNPEKFDPG HFLDENGKFK KSDYFMPFST GKRICAGEGL ARMELFLFLT SILQNFNLKP LVHPKDIDIT PMLIGLGSVP PAFQLCFIPS // ID CP238_MOUSE Reviewed; 490 AA. AC P56655; B2RWV4; F8VPK7; DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot. DT 03-OCT-2012, sequence version 2. DT 19-MAR-2014, entry version 98. DE RecName: Full=Cytochrome P450 2C38; DE EC=1.14.14.1; DE AltName: Full=CYPIIC38; GN Name=Cyp2c38; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=CD-1; RX PubMed=9721182; DOI=10.1006/abbi.1998.0806; RA Luo G., Zeldin D.C., Blaisdell J.A., Hodgson E., Goldstein J.A.; RT "Cloning and expression of murine CYP2Cs and their ability to RT metabolize arachidonic acid."; RL Arch. Biochem. Biophys. 357:45-57(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: Metabolizes arachidonic acid to produce 11,12- CC epoxyeicosatrienoic acid (EET). CC -!- CATALYTIC ACTIVITY: RH + reduced flavoprotein + O(2) = ROH + CC oxidized flavoprotein + H(2)O. CC -!- COFACTOR: Heme group (By similarity). CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral CC membrane protein. Microsome membrane; Peripheral membrane protein. CC -!- TISSUE SPECIFICITY: Liver, brain, kidney, and intestine, with CC trace amounts in lung and heart. CC -!- INDUCTION: P450 can be induced to high levels in liver and other CC tissues by various foreign compounds, including drugs, pesticides, CC and carcinogens. CC -!- SIMILARITY: Belongs to the cytochrome P450 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF047725; AAD13720.1; -; mRNA. DR EMBL; AC139233; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC150721; AAI50722.1; -; mRNA. DR RefSeq; NP_034132.2; NM_010002.3. DR UniGene; Mm.42100; -. DR ProteinModelPortal; P56655; -. DR SMR; P56655; 28-490. DR MINT; MINT-1865676; -. DR PaxDb; P56655; -. DR PRIDE; P56655; -. DR Ensembl; ENSMUST00000035488; ENSMUSP00000044722; ENSMUSG00000032808. DR GeneID; 13097; -. DR KEGG; mmu:13097; -. DR CTD; 13097; -. DR MGI; MGI:1306819; Cyp2c38. DR eggNOG; COG2124; -. DR GeneTree; ENSGT00680000099783; -. DR HOGENOM; HOG000036992; -. DR HOVERGEN; HBG015789; -. DR InParanoid; B2RWV4; -. DR KO; K07413; -. DR OrthoDB; EOG7RBZ85; -. DR TreeFam; TF352043; -. DR NextBio; 283082; -. DR PRO; PR:P56655; -. DR Genevestigator; P56655; -. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0070330; F:aromatase activity; IEA:UniProtKB-EC. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR Gene3D; 1.10.630.10; -; 1. DR InterPro; IPR001128; Cyt_P450. DR InterPro; IPR017972; Cyt_P450_CS. DR InterPro; IPR002401; Cyt_P450_E_grp-I. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00463; EP450I. DR PRINTS; PR00385; P450. DR SUPFAM; SSF48264; SSF48264; 1. DR PROSITE; PS00086; CYTOCHROME_P450; 1. PE 2: Evidence at transcript level; KW Complete proteome; Endoplasmic reticulum; Heme; Iron; Membrane; KW Metal-binding; Microsome; Monooxygenase; Oxidoreductase; KW Reference proteome. FT CHAIN 1 490 Cytochrome P450 2C38. FT /FTId=PRO_0000051721. FT METAL 435 435 Iron (heme axial ligand) (By similarity). FT CONFLICT 60 60 T -> A (in Ref. 1; AAD13720 and 3; FT AAI50722). FT CONFLICT 98 98 E -> G (in Ref. 1; AAD13720 and 3; FT AAI50722). FT CONFLICT 125 125 R -> H (in Ref. 1; AAD13720 and 3; FT AAI50722). FT CONFLICT 188 188 D -> H (in Ref. 1; AAD13720 and 3; FT AAI50722). FT CONFLICT 253 253 E -> A (in Ref. 1; AAD13720 and 3; FT AAI50722). FT CONFLICT 257 257 V -> F (in Ref. 1; AAD13720 and 3; FT AAI50722). FT CONFLICT 344 344 R -> H (in Ref. 1; AAD13720 and 3; FT AAI50722). FT CONFLICT 470 470 I -> M (in Ref. 1; AAD13720 and 3; FT AAI50722). FT CONFLICT 478 478 T -> A (in Ref. 1; AAD13720 and 3; FT AAI50722). SQ SEQUENCE 490 AA; 56229 MW; 876444B4A6C1343A CRC64; MDLVTFLVLT LSSLILLSLW RQRSRRGRLP PGPTPFPIIG NFLQIDVKNF NQSLTNFSKT YGPVFTLYLG SRPIVVLHGY EAVKEALIDH GEEFSGRENI PMSEKINNGL GITFSNGNSW KETRRFTLMT LRNLGMGKRN IEDRVREEAQ CLVEELRKTK GSPCDPTFIL SCAPCNVICS IIFQDRFDYK DKDFLMLMKK LNENVKILSS PWLQVCNNFP LLIDYCPGSH HKVLKNFKYI RSYLLEKVKE HQESLDVTNP RDFIDYFLIK QKQANHIEQA EYSLENLVCT INNLFAAGTE TTSTTLRYAL LLLMKYPDVT AKVQEEIDHV VGRHRSPCMQ DRSRMPYTDA MIHEVQRFIN LVPNNLPHAV TCDIKFRNYI IPKGTTVVTS LTSVLHDSKE FPNPEMFDPG HFLDANGNFK KSDYFMTFSA GKRVCAGEGL ARMELFLILT TILQNFKLKS LVHPKDIDMI PFVNGLITLP PHYQLCFIPL // ID CP270_MOUSE Reviewed; 489 AA. AC Q91W64; Q5GLY9; Q80VW0; Q8R120; Q8VC00; DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot. DT 06-DEC-2005, sequence version 2. DT 19-FEB-2014, entry version 104. DE RecName: Full=Cytochrome P450 2C70; DE EC=1.14.14.1; DE AltName: Full=CYPIIC70; GN Name=Cyp2c70; Synonyms=Cyp2c-70, Cyp2c22; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=BALB/c; RA Zhao Y., Wang H., Goldstein J.A., Zeldin D.C.; RT "Molecular cloning, expression, and characterization of four novel RT mouse cytochrome P450 (CYP) genes (CYP2C65, CYP2C66, CYP2C53 and RT CYP2C70)."; RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Liver; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: Cytochromes P450 are a group of heme-thiolate CC monooxygenases. In liver microsomes, this enzyme is involved in an CC NADPH-dependent electron transport pathway. It oxidizes a variety CC of structurally unrelated compounds, including steroids, fatty CC acids, and xenobiotics (By similarity). CC -!- CATALYTIC ACTIVITY: RH + reduced flavoprotein + O(2) = ROH + CC oxidized flavoprotein + H(2)O. CC -!- COFACTOR: Heme group (By similarity). CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral CC membrane protein. Microsome membrane; Peripheral membrane protein. CC -!- INDUCTION: P450 can be induced to high levels in liver and other CC tissues by various foreign compounds, including drugs, pesticides, CC and carcinogens. CC -!- SIMILARITY: Belongs to the cytochrome P450 family. CC -!- SEQUENCE CAUTION: CC Sequence=AAH25822.1; Type=Erroneous initiation; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AY227736; AAP55509.1; -; mRNA. DR EMBL; BC016494; AAH16494.1; -; mRNA. DR EMBL; BC022151; AAH22151.1; -; mRNA. DR EMBL; BC023894; AAH23894.2; -; mRNA. DR EMBL; BC025822; AAH25822.1; ALT_INIT; mRNA. DR EMBL; BC034831; AAH34831.1; -; mRNA. DR RefSeq; NP_663474.2; NM_145499.2. DR UniGene; Mm.29119; -. DR ProteinModelPortal; Q91W64; -. DR SMR; Q91W64; 28-489. DR IntAct; Q91W64; 2. DR MINT; MINT-1863855; -. DR PhosphoSite; Q91W64; -. DR PaxDb; Q91W64; -. DR PRIDE; Q91W64; -. DR Ensembl; ENSMUST00000051846; ENSMUSP00000060584; ENSMUSG00000060613. DR GeneID; 226105; -. DR KEGG; mmu:226105; -. DR UCSC; uc008hkj.2; mouse. DR CTD; 226105; -. DR MGI; MGI:2385878; Cyp2c70. DR eggNOG; COG2124; -. DR GeneTree; ENSGT00680000099783; -. DR HOGENOM; HOG000036992; -. DR HOVERGEN; HBG015789; -. DR InParanoid; Q91W64; -. DR KO; K07413; -. DR OrthoDB; EOG7RBZ85; -. DR TreeFam; TF352043; -. DR ChiTaRS; Cyp2c70; mouse. DR NextBio; 377994; -. DR PRO; PR:Q91W64; -. DR ArrayExpress; Q91W64; -. DR Bgee; Q91W64; -. DR Genevestigator; Q91W64; -. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0070330; F:aromatase activity; IEA:UniProtKB-EC. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR Gene3D; 1.10.630.10; -; 1. DR InterPro; IPR001128; Cyt_P450. DR InterPro; IPR017972; Cyt_P450_CS. DR InterPro; IPR002401; Cyt_P450_E_grp-I. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00463; EP450I. DR PRINTS; PR00385; P450. DR SUPFAM; SSF48264; SSF48264; 1. DR PROSITE; PS00086; CYTOCHROME_P450; 1. PE 2: Evidence at transcript level; KW Complete proteome; Endoplasmic reticulum; Heme; Iron; Membrane; KW Metal-binding; Microsome; Monooxygenase; Oxidoreductase; KW Reference proteome. FT CHAIN 1 489 Cytochrome P450 2C70. FT /FTId=PRO_0000051726. FT METAL 434 434 Iron (heme axial ligand) (By similarity). FT CONFLICT 46 46 D -> Y (in Ref. 1; AAP55509 and 2; FT AAH16494). FT CONFLICT 130 130 V -> A (in Ref. 1; AAP55509). SQ SEQUENCE 489 AA; 56020 MW; 90973D9B05964B1B CRC64; MALFIFLGIW LSCFLFLFLW NQHRGRGKLP PGPTPLPIVG NILQVDVKNI SKSMGMLAKK YGPVFTVYLG MKPTVVLHGY KAMKEALIDQ GDEFSDKTDS SLLSRTSQGL GIVFSNGETW KQTRRFSLMV LRSMGMGKKT IEDRIQEEIL YMLDALRKTN GSPCDPSFLL ACVPCNVIST VIFQHRFDYN DQTFQDFMEN FHRKIEILAS PWSQLCSAYP ILYYLPGIHN RFLKDVTQQK KFILEEINRH QKSLDLSNPQ DFIDYFLIKM EKEKHNQKSE FTMDNLVVSI GDLFGAGTET TSSTVKYGLL LLLKYPEVTA KIQEEIAHVI GRHRRPTMQD RNHMPYTDAV LHEIQRYIDF VPIPSPRKTT QDVEFRGYHI PKGTSVMACL TSVLNDDKEF PNPEKFDPGH FLDEKGNFKK SDYFVAFSAG RRACIGEGLA RMEMFLILTN ILQHFTLKPL VKPEDIDTKP VQTGLLHVPP PFELCFIPV // ID CP26A_MOUSE Reviewed; 497 AA. AC O55127; Q9R1F4; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1998, sequence version 1. DT 19-FEB-2014, entry version 107. DE RecName: Full=Cytochrome P450 26A1; DE EC=1.14.-.-; DE AltName: Full=Cytochrome P450RAI; DE AltName: Full=Retinoic acid 4-hydroxylase; DE AltName: Full=Retinoic acid-metabolizing cytochrome; GN Name=Cyp26a1; Synonyms=Cyp26, P450ra; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=C3H; RX PubMed=9250660; DOI=10.1093/emboj/16.14.4163; RA Fujii H., Sato T., Kaneko S., Gotoh O., Fujii-Kuriyama Y., Osawa K., RA Kato S., Hamada H.; RT "Metabolic inactivation of retinoic acid by a novel P450 RT differentially expressed in developing mouse embryos."; RL EMBO J. 16:4163-4173(1997). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=9442090; DOI=10.1074/jbc.273.4.2409; RA Abu-Abed S.S., Beckett B.R., Chiba H., Chithalen J.V., Jones G., RA Metzger D., Chambon P., Petkovich M.; RT "Mouse P450RAI (CYP26) expression and retinoic acid-inducible retinoic RT acid metabolism in F9 cells are regulated by retinoic acid receptor RT gamma and retinoid X receptor alpha."; RL J. Biol. Chem. 273:2409-2415(1998). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Tooth; RX PubMed=11063033; RA Paine C.T., Paine M.L., Snead M.L.; RT "Identification of tuftelin- and amelogenin-interacting proteins using RT the yeast two-hybrid system."; RL Connect. Tissue Res. 38:257-267(1998). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Liver; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: Plays a key role in retinoic acid metabolism. Acts on CC retinoids, including all-trans-retinoic acid (RA) and its CC stereoisomer 9-cis-RA. Capable of both 4-hydroxylation and 18- CC hydroxylation. Responsible for generation of several hydroxylated CC forms of RA, including 4-OH-RA, 4-oxo-RA and 18-OH-RA. CC -!- COFACTOR: Heme group (By similarity). CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral CC membrane protein. Microsome membrane; Peripheral membrane protein. CC -!- INDUCTION: By retinoic acid. CC -!- SIMILARITY: Belongs to the cytochrome P450 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; Y12657; CAA73206.1; -; mRNA. DR EMBL; AF115769; AAD17217.1; -; mRNA. DR EMBL; BC012673; AAH12673.1; -; mRNA. DR RefSeq; NP_031837.2; NM_007811.2. DR UniGene; Mm.42230; -. DR ProteinModelPortal; O55127; -. DR SMR; O55127; 41-490. DR STRING; 10090.ENSMUSP00000025946; -. DR PRIDE; O55127; -. DR Ensembl; ENSMUST00000025946; ENSMUSP00000025946; ENSMUSG00000024987. DR GeneID; 13082; -. DR KEGG; mmu:13082; -. DR UCSC; uc008his.2; mouse. DR CTD; 1592; -. DR MGI; MGI:1096359; Cyp26a1. DR eggNOG; COG2124; -. DR GeneTree; ENSGT00660000095370; -. DR HOGENOM; HOG000220829; -. DR HOVERGEN; HBG051099; -. DR InParanoid; O55127; -. DR KO; K07437; -. DR OrthoDB; EOG7F24SP; -. DR TreeFam; TF105093; -. DR NextBio; 283042; -. DR PRO; PR:O55127; -. DR Bgee; O55127; -. DR Genevestigator; O55127; -. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0008401; F:retinoic acid 4-hydroxylase activity; IEA:Ensembl. DR GO; GO:0001972; F:retinoic acid binding; IEA:Ensembl. DR GO; GO:0009952; P:anterior/posterior pattern specification; IMP:MGI. DR GO; GO:0071300; P:cellular response to retinoic acid; IEP:UniProtKB. DR GO; GO:0007417; P:central nervous system development; IMP:MGI. DR GO; GO:0014032; P:neural crest cell development; IGI:MGI. DR GO; GO:0034653; P:retinoic acid catabolic process; ISA:MGI. DR GO; GO:0048384; P:retinoic acid receptor signaling pathway; IGI:MGI. DR Gene3D; 1.10.630.10; -; 1. DR InterPro; IPR001128; Cyt_P450. DR InterPro; IPR017972; Cyt_P450_CS. DR InterPro; IPR002403; Cyt_P450_E_grp-IV. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00465; EP450IV. DR PRINTS; PR00385; P450. DR SUPFAM; SSF48264; SSF48264; 1. DR PROSITE; PS00086; CYTOCHROME_P450; 1. PE 2: Evidence at transcript level; KW Complete proteome; Endoplasmic reticulum; Heme; Iron; Membrane; KW Metal-binding; Microsome; Monooxygenase; Oxidoreductase; KW Reference proteome. FT CHAIN 1 497 Cytochrome P450 26A1. FT /FTId=PRO_0000051981. FT METAL 442 442 Iron (heme axial ligand) (Potential). FT CONFLICT 9 9 S -> T (in Ref. 3; AAD17217). FT CONFLICT 154 154 L -> P (in Ref. 4; AAH12673). FT CONFLICT 356 356 I -> T (in Ref. 4; AAH12673). FT CONFLICT 492 492 Y -> H (in Ref. 4; AAH12673). SQ SEQUENCE 497 AA; 56178 MW; 33B07D7C29134471 CRC64; MGLPALLASA LCTFVLPLLL FLAALKLWDL YCVSSRDRSC ALPLPPGTMG FPFFGETLQM VLQRRKFLQM KRRKYGFIYK THLFGRPTVR VMGADNVRRI LLGEHRLVSV HWPASVRTIL GAGCLSNLHD SSHKQRKKVI MQAFSREALQ CYVLVIAEEV SSCLEQWLSC GERGLLVYPE VKRLMFRIAM RILLGCEPGP AGGGEDEQQL VEAFEEMTRN LFSLPIDVPF SGLYRGVKAR NLIHARIEEN IRAKIRRLQA TEPDGGCKDA LQLLIEHSWE RGERLDMQAL KQSSTELLFG GHETTASAAT SLITYLGLYP HVLQKVREEI KSKGLLCKSN QDNKLDMETL EQLKYIGCVI KETLRLNPPV PGGFRVALKT FELNGYQIPK GWNVIYSICD THDVADIFTN KEEFNPDRFI VPHPEDASRF SFIPFGGGLR SCVGKEFAKI LLKIFTVELA RHCDWQLLNG PPTMKTSPTV YPVDNLPARF TYFQGDI // ID CP24A_MOUSE Reviewed; 514 AA. AC Q64441; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 19-FEB-2014, entry version 107. DE RecName: Full=1,25-dihydroxyvitamin D(3) 24-hydroxylase, mitochondrial; DE Short=24-OHase; DE Short=Vitamin D(3) 24-hydroxylase; DE EC=1.14.13.126; DE AltName: Full=Cytochrome P450 24A1; DE AltName: Full=Cytochrome P450-CC24; DE Flags: Precursor; GN Name=Cyp24a1; Synonyms=Cyp-24, Cyp24; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=C57BL/6; TISSUE=Kidney; RX PubMed=7578252; DOI=10.1016/0167-4781(95)00147-9; RA Itoh S., Yoshimura T., Iemura O., Yamada E., Tsujikawa K., Kohama Y., RA Mimura T.; RT "Molecular cloning of 25-hydroxyvitamin D-3 24-hydroxylase (Cyp-24) RT from mouse kidney: its inducibility by vitamin D-3."; RL Biochim. Biophys. Acta 1264:26-28(1995). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=ddY; TISSUE=Kidney; RX PubMed=9165006; DOI=10.1210/en.138.6.2233; RA Akeno N., Saikatsu S., Kawane T., Horiuchi N.; RT "Mouse vitamin D-24-hydroxylase: molecular cloning, tissue RT distribution, and transcriptional regulation by 1alpha,25- RT dihydroxyvitamin D3."; RL Endocrinology 138:2233-2240(1997). RN [3] RP INDUCTION. RX PubMed=14528024; DOI=10.1210/me.2003-0048; RA Tsujikawa H., Kurotaki Y., Fujimori T., Fukuda K., Nabeshima Y.; RT "Klotho, a gene related to a syndrome resembling human premature RT aging, functions in a negative regulatory circuit of vitamin D RT endocrine system."; RL Mol. Endocrinol. 17:2393-2403(2003). CC -!- FUNCTION: Has a role in maintaining calcium homeostasis. Catalyzes CC the NADPH-dependent 24-hydroxylation of calcidiol (25- CC hydroxyvitamin D(3)) and calcitriol (1-alpha,25-dihydroxyvitamin CC D(3)). The enzyme can perform up to 6 rounds of hydroxylation of CC calcitriol leading to calcitroic acid. CC -!- CATALYTIC ACTIVITY: Calcitriol + NADPH + O(2) = calcitetrol + CC NADP(+) + H(2)O. CC -!- CATALYTIC ACTIVITY: Calcidiol + NADPH + O(2) = secalciferol + CC NADP(+) + H(2)O. CC -!- COFACTOR: Heme group (By similarity). CC -!- SUBCELLULAR LOCATION: Mitochondrion. CC -!- INDUCTION: By 1,25-dihydroxyvitamin D(3) in kidney. CC -!- SIMILARITY: Belongs to the cytochrome P450 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; D49438; BAA08416.1; -; mRNA. DR EMBL; D89669; BAA21843.1; -; mRNA. DR PIR; S60033; S60033. DR RefSeq; NP_034126.1; NM_009996.3. DR UniGene; Mm.6575; -. DR ProteinModelPortal; Q64441; -. DR SMR; Q64441; 51-514. DR STRING; 10090.ENSMUSP00000047954; -. DR PhosphoSite; Q64441; -. DR PaxDb; Q64441; -. DR PRIDE; Q64441; -. DR Ensembl; ENSMUST00000038824; ENSMUSP00000047954; ENSMUSG00000038567. DR GeneID; 13081; -. DR KEGG; mmu:13081; -. DR UCSC; uc008ocb.1; mouse. DR CTD; 1591; -. DR MGI; MGI:88593; Cyp24a1. DR eggNOG; COG2124; -. DR GeneTree; ENSGT00550000074304; -. DR HOGENOM; HOG000276540; -. DR HOVERGEN; HBG099053; -. DR InParanoid; Q64441; -. DR KO; K07436; -. DR OMA; QHDTLAE; -. DR OrthoDB; EOG7ZGX4B; -. DR TreeFam; TF105094; -. DR NextBio; 283038; -. DR PRO; PR:Q64441; -. DR ArrayExpress; Q64441; -. DR Bgee; Q64441; -. DR Genevestigator; Q64441; -. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR GO; GO:0030342; F:1-alpha,25-dihydroxyvitamin D3 24-hydroxylase activity; IEA:Ensembl. DR GO; GO:0008403; F:25-hydroxycholecalciferol-24-hydroxylase activity; IMP:MGI. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0001649; P:osteoblast differentiation; IEA:Ensembl. DR GO; GO:0033280; P:response to vitamin D; IEA:Ensembl. DR GO; GO:0042359; P:vitamin D metabolic process; IMP:MGI. DR Gene3D; 1.10.630.10; -; 1. DR InterPro; IPR001128; Cyt_P450. DR InterPro; IPR017972; Cyt_P450_CS. DR InterPro; IPR002401; Cyt_P450_E_grp-I. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00463; EP450I. DR PRINTS; PR00385; P450. DR SUPFAM; SSF48264; SSF48264; 1. DR PROSITE; PS00086; CYTOCHROME_P450; 1. PE 2: Evidence at transcript level; KW Complete proteome; Heme; Iron; Metal-binding; Mitochondrion; KW Monooxygenase; NADP; Oxidoreductase; Reference proteome; KW Transit peptide. FT TRANSIT 1 35 Mitochondrion (By similarity). FT CHAIN 36 514 1,25-dihydroxyvitamin D(3) 24- FT hydroxylase, mitochondrial. FT /FTId=PRO_0000003616. FT METAL 462 462 Iron (heme axial ligand) (By similarity). SQ SEQUENCE 514 AA; 59453 MW; 3D38BA9235177A42 CRC64; MSCPIDKRRP LIAFLRRLRD LGQPPRSVTS KAHVKRAPKE VPLCPLMTDG ETRNVTSLPG PTNWPLLGSL LEIFWKGGLK KQHDTLAEYH KKYGQIFRMK LGSFDSVHLG SPSLLEALYR TESAHPQRLE IKPWKAYRDH RNEAYGLMIL EGQEWQRVRS AFQKKLMKPV EIMKLDKKIN EVLADFMGQI DELRDERGRI QDLYSELNKW SFESICLVLY EKRFGLLQKD TEEEALTFIA AIKTMMSTFG KMMVTPVELH KRLNTKVWQA HTLAWDTIFK SVKPCIDHRL ERYSQQPGAD FLCDIYQQDH LSKKELYAAV TELQLAAVET TANSLMWILY NLSRNPQVQQ RLLREIQSVL PDNQTPRAED VRNMPYLKAC LKESMRLTPS VPFTTRTLDK PTVLGEYTLP KGTVLTLNTQ VLGSSEDNFE DADKFRPERW LEKEKKINPF AHLPFGVGKR MCIGRRLAEL QLHLALCWII QKYNIVATDS EPVEMLHLGI LVPSRELPIA FCPR // ID CP2A4_MOUSE Reviewed; 494 AA. AC P15392; Q91XG2; DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot. DT 03-OCT-2012, sequence version 3. DT 19-FEB-2014, entry version 108. DE RecName: Full=Cytochrome P450 2A4; DE EC=1.14.14.1; DE AltName: Full=CYPIIA4; DE AltName: Full=Cytochrome P450-15-alpha; DE AltName: Full=Cytochrome P450-IIA3.1; DE AltName: Full=Testosterone 15-alpha-hydroxylase; GN Name=Cyp2a4; Synonyms=Cyp2a-4; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC TISSUE=Liver; RX PubMed=2703500; RA Lindberg R., Burkhart B., Ichikawa T., Negishi M.; RT "The structure and characterization of type I P-450(15) alpha gene as RT major steroid 15 alpha-hydroxylase and its comparison with type II P- RT 450(15) alpha gene."; RL J. Biol. Chem. 264:6465-6471(1989). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=3346244; RA Squires E.J., Negishi M.; RT "Reciprocal regulation of sex-dependent expression of testosterone 15 RT alpha-hydroxylase (P-450(15 alpha)) in liver and kidney of male mice RT by androgen. Evidence for a single gene."; RL J. Biol. Chem. 263:4166-4171(1988). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Kidney; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP MUTAGENESIS. RX PubMed=2733794; DOI=10.1038/339632a0; RA Lindberg R., Negishi M.; RT "Alteration of mouse cytochrome P450coh substrate specificity by RT mutation of a single amino-acid residue."; RL Nature 339:632-634(1989). RN [6] RP TISSUE SPECIFICITY. RX PubMed=10490589; RA Lavery D.J., Lopez-Molina L., Margueron R., Fleury-Olela F., RA Conquet F., Schibler U., Bonfils C.; RT "Circadian expression of the steroid 15 alpha-hydroxylase (Cyp2a4) and RT coumarin 7-hydroxylase (Cyp2a5) genes in mouse liver is regulated by RT the PAR leucine zipper transcription factor DBP."; RL Mol. Cell. Biol. 19:6488-6499(1999). CC -!- FUNCTION: Highly active in the 15-alpha-hydroxylation of CC testosterone. Also active in the 15-alpha-hydroxylation of CC progesterone and androstenedione. Little or no activity on CC corticosterone, pregnenolone, dehydroepiandrosterone, estradiol or CC estriol. CC -!- CATALYTIC ACTIVITY: RH + reduced flavoprotein + O(2) = ROH + CC oxidized flavoprotein + H(2)O. CC -!- COFACTOR: Heme group (By similarity). CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral CC membrane protein. Microsome membrane; Peripheral membrane protein. CC -!- TISSUE SPECIFICITY: Kidney and lung. Expressed in liver, with a CC strong circadian rhythmicity. Circadian expression is regulated by CC DBP. CC -!- MISCELLANEOUS: There are only 11 differences between the sequence CC of testosterone 15-alpha-hydroxylase and that of coumarin 7- CC hydroxylase. By site-directed mutagenesis it has been shown that CC modification of position 209 is sufficient to convert the CC specificity of the two forms of the enzyme. CC -!- SIMILARITY: Belongs to the cytochrome P450 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M26208; AAA37797.1; -; Genomic_DNA. DR EMBL; M25146; AAA37797.1; JOINED; Genomic_DNA. DR EMBL; M25147; AAA37797.1; JOINED; Genomic_DNA. DR EMBL; M26202; AAA37797.1; JOINED; Genomic_DNA. DR EMBL; M26203; AAA37797.1; JOINED; Genomic_DNA. DR EMBL; M26205; AAA37797.1; JOINED; Genomic_DNA. DR EMBL; M26206; AAA37797.1; JOINED; Genomic_DNA. DR EMBL; M26207; AAA37797.1; JOINED; Genomic_DNA. DR EMBL; J03549; AAA40426.1; -; mRNA. DR EMBL; M19319; AAA40429.1; -; mRNA. DR EMBL; AC161798; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC010761; AAH10761.1; -; mRNA. DR EMBL; BC063778; AAH63778.1; -; mRNA. DR PIR; A33531; A33531. DR PIR; S03979; S03979. DR PIR; S16068; S16068. DR RefSeq; NP_034127.2; NM_009997.2. DR UniGene; Mm.154643; -. DR UniGene; Mm.389848; -. DR ProteinModelPortal; P15392; -. DR SMR; P15392; 31-494. DR MINT; MINT-4080270; -. DR STRING; 10090.ENSMUSP00000096254; -. DR PhosphoSite; P15392; -. DR PaxDb; P15392; -. DR PRIDE; P15392; -. DR Ensembl; ENSMUST00000098657; ENSMUSP00000096254; ENSMUSG00000074254. DR GeneID; 13086; -. DR KEGG; mmu:13086; -. DR UCSC; uc009fui.1; mouse. DR CTD; 13086; -. DR MGI; MGI:88596; Cyp2a4. DR eggNOG; COG2124; -. DR GeneTree; ENSGT00670000097868; -. DR HOGENOM; HOG000036992; -. DR HOVERGEN; HBG015789; -. DR InParanoid; P15392; -. DR KO; K07411; -. DR OrthoDB; EOG7RBZ85; -. DR TreeFam; TF352043; -. DR ChiTaRS; Cyp2a4; mouse. DR NextBio; 283050; -. DR PRO; PR:P15392; -. DR Genevestigator; P15392; -. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0070330; F:aromatase activity; IEA:UniProtKB-EC. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0035634; P:response to stilbenoid; IEP:UniProtKB. DR Gene3D; 1.10.630.10; -; 1. DR InterPro; IPR001128; Cyt_P450. DR InterPro; IPR017972; Cyt_P450_CS. DR InterPro; IPR002401; Cyt_P450_E_grp-I. DR InterPro; IPR008067; Cyt_P450_E_grp-I_CYP2A-like. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00463; EP450I. DR PRINTS; PR01684; EP450ICYP2A. DR PRINTS; PR00385; P450. DR SUPFAM; SSF48264; SSF48264; 1. DR PROSITE; PS00086; CYTOCHROME_P450; 1. PE 2: Evidence at transcript level; KW Complete proteome; Endoplasmic reticulum; Heme; Iron; Membrane; KW Metal-binding; Microsome; Monooxygenase; Oxidoreductase; KW Reference proteome. FT CHAIN 1 494 Cytochrome P450 2A4. FT /FTId=PRO_0000051666. FT METAL 439 439 Iron (heme axial ligand). FT CONFLICT 86 86 T -> A (in Ref. 1; AAA37797 and 2; FT AAA40426/AAA40429). FT CONFLICT 129 129 R -> S (in Ref. 1; AAA37797 and 2; FT AAA40426/AAA40429). FT CONFLICT 133 133 T -> A (in Ref. 1; AAA37797 and 2; FT AAA40426/AAA40429). FT CONFLICT 296 296 L -> Q (in Ref. 2; AAA40426/AAA40429). FT CONFLICT 306 306 V -> G (in Ref. 2; AAA40426/AAA40429). FT CONFLICT 467 467 E -> A (in Ref. 1; AAA37797 and 2; FT AAA40426/AAA40429). SQ SEQUENCE 494 AA; 56782 MW; B75D17F6EAF4A8EC CRC64; MLTSGLLLVA AVAFLSVLVL MSVWKQRKLS GKLPPGPTPL PFVGNFLQLN TEQMYNSLMK ISQRYGPVFT IYLGSRRIVV LCGQETVKEA LVDQAEEFSG RGEQATFDWL FKGYGIAFSS GERAKQLRRF SITTLRDFGV GKRGIEERIQ EEAGFLIDSF RKTNGAFIDP TFYLSRTVSN VISSIVFGDR FDYEDKEFLS LLRMMLGSLQ FTATSMGQVY EMFSSVMKHL PGPQQQAFKE LQGLEDFITK KVEHNQRTLD PNSPRDFIDS FLIRMLEEKK NPNTEFYMKN LVLTTLNLFF AGTETVSTTL RYGFLLLMKY PDIEAKVHEE IDRVIGRNRQ PKYEDRMKMP YTEAVIHEIQ RFADLIPMGL ARRVTKDTKF RDFLLPKGTE VFPMLGSVLK DPKFFSNPKD FNPKHFLDDK GQFKKSDAFV PFSIGKRYCF GEGLARMELF LFLTNIMQNF HFKSTQEPQD IDVSPRLVGF VTIPPTYTMS FLSR // ID CP20A_MOUSE Reviewed; 462 AA. AC Q8BKE6; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 19-FEB-2014, entry version 87. DE RecName: Full=Cytochrome P450 20A1; DE EC=1.14.-.-; GN Name=Cyp20a1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Eye; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). CC -!- CATALYTIC ACTIVITY: RH + reduced flavoprotein + O(2) = ROH + CC oxidized flavoprotein + H(2)O. CC -!- COFACTOR: Heme group (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein CC (Potential). CC -!- SIMILARITY: Belongs to the cytochrome P450 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK053388; BAC35373.1; -; mRNA. DR RefSeq; NP_084289.1; NM_030013.2. DR UniGene; Mm.197640; -. DR ProteinModelPortal; Q8BKE6; -. DR SMR; Q8BKE6; 31-461. DR PhosphoSite; Q8BKE6; -. DR PaxDb; Q8BKE6; -. DR PRIDE; Q8BKE6; -. DR Ensembl; ENSMUST00000060608; ENSMUSP00000050823; ENSMUSG00000049439. DR GeneID; 77951; -. DR KEGG; mmu:77951; -. DR UCSC; uc007ben.1; mouse. DR CTD; 57404; -. DR MGI; MGI:1925201; Cyp20a1. DR eggNOG; COG2124; -. DR GeneTree; ENSGT00500000044939; -. DR HOGENOM; HOG000111913; -. DR HOVERGEN; HBG076231; -. DR InParanoid; Q8BKE6; -. DR KO; K07435; -. DR OMA; QKNHGTV; -. DR TreeFam; TF105089; -. DR NextBio; 347877; -. DR PRO; PR:Q8BKE6; -. DR ArrayExpress; Q8BKE6; -. DR Bgee; Q8BKE6; -. DR Genevestigator; Q8BKE6; -. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW. DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro. DR Gene3D; 1.10.630.10; -; 1. DR InterPro; IPR001128; Cyt_P450. DR InterPro; IPR002401; Cyt_P450_E_grp-I. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00463; EP450I. DR SUPFAM; SSF48264; SSF48264; 1. PE 2: Evidence at transcript level; KW Complete proteome; Heme; Iron; Membrane; Metal-binding; Monooxygenase; KW Oxidoreductase; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 462 Cytochrome P450 20A1. FT /FTId=PRO_0000318096. FT TRANSMEM 4 24 Helical; (Potential). FT METAL 409 409 Iron (heme axial ligand) (By similarity). SQ SEQUENCE 462 AA; 52149 MW; 4ADF835E04E291F3 CRC64; MLDFAIFAVT FLLALVGAVL YLYPASRQAS GIPGLTPTEE KDGNLPDIVN SGSLHEFLVN LHERYGPVVS FWFGRRLVVS LGTTDVLKQH FNPNKTSDPF ETMLKSLLGY QSGGGSAGED HVRRKLYGDA VTASLHSNFP LLLQLSEELL DKWLSYPETQ HIPLSQHMLG FALKFVTRMV LGSTFEDEQE VIRFQKIHGT VWSEIGKGFL DGSLDKNTTR KKQYQEALMQ LESTLKKIIK ERKGGNFRQH TFIDSLTQGK LNEQQILEDC VVFSLASCII TARLCTWTIH FLTTTGEVQK KLCKEIDQVL GEGPITSEKI EQLSYCQQVL FETVRTAKLT PVSARLQDIE GKVGPFVIPK ETLVLYALGV VLQDPSTWPL PHRFDPDRFA DEPVMKVFSS LGFSGTWECP ELRFAYMVTA VLVSVLLKRL RLLAVDRQVF EMKYELVTSA REEAWITVSK RH // ID CP27A_MOUSE Reviewed; 533 AA. AC Q9DBG1; DT 03-OCT-2003, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 19-MAR-2014, entry version 103. DE RecName: Full=Sterol 26-hydroxylase, mitochondrial; DE EC=1.14.13.15; DE AltName: Full=5-beta-cholestane-3-alpha,7-alpha,12-alpha-triol 27-hydroxylase; DE AltName: Full=Cytochrome P-450C27/25; DE AltName: Full=Cytochrome P450 27; DE AltName: Full=Sterol 27-hydroxylase; DE AltName: Full=Vitamin D(3) 25-hydroxylase; DE Flags: Precursor; GN Name=Cyp27a1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Liver; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Liver; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-142; LYS-232; LYS-285; RP LYS-296; LYS-375; LYS-512 AND LYS-523, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23576753; DOI=10.1073/pnas.1302961110; RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., RA Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.; RT "Label-free quantitative proteomics of the lysine acetylome in RT mitochondria identifies substrates of SIRT3 in metabolic pathways."; RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013). CC -!- FUNCTION: Catalyzes the first step in the oxidation of the side CC chain of sterol intermediates; the 27-hydroxylation of 5-beta- CC cholestane-3-alpha,7-alpha,12-alpha-triol. Has also a vitamin D3- CC 25-hydroxylase activity (By similarity). CC -!- CATALYTIC ACTIVITY: 5-beta-cholestane-3-alpha,7-alpha,12-alpha- CC triol + 3 NADPH + 3 O(2) = (25R)-3-alpha,7-alpha,12-alpha- CC trihydroxy-5-beta-cholestan-26-oate + 3 NADP(+) + 4 H(2)O. CC -!- COFACTOR: Heme group (By similarity). CC -!- PATHWAY: Hormone biosynthesis; cholecalciferol biosynthesis. CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane (By similarity). CC -!- PTM: Acetylation of Lys-125 and Lys-285 is observed in liver CC mitochondria from fasted mice but not from fed mice. CC -!- SIMILARITY: Belongs to the cytochrome P450 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK004977; BAB23713.1; -; mRNA. DR EMBL; BC055028; AAH55028.1; -; mRNA. DR RefSeq; NP_077226.2; NM_024264.4. DR UniGene; Mm.85083; -. DR ProteinModelPortal; Q9DBG1; -. DR SMR; Q9DBG1; 57-532. DR MINT; MINT-1860912; -. DR PhosphoSite; Q9DBG1; -. DR PaxDb; Q9DBG1; -. DR PRIDE; Q9DBG1; -. DR Ensembl; ENSMUST00000027356; ENSMUSP00000027356; ENSMUSG00000026170. DR GeneID; 104086; -. DR KEGG; mmu:104086; -. DR UCSC; uc007bna.1; mouse. DR CTD; 1593; -. DR MGI; MGI:88594; Cyp27a1. DR eggNOG; COG2124; -. DR GeneTree; ENSGT00550000074304; -. DR HOGENOM; HOG000253961; -. DR HOVERGEN; HBG106909; -. DR InParanoid; Q9DBG1; -. DR KO; K00488; -. DR OMA; QISGYLH; -. DR OrthoDB; EOG7ZGX4B; -. DR TreeFam; TF105094; -. DR UniPathway; UPA00955; -. DR NextBio; 356493; -. DR PRO; PR:Q9DBG1; -. DR ArrayExpress; Q9DBG1; -. DR Bgee; Q9DBG1; -. DR Genevestigator; Q9DBG1; -. DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:MGI. DR GO; GO:0047749; F:cholestanetriol 26-monooxygenase activity; IEA:UniProtKB-EC. DR GO; GO:0031073; F:cholesterol 26-hydroxylase activity; IEA:Ensembl. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0030343; F:vitamin D3 25-hydroxylase activity; IEA:Ensembl. DR GO; GO:0008203; P:cholesterol metabolic process; IEA:Ensembl. DR Gene3D; 1.10.630.10; -; 1. DR InterPro; IPR001128; Cyt_P450. DR InterPro; IPR017972; Cyt_P450_CS. DR InterPro; IPR002401; Cyt_P450_E_grp-I. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00463; EP450I. DR PRINTS; PR00385; P450. DR SUPFAM; SSF48264; SSF48264; 1. DR PROSITE; PS00086; CYTOCHROME_P450; 1. PE 1: Evidence at protein level; KW Acetylation; Complete proteome; Heme; Iron; Membrane; Metal-binding; KW Mitochondrion; Monooxygenase; NADP; Oxidoreductase; KW Reference proteome; Transit peptide. FT TRANSIT 1 32 Mitochondrion (By similarity). FT CHAIN 33 533 Sterol 26-hydroxylase, mitochondrial. FT /FTId=PRO_0000003619. FT REGION 386 400 Sterol-binding (Potential). FT METAL 479 479 Iron (heme axial ligand) (By similarity). FT MOD_RES 142 142 N6-acetyllysine. FT MOD_RES 232 232 N6-acetyllysine. FT MOD_RES 285 285 N6-acetyllysine. FT MOD_RES 296 296 N6-acetyllysine. FT MOD_RES 375 375 N6-acetyllysine. FT MOD_RES 512 512 N6-acetyllysine. FT MOD_RES 523 523 N6-acetyllysine. SQ SEQUENCE 533 AA; 60720 MW; A7F808CA505EF4E6 CRC64; MAAWSRTRLR WTLLDPRVVG RGLCPQGARA KATIPAALQA QESTEGPGTG QDRPRLRSPA ELPGTGTLQF LFQLFLQGYV LHLPDLQVLN KTKYGPMWTT SFGTYTNVNL ASAPLLEQVM RQEGKYPIRD HMDQWKDHRD HKGLTYGIFI AQGEQWYHLR QALKQRLLKP DEAALYTDAL NEVISDFITR LDQVRAESES GDQVPDMAHL LYHLALEAIT YILFEKRIGC LKPSIPEDTA AFIRSVAIMF QNSVYITFLP KWTRPLLPFW KRYLNGWDNI FSFGKKLIDE KVQELKAQLQ ETGPDGVRVS GYLHFLLTNE LLSTQETIGT FPELLLAGVD TTSNTLTWAL YHLSKSPEIQ EALHKEVTGV VPFGKVPQHK DFAHMPLLKA VIKETLRLYP VVPTNSRIIT EKETEINGFL FPKNTQFVLC HYVVSRDPSV FPEPNSFQPH RWLRKKEADN PGILHPFGSV PFGYGVRSCL GRRIAELEMQ LMLSRLVQKY EIALAPGMGE VKTVSRIVLV PSKKVRLHFL QRQ // ID CP2AC_MOUSE Reviewed; 492 AA. AC P56593; Q8VCW9; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 2. DT 19-FEB-2014, entry version 110. DE RecName: Full=Cytochrome P450 2A12; DE EC=1.14.14.1; DE AltName: Full=CYPIIA12; DE AltName: Full=Steroid hormones 7-alpha-hydroxylase; DE AltName: Full=Testosterone 7-alpha-hydroxylase; GN Name=Cyp2a12; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND MUTAGENESIS. RC STRAIN=AKR/J; TISSUE=Liver; RX PubMed=8484736; RA Iwasaki M., Lindberg R.L.P., Juvonen R.O., Negishi M.; RT "Site-directed mutagenesis of mouse steroid 7 alpha-hydroxylase RT (cytochrome P-450(7) alpha): role of residue-209 in determining RT steroid-cytochrome P-450 interaction."; RL Biochem. J. 291:569-573(1993). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Liver; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: Highly active in the 7-alpha-hydroxylation of CC testosterone. CC -!- CATALYTIC ACTIVITY: RH + reduced flavoprotein + O(2) = ROH + CC oxidized flavoprotein + H(2)O. CC -!- COFACTOR: Heme group (By similarity). CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral CC membrane protein. Microsome membrane; Peripheral membrane protein. CC -!- TISSUE SPECIFICITY: Liver. CC -!- SIMILARITY: Belongs to the cytochrome P450 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L06463; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; CH466593; EDL24208.1; -; Genomic_DNA. DR EMBL; BC018356; AAH18356.1; -; mRNA. DR EMBL; BC094017; AAH94017.1; -; mRNA. DR PIR; S32491; S32491. DR RefSeq; NP_598418.1; NM_133657.1. DR UniGene; Mm.20770; -. DR ProteinModelPortal; P56593; -. DR SMR; P56593; 30-491. DR IntAct; P56593; 1. DR MINT; MINT-4119632; -. DR STRING; 10090.ENSMUSP00000074990; -. DR PhosphoSite; P56593; -. DR PaxDb; P56593; -. DR PRIDE; P56593; -. DR Ensembl; ENSMUST00000075552; ENSMUSP00000074990; ENSMUSG00000060407. DR GeneID; 13085; -. DR KEGG; mmu:13085; -. DR UCSC; uc009fux.1; mouse. DR CTD; 13085; -. DR MGI; MGI:105055; Cyp2a12. DR eggNOG; COG2124; -. DR GeneTree; ENSGT00670000097868; -. DR HOGENOM; HOG000036992; -. DR HOVERGEN; HBG015789; -. DR InParanoid; Q8VCW9; -. DR KO; K07411; -. DR OMA; PTIYLSK; -. DR OrthoDB; EOG7RBZ85; -. DR TreeFam; TF352043; -. DR NextBio; 283046; -. DR PRO; PR:P56593; -. DR Bgee; P56593; -. DR Genevestigator; P56593; -. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0070330; F:aromatase activity; IEA:UniProtKB-EC. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR Gene3D; 1.10.630.10; -; 1. DR InterPro; IPR001128; Cyt_P450. DR InterPro; IPR017972; Cyt_P450_CS. DR InterPro; IPR002401; Cyt_P450_E_grp-I. DR InterPro; IPR008067; Cyt_P450_E_grp-I_CYP2A-like. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00463; EP450I. DR PRINTS; PR01684; EP450ICYP2A. DR PRINTS; PR00385; P450. DR SUPFAM; SSF48264; SSF48264; 1. DR PROSITE; PS00086; CYTOCHROME_P450; 1. PE 1: Evidence at protein level; KW Complete proteome; Endoplasmic reticulum; Heme; Iron; Membrane; KW Metal-binding; Microsome; Monooxygenase; Oxidoreductase; KW Reference proteome. FT CHAIN 1 492 Cytochrome P450 2A12. FT /FTId=PRO_0000051675. FT METAL 437 437 Iron (heme axial ligand) (By similarity). FT MUTAGEN 206 206 Q->G: Same as wild-type. FT MUTAGEN 208 208 N->L: Stabilizes the protein, 17-fold FT lower Vmax. FT MUTAGEN 209 209 K->Q: Same as wild-type. FT CONFLICT 147 147 R -> H (in Ref. 1; L06463). FT CONFLICT 375 375 D -> N (in Ref. 1; L06463). FT CONFLICT 386 386 G -> A (in Ref. 1; L06463). FT CONFLICT 449 450 LF -> FL (in Ref. 1; L06463). SQ SEQUENCE 492 AA; 56179 MW; 38FD449996825F44 CRC64; MLGSGLLLLA ILAFLSVMVL VSVWQQKIRG KLPPGPIPLP FIGNYLQLNR KDVYSSITQL QEHYGPVFTI HLGPRRVVVL YGYDAVKEAL VDHAEEFSGR GEQATFNTLF KGYGVAFSNG ERAKQLRRFS IATLRDFGMG KRGVEERIQE EAGCLIKMLQ GTCGAPIDPT IYLSKTASNV ISSIVFGDRF NYEDKEFLSL LQMMGQVNKF AASPTGQLYD MFHSVMKYLP GPQQQIIKDS HKLEDFMIQK VKQNQSTLDP NSPRDFIDSF LIHMQKEKYV NSEFHMKNLV MTSLNLFFAG SETVSSTLRY GFLLLMKHPD VEAKVHEEID RVIGRNRQPQ YEDHMKMPYT QAVINEIQRF SNFAPLGIPR RITKDTSFRG FFLPKGTEVF PILGSLMTDP KFFSSPKDFN PQHFLDDKGQ LKKIPAFLPF STGKRFCLGD SLAKMELFLF FTTILQNFRF KFPRKLEDIN ESPTPEGFTR IIPKYTMSFV PI // ID CP2B9_MOUSE Reviewed; 491 AA. AC P12790; Q64463; DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot. DT 18-SEP-2013, sequence version 2. DT 19-FEB-2014, entry version 114. DE RecName: Full=Cytochrome P450 2B9; DE EC=1.14.14.1; DE AltName: Full=CYPIIB9; DE AltName: Full=Cytochrome P450 clone PF26; DE AltName: Full=Cytochrome P450-16-alpha; DE AltName: Full=Testosterone 16-alpha hydroxylase; GN Name=Cyp2b9; Synonyms=Cyp2b-9, Rip; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Liver; RX PubMed=3219345; DOI=10.1021/bi00417a035; RA Noshiro M., Lakso M., Kawajiri K., Negishi M.; RT "Rip locus: regulation of female-specific isozyme (I-P-450(16 alpha) RT of testosterone 16 alpha-hydroxylase in mouse liver, chromosome RT localization, and cloning of P-450 cDNA."; RL Biochemistry 27:6434-6443(1988). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=1997326; DOI=10.1111/j.1432-1033.1991.tb15728.x; RA Lakso M., Masaki R., Noshiro M., Negishi M.; RT "Structures and characterization of sex-specific mouse cytochrome P- RT 450 genes as members within a large family. Duplication boundary and RT evolution."; RL Eur. J. Biochem. 195:477-486(1991). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: Cytochromes P450 are a group of heme-thiolate CC monooxygenases. In liver microsomes, this enzyme is involved in an CC NADPH-dependent electron transport pathway. It oxidizes a variety CC of structurally unrelated compounds, including steroids, fatty CC acids, and xenobiotics. CC -!- CATALYTIC ACTIVITY: RH + reduced flavoprotein + O(2) = ROH + CC oxidized flavoprotein + H(2)O. CC -!- COFACTOR: Heme group (By similarity). CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral CC membrane protein. Microsome membrane; Peripheral membrane protein. CC -!- SIMILARITY: Belongs to the cytochrome P450 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M21855; AAA40424.1; -; mRNA. DR EMBL; M60273; AAA03648.1; -; Genomic_DNA. DR EMBL; M60267; AAA03648.1; JOINED; Genomic_DNA. DR EMBL; M60268; AAA03648.1; JOINED; Genomic_DNA. DR EMBL; M60269; AAA03648.1; JOINED; Genomic_DNA. DR EMBL; M60270; AAA03648.1; JOINED; Genomic_DNA. DR EMBL; M60271; AAA03648.1; JOINED; Genomic_DNA. DR EMBL; M60272; AAA03648.1; JOINED; Genomic_DNA. DR EMBL; AC157782; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC120525; AAI20526.1; -; mRNA. DR EMBL; BC120527; AAI20528.1; -; mRNA. DR PIR; A31047; A31047. DR PIR; I84735; I84735. DR RefSeq; NP_034130.1; NM_010000.2. DR UniGene; Mm.14413; -. DR ProteinModelPortal; P12790; -. DR IntAct; P12790; 1. DR STRING; 10090.ENSMUSP00000080846; -. DR PhosphoSite; P12790; -. DR PaxDb; P12790; -. DR PRIDE; P12790; -. DR Ensembl; ENSMUST00000082214; ENSMUSP00000080846; ENSMUSG00000040660. DR GeneID; 13094; -. DR KEGG; mmu:13094; -. DR UCSC; uc009fuh.1; mouse. DR CTD; 13094; -. DR MGI; MGI:88600; Cyp2b9. DR eggNOG; COG2124; -. DR GeneTree; ENSGT00670000097868; -. DR HOGENOM; HOG000036992; -. DR HOVERGEN; HBG015789; -. DR InParanoid; P12790; -. DR KO; K07412; -. DR OrthoDB; EOG77M8NM; -. DR TreeFam; TF352043; -. DR NextBio; 283070; -. DR PRO; PR:P12790; -. DR Genevestigator; P12790; -. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0070330; F:aromatase activity; IEA:UniProtKB-EC. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0035634; P:response to stilbenoid; IEP:UniProtKB. DR Gene3D; 1.10.630.10; -; 1. DR InterPro; IPR001128; Cyt_P450. DR InterPro; IPR017972; Cyt_P450_CS. DR InterPro; IPR002401; Cyt_P450_E_grp-I. DR InterPro; IPR008068; Cyt_P450_E_grp-I_CYP2B-like. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00463; EP450I. DR PRINTS; PR01685; EP450ICYP2B. DR PRINTS; PR00385; P450. DR SUPFAM; SSF48264; SSF48264; 1. DR PROSITE; PS00086; CYTOCHROME_P450; 1. PE 2: Evidence at transcript level; KW Complete proteome; Endoplasmic reticulum; Heme; Iron; Membrane; KW Metal-binding; Microsome; Monooxygenase; Oxidoreductase; KW Phosphoprotein; Reference proteome. FT CHAIN 1 491 Cytochrome P450 2B9. FT /FTId=PRO_0000051684. FT METAL 436 436 Iron (heme axial ligand) (By similarity). FT MOD_RES 128 128 Phosphoserine; by PKA (By similarity). FT CONFLICT 298 298 A -> V (in Ref. 1; AAA40424). FT CONFLICT 412 412 H -> Q (in Ref. 1; AAA40424). SQ SEQUENCE 491 AA; 55741 MW; C1E790A7DD1A7298 CRC64; MDPSVLLLLA VLLSLFLLLV RGHAKIHGHL PPGPHPLPLL GNLLQMDRGG LLKCFIQLQE KHGDVFTVHL GPRPVVVLCG TQTIREALVD HAEAFSGRGT IAAAQLVMQD YGIFFASGQR WKTLRRFSLA TMKEFGMGKR SVEERIKEEA QCLVEELKKY QGVPLDPTFL FQCITANIIC SIVFGERFDY TDDQFLHLLN LMYKIFSLLS SFSGQMFELF SGFLKYFPGV HRQIVKKQQE LLDYIAHSVE KHKATLDPSA PRDYIDTYLL RMEKEKSNHN TEFHHQNLMM SVLSLFFAGT ETTSATLHYG VLLMLKYPHV TEKVQKEIDQ VIGSHRLPTL DDRTKMPYTD AVIHEIQRFS DLVPIGLPHK VIKDTLFRGY LLPKNTEVYP VLSSALHDPQ YFEQPDKFNP EHFLDANGAL KKCEAFLPFS TGKRICLGES IARNELFIFF TTILQNFSVA SPVAPKDIDL TPKESGIGKI PPAHQIYFLA R // ID CP27B_MOUSE Reviewed; 507 AA. AC O35084; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1998, sequence version 2. DT 19-FEB-2014, entry version 108. DE RecName: Full=25-hydroxyvitamin D-1 alpha hydroxylase, mitochondrial; DE EC=1.14.13.13; DE AltName: Full=25-OHD-1 alpha-hydroxylase; DE AltName: Full=25-hydroxyvitamin D(3) 1-alpha-hydroxylase; DE Short=VD3 1A hydroxylase; DE AltName: Full=Calcidiol 1-monooxygenase; DE AltName: Full=Cytochrome P450 subfamily XXVIIB polypeptide 1; DE AltName: Full=Cytochrome P450C1 alpha; DE AltName: Full=Cytochrome P450VD1-alpha; DE AltName: Full=Cytochrome p450 27B1; DE Flags: Precursor; GN Name=Cyp27b1; Synonyms=Cyp27b, Cyp40; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Kidney; RX PubMed=9295274; DOI=10.1126/science.277.5333.1827; RA Takeyama K., Kitanaka S., Sato T., Kobori M., Yanagisawa J., Kato S.; RT "25-hydroxyvitamin D3 1alpha-hydroxylase and vitamin D synthesis."; RL Science 277:1827-1830(1997). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=129; RA Kimmel-Jehan C., DeLuca H.F.; RT "Cloning of the mouse 25-hydroxyvitamin D3 1-alpha hydroxylase gene."; RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=129/SvJ; RX PubMed=11149489; DOI=10.1359/jbmr.2001.16.1.46; RA Panda D.K., Al-Kawas S., Seldin M.F., Hendy G.N., Goltzman D.; RT "25-hydroxyvitamin D 1alpha-hydroxylase: structure of the mouse gene, RT chromosomal assignment, and developmental expression."; RL J. Bone Miner. Res. 16:46-56(2001). CC -!- FUNCTION: Catalyzes the conversion of 25-hydroxyvitamin D3 CC (25(OH)D) to 1-alpha,25-dihydroxyvitamin D3 (1,25(OH)2D) plays an CC important role in normal bone growth, calcium metabolism, and CC tissue differentiation. CC -!- CATALYTIC ACTIVITY: Calcidiol + NADPH + O(2) = calcitriol + CC NADP(+) + H(2)O. CC -!- COFACTOR: Heme group (By similarity). CC -!- PATHWAY: Hormone biosynthesis; cholecalciferol biosynthesis. CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane. CC -!- TISSUE SPECIFICITY: Kidney. CC -!- SIMILARITY: Belongs to the cytochrome P450 family. CC -!- SEQUENCE CAUTION: CC Sequence=BAA22434.1; Type=Erroneous initiation; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AB006034; BAA22434.1; ALT_INIT; mRNA. DR EMBL; AF235021; AAK15024.1; -; Genomic_DNA. DR EMBL; AF286219; AAG44889.1; -; Genomic_DNA. DR RefSeq; NP_034139.2; NM_010009.2. DR UniGene; Mm.6216; -. DR ProteinModelPortal; O35084; -. DR SMR; O35084; 35-504. DR STRING; 10090.ENSMUSP00000006907; -. DR PhosphoSite; O35084; -. DR PaxDb; O35084; -. DR PRIDE; O35084; -. DR Ensembl; ENSMUST00000165764; ENSMUSP00000130005; ENSMUSG00000006724. DR GeneID; 13115; -. DR KEGG; mmu:13115; -. DR UCSC; uc007hht.2; mouse. DR CTD; 1594; -. DR MGI; MGI:1098274; Cyp27b1. DR eggNOG; COG2124; -. DR GeneTree; ENSGT00550000074304; -. DR HOGENOM; HOG000253961; -. DR HOVERGEN; HBG106909; -. DR InParanoid; O35084; -. DR KO; K07438; -. DR OMA; LHSEITA; -. DR OrthoDB; EOG7ZGX4B; -. DR TreeFam; TF105094; -. DR BRENDA; 1.14.13.13; 3474. DR UniPathway; UPA00955; -. DR NextBio; 283134; -. DR PRO; PR:O35084; -. DR ArrayExpress; O35084; -. DR Bgee; O35084; -. DR Genevestigator; O35084; -. DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR GO; GO:0004498; F:calcidiol 1-monooxygenase activity; IDA:BHF-UCL. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0030282; P:bone mineralization; IEA:Ensembl. DR GO; GO:0055074; P:calcium ion homeostasis; IEA:Ensembl. DR GO; GO:0006816; P:calcium ion transport; IMP:MGI. DR GO; GO:0046697; P:decidualization; IEA:Ensembl. DR GO; GO:0070314; P:G1 to G0 transition; IEA:Ensembl. DR GO; GO:0010956; P:negative regulation of calcidiol 1-monooxygenase activity; IEA:Ensembl. DR GO; GO:0030308; P:negative regulation of cell growth; IEA:Ensembl. DR GO; GO:0008285; P:negative regulation of cell proliferation; IEA:Ensembl. DR GO; GO:0045618; P:positive regulation of keratinocyte differentiation; IEA:Ensembl. DR GO; GO:0010980; P:positive regulation of vitamin D 24-hydroxylase activity; IEA:Ensembl. DR GO; GO:0070564; P:positive regulation of vitamin D receptor signaling pathway; IEA:Ensembl. DR GO; GO:0030500; P:regulation of bone mineralization; IEA:Ensembl. DR GO; GO:0043627; P:response to estrogen; IEA:Ensembl. DR GO; GO:0034341; P:response to interferon-gamma; IEA:Ensembl. DR GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl. DR GO; GO:0033280; P:response to vitamin D; IDA:BHF-UCL. DR GO; GO:0042369; P:vitamin D catabolic process; IDA:BHF-UCL. DR Gene3D; 1.10.630.10; -; 1. DR InterPro; IPR001128; Cyt_P450. DR InterPro; IPR017972; Cyt_P450_CS. DR InterPro; IPR002401; Cyt_P450_E_grp-I. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00463; EP450I. DR PRINTS; PR00385; P450. DR SUPFAM; SSF48264; SSF48264; 1. DR PROSITE; PS00086; CYTOCHROME_P450; 1. PE 2: Evidence at transcript level; KW Complete proteome; Heme; Iron; Membrane; Metal-binding; Mitochondrion; KW Monooxygenase; NADP; Oxidoreductase; Reference proteome; KW Transit peptide. FT TRANSIT 1 ? Mitochondrion (Potential). FT CHAIN ? 507 25-hydroxyvitamin D-1 alpha hydroxylase, FT mitochondrial. FT /FTId=PRO_0000003623. FT METAL 454 454 Iron (heme axial ligand) (By similarity). SQ SEQUENCE 507 AA; 56225 MW; 0669B4478C461B83 CRC64; MTQAVKLASR VFHRIHLPLQ LDASLGSRGS ESVLRSLSDI PGPSTLSFLA ELFCKGGLSR LHELQVHGAA RYGPIWSGSF GTLRTVYVAD PTLVEQLLRQ ESHCPERCSF SSWAEHRRRH QRACGLLTAD GEEWQRLRSL LAPLLLRPQA AAGYAGTLDN VVRDLVRRLR RQRGRGSGLP GLVLDVAGEF YKFGLESIGA VLLGSRLGCL EAEVPPDTET FIHAVGSVFV STLLTMAMPN WLHHLIPGPW ARLCRDWDQM FAFAQRHVEL REGEAAMRNQ GKPEEDMPSG HHLTHFLFRE KVSVQSIVGN VTELLLAGVD TVSNTLSWTL YELSRHPDVQ TALHSEITAG TRGSCAHPHG TALSQLPLLK AVIKEVLRLY PVVPGNSRVP DRDIRVGNYV IPQDTLVSLC HYATSRDPTQ FPDPNSFNPA RWLGEGPTPH PFASLPFGFG KRSCIGRRLA ELELQMALSQ ILTHFEVLPE PGALPIKPMT RTVLVPERSI NLQFVDR // ID CP2A5_MOUSE Reviewed; 494 AA. AC P20852; DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1991, sequence version 1. DT 22-JAN-2014, entry version 108. DE RecName: Full=Cytochrome P450 2A5; DE EC=1.14.14.1; DE AltName: Full=CYPIIA5; DE AltName: Full=Coumarin 7-hydroxylase; DE AltName: Full=Cytochrome P450-15-COH; DE AltName: Full=Cytochrome P450-IIA3.2; GN Name=Cyp2a5; Synonyms=Cyp2a-5; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC TISSUE=Kidney; RX PubMed=2703500; RA Lindberg R., Burkhart B., Ichikawa T., Negishi M.; RT "The structure and characterization of type I P-450(15) alpha gene as RT major steroid 15 alpha-hydroxylase and its comparison with type II P- RT 450(15) alpha gene."; RL J. Biol. Chem. 264:6465-6471(1989). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=17NC/Z; RA Jounaidi Y.; RT "cDNA and amino acid sequence of a new cyp2a isoform overexpressed in RT chemically induced mouse hepatoma."; RL Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases. RN [3] RP MUTAGENESIS. RX PubMed=2733794; DOI=10.1038/339632a0; RA Lindberg R., Negishi M.; RT "Alteration of mouse cytochrome P450coh substrate specificity by RT mutation of a single amino-acid residue."; RL Nature 339:632-634(1989). RN [4] RP TISSUE SPECIFICITY. RX PubMed=10490589; RA Lavery D.J., Lopez-Molina L., Margueron R., Fleury-Olela F., RA Conquet F., Schibler U., Bonfils C.; RT "Circadian expression of the steroid 15 alpha-hydroxylase (Cyp2a4) and RT coumarin 7-hydroxylase (Cyp2a5) genes in mouse liver is regulated by RT the PAR leucine zipper transcription factor DBP."; RL Mol. Cell. Biol. 19:6488-6499(1999). CC -!- FUNCTION: Exhibits a high coumarin 7-hydroxylase activity. CC -!- CATALYTIC ACTIVITY: RH + reduced flavoprotein + O(2) = ROH + CC oxidized flavoprotein + H(2)O. CC -!- COFACTOR: Heme group (By similarity). CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral CC membrane protein. Microsome membrane; Peripheral membrane protein. CC -!- TISSUE SPECIFICITY: Liver, with a strong circadian rhythmicity. CC Circadian expression is regulated by DBP. CC -!- DEVELOPMENTAL STAGE: In liver; activity 6 fold higher in females CC than in males. CC -!- MISCELLANEOUS: There are only 11 differences between the sequence CC of testosterone 15-alpha-hydroxylase and that of coumarin 7- CC hydroxylase. By site-directed mutagenesis it has been shown that CC modification of position 209 is sufficient to convert the CC specificity of the two forms of the enzyme. CC -!- SIMILARITY: Belongs to the cytochrome P450 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M25211; AAA37798.1; -; Genomic_DNA. DR EMBL; M26204; AAA37798.1; JOINED; Genomic_DNA. DR EMBL; M25205; AAA37798.1; JOINED; Genomic_DNA. DR EMBL; M25206; AAA37798.1; JOINED; Genomic_DNA. DR EMBL; M25207; AAA37798.1; JOINED; Genomic_DNA. DR EMBL; M25208; AAA37798.1; JOINED; Genomic_DNA. DR EMBL; M25209; AAA37798.1; JOINED; Genomic_DNA. DR EMBL; M25210; AAA37798.1; JOINED; Genomic_DNA. DR EMBL; X89864; CAA61963.1; -; mRNA. DR PIR; B33531; B33531. DR UniGene; Mm.389848; -. DR ProteinModelPortal; P20852; -. DR SMR; P20852; 31-494. DR MINT; MINT-1862789; -. DR BindingDB; P20852; -. DR ChEMBL; CHEMBL4085; -. DR PhosphoSite; P20852; -. DR PaxDb; P20852; -. DR PRIDE; P20852; -. DR MGI; MGI:88597; Cyp2a5. DR eggNOG; COG2124; -. DR HOGENOM; HOG000036992; -. DR HOVERGEN; HBG015789; -. DR InParanoid; P20852; -. DR SABIO-RK; P20852; -. DR PRO; PR:P20852; -. DR Genevestigator; P20852; -. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0070330; F:aromatase activity; IEA:UniProtKB-EC. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0035634; P:response to stilbenoid; IEP:UniProtKB. DR Gene3D; 1.10.630.10; -; 1. DR InterPro; IPR001128; Cyt_P450. DR InterPro; IPR017972; Cyt_P450_CS. DR InterPro; IPR002401; Cyt_P450_E_grp-I. DR InterPro; IPR008067; Cyt_P450_E_grp-I_CYP2A-like. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00463; EP450I. DR PRINTS; PR01684; EP450ICYP2A. DR PRINTS; PR00385; P450. DR SUPFAM; SSF48264; SSF48264; 1. DR PROSITE; PS00086; CYTOCHROME_P450; 1. PE 2: Evidence at transcript level; KW Complete proteome; Endoplasmic reticulum; Heme; Iron; Membrane; KW Metal-binding; Microsome; Monooxygenase; Oxidoreductase; KW Reference proteome. FT CHAIN 1 494 Cytochrome P450 2A5. FT /FTId=PRO_0000051667. FT METAL 439 439 Iron (heme axial ligand). SQ SEQUENCE 494 AA; 56741 MW; 1C2516D5FA2551D0 CRC64; MLTSGLLLVA AVAFLSVLVL MSVWKQRKLS GKLPPGPTPL PFIGNFLQLN TEQMYNSLMK ISQRYGPVFT IYLGPRRIVV LCGQEAVKEA LVDQAEEFSG RGEQATFDWL FKGYGVVFSS GERAKQLRRF SIATLRDFGV GKRGIEERIQ EEAGFLIDSF RKTNGAFIDP TFYLSRTVSN VISSIVFGDR FDYEDKEFLS LLRMMLGSFQ FTATSMGQLY EMFSSVMKHL PGPQQQAFKE LQGLEDFITK KVEHNQRTLD PNSPRDFIDS FLIRMLEEKK NPNTEFYMKN LVLTTLNLFF AGTETVSTTL RYGFLLLMKH PDIEAKVHEE IDRVIGRNRQ PKYEDRMKMP YTEAVIHEIQ RFADMIPMGL ARRVTKDTKF RDFLLPKGTE VFPMLGSVLK DPKFFSNPKD FNPKHFLDDK GQFKKNDAFV PFSIGKRYCF GEGLARMELF LFLTNIMQNF HFKSTQAPQD IDVSPRLVGF ATIPPTYTMS FLSR // ID CP2BA_MOUSE Reviewed; 500 AA. AC P12791; Q62397; DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1989, sequence version 1. DT 19-FEB-2014, entry version 113. DE RecName: Full=Cytochrome P450 2B10; DE EC=1.14.14.1; DE AltName: Full=CYPIIB10; DE AltName: Full=CYPIIB20; DE AltName: Full=Cytochrome P450 2B20; DE AltName: Full=Cytochrome P450 clone PF3/46; DE AltName: Full=Cytochrome P450-16-alpha; DE AltName: Full=P24; DE AltName: Full=Testosterone 16-alpha hydroxylase; GN Name=Cyp2b10; Synonyms=Cyp2b-10, Cyp2b20; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=3219345; DOI=10.1021/bi00417a035; RA Noshiro M., Lakso M., Kawajiri K., Negishi M.; RT "Rip locus: regulation of female-specific isozyme (I-P-450(16 alpha) RT of testosterone 16 alpha-hydroxylase in mouse liver, chromosome RT localization, and cloning of P-450 cDNA."; RL Biochemistry 27:6434-6443(1988). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-452 (ISOFORM 2). RC STRAIN=BALB/c; TISSUE=Liver; RX PubMed=8831708; DOI=10.1006/bbrc.1996.1447; RA Damon M., Fautrel A., Marc N., Guillouzo A., Corcos L.; RT "Isolation of a new mouse cDNA clone: hybrid form of cytochrome P450 RT 2b10 and NADPH-cytochrome P450 oxidoreductase."; RL Biochem. Biophys. Res. Commun. 226:900-905(1996). RN [3] RP PROTEIN SEQUENCE OF 1-15, AND INDUCTION. RX PubMed=2779523; RA Bornheim L.M., Correia M.A.; RT "Purification and characterization of a mouse liver cytochrome P-450 RT induced by cannabidiol."; RL Mol. Pharmacol. 36:377-383(1989). CC -!- FUNCTION: Cytochromes P450 are a group of heme-thiolate CC monooxygenases. In liver microsomes, this enzyme is involved in an CC NADPH-dependent electron transport pathway. It oxidizes a variety CC of structurally unrelated compounds, including steroids, fatty CC acids, and xenobiotics. CC -!- CATALYTIC ACTIVITY: RH + reduced flavoprotein + O(2) = ROH + CC oxidized flavoprotein + H(2)O. CC -!- COFACTOR: Heme group (By similarity). CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral CC membrane protein. Microsome membrane; Peripheral membrane protein. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P12791-1; Sequence=Displayed; CC Name=2; CC IsoId=P12791-2; Sequence=VSP_022500; CC -!- INDUCTION: Up-regulated by cannabidiol. CC -!- SIMILARITY: Belongs to the cytochrome P450 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M21856; AAA40425.1; -; mRNA. DR EMBL; X99715; CAA68051.1; ALT_SEQ; mRNA. DR PIR; B31047; B31047. DR UniGene; Mm.218749; -. DR ProteinModelPortal; P12791; -. DR SMR; P12791; 28-500. DR ChEMBL; CHEMBL1907983; -. DR PaxDb; P12791; -. DR PRIDE; P12791; -. DR MGI; MGI:88598; Cyp2b10. DR eggNOG; COG2124; -. DR HOGENOM; HOG000036992; -. DR HOVERGEN; HBG015789; -. DR InParanoid; P12791; -. DR ChiTaRS; Cyp2b10; mouse. DR PRO; PR:P12791; -. DR Genevestigator; P12791; -. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0070330; F:aromatase activity; IEA:UniProtKB-EC. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR Gene3D; 1.10.630.10; -; 1. DR InterPro; IPR001128; Cyt_P450. DR InterPro; IPR002401; Cyt_P450_E_grp-I. DR InterPro; IPR008068; Cyt_P450_E_grp-I_CYP2B-like. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00463; EP450I. DR PRINTS; PR01685; EP450ICYP2B. DR PRINTS; PR00385; P450. DR SUPFAM; SSF48264; SSF48264; 1. PE 1: Evidence at protein level; KW Alternative splicing; Complete proteome; Direct protein sequencing; KW Endoplasmic reticulum; Heme; Iron; Membrane; Metal-binding; Microsome; KW Monooxygenase; Oxidoreductase; Phosphoprotein; Reference proteome. FT CHAIN 1 500 Cytochrome P450 2B10. FT /FTId=PRO_0000051685. FT METAL 445 445 Iron (heme axial ligand). FT MOD_RES 128 128 Phosphoserine; by PKA (By similarity). FT VAR_SEQ 433 441 Missing (in isoform 2). FT /FTId=VSP_022500. FT CONFLICT 55 55 L -> F (in Ref. 2; CAA68051). FT CONFLICT 178 178 V -> I (in Ref. 2; CAA68051). FT CONFLICT 251 253 RHK -> KHR (in Ref. 2; CAA68051). FT CONFLICT 280 281 NA -> HT (in Ref. 2; CAA68051). FT CONFLICT 298 298 V -> A (in Ref. 2; CAA68051). FT CONFLICT 308 308 H -> R (in Ref. 2; CAA68051). FT CONFLICT 321 321 T -> A (in Ref. 2; CAA68051). FT CONFLICT 349 349 S -> T (in Ref. 2; CAA68051). FT CONFLICT 376 376 L -> M (in Ref. 2; CAA68051). FT CONFLICT 412 412 Q -> H (in Ref. 2; CAA68051). SQ SEQUENCE 500 AA; 56744 MW; F660A00D8D0FBA94 CRC64; MEPSVLLLLA LLVGFLLLLA RGHPKSRGNF PPGPRPLPLL GNLLQMDRGG LLKSLIQLRE KYGDVFTVHL GPRPVVMLCG TDTIREALVG QAEAFSGRGT VAVVEPTFKE YGVIFANGER WKTLRRFSLA TMRDFGMGKR SVEERIQEEA QCLVEELRKS QGAPLDPTFL FQCITANVIC SIVFGERFEY TDRQFLRLLE LFYQTFSLIS SFSSQMFELF SGFLKYFPGA HRQISKNLQE LLDYIGHSVE RHKATLDPSV PRDFIDIYLL RMEKEKSNQN AEFHHQNLMM SVLSLFFVGT ETSSTTLHYG FLLMLKYPHV TEKVQKEIDQ VIGSHRLPTL DDRTKMPYSD AVIHEIQRFS DLIPIGVPHR VTKDTLFRGY LLPKNTEVYP ILSSALHDPQ YFEQPDSFNP DQFLDANGAL KKSEAFLPFS TGQIFDQKSV GKRICLGESI ARSELFLFFT SILQNFSVAS HVAPKDIDLT PKESGIGKIP PTYQICFLAR // ID CP26B_MOUSE Reviewed; 512 AA. AC Q811W2; Q3TM12; DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2003, sequence version 1. DT 19-FEB-2014, entry version 108. DE RecName: Full=Cytochrome P450 26B1; DE EC=1.14.-.-; DE AltName: Full=Cytochrome P450 retinoic acid-inactivating 2; DE Short=Cytochrome P450RAI-2; GN Name=Cyp26b1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY. RC STRAIN=C57BL/6; TISSUE=Testis; RX PubMed=12617826; DOI=10.1016/S1567-133X(02)00022-4; RA Menke D.B., Page D.C.; RT "Sexually dimorphic gene expression in the developing mouse gonad."; RL Gene Expr. Patterns 2:359-367(2002). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Embryo, and Mammary gland; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6; TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP FUNCTION, DISRUPTION PHENOTYPE, AND DEVELOPMENTAL STAGE. RX PubMed=16574820; DOI=10.1126/science.1125691; RA Bowles J., Knight D., Smith C., Wilhelm D., Richman J., Mamiya S., RA Yashiro K., Chawengsaksophak K., Wilson M.J., Rossant J., Hamada H., RA Koopman P.; RT "Retinoid signaling determines germ cell fate in mice."; RL Science 312:596-600(2006). RN [7] RP FUNCTION, AND DEVELOPMENTAL STAGE. RX PubMed=16461896; DOI=10.1073/pnas.0510813103; RA Koubova J., Menke D.B., Zhou Q., Capel B., Griswold M.D., Page D.C.; RT "Retinoic acid regulates sex-specific timing of meiotic initiation in RT mice."; RL Proc. Natl. Acad. Sci. U.S.A. 103:2474-2479(2006). RN [8] RP FUNCTION. RX PubMed=19838304; DOI=10.1371/journal.pone.0007501; RA Li H., MacLean G., Cameron D., Clagett-Dame M., Petkovich M.; RT "Cyp26b1 expression in murine Sertoli cells is required to maintain RT male germ cells in an undifferentiated state during embryogenesis."; RL PLoS ONE 4:E7501-E7501(2009). RN [9] RP FUNCTION IN SKELETAL DEVELOPMENT. RX PubMed=22019272; DOI=10.1016/j.ajhg.2011.09.015; RA Laue K., Pogoda H.M., Daniel P.B., van Haeringen A., Alanay Y., RA von Ameln S., Rachwalski M., Morgan T., Gray M.J., Breuning M.H., RA Sawyer G.M., Sutherland-Smith A.J., Nikkels P.G., Kubisch C., RA Bloch W., Wollnik B., Hammerschmidt M., Robertson S.P.; RT "Craniosynostosis and multiple skeletal anomalies in humans and RT zebrafish result from a defect in the localized degradation of RT retinoic acid."; RL Am. J. Hum. Genet. 89:595-606(2011). CC -!- FUNCTION: Involved in the metabolism of retinoic acid (RA), CC rendering this classical morphogen inactive through oxidation. CC Involved in the specific inactivation of all-trans-retinoic acid CC (all-trans-RA), with a preference for the following substrates: CC all-trans-RA > 9-cis-RA > 13-cis-RA. Generates several CC hydroxylated forms of RA, including 4-OH-RA, 4-oxo-RA, and 18-OH- CC RA. Esential for postnatal survival. Plays a central role in germ CC cell development: acts by degrading RA in the developing testis, CC preventing STRA8 expression, thereby leading to delay of meiosis. CC Required for the maintenance of the undifferentiated state of male CC germ cells during embryonic development in Sertoli cells, inducing CC arrest in G0 phase of the cell cycle and preventing meiotic entry. CC Plays a role in skeletal development, both at the level of CC patterning and in the ossification of bone and the establishment CC of some synovial joints. CC -!- COFACTOR: Heme group (By similarity). CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral CC membrane protein (By similarity). Microsome membrane; Peripheral CC membrane protein (By similarity). CC -!- DEVELOPMENTAL STAGE: In the embryonic male gonad, expressed in CC somatic cells as early as E11.5 and persist throughout CC development. Expression is detected in peritubular myoepithelial CC cells in the postnatal testis, while expression is absent in CC developing and adult ovaries. CC -!- DISRUPTION PHENOTYPE: Germ cells enter meiosis precociously in CC embryonic testes, due to strong-up-regulation of Stra8. CC -!- SIMILARITY: Belongs to the cytochrome P450 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AY134662; AAN08613.1; -; mRNA. DR EMBL; AK137124; BAE23242.1; -; mRNA. DR EMBL; AK166211; BAE38630.1; -; mRNA. DR EMBL; AC153606; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH466523; EDK99117.1; -; Genomic_DNA. DR EMBL; BC059246; AAH59246.1; -; mRNA. DR RefSeq; NP_001171184.1; NM_001177713.1. DR RefSeq; NP_780684.1; NM_175475.3. DR UniGene; Mm.255246; -. DR ProteinModelPortal; Q811W2; -. DR SMR; Q811W2; 47-493. DR STRING; 10090.ENSMUSP00000076886; -. DR PhosphoSite; Q811W2; -. DR PRIDE; Q811W2; -. DR Ensembl; ENSMUST00000077705; ENSMUSP00000076886; ENSMUSG00000063415. DR Ensembl; ENSMUST00000168003; ENSMUSP00000128391; ENSMUSG00000063415. DR GeneID; 232174; -. DR KEGG; mmu:232174; -. DR UCSC; uc009coy.2; mouse. DR CTD; 56603; -. DR MGI; MGI:2176159; Cyp26b1. DR GeneTree; ENSGT00660000095370; -. DR HOGENOM; HOG000220829; -. DR HOVERGEN; HBG051099; -. DR InParanoid; Q811W2; -. DR KO; K12664; -. DR OMA; GIQARQT; -. DR OrthoDB; EOG7F24SP; -. DR TreeFam; TF105093; -. DR NextBio; 380970; -. DR PRO; PR:Q811W2; -. DR Bgee; Q811W2; -. DR Genevestigator; Q811W2; -. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0008401; F:retinoic acid 4-hydroxylase activity; IEA:Ensembl. DR GO; GO:0001972; F:retinoic acid binding; IEA:Ensembl. DR GO; GO:0060349; P:bone morphogenesis; IEA:Ensembl. DR GO; GO:0001709; P:cell fate determination; IMP:MGI. DR GO; GO:0071300; P:cellular response to retinoic acid; IEP:UniProtKB. DR GO; GO:0070268; P:cornification; IMP:MGI. DR GO; GO:0030326; P:embryonic limb morphogenesis; IMP:MGI. DR GO; GO:0061436; P:establishment of skin barrier; IMP:MGI. DR GO; GO:0007140; P:male meiosis; IMP:MGI. DR GO; GO:0048387; P:negative regulation of retinoic acid receptor signaling pathway; IMP:MGI. DR GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB. DR GO; GO:2001037; P:positive regulation of tongue muscle cell differentiation; IMP:UniProtKB. DR GO; GO:0009954; P:proximal/distal pattern formation; IMP:MGI. DR GO; GO:0034653; P:retinoic acid catabolic process; IC:MGI. DR GO; GO:0048384; P:retinoic acid receptor signaling pathway; IMP:UniProtKB. DR GO; GO:0007283; P:spermatogenesis; IMP:MGI. DR GO; GO:0043587; P:tongue morphogenesis; IMP:UniProtKB. DR Gene3D; 1.10.630.10; -; 1. DR InterPro; IPR001128; Cyt_P450. DR InterPro; IPR017972; Cyt_P450_CS. DR InterPro; IPR002403; Cyt_P450_E_grp-IV. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00465; EP450IV. DR PRINTS; PR00385; P450. DR SUPFAM; SSF48264; SSF48264; 1. DR PROSITE; PS00086; CYTOCHROME_P450; 1. PE 1: Evidence at protein level; KW Complete proteome; Endoplasmic reticulum; Heme; Iron; Membrane; KW Metal-binding; Microsome; Monooxygenase; Oxidoreductase; KW Reference proteome. FT CHAIN 1 512 Cytochrome P450 26B1. FT /FTId=PRO_0000416905. FT METAL 441 441 Iron (heme axial ligand) (Potential). FT CONFLICT 67 68 LQ -> TR (in Ref. 2; BAE38630). SQ SEQUENCE 512 AA; 57375 MW; AAA063DE5718824E CRC64; MLFEGLELVS ALATLAACLV SVTLLLAVSQ QLWQLRWAAT RDKSCKLPIP KGSMGFPLIG ETGHWLLQGS GFQSSRREKY GNVFKTHLLG RPLIRVTGAE NVRKILLGEH QLVSTEWPRS ARVLLGPNTV ANSIGDIHRN KRKVFSKIFS HEALESYLPK IQLVIQDTLR AWSSQPEAIN VYQEAQRLTF RMAVRVLLGF SIPEEDLGHL FEVYQQFVEN VFSLPVDLPF SGYRRGIQAR QILQKGLEKA IREKLQCTQG KDYSDALDIL IESSKEHGKE MTMQELKDGT LELIFAAYAT TASASTSLIM QLLKHPAVLE KLREELRAQG LLHGGGCPCE GTLRLDTLSS LRYLDCVIKE VMRLFTPVSG GYRTVLQTFE LDGFQIPKGW SVMYSIRDTH DTAPVFKDVN VFDPDRFSQA RSEDKDGRFH YLPFGGGVRT CLGKHLAKLF LKVLAVELAS TSRFELATRT FPRITLVPVL HPVDGLSVKF FGLDSNQNEI LPETEAMLSA TV // ID CP255_MOUSE Reviewed; 490 AA. AC Q9D816; DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 19-FEB-2014, entry version 95. DE RecName: Full=Cytochrome P450 2C55; DE EC=1.14.14.1; DE AltName: Full=CYPIIC55; GN Name=Cyp2c55; Synonyms=Cyp2c-55; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY. RC STRAIN=C57BL/6; TISSUE=Colon; RX PubMed=15102943; DOI=10.1124/mol.65.5.1148; RA Wang H., Zhao Y., Bradbury J.A., Graves J.P., Foley J., RA Blaisdell J.A., Goldstein J.A., Zeldin D.C.; RT "Cloning, expression, and characterization of three new mouse RT cytochrome p450 enzymes and partial characterization of their fatty RT acid oxidation activities."; RL Mol. Pharmacol. 65:1148-1158(2004). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Small intestine; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Colon; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: Metabolizes arachidonic acid mainly to 19- CC hydroxyeicosatetraenoic acid (HETE). CC -!- CATALYTIC ACTIVITY: RH + reduced flavoprotein + O(2) = ROH + CC oxidized flavoprotein + H(2)O. CC -!- COFACTOR: Heme group (By similarity). CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral CC membrane protein. Microsome membrane; Peripheral membrane protein. CC -!- TISSUE SPECIFICITY: Highest level in colon. Low levels in liver CC and small intestine. CC -!- INDUCTION: P450 can be induced to high levels in liver and other CC tissues by various foreign compounds, including drugs, pesticides, CC and carcinogens. CC -!- SIMILARITY: Belongs to the cytochrome P450 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AY206875; AAO52738.1; -; mRNA. DR EMBL; AK008580; BAB25759.1; -; mRNA. DR EMBL; BC010824; AAH10824.1; -; mRNA. DR RefSeq; NP_082365.1; NM_028089.3. DR UniGene; Mm.142581; -. DR ProteinModelPortal; Q9D816; -. DR SMR; Q9D816; 30-489. DR MINT; MINT-1870122; -. DR STRING; 10090.ENSMUSP00000025966; -. DR PhosphoSite; Q9D816; -. DR PaxDb; Q9D816; -. DR PRIDE; Q9D816; -. DR Ensembl; ENSMUST00000025966; ENSMUSP00000025966; ENSMUSG00000025002. DR GeneID; 72082; -. DR KEGG; mmu:72082; -. DR UCSC; uc008hju.1; mouse. DR CTD; 72082; -. DR MGI; MGI:1919332; Cyp2c55. DR eggNOG; COG2124; -. DR GeneTree; ENSGT00680000099783; -. DR HOGENOM; HOG000036992; -. DR HOVERGEN; HBG015789; -. DR InParanoid; Q9D816; -. DR KO; K07413; -. DR OMA; IQEEASC; -. DR OrthoDB; EOG7RBZ85; -. DR TreeFam; TF352043; -. DR NextBio; 335388; -. DR PRO; PR:Q9D816; -. DR Bgee; Q9D816; -. DR Genevestigator; Q9D816; -. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0070330; F:aromatase activity; IEA:UniProtKB-EC. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR Gene3D; 1.10.630.10; -; 1. DR InterPro; IPR001128; Cyt_P450. DR InterPro; IPR017972; Cyt_P450_CS. DR InterPro; IPR002401; Cyt_P450_E_grp-I. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00463; EP450I. DR PRINTS; PR00385; P450. DR SUPFAM; SSF48264; SSF48264; 1. DR PROSITE; PS00086; CYTOCHROME_P450; 1. PE 2: Evidence at transcript level; KW Complete proteome; Endoplasmic reticulum; Heme; Iron; Membrane; KW Metal-binding; Microsome; Monooxygenase; Oxidoreductase; KW Reference proteome. FT CHAIN 1 490 Cytochrome P450 2C55. FT /FTId=PRO_0000282959. FT METAL 435 435 Iron (heme axial ligand) (By similarity). SQ SEQUENCE 490 AA; 56096 MW; 5CB0F771C0268FEC CRC64; MDPVLVLVLT LSCLLLLSLW RQNSGRGKLP PGPTPFPIIG NILQIDIKNI SKSFNYFSKV YGPVFTLYFG SKPTVVVHGY EAVKEALDDL GEEFSGRGSF QIFERINNDL GVIFSNGTKW KELRRFSIMT LRSFGMGKRS IEDRIQEEAS CLVEELRKAN GSLCDPTFIL SCAPSNVICS VIFHNRFDYK DEKFLNLMER LNENFKILNS PWMQVYNALP TLINYLPGSH NKVIKNFTEI KSYILGRVKE HQETLDMDNP RDFIDCFLIK MEQEKHNPHS EFTIESLMAT VTDIFVAGTE TTNITLRYGL LLLLKHTEVT AKVQAEIDHV IGRHRSPCMQ DRTRMPYTDA MVHEIQRYID LIPNNVPHAA TCNVRFRSYF IPKGTELVTS LTSVLHDDKE FPNPEVFDPG HFLDENGNFK KSDYFMPFSI GKRMCVGEAL ARTELFLILT TILQNFNLKS LVDTKDIDTT PVANTFGRVP PSYQLYFIPR // ID CP2BJ_MOUSE Reviewed; 492 AA. AC O55071; B2RQK1; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1998, sequence version 1. DT 19-FEB-2014, entry version 105. DE RecName: Full=Cytochrome P450 2B19; DE EC=1.14.14.1; DE AltName: Full=CYPIIB19; GN Name=Cyp2b19; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=C57BL/6; TISSUE=Skin; RX PubMed=9799616; DOI=10.1006/geno.1998.5533; RA Keeney D.S.; RT "The novel skin-specific cytochrome P450 Cyp2b19 maps to proximal RT chromosome 7 in the mouse, near a cluster of Cyp2 family genes."; RL Genomics 53:417-419(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: Cytochromes P450 are a group of heme-thiolate CC monooxygenases. In liver microsomes, this enzyme is involved in an CC NADPH-dependent electron transport pathway. It oxidizes a variety CC of structurally unrelated compounds, including steroids, fatty CC acids, and xenobiotics. CC -!- CATALYTIC ACTIVITY: RH + reduced flavoprotein + O(2) = ROH + CC oxidized flavoprotein + H(2)O. CC -!- COFACTOR: Heme group (By similarity). CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral CC membrane protein. Microsome membrane; Peripheral membrane protein. CC -!- TISSUE SPECIFICITY: Expressed only in differentiated keratinocytes CC in skin. CC -!- SIMILARITY: Belongs to the cytochrome P450 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF047529; AAC78770.1; -; mRNA. DR EMBL; BC137965; AAI37966.1; -; mRNA. DR EMBL; BC137966; AAI37967.1; -; mRNA. DR RefSeq; NP_031840.1; NM_007814.1. DR UniGene; Mm.14098; -. DR ProteinModelPortal; O55071; -. DR SMR; O55071; 29-492. DR PhosphoSite; O55071; -. DR PaxDb; O55071; -. DR PRIDE; O55071; -. DR Ensembl; ENSMUST00000077855; ENSMUSP00000077021; ENSMUSG00000066704. DR GeneID; 13090; -. DR KEGG; mmu:13090; -. DR UCSC; uc009fus.1; mouse. DR CTD; 13090; -. DR MGI; MGI:107303; Cyp2b19. DR eggNOG; COG2124; -. DR GeneTree; ENSGT00670000097868; -. DR HOGENOM; HOG000036992; -. DR HOVERGEN; HBG015789; -. DR InParanoid; B2RQK1; -. DR KO; K07412; -. DR OMA; IVANIIC; -. DR OrthoDB; EOG7RBZ85; -. DR TreeFam; TF352043; -. DR NextBio; 283066; -. DR PRO; PR:O55071; -. DR Bgee; O55071; -. DR Genevestigator; O55071; -. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0070330; F:aromatase activity; IEA:UniProtKB-EC. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR Gene3D; 1.10.630.10; -; 1. DR InterPro; IPR001128; Cyt_P450. DR InterPro; IPR017972; Cyt_P450_CS. DR InterPro; IPR002401; Cyt_P450_E_grp-I. DR InterPro; IPR008068; Cyt_P450_E_grp-I_CYP2B-like. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00463; EP450I. DR PRINTS; PR01685; EP450ICYP2B. DR PRINTS; PR00385; P450. DR SUPFAM; SSF48264; SSF48264; 1. DR PROSITE; PS00086; CYTOCHROME_P450; 1. PE 2: Evidence at transcript level; KW Complete proteome; Endoplasmic reticulum; Heme; Iron; Membrane; KW Metal-binding; Microsome; Monooxygenase; Oxidoreductase; KW Phosphoprotein; Reference proteome. FT CHAIN 1 492 Cytochrome P450 2B19. FT /FTId=PRO_0000051689. FT METAL 437 437 Iron (heme axial ligand) (By similarity). FT MOD_RES 129 129 Phosphoserine; by PKA (By similarity). SQ SEQUENCE 492 AA; 55997 MW; 9E685AF61EE2DFA2 CRC64; MEFSVLLLLA LTTGFLIFLV SQSQPKTHGH FPPGPRPLPF LGNLLQMDRR GLLSSFIQLQ EKYGDVFTVH LGPRPVVMLC GTDTIREALV NQAEAFSGRG TVAVLDPIVQ GYGVIFSSGE RWKTLRRFSL ATMRDFGMGK RSVEERIKEE AQCLVEELKK YKGAPLNPTF YFQCIVANII CSIVFGERFD YKDHQFLHLL NLIYQTFSLM SSLSSQVFEL FSAILKYFPG AHRQISKNLQ EILDYIGHSV EKHRATLDPS APRDFIDTYL LRMEKEKSNH HTEFHHQNLV ISVLSLFFAG TETTSTTLRY SFLIMLKYPH VAEKVQKEID QVIGSHRLPT LDDRTKMPYT DAVIHEIQRF TDLAPIGLPH KVTKDTLFRG YLIPKNTEVY PILSSALHDP RYFEQPDSFN PEHFLDANGA LKTNEAFMPF STGKRICLGE GIARNELFLF FTTILQNFSL ASPVAPENID LIPNNSGATK TPPQYQIHFL SR // ID CP2CT_MOUSE Reviewed; 490 AA. AC Q64458; E9QMD8; Q8WUN8; DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 2. DT 19-MAR-2014, entry version 120. DE RecName: Full=Cytochrome P450 2C29; DE EC=1.14.14.1; DE AltName: Full=Aldehyde oxygenase; DE AltName: Full=CYPIIC29; DE AltName: Full=Cytochrome P-450 MUT-2; GN Name=Cyp2c29; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=C57BL/6; TISSUE=Liver; RX PubMed=8130255; DOI=10.1016/0005-2728(94)90237-2; RA Matsunaga T., Watanabe K., Yamamoto I., Negishi M., Gonzalez F.J., RA Yoshimura H.; RT "cDNA cloning and sequence of CYP2C29 encoding P-450 MUT-2, a RT microsomal aldehyde oxygenase."; RL Biochim. Biophys. Acta 1184:299-301(1994). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Liver; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-249; LYS-252 AND LYS-375, RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23576753; DOI=10.1073/pnas.1302961110; RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., RA Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.; RT "Label-free quantitative proteomics of the lysine acetylome in RT mitochondria identifies substrates of SIRT3 in metabolic pathways."; RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013). CC -!- FUNCTION: Metabolizes arachidonic acid to produce 14,15-cis- CC epoxyeicosatrienoic acid (EET). CC -!- CATALYTIC ACTIVITY: RH + reduced flavoprotein + O(2) = ROH + CC oxidized flavoprotein + H(2)O. CC -!- COFACTOR: Heme group (By similarity). CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral CC membrane protein. Microsome membrane; Peripheral membrane protein. CC -!- INDUCTION: P450 can be induced to high levels in liver and other CC tissues by various foreign compounds, including drugs, pesticides, CC and carcinogens. CC -!- SIMILARITY: Belongs to the cytochrome P450 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; D17674; BAA04555.1; -; mRNA. DR EMBL; AC120840; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC139233; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC019908; AAH19908.1; -; mRNA. DR PIR; I49610; I49610. DR RefSeq; NP_031841.3; NM_007815.3. DR UniGene; Mm.20764; -. DR ProteinModelPortal; Q64458; -. DR SMR; Q64458; 30-490. DR IntAct; Q64458; 3. DR MINT; MINT-1864139; -. DR PhosphoSite; Q64458; -. DR PaxDb; Q64458; -. DR PRIDE; Q64458; -. DR Ensembl; ENSMUST00000003137; ENSMUSP00000003137; ENSMUSG00000003053. DR GeneID; 13095; -. DR KEGG; mmu:13095; -. DR UCSC; uc008hjz.1; mouse. DR CTD; 13095; -. DR MGI; MGI:103238; Cyp2c29. DR eggNOG; COG2124; -. DR GeneTree; ENSGT00680000099783; -. DR HOGENOM; HOG000036992; -. DR HOVERGEN; HBG015789; -. DR InParanoid; Q64458; -. DR KO; K07413; -. DR OMA; KQANNIE; -. DR TreeFam; TF352043; -. DR ChiTaRS; Cyp2c29; mouse. DR NextBio; 283074; -. DR PRO; PR:Q64458; -. DR ArrayExpress; Q64458; -. DR Bgee; Q64458; -. DR Genevestigator; Q64458; -. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0070330; F:aromatase activity; IEA:UniProtKB-EC. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR Gene3D; 1.10.630.10; -; 1. DR InterPro; IPR001128; Cyt_P450. DR InterPro; IPR017972; Cyt_P450_CS. DR InterPro; IPR002401; Cyt_P450_E_grp-I. DR InterPro; IPR008068; Cyt_P450_E_grp-I_CYP2B-like. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00463; EP450I. DR PRINTS; PR01685; EP450ICYP2B. DR PRINTS; PR00385; P450. DR SUPFAM; SSF48264; SSF48264; 1. DR PROSITE; PS00086; CYTOCHROME_P450; 1. PE 1: Evidence at protein level; KW Acetylation; Complete proteome; Endoplasmic reticulum; Heme; Iron; KW Membrane; Metal-binding; Microsome; Monooxygenase; Oxidoreductase; KW Reference proteome. FT CHAIN 1 490 Cytochrome P450 2C29. FT /FTId=PRO_0000051717. FT METAL 435 435 Iron (heme axial ligand) (By similarity). FT MOD_RES 249 249 N6-acetyllysine. FT MOD_RES 252 252 N6-acetyllysine. FT MOD_RES 375 375 N6-acetyllysine. FT CONFLICT 106 106 I -> M (in Ref. 3; AAH19908). FT CONFLICT 415 415 G -> A (in Ref. 1; BAA04555). SQ SEQUENCE 490 AA; 55716 MW; 17D6FF46002E169A CRC64; MDLVVFLALT LSCLILLSLW RQSSGRGKLP PGPTPLPIIG NFLQIDVKNI SQSFTNFSKA YGPVFTLYLG SKPTVILHGY EAVKEALIDR GEEFAGRGSF PMAEKIIKGF GVVFSNGNRW KEMRRFTLMT LRNLGMGKRN IEDRVQEEAQ CLVEELRKTK GSPCDPTFIL SCAPCNVICS IIFQNRFDYK DKEFLILMDK INENVKILSS PWLQVCNSFP SLIDYCPGSH HKIVKNFNYL KSYLLEKIKE HKESLDVTNP RDFIDYYLIK QKQVNHIEQS EFSLENLAST INDLFGAGTE TTSTTLRYAL LLLLKYPDVT AKVQEEIDRV VGRHRSPCMQ DRSHMPYTDA MIHEVQRFID LLPTSLPHAV TCDIKFRKYL IPKGTTVITS LSSVLHDSKE FPNPEMFDPG HFLNGNGNFK KSDYFMPFST GKRICAGEGL ARMELFLILT TILQNFKLKS LVHPKEIDIT PVMNGFASLP PPYQLCFIPL // ID CP2D9_MOUSE Reviewed; 504 AA. AC P11714; Q64489; Q921V1; DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 2. DT 19-FEB-2014, entry version 111. DE RecName: Full=Cytochrome P450 2D9; DE EC=1.14.14.1; DE AltName: Full=CYPIID9; DE AltName: Full=Cytochrome P450-16-alpha; DE AltName: Full=Cytochrome P450CA; DE AltName: Full=Testosterone 16-alpha hydroxylase; GN Name=Cyp2d9; Synonyms=Cyp2d-9; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=2831949; DOI=10.1021/bi00400a029; RA Wong G., Kawajiri K., Negishi M.; RT "Gene family of male-specific testosterone 16 alpha-hydroxylase (C-P- RT 450(16) alpha) in mouse liver: cDNA sequences, neonatal imprinting, RT and reversible regulation by androgen."; RL Biochemistry 26:8683-8690(1987). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=129/J; TISSUE=Liver; RX PubMed=2788458; DOI=10.1021/bi00437a039; RA Ichikawa T., Itakura T., Negishi M.; RT "Functional characterization of two cytochrome P-450s within the RT mouse, male-specific steroid 16 alpha-hydroxylase gene family: RT expression in mammalian cells and chimeric proteins."; RL Biochemistry 28:4779-4784(1989). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=2914938; RA Wong G., Itakura T., Kawajiri K., Skow L., Negishi M.; RT "Gene family of male-specific testosterone 16 alpha-hydroxylase (C-P- RT 450(16 alpha)) in mice. Organization, differential regulation, and RT chromosome localization."; RL J. Biol. Chem. 264:2920-2927(1989). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Mammary tumor; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: Cytochromes P450 are a group of heme-thiolate CC monooxygenases. In liver microsomes, this enzyme is involved in an CC NADPH-dependent electron transport pathway. It oxidizes a variety CC of structurally unrelated compounds, including steroids, fatty CC acids, and xenobiotics. CC -!- CATALYTIC ACTIVITY: RH + reduced flavoprotein + O(2) = ROH + CC oxidized flavoprotein + H(2)O. CC -!- COFACTOR: Heme group (By similarity). CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral CC membrane protein. Microsome membrane; Peripheral membrane protein. CC -!- INDUCTION: P450 can be induced to high levels in liver and other CC tissues by various foreign compounds, including drugs, pesticides, CC and carcinogens. CC -!- SIMILARITY: Belongs to the cytochrome P450 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M23998; AAA40427.1; -; mRNA. DR EMBL; M23997; AAA40428.1; ALT_SEQ; mRNA. DR EMBL; M27168; AAA39876.1; -; mRNA. DR EMBL; M24267; AAA75462.1; -; Genomic_DNA. DR EMBL; M24262; AAA75462.1; JOINED; Genomic_DNA. DR EMBL; CH466550; EDL04501.1; -; Genomic_DNA. DR EMBL; BC010593; AAH10593.1; -; mRNA. DR EMBL; BC094015; AAH94015.1; -; mRNA. DR PIR; B27384; B27384. DR PIR; S15806; A27384. DR RefSeq; NP_034136.2; NM_010006.2. DR UniGene; Mm.226708; -. DR ProteinModelPortal; P11714; -. DR SMR; P11714; 51-500. DR IntAct; P11714; 1. DR MINT; MINT-4122639; -. DR PaxDb; P11714; -. DR PRIDE; P11714; -. DR Ensembl; ENSMUST00000089129; ENSMUSP00000086530; ENSMUSG00000068086. DR GeneID; 13105; -. DR KEGG; mmu:13105; -. DR UCSC; uc007wzg.2; mouse. DR CTD; 13105; -. DR MGI; MGI:88606; Cyp2d9. DR eggNOG; COG2124; -. DR GeneTree; ENSGT00730000110385; -. DR HOGENOM; HOG000036991; -. DR HOVERGEN; HBG015789; -. DR InParanoid; Q921V1; -. DR KO; K07414; -. DR OrthoDB; EOG7RBZ85; -. DR TreeFam; TF352043; -. DR NextBio; 283098; -. DR PRO; PR:P11714; -. DR Bgee; P11714; -. DR Genevestigator; P11714; -. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0070330; F:aromatase activity; IEA:UniProtKB-EC. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR Gene3D; 1.10.630.10; -; 1. DR InterPro; IPR001128; Cyt_P450. DR InterPro; IPR017972; Cyt_P450_CS. DR InterPro; IPR002401; Cyt_P450_E_grp-I. DR InterPro; IPR008069; Cyt_P450_E_grp-I_CYP2D-like. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00463; EP450I. DR PRINTS; PR01686; EP450ICYP2D. DR PRINTS; PR00385; P450. DR SUPFAM; SSF48264; SSF48264; 1. DR PROSITE; PS00086; CYTOCHROME_P450; 1. PE 2: Evidence at transcript level; KW Complete proteome; Endoplasmic reticulum; Heme; Iron; Membrane; KW Metal-binding; Microsome; Monooxygenase; Oxidoreductase; KW Reference proteome. FT CHAIN 1 504 Cytochrome P450 2D9. FT /FTId=PRO_0000051734. FT METAL 446 446 Iron (heme axial ligand). FT CONFLICT 54 55 LG -> QD (in Ref. 2; AAA39876). FT CONFLICT 281 281 E -> Q (in Ref. 1; AAA40428/AAA40427, 2; FT AAA39876 and 3; AAA75462). SQ SEQUENCE 504 AA; 56950 MW; 6DC93B3985EFB8A2 CRC64; MELLTGTDLW PVAIFTVIFI LLVDLTHQRQ RWTSRYPPGP VPWPVLGNLL QVDLGNMPYS LYKLQNRYGD VFSLQMAWKP MVVINGLKAM KEMLLTCGED TADRPPVPIF EYLGVKPGSQ GVVLAPYGPE WREQRRFSVS TLRNFGLGKK SLEDWVTKEA NHLCDAFTAQ AGQPINPNPM LNKSTCNVIA SLIFARRFEY EDPFLIRMLK VLEQSLTEVS GLIPEVLNAF PILLRIPRLA DKALQGQKSF IAILDNLLTE NRTTWDPVQA PRNLTDAFLA EIEKAKGNPE SSFNDENLLM VVRDLFGAGM LTTSTTLSWA LMLMILHPDV QRRVQQEIDE VIGQVRHPEM ADQAHMPYTN AVIHEVQRFG DIVPVNLPRI TSHDIEVQDF LIPKGTILLP NMSSMLKDES VWEKPLRFHP EHFLDAQGHF VKPEAFMPFS AGRRSCLGEA LARMELFLFF TCLLQRFSFS VPDGQPQPSN SGVYGILVAP SPYQLCAVVR DQGH // ID CP2DA_MOUSE Reviewed; 504 AA. AC P24456; Q64490; DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-1998, sequence version 2. DT 19-FEB-2014, entry version 121. DE RecName: Full=Cytochrome P450 2D10; DE EC=1.14.14.1; DE AltName: Full=CYPIID10; DE AltName: Full=Cytochrome P450-16-alpha; DE AltName: Full=Cytochrome P450CB; DE AltName: Full=Testosterone 16-alpha hydroxylase; GN Name=Cyp2d10; Synonyms=Cyp2d-10; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE. RX PubMed=2914938; RA Wong G., Itakura T., Kawajiri K., Skow L., Negishi M.; RT "Gene family of male-specific testosterone 16 alpha-hydroxylase (C-P- RT 450(16 alpha)) in mice. Organization, differential regulation, and RT chromosome localization."; RL J. Biol. Chem. 264:2920-2927(1989). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=129/J; TISSUE=Liver; RX PubMed=2788458; DOI=10.1021/bi00437a039; RA Ichikawa T., Itakura T., Negishi M.; RT "Functional characterization of two cytochrome P-450s within the RT mouse, male-specific steroid 16 alpha-hydroxylase gene family: RT expression in mammalian cells and chimeric proteins."; RL Biochemistry 28:4779-4784(1989). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Liver, and Salivary gland; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: Cytochromes P450 are a group of heme-thiolate CC monooxygenases. In liver microsomes, this enzyme is involved in an CC NADPH-dependent electron transport pathway. It oxidizes a variety CC of structurally unrelated compounds, including steroids, fatty CC acids, and xenobiotics. CC -!- CATALYTIC ACTIVITY: RH + reduced flavoprotein + O(2) = ROH + CC oxidized flavoprotein + H(2)O. CC -!- COFACTOR: Heme group (By similarity). CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral CC membrane protein. Microsome membrane; Peripheral membrane protein. CC -!- INDUCTION: P450 can be induced to high levels in liver and other CC tissues by various foreign compounds, including drugs, pesticides, CC and carcinogens. CC -!- SIMILARITY: Belongs to the cytochrome P450 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M24263; AAA79023.1; -; Genomic_DNA. DR EMBL; M27167; AAA39878.1; -; mRNA. DR EMBL; BC010989; AAH10989.1; -; mRNA. DR EMBL; BC057924; AAH57924.1; -; mRNA. DR PIR; A30247; A30247. DR RefSeq; NP_034135.2; NM_010005.3. DR UniGene; Mm.174372; -. DR ProteinModelPortal; P24456; -. DR SMR; P24456; 51-500. DR IntAct; P24456; 7. DR MINT; MINT-1862539; -. DR STRING; 10090.ENSMUSP00000072555; -. DR PhosphoSite; P24456; -. DR PaxDb; P24456; -. DR PRIDE; P24456; -. DR Ensembl; ENSMUST00000072776; ENSMUSP00000072555; ENSMUSG00000094806. DR GeneID; 13101; -. DR KEGG; mmu:13101; -. DR UCSC; uc007wzf.2; mouse. DR CTD; 13101; -. DR MGI; MGI:88602; Cyp2d10. DR eggNOG; COG2124; -. DR GeneTree; ENSGT00730000110385; -. DR HOGENOM; HOG000036991; -. DR HOVERGEN; HBG015789; -. DR InParanoid; P24456; -. DR KO; K07414; -. DR OMA; STHGFFA; -. DR OrthoDB; EOG7RBZ85; -. DR TreeFam; TF352043; -. DR NextBio; 283094; -. DR PRO; PR:P24456; -. DR Bgee; P24456; -. DR Genevestigator; P24456; -. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0070330; F:aromatase activity; IEA:UniProtKB-EC. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR Gene3D; 1.10.630.10; -; 1. DR InterPro; IPR001128; Cyt_P450. DR InterPro; IPR017972; Cyt_P450_CS. DR InterPro; IPR002401; Cyt_P450_E_grp-I. DR InterPro; IPR008069; Cyt_P450_E_grp-I_CYP2D-like. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00463; EP450I. DR PRINTS; PR01686; EP450ICYP2D. DR PRINTS; PR00385; P450. DR SUPFAM; SSF48264; SSF48264; 1. DR PROSITE; PS00086; CYTOCHROME_P450; 1. PE 2: Evidence at transcript level; KW Complete proteome; Endoplasmic reticulum; Heme; Iron; Membrane; KW Metal-binding; Microsome; Monooxygenase; Oxidoreductase; KW Reference proteome. FT CHAIN 1 504 Cytochrome P450 2D10. FT /FTId=PRO_0000051735. FT METAL 446 446 Iron (heme axial ligand). FT CONFLICT 46 46 L -> Q (in Ref. 2; AAA39878). FT CONFLICT 221 224 GLIP -> LAYS (in Ref. 1; AAA79023). SQ SEQUENCE 504 AA; 57233 MW; 41375F9834489401 CRC64; MELLTGAGLW SVAIFTVIFI LLVDLMHRHQ RWTSRYPPGP VPWPVLGNLL QVDLDNMPYS LYKLQNRYGD VFSLQMGWKP MVVINGLKAM KEVLLTCGED TADRPQVPIF EYLGVKPGSQ GVVLAPYGPE WREQRRFSVS TLRNFGLGKK SLEDWVTKEA RHLCDAFTAQ AGQPINPNTM LNNAVCNVIA SLIFARRFEY EDPYLIRMQK VLEDSLTEIS GLIPEVLNMF PILLRIPGLP GKVFQGQKSL LAIVENLLTE NRNTWDPDQP PRNLTDAFLA EIEKVKGNAE SSFNDENLRM VVLDLFTAGM VTTSTTLSWA LLLMILHPDV QRRVQQEIDA VIGQVRHPEM ADQARMPYTN AVIHEVQRFG DIAPLNLPRI TSRDIEVQDF LIPKGSILIP NMSSVLKDET VWEKPLRFHP EHFLDAQGHF VKPEAFMPFS AGRRSCLGEP LARMELFLFF TCLLQHFSFS VPNGQPRPRN LGVFPFPVAP YPYQLCAVMR EQGH // ID CP2DB_MOUSE Reviewed; 504 AA. AC P24457; E9Q750; DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot. DT 18-SEP-2013, sequence version 2. DT 19-MAR-2014, entry version 104. DE RecName: Full=Cytochrome P450 2D11; DE EC=1.14.14.1; DE AltName: Full=CYPIID11; DE AltName: Full=Cytochrome P450-16-alpha; DE AltName: Full=Cytochrome P450CC; DE AltName: Full=Testosterone 16-alpha hydroxylase; GN Name=Cyp2d11; Synonyms=Cyp2d-11; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=2914938; RA Wong G., Itakura T., Kawajiri K., Skow L., Negishi M.; RT "Gene family of male-specific testosterone 16 alpha-hydroxylase (C-P- RT 450(16 alpha)) in mice. Organization, differential regulation, and RT chromosome localization."; RL J. Biol. Chem. 264:2920-2927(1989). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). CC -!- FUNCTION: Cytochromes P450 are a group of heme-thiolate CC monooxygenases. In liver microsomes, this enzyme is involved in an CC NADPH-dependent electron transport pathway. It oxidizes a variety CC of structurally unrelated compounds, including steroids, fatty CC acids, and xenobiotics. CC -!- CATALYTIC ACTIVITY: RH + reduced flavoprotein + O(2) = ROH + CC oxidized flavoprotein + H(2)O. CC -!- COFACTOR: Heme group (By similarity). CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral CC membrane protein. Microsome membrane; Peripheral membrane protein. CC -!- INDUCTION: P450 can be induced to high levels in liver and other CC tissues by various foreign compounds, including drugs, pesticides, CC and carcinogens. CC -!- SIMILARITY: Belongs to the cytochrome P450 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M24264; AAA37514.1; -; Genomic_DNA. DR EMBL; AC113593; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR PIR; S19169; S19169. DR RefSeq; NP_001098001.1; NM_001104531.1. DR UniGene; Mm.482764; -. DR ProteinModelPortal; P24457; -. DR MINT; MINT-1838193; -. DR STRING; 10090.ENSMUSP00000086528; -. DR PaxDb; P24457; -. DR PRIDE; P24457; -. DR Ensembl; ENSMUST00000170255; ENSMUSP00000130338; ENSMUSG00000068085. DR GeneID; 545123; -. DR KEGG; mmu:545123; -. DR CTD; 545123; -. DR MGI; MGI:88603; Cyp2d11. DR eggNOG; COG2124; -. DR GeneTree; ENSGT00730000110385; -. DR HOGENOM; HOG000036991; -. DR HOVERGEN; HBG015789; -. DR InParanoid; P24457; -. DR KO; K07414; -. DR OMA; ECFTEIS; -. DR OrthoDB; EOG7RBZ85; -. DR TreeFam; TF352043; -. DR NextBio; 412286; -. DR PRO; PR:P24457; -. DR Genevestigator; P24457; -. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0070330; F:aromatase activity; IEA:UniProtKB-EC. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR Gene3D; 1.10.630.10; -; 1. DR InterPro; IPR001128; Cyt_P450. DR InterPro; IPR017972; Cyt_P450_CS. DR InterPro; IPR002401; Cyt_P450_E_grp-I. DR InterPro; IPR008069; Cyt_P450_E_grp-I_CYP2D-like. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00463; EP450I. DR PRINTS; PR01686; EP450ICYP2D. DR PRINTS; PR00385; P450. DR SUPFAM; SSF48264; SSF48264; 1. DR PROSITE; PS00086; CYTOCHROME_P450; 1. PE 2: Evidence at transcript level; KW Complete proteome; Endoplasmic reticulum; Heme; Iron; Membrane; KW Metal-binding; Microsome; Monooxygenase; Oxidoreductase; KW Reference proteome. FT CHAIN 1 504 Cytochrome P450 2D11. FT /FTId=PRO_0000051737. FT METAL 446 446 Iron (heme axial ligand) (By similarity). FT CONFLICT 55 55 G -> D (in Ref. 1; AAA37514). FT CONFLICT 77 77 G -> A (in Ref. 1; AAA37514). FT CONFLICT 93 93 V -> M (in Ref. 1; AAA37514). FT CONFLICT 106 106 Q -> P (in Ref. 1; AAA37514). FT CONFLICT 132 132 Q -> R (in Ref. 1; AAA37514). FT CONFLICT 154 154 D -> E (in Ref. 1; AAA37514). FT CONFLICT 174 174 S -> P (in Ref. 1; AAA37514). FT CONFLICT 179 179 T -> P (in Ref. 1; AAA37514). FT CONFLICT 183 185 NAV -> KST (in Ref. 1; AAA37514). FT CONFLICT 204 204 Y -> F (in Ref. 1; AAA37514). FT CONFLICT 289 289 P -> A (in Ref. 1; AAA37514). FT CONFLICT 303 303 G -> L (in Ref. 1; AAA37514). FT CONFLICT 371 386 DIAPLPLPRITSRDIE -> TLLHCLCHASQVVTFTQ (in FT Ref. 1; AAA37514). FT CONFLICT 402 402 M -> L (in Ref. 1; AAA37514). FT CONFLICT 408 408 D -> G (in Ref. 1; AAA37514). FT CONFLICT 500 500 R -> H (in Ref. 1; AAA37514). SQ SEQUENCE 504 AA; 56988 MW; 2C432A8B5848E946 CRC64; MELLTGAGLW SVAIFTVIFI LLVDLMHRHQ HWTSRCPPGP VPWPVLGNLL QVDLGNMPYS LYKLQNRYGD VFSLQMGWKP MVVINGLKAM KEVLLTCGED TADRPQVPIF EYLGVKPGSQ GVVLAPYGPE WQEQRRFSVS TLRNFGLGKK SLEDWVTKEA RHLCDAFTAQ AGQSINPNTM LNNAVCNVIA SLIFARRFEY EDPYLIRMLK MLKECFTEIS GFIPGVLNEF PIFLRIPGLA DMVFQGQKSF MAILDNLLTE NRTTWDPDQP PRNLTDAFLA EIEKAKGNPE SSFNDENLRM VVGDLFTAGM VTTSTTLSWA LLLMILHPDV QRRVQQEIDA VIGQVQHPEM ADQARMPYTN AVIHEVQRFG DIAPLPLPRI TSRDIEVQDF LVTKGSTLIP NMSSVLKDET VWEKPLRFHP EHFLDAQGHF VKPEAFMPFS AGHRSCLGEA LARMELFLFF TCLLQRFSIS VPDGQPQPSN YRVHAIPVAP FPYQLCAVMR EQGH // ID CP2DQ_MOUSE Reviewed; 500 AA. AC Q8CIM7; Q9DBJ5; DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 19-FEB-2014, entry version 95. DE RecName: Full=Cytochrome P450 2D26; DE EC=1.14.14.1; DE AltName: Full=CYPIID26; GN Name=Cyp2d26; Synonyms=Cyp2d-26; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Liver; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Kidney; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: Cytochromes P450 are a group of heme-thiolate CC monooxygenases. In liver microsomes, this enzyme is involved in an CC NADPH-dependent electron transport pathway. It oxidizes a variety CC of structurally unrelated compounds, including steroids, fatty CC acids, and xenobiotics (By similarity). CC -!- CATALYTIC ACTIVITY: RH + reduced flavoprotein + O(2) = ROH + CC oxidized flavoprotein + H(2)O. CC -!- COFACTOR: Heme group (By similarity). CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral CC membrane protein (By similarity). Microsome membrane; Peripheral CC membrane protein (By similarity). CC -!- INDUCTION: P450 can be induced to high levels in liver and other CC tissues by various foreign compounds, including drugs, pesticides, CC and carcinogens. CC -!- SIMILARITY: Belongs to the cytochrome P450 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK004915; BAB23666.1; -; mRNA. DR EMBL; BC023241; AAH23241.1; -; mRNA. DR RefSeq; NP_083838.1; NM_029562.2. DR UniGene; Mm.439931; -. DR ProteinModelPortal; Q8CIM7; -. DR SMR; Q8CIM7; 51-500. DR IntAct; Q8CIM7; 6. DR MINT; MINT-1862922; -. DR STRING; 10090.ENSMUSP00000006094; -. DR PhosphoSite; Q8CIM7; -. DR PaxDb; Q8CIM7; -. DR PRIDE; Q8CIM7; -. DR Ensembl; ENSMUST00000006094; ENSMUSP00000006094; ENSMUSG00000022445. DR GeneID; 76279; -. DR KEGG; mmu:76279; -. DR UCSC; uc007wzn.1; mouse. DR CTD; 76279; -. DR MGI; MGI:1923529; Cyp2d26. DR eggNOG; COG2124; -. DR GeneTree; ENSGT00730000110385; -. DR HOGENOM; HOG000036991; -. DR HOVERGEN; HBG015789; -. DR InParanoid; Q8CIM7; -. DR KO; K07414; -. DR OrthoDB; EOG7RBZ85; -. DR TreeFam; TF352043; -. DR NextBio; 344895; -. DR PRO; PR:Q8CIM7; -. DR Bgee; Q8CIM7; -. DR Genevestigator; Q8CIM7; -. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0070330; F:aromatase activity; IEA:UniProtKB-EC. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0007565; P:female pregnancy; IEA:Ensembl. DR GO; GO:0042493; P:response to drug; IEA:Ensembl. DR Gene3D; 1.10.630.10; -; 1. DR InterPro; IPR001128; Cyt_P450. DR InterPro; IPR017972; Cyt_P450_CS. DR InterPro; IPR002401; Cyt_P450_E_grp-I. DR InterPro; IPR008069; Cyt_P450_E_grp-I_CYP2D-like. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00463; EP450I. DR PRINTS; PR01686; EP450ICYP2D. DR PRINTS; PR00385; P450. DR SUPFAM; SSF48264; SSF48264; 1. DR PROSITE; PS00086; CYTOCHROME_P450; 1. PE 2: Evidence at transcript level; KW Complete proteome; Endoplasmic reticulum; Heme; Iron; Membrane; KW Metal-binding; Microsome; Monooxygenase; Oxidoreductase; KW Reference proteome. FT CHAIN 1 500 Cytochrome P450 2D26. FT /FTId=PRO_0000051746. FT METAL 446 446 Iron (heme axial ligand). FT CONFLICT 263 263 L -> S (in Ref. 1; BAB23666). SQ SEQUENCE 500 AA; 56976 MW; B3DDCD88DFA3F265 CRC64; MGLLVGDDLW AVVIFTAIFL LLVDLVHRRQ RWTACYPPGP VPFPGLGNLL QVDFENIPYS FYKLQNRYGN VFSLQMAWKP VVVVNGLKAV RELLVTYGED TSDRPLMPIY NHIGYGHKSK GVILAPYGPE WREQRRFSVS TLRDFGLGKK SLEQWVTEEA GHLCDAFTKE AEHPFNPSPL LSKAVSNVIA SLIYARRFEY EDPFFNRMLK TLKESLGEDT GFVGEVLNAI PMLLHIPGLP DKAFPKLNSF IALVNKMLIE HDLTWDPAQP PRDLTDAFLA EVEKAKGNPE SSFNDKNLRI VVIDLFMAGM VTTSTTLSWA LLLMILHPDV QRRVHQEIDE VIGHVRHPEM ADQARMPYTN AVIHEVQRFA DIVPTNLPHM TSRDIKFQDF FIPKGTTLIP NLSSVLKDET VWEKPLRFYP EHFLDAQGHF VKHEAFMPFS AGRRSCLGEP LARMELFLFF TCLLQRFSFS VPDGQPRPSD YGIYTMPVTP EPYQLCAVAR // ID CP2E1_MOUSE Reviewed; 493 AA. AC Q05421; Q9Z198; DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1994, sequence version 1. DT 19-FEB-2014, entry version 131. DE RecName: Full=Cytochrome P450 2E1; DE EC=1.14.13.-; DE AltName: Full=4-nitrophenol 2-hydroxylase; DE EC=1.14.13.n7; DE AltName: Full=CYPIIE1; DE AltName: Full=Cytochrome P450-ALC; DE AltName: Full=Cytochrome P450-J; GN Name=Cyp2e1; Synonyms=Cyp2e, Cyp2e-1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=C57BL/6S; TISSUE=Liver; RX PubMed=8344939; RA Davis J.F., Felder M.R.; RT "Mouse ethanol-inducible cytochrome P-450 (P450IIE1). Characterization RT of cDNA clones and testosterone induction in kidney tissue."; RL J. Biol. Chem. 268:16584-16589(1993). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=BALB/c; TISSUE=Liver; RX PubMed=1536649; RA Freeman J.E., Stirling D., Russel A.L., Wolf C.R.; RT "cDNA sequence, deduced amino acid sequence, predicted gene structure RT and chemical regulation of mouse Cyp2e1."; RL Biochem. J. 281:689-695(1992). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Kidney; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] OF 455-493. RC TISSUE=Liver; RX PubMed=6851839; RA Ivanov P.L., Ryskov A.P., Kramerov D.A., Georgiev G.P.; RT "Primary structure of the repeating element B2 and of the adjoining RT sequences in cloned mRNA actively transcribing in mouse liver cells."; RL Dokl. Akad. Nauk SSSR 269:227-230(1983). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 455-493. RX PubMed=6194512; DOI=10.1093/nar/11.18.6541; RA Ryskov A.P., Ivanov P.L., Kramerov D.A., Georgiev G.P.; RT "Mouse ubiquitous B2 repeat in polysomal and cytoplasmic poly(A)+RNAs: RT unidirectional orientation and 3'-end localization."; RL Nucleic Acids Res. 11:6541-6558(1983). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] OF 455-493. RA Ryskov A.P., Ivanov P.L., Kramerov D.A., Georgiev G.P.; RT "Universal orientation and 3' terminal localization of repetitive RT sequences of the B2 family in mRNA."; RL Mol. Biol. (Mosk.) 18:74-83(1984). CC -!- FUNCTION: Metabolizes several precarcinogens, drugs, and solvents CC to reactive metabolites (By similarity). CC -!- CATALYTIC ACTIVITY: 4-nitrophenol + NADPH + O(2) = 4-nitrocatechol CC + NADP(+) + H(2)O. CC -!- COFACTOR: Heme group (By similarity). CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral CC membrane protein. Microsome membrane; Peripheral membrane protein. CC -!- TISSUE SPECIFICITY: Highest level in the liver and to a lesser CC extent in the kidney, with a higher level in the male kidney than CC in the female. CC -!- DEVELOPMENTAL STAGE: Detectable in the female liver on day 1 and CC reaches steady state levels on days 16-20. CC -!- INDUCTION: By ethanol and acetone in the liver and by testosterone CC in the kidney and adrenal tissues. CC -!- SIMILARITY: Belongs to the cytochrome P450 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L11650; AAA39879.1; -; mRNA. DR EMBL; X62595; CAA44481.1; -; mRNA. DR EMBL; BC013451; AAH13451.1; -; mRNA. DR EMBL; M54877; AAA37275.1; -; mRNA. DR EMBL; X01026; CAA25510.1; ALT_SEQ; mRNA. DR PIR; A47350; A47350. DR PIR; S19657; A21231. DR RefSeq; NP_067257.1; NM_021282.2. DR UniGene; Mm.21758; -. DR ProteinModelPortal; Q05421; -. DR SMR; Q05421; 32-493. DR IntAct; Q05421; 2. DR MINT; MINT-1862880; -. DR PhosphoSite; Q05421; -. DR PaxDb; Q05421; -. DR PRIDE; Q05421; -. DR Ensembl; ENSMUST00000026552; ENSMUSP00000026552; ENSMUSG00000025479. DR GeneID; 13106; -. DR KEGG; mmu:13106; -. DR UCSC; uc009kic.1; mouse. DR CTD; 1571; -. DR MGI; MGI:88607; Cyp2e1. DR eggNOG; COG2124; -. DR GeneTree; ENSGT00680000099783; -. DR HOGENOM; HOG000036992; -. DR HOVERGEN; HBG015789; -. DR InParanoid; Q05421; -. DR KO; K07415; -. DR OMA; PMYTMEN; -. DR OrthoDB; EOG7RBZ85; -. DR TreeFam; TF352043; -. DR BioCyc; MetaCyc:MONOMER-12920; -. DR ChiTaRS; CYP2E1; mouse. DR NextBio; 283102; -. DR PRO; PR:Q05421; -. DR Bgee; Q05421; -. DR Genevestigator; Q05421; -. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI. DR GO; GO:0000139; C:Golgi membrane; IEA:Ensembl. DR GO; GO:0031227; C:intrinsic component of endoplasmic reticulum membrane; IEA:Ensembl. DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl. DR GO; GO:0020037; F:heme binding; ISS:UniProtKB. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0004497; F:monooxygenase activity; IDA:MGI. DR GO; GO:0016709; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen; IEA:UniProtKB-EC. DR GO; GO:0016712; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen; IEA:Ensembl. DR GO; GO:0017144; P:drug metabolic process; IEA:Ensembl. DR GO; GO:0046483; P:heterocycle metabolic process; IEA:Ensembl. DR GO; GO:0016098; P:monoterpenoid metabolic process; IEA:Ensembl. DR GO; GO:0042493; P:response to drug; IEA:Ensembl. DR GO; GO:0045471; P:response to ethanol; IEA:Ensembl. DR GO; GO:0010243; P:response to organonitrogen compound; IEA:Ensembl. DR GO; GO:0010193; P:response to ozone; IEA:Ensembl. DR GO; GO:0008202; P:steroid metabolic process; IEA:Ensembl. DR GO; GO:0006641; P:triglyceride metabolic process; IEA:Ensembl. DR Gene3D; 1.10.630.10; -; 1. DR InterPro; IPR001128; Cyt_P450. DR InterPro; IPR017972; Cyt_P450_CS. DR InterPro; IPR002401; Cyt_P450_E_grp-I. DR InterPro; IPR008070; Cyt_P450_E_grp-I_CYP2E-like. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00463; EP450I. DR PRINTS; PR01687; EP450ICYP2E. DR PRINTS; PR00385; P450. DR SUPFAM; SSF48264; SSF48264; 1. DR PROSITE; PS00086; CYTOCHROME_P450; 1. PE 2: Evidence at transcript level; KW Complete proteome; Endoplasmic reticulum; Heme; Iron; Membrane; KW Metal-binding; Microsome; Monooxygenase; NADP; Oxidoreductase; KW Reference proteome. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 493 Cytochrome P450 2E1. FT /FTId=PRO_0000051755. FT REGION 298 303 Substrate binding (By similarity). FT METAL 437 437 Iron (heme axial ligand) (By similarity). SQ SEQUENCE 493 AA; 56805 MW; 4031AB016DA56A9C CRC64; MAVLGITVAL LVWIATLLLV SIWKQIYRSW NLPPGPFPIP FFGNIFQLDL KDIPKSLTKL AKRFGPVFTL HLGQRRIVVL HGYKAVKEVL LNHKNEFSGR GDIPVFQEYK NKGIIFNNGP TWKDVRRFSL SILRDWGMGK QGNEARIQRE AHFLVEELKK TKGQPFDPTF LIGCAPCNVI ADILFNKRFD YDDKKCLELM SLFNENFYLL STPWIQAYNY FSDYLQYLPG SHRKVMKNVS EIRQYTLGKA KEHLKSLDIN CPRDVTDCLL IEMEKEKHSQ EPMYTMENIS VTLADLFFAG TETTSTTLRY GLLILMKYPE IEEKLHEEID RVIGPSRAPA VRDRMNMPYM DAVVHEIQRF INLVPSNLPH EATRDTVFRG YVIPKGTVVI PTLDSLLFDN YEFPDPETFK PEHFLNENGK FKYSDYFKAF SAGKRVCVGE GLARMELFLL LSAILQHFNL KSLVDPKDID LSPVTIGFGS IPREFKLCVI PRS // ID CP2F2_MOUSE Reviewed; 491 AA. AC P33267; DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1994, sequence version 1. DT 19-FEB-2014, entry version 119. DE RecName: Full=Cytochrome P450 2F2; DE EC=1.14.14.-; DE AltName: Full=CYPIIF2; DE AltName: Full=Cytochrome P450-NAH-2; DE AltName: Full=Naphthalene dehydrogenase; DE AltName: Full=Naphthalene hydroxylase; GN Name=Cyp2f2; Synonyms=Cyp2f-2; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY. RX PubMed=1981702; RA Nagata K., Martin B.M., Gillette J.R., Sasame H.A.; RT "Isozymes of cytochrome P-450 that metabolize naphthalene in liver and RT lung of untreated mice."; RL Drug Metab. Dispos. 18:557-564(1990). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY. RC STRAIN=Swiss; TISSUE=Lung; RX PubMed=1742282; DOI=10.1021/bi00112a009; RA Ritter J.K., Owens I.S., Negishi M., Nagata K., Sheen Y.Y., RA Gillette J.R., Sasame H.A.; RT "Mouse pulmonary cytochrome P-450 naphthalene hydroxylase: cDNA RT cloning, sequence, and expression in Saccharomyces cerevisiae."; RL Biochemistry 30:11430-11437(1991). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Liver; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: Involved in the regio- and stereoselective CC transformation of naphthalene to trans-1R-hydroxy-2R-glutathionyl- CC 1,2-dihydronaphthalene in the presence of glutathione and CC glutathione S-transferases. It specifically catalyzes the CC production of a very reactive and potentially toxic intermediate, CC the 2R,2S arene oxide, that is associated with necrosis of the CC unciliated bronchiolar epithelial cells or Clara cells in lung. CC -!- COFACTOR: Heme group (By similarity). CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral CC membrane protein. Microsome membrane; Peripheral membrane protein. CC -!- TISSUE SPECIFICITY: Clara cells in lung and liver. CC -!- SIMILARITY: Belongs to the cytochrome P450 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M77497; AAA37517.1; ALT_SEQ; mRNA. DR EMBL; BC011089; AAH11089.1; -; mRNA. DR EMBL; BC024742; AAH24742.1; -; mRNA. DR PIR; A39302; A39302. DR RefSeq; NP_031843.2; NM_007817.2. DR UniGene; Mm.4515; -. DR ProteinModelPortal; P33267; -. DR SMR; P33267; 28-487. DR IntAct; P33267; 2. DR MINT; MINT-1862621; -. DR STRING; 10090.ENSMUSP00000003100; -. DR PhosphoSite; P33267; -. DR PaxDb; P33267; -. DR PRIDE; P33267; -. DR Ensembl; ENSMUST00000003100; ENSMUSP00000003100; ENSMUSG00000052974. DR GeneID; 13107; -. DR KEGG; mmu:13107; -. DR UCSC; uc009fuy.1; mouse. DR CTD; 13107; -. DR MGI; MGI:88608; Cyp2f2. DR eggNOG; COG2124; -. DR GeneTree; ENSGT00670000097868; -. DR HOGENOM; HOG000036992; -. DR HOVERGEN; HBG015789; -. DR InParanoid; P33267; -. DR KO; K07416; -. DR OMA; HAFLILM; -. DR OrthoDB; EOG7RBZ85; -. DR TreeFam; TF352043; -. DR NextBio; 283106; -. DR PRO; PR:P33267; -. DR Bgee; P33267; -. DR Genevestigator; P33267; -. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0016712; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen; IEA:Ensembl. DR GO; GO:0019825; F:oxygen binding; IEA:InterPro. DR GO; GO:0018931; P:naphthalene metabolic process; IMP:MGI. DR GO; GO:0009636; P:response to toxic substance; IMP:MGI. DR GO; GO:0018979; P:trichloroethylene metabolic process; IEA:Ensembl. DR Gene3D; 1.10.630.10; -; 1. DR InterPro; IPR001128; Cyt_P450. DR InterPro; IPR017972; Cyt_P450_CS. DR InterPro; IPR020469; Cyt_P450_CYP2_fam. DR InterPro; IPR002401; Cyt_P450_E_grp-I. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00463; EP450I. DR PRINTS; PR01957; EP450ICYP2F. DR PRINTS; PR00385; P450. DR SUPFAM; SSF48264; SSF48264; 1. DR PROSITE; PS00086; CYTOCHROME_P450; 1. PE 2: Evidence at transcript level; KW Complete proteome; Endoplasmic reticulum; Heme; Iron; Membrane; KW Metal-binding; Microsome; Monooxygenase; Oxidoreductase; KW Reference proteome. FT CHAIN 1 491 Cytochrome P450 2F2. FT /FTId=PRO_0000051760. FT METAL 436 436 Iron (heme axial ligand) (By similarity). SQ SEQUENCE 491 AA; 55949 MW; F56AEB956E7EBD25 CRC64; MDGVSTAILL LLLAVISLSL TFSSRGKGQL PPGPKPLPIL GNLLQLRSQD LLTSLTKLSK EYGSVFTVYL GSRPVIVLSG YQTVKEALVD KGEEFSGRGA YPVFFNFTRG NGIAFSDGER WKILRRFSVQ ILRNFGMGKR SIEERILEEG SFLLEVLRKM EGKPFDPVFI LSRSVSNIIC SVVFGSRFDY DDERLLTIIH FINDNFKIMS SPWGEMYNIF PSVLDWIPGP HKRLFRNFGG MKDLIARSVR EHQDSLDPNS PRDFIDCFLT KMAQEKQDPL SHFNMDTLLM TTHNLLFGGT ETVGTTLRHA FLILMKYPKV QARVQEEIDR VVGRSRMPTL EDRTSMPYTD AVIHEVQRFA DVIPMNLPHR VTRDTPFRGF LIPKGTDVIT LLNTVHYDSD QFKTPQEFNP EHFLDDNHSF KKSPAFMPFS AGRRLCLGEP LARMELFIYF TSILQNFTLQ PLVDPEDIDL TPLSSGLGNL PRPFQLCMHI R // ID CP2J5_MOUSE Reviewed; 501 AA. AC O54749; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1998, sequence version 1. DT 19-FEB-2014, entry version 111. DE RecName: Full=Cytochrome P450 2J5; DE EC=1.14.14.1; DE AltName: Full=Arachidonic acid epoxygenase; DE AltName: Full=CYPIIJ5; GN Name=Cyp2j5; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=C57BL/6 X CBA; TISSUE=Liver; RX PubMed=9570962; DOI=10.1006/geno.1998.5235; RA Ma J., Ramachandran S., Fiedorek F.T. Jr., Zeldin D.C.; RT "Mapping of the CYP2J cytochrome P450 genes to human chromosome 1 and RT mouse chromosome 4."; RL Genomics 49:152-155(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Liver; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- CATALYTIC ACTIVITY: RH + reduced flavoprotein + O(2) = ROH + CC oxidized flavoprotein + H(2)O. CC -!- COFACTOR: Heme group (By similarity). CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral CC membrane protein. Microsome membrane; Peripheral membrane protein. CC -!- SIMILARITY: Belongs to the cytochrome P450 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U62294; AAB87635.1; -; mRNA. DR EMBL; BC021624; AAH21624.1; -; mRNA. DR RefSeq; NP_034137.1; NM_010007.4. DR UniGene; Mm.12838; -. DR ProteinModelPortal; O54749; -. DR SMR; O54749; 44-499. DR IntAct; O54749; 3. DR MINT; MINT-4091722; -. DR STRING; 10090.ENSMUSP00000030299; -. DR PhosphoSite; O54749; -. DR PaxDb; O54749; -. DR PRIDE; O54749; -. DR Ensembl; ENSMUST00000030299; ENSMUSP00000030299; ENSMUSG00000052520. DR GeneID; 13109; -. DR KEGG; mmu:13109; -. DR UCSC; uc008ttl.1; mouse. DR CTD; 13109; -. DR MGI; MGI:1270149; Cyp2j5. DR eggNOG; COG2124; -. DR HOGENOM; HOG000036991; -. DR HOVERGEN; HBG015789; -. DR InParanoid; O54749; -. DR KO; K07418; -. DR OrthoDB; EOG7PK8ZF; -. DR TreeFam; TF352043; -. DR NextBio; 283114; -. DR PRO; PR:O54749; -. DR ArrayExpress; O54749; -. DR Bgee; O54749; -. DR Genevestigator; O54749; -. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0070330; F:aromatase activity; IEA:UniProtKB-EC. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR Gene3D; 1.10.630.10; -; 1. DR InterPro; IPR001128; Cyt_P450. DR InterPro; IPR017972; Cyt_P450_CS. DR InterPro; IPR002401; Cyt_P450_E_grp-I. DR InterPro; IPR008071; Cyt_P450_E_grp-I_CYP2J-like. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00463; EP450I. DR PRINTS; PR01688; EP450ICYP2J. DR PRINTS; PR00385; P450. DR SUPFAM; SSF48264; SSF48264; 1. DR PROSITE; PS00086; CYTOCHROME_P450; 1. PE 2: Evidence at transcript level; KW Complete proteome; Endoplasmic reticulum; Heme; Iron; Membrane; KW Metal-binding; Microsome; Monooxygenase; Oxidoreductase; KW Reference proteome. FT CHAIN 1 501 Cytochrome P450 2J5. FT /FTId=PRO_0000051771. FT METAL 447 447 Iron (heme axial ligand) (By similarity). SQ SEQUENCE 501 AA; 57784 MW; C67F2E79DD64AF99 CRC64; MIMFLSSLVT TFWEALHLKT LVLAVVTFLF LINILRSRHP KNYPPGPWRL PFVGNFFQID TKQTHLVLQQ FVKKYGNVFS LELGQSPVVV VSGLPLIKEM FTHLDQNFVN RFMTPVRERI TGKNGLVVSN GQTWKEQRRL ALMALRNFGL GKKSLEERIQ EETHHLVEAI REEGGQPFNP HLKLINAVSN IICSVTFGER FDYEDCQFQE LLQLLDETMH LMGSSAGQLY NGFPCIMKYL PGPHQKIFRN WGKLKLFVSH IVKKHEKDWN PDEPRDFIDA FLIEMQKDPD RTTSFNEENL ISTTLDLFLG GTETTSSTLR WALLYMSSYP EIQENVQAEI DRVIGHKRQV SLSDRESMPY TNAVIHEVQR MGNIVPLNSS REVTVDTKFN GFHLPKGTMI LTNLTALHRD PKEWATPEVF NPEHFLENGQ FKKRESFLPF SMGKRACLGE QLAKSELFIF FSALMQKFTF KPPINEKLSL KFRMGLILSP ASYRICAIPR V // ID CP2J6_MOUSE Reviewed; 501 AA. AC O54750; Q8BR78; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 2. DT 19-MAR-2014, entry version 110. DE RecName: Full=Cytochrome P450 2J6; DE EC=1.14.14.1; DE AltName: Full=Arachidonic acid epoxygenase; DE AltName: Full=CYPIIJ6; GN Name=Cyp2j6; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=C57BL/6 X CBA; TISSUE=Liver; RX PubMed=9570962; DOI=10.1006/geno.1998.5235; RA Ma J., Ramachandran S., Fiedorek F.T. Jr., Zeldin D.C.; RT "Mapping of the CYP2J cytochrome P450 genes to human chromosome 1 and RT mouse chromosome 4."; RL Genomics 49:152-155(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Limb; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- CATALYTIC ACTIVITY: RH + reduced flavoprotein + O(2) = ROH + CC oxidized flavoprotein + H(2)O. CC -!- COFACTOR: Heme group (By similarity). CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral CC membrane protein. Microsome membrane; Peripheral membrane protein. CC -!- SIMILARITY: Belongs to the cytochrome P450 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U62295; AAB87636.1; -; mRNA. DR EMBL; AK045421; BAC32356.1; -; mRNA. DR EMBL; AK165663; BAE38325.1; -; mRNA. DR EMBL; AL683816; CAM13966.1; -; Genomic_DNA. DR EMBL; CH466527; EDL30913.1; -; Genomic_DNA. DR EMBL; BC050832; AAH50832.1; -; mRNA. DR RefSeq; NP_034138.3; NM_010008.4. DR UniGene; Mm.98200; -. DR ProteinModelPortal; O54750; -. DR SMR; O54750; 44-495. DR PaxDb; O54750; -. DR PRIDE; O54750; -. DR Ensembl; ENSMUST00000030303; ENSMUSP00000030303; ENSMUSG00000052914. DR GeneID; 13110; -. DR KEGG; mmu:13110; -. DR UCSC; uc008tti.2; mouse. DR CTD; 13110; -. DR MGI; MGI:1270148; Cyp2j6. DR eggNOG; COG2124; -. DR GeneTree; ENSGT00730000110385; -. DR HOGENOM; HOG000036991; -. DR HOVERGEN; HBG015789; -. DR InParanoid; Q8BR78; -. DR KO; K07418; -. DR OMA; MYLETTM; -. DR OrthoDB; EOG7RBZ85; -. DR TreeFam; TF352043; -. DR ChiTaRS; Cyp2j6; mouse. DR NextBio; 283118; -. DR PRO; PR:O54750; -. DR Bgee; O54750; -. DR Genevestigator; O54750; -. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0070330; F:aromatase activity; IEA:UniProtKB-EC. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0003958; F:NADPH-hemoprotein reductase activity; IEA:Ensembl. DR GO; GO:0019369; P:arachidonic acid metabolic process; IEA:Ensembl. DR GO; GO:0007565; P:female pregnancy; IEA:Ensembl. DR GO; GO:0014070; P:response to organic cyclic compound; IEA:Ensembl. DR GO; GO:0001523; P:retinoid metabolic process; IEA:Ensembl. DR Gene3D; 1.10.630.10; -; 1. DR InterPro; IPR001128; Cyt_P450. DR InterPro; IPR017972; Cyt_P450_CS. DR InterPro; IPR002401; Cyt_P450_E_grp-I. DR InterPro; IPR008071; Cyt_P450_E_grp-I_CYP2J-like. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00463; EP450I. DR PRINTS; PR01688; EP450ICYP2J. DR PRINTS; PR00385; P450. DR SUPFAM; SSF48264; SSF48264; 1. DR PROSITE; PS00086; CYTOCHROME_P450; 1. PE 2: Evidence at transcript level; KW Complete proteome; Endoplasmic reticulum; Heme; Iron; Membrane; KW Metal-binding; Microsome; Monooxygenase; Oxidoreductase; KW Reference proteome. FT CHAIN 1 501 Cytochrome P450 2J6. FT /FTId=PRO_0000051772. FT METAL 447 447 Iron (heme axial ligand) (By similarity). FT CONFLICT 369 369 Q -> R (in Ref. 1; AAB87636). SQ SEQUENCE 501 AA; 57792 MW; 4E5A257C5C9C1CE7 CRC64; MLAATGSLLA TIWAALHPRT LLVAAVTFLL LADYFKNRRP KNYPPGPWGL PFVGNIFQLD FGQPHLSIQP LVKKYGNIFS LNLGDITSVV ITGLPLIKEA LTQMEQNIMN RPLSVMQERI SNKNGLIFSS GQIWKEQRRF ALMTLRNFGL GKKSLEERMQ EEASHLVEAI REEEGKPFNP HFSINNAVSN IICSVTFGER FDYHDSRFQE MLRLLDEVMY LETTMISQLY NIFPWIMKYI PGSHQKVFRN WEKLKLFVSC MIDDHRKDWN PDEPRDFIDA FLKEMTKYPE KTTSFNEENL ICSTLDLFFA GTETTSTTLR WALLYMALYP EVQEKVQAEI DRVIGQKRAA RLADRESMPY TNAVIHEVQR MGNIIPLNVP REVAMDTNLN GFHLPKGTMV LTNLTALHRD PKEWATPDVF NPEHFLENGQ FKKRESFLPF SMGKRACLGE QLARSELFIF FTSLMQKFTF NPPINEKLSP KFRNGLTLSP VSHRICAVPR Q // ID CP2R1_MOUSE Reviewed; 501 AA. AC Q6VVW9; DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 19-FEB-2014, entry version 79. DE RecName: Full=Vitamin D 25-hydroxylase; DE EC=1.14.13.15; DE AltName: Full=Cytochrome P450 2R1; GN Name=Cyp2r1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY. RC STRAIN=C57BL/6Jx129SvEv; RX PubMed=12867411; DOI=10.1074/jbc.M307028200; RA Cheng J.B., Motola D.L., Mangelsdorf D.J., Russell D.W.; RT "De-orphanization of cytochrome P450 2R1: a microsomal vitamin D 25- RT hydroxylase."; RL J. Biol. Chem. 278:38084-38093(2003). CC -!- FUNCTION: Has a D-25-hydroxylase activity on both forms of vitamin CC D, vitamin D(2) and D(3). CC -!- CATALYTIC ACTIVITY: 5-beta-cholestane-3-alpha,7-alpha,12-alpha- CC triol + 3 NADPH + 3 O(2) = (25R)-3-alpha,7-alpha,12-alpha- CC trihydroxy-5-beta-cholestan-26-oate + 3 NADP(+) + 4 H(2)O. CC -!- COFACTOR: Heme group (By similarity). CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral CC membrane protein. Microsome membrane; Peripheral membrane protein. CC -!- TISSUE SPECIFICITY: Highly expressed in the liver and testis. CC -!- SIMILARITY: Belongs to the cytochrome P450 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AY323818; AAQ23115.1; -; mRNA. DR RefSeq; NP_796356.2; NM_177382.3. DR UniGene; Mm.108037; -. DR ProteinModelPortal; Q6VVW9; -. DR SMR; Q6VVW9; 49-501. DR PRIDE; Q6VVW9; -. DR Ensembl; ENSMUST00000032908; ENSMUSP00000032908; ENSMUSG00000030670. DR GeneID; 244209; -. DR KEGG; mmu:244209; -. DR UCSC; uc009jid.1; mouse. DR CTD; 120227; -. DR MGI; MGI:2449771; Cyp2r1. DR eggNOG; COG2124; -. DR GeneTree; ENSGT00730000110808; -. DR HOGENOM; HOG000036991; -. DR HOVERGEN; HBG015789; -. DR InParanoid; Q6VVW9; -. DR KO; K07419; -. DR OMA; RETEACT; -. DR OrthoDB; EOG7RBZ85; -. DR TreeFam; TF352043; -. DR NextBio; 386174; -. DR PRO; PR:Q6VVW9; -. DR ArrayExpress; Q6VVW9; -. DR Bgee; Q6VVW9; -. DR Genevestigator; Q6VVW9; -. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0047749; F:cholestanetriol 26-monooxygenase activity; IEA:UniProtKB-EC. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0030343; F:vitamin D3 25-hydroxylase activity; IDA:MGI. DR GO; GO:0010164; P:response to cesium ion; IEA:Ensembl. DR GO; GO:0010212; P:response to ionizing radiation; IEA:Ensembl. DR Gene3D; 1.10.630.10; -; 1. DR InterPro; IPR001128; Cyt_P450. DR InterPro; IPR017972; Cyt_P450_CS. DR InterPro; IPR002401; Cyt_P450_E_grp-I. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00463; EP450I. DR PRINTS; PR00385; P450. DR SUPFAM; SSF48264; SSF48264; 1. DR PROSITE; PS00086; CYTOCHROME_P450; 1. PE 2: Evidence at transcript level; KW Complete proteome; Endoplasmic reticulum; Heme; Iron; Membrane; KW Metal-binding; Microsome; Monooxygenase; NADP; Oxidoreductase; KW Reference proteome. FT CHAIN 1 501 Vitamin D 25-hydroxylase. FT /FTId=PRO_0000051779. FT METAL 448 448 Iron (heme axial ligand) (By similarity). FT BINDING 250 250 Substrate; via carbonyl oxygen (By FT similarity). SQ SEQUENCE 501 AA; 57313 MW; C1A1BAD71E630A98 CRC64; MLELPGARAC AGALAGALLL LLFVLVVRQL LRQRRPAGFP PGPPRLPFVG NICSLALSAD LPHVYMRKQS RVYGEIFSLD LGGISTVVLN GYDVVKECLV HQSEIFADRP CLPLFMKMTK MGGLLNSRYG RGWIDHRRLA VNSFHYFGSG QKSFESKILE ETWSLIDAIE TYKGGPFDLK QLITNAVSNI TNLILFGERF TYEDTDFQHM IELFSENVEL AASAPVFLYN AFPWIGILPF GKHQRLFRNA DVVYDFLSRL IEKAAVNRKP HLPHHFVDAY LDEMDQGQND PLSTFSKENL IFSVGELIIA GTETTTNVLR WAILFMALYP NIQGQVHKEI DLIVGHNRRP SWEYKCKMPY TEAVLHEVLR FCNIVPLGIF HATSEDAVVR GYSIPKGTTV ITNLYSVHFD EKYWKDPDMF YPERFLDSNG YFTKKEALIP FSLGRRHCLG EQLARMEMFL FFTSLLQQFH LHFPHELVPN LKPRLGMTLQ PQPYLICAER R // ID CP2S1_MOUSE Reviewed; 501 AA. AC Q9DBX6; DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 19-FEB-2014, entry version 96. DE RecName: Full=Cytochrome P450 2S1; DE EC=1.14.14.1; DE AltName: Full=CYPIIS1; GN Name=Cyp2s1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Lung; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Embryonic germ cell; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: Has a potential importance for extrahepatic xenobiotic CC metabolism (By similarity). CC -!- CATALYTIC ACTIVITY: RH + reduced flavoprotein + O(2) = ROH + CC oxidized flavoprotein + H(2)O. CC -!- COFACTOR: Heme group (By similarity). CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral CC membrane protein (By similarity). Microsome membrane; Peripheral CC membrane protein (By similarity). CC -!- SIMILARITY: Belongs to the cytochrome P450 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK004699; BAB23484.1; -; mRNA. DR EMBL; AK087069; BAC39794.1; -; mRNA. DR EMBL; BC064733; AAH64733.1; -; mRNA. DR RefSeq; NP_083051.1; NM_028775.3. DR UniGene; Mm.275188; -. DR ProteinModelPortal; Q9DBX6; -. DR SMR; Q9DBX6; 31-492. DR IntAct; Q9DBX6; 1. DR MINT; MINT-4091732; -. DR PhosphoSite; Q9DBX6; -. DR PaxDb; Q9DBX6; -. DR PRIDE; Q9DBX6; -. DR Ensembl; ENSMUST00000043314; ENSMUSP00000041175; ENSMUSG00000040703. DR GeneID; 74134; -. DR KEGG; mmu:74134; -. DR UCSC; uc009fub.1; mouse. DR CTD; 29785; -. DR MGI; MGI:1921384; Cyp2s1. DR eggNOG; COG2124; -. DR GeneTree; ENSGT00670000097868; -. DR HOGENOM; HOG000036992; -. DR HOVERGEN; HBG015789; -. DR InParanoid; Q9DBX6; -. DR KO; K07420; -. DR OMA; AFTIQQV; -. DR OrthoDB; EOG7RBZ85; -. DR TreeFam; TF352043; -. DR NextBio; 339870; -. DR PRO; PR:Q9DBX6; -. DR ArrayExpress; Q9DBX6; -. DR Bgee; Q9DBX6; -. DR Genevestigator; Q9DBX6; -. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0070330; F:aromatase activity; IEA:UniProtKB-EC. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR Gene3D; 1.10.630.10; -; 1. DR InterPro; IPR001128; Cyt_P450. DR InterPro; IPR002401; Cyt_P450_E_grp-I. DR InterPro; IPR008067; Cyt_P450_E_grp-I_CYP2A-like. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00463; EP450I. DR PRINTS; PR01684; EP450ICYP2A. DR PRINTS; PR00385; P450. DR SUPFAM; SSF48264; SSF48264; 1. PE 2: Evidence at transcript level; KW Complete proteome; Endoplasmic reticulum; Heme; Iron; Membrane; KW Metal-binding; Microsome; Monooxygenase; Oxidoreductase; KW Reference proteome. FT CHAIN 1 501 Cytochrome P450 2S1. FT /FTId=PRO_0000051781. FT METAL 441 441 Iron (heme axial ligand) (By similarity). SQ SEQUENCE 501 AA; 55632 MW; D12575F3F8D7B019 CRC64; MEAASTWALL LALLLLLLLL SLTLFRTPAR GYLPPGPTPL PLLGNLLQLR PGALYSGLLR LSKKYGPVFT VYLGPWRRVV VLVGHDAVRE ALGGQAEEFS GRGTLATLDK TFDGHGVFFA NGERWKQLRK FTLLALRDLG MGKREGEELI QAEVQSLVEA FQKTEGRPFN PSMLLAQATS NVVCSLVFGI RLPYDDKEFQ AVIQAASGTL LGISSPWGQA YEMFSWLLQP LPGPHTQLQH HLGTLAAFTI QQVQKHQGRF QTSGPARDVV DAFLLKMAQE KQDPGTEFTE KNLLMTVTYL LFAGTMTIGA TIRYALLLLL RYPQVQQRVR EELIQELGPG RAPSLSDRVR LPYTDAVLHE AQRLLALVPM GMPHTITRTT CFRGYTLPKG TEVFPLIGSI LHDPAVFQNP GEFHPGRFLD EDGRLRKHEA FLPYSLGKRV CLGEGLARAE LWLFFTSILQ AFSLETPCPP GDLSLKPAIS GLFNIPPDFQ LRVWPTGDQS R // ID CP2U1_MOUSE Reviewed; 530 AA. AC Q9CX98; Q8BIM3; DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot. DT 26-JUN-2007, sequence version 2. DT 19-MAR-2014, entry version 104. DE RecName: Full=Cytochrome P450 2U1; DE EC=1.14.14.1; GN Name=Cyp2u1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3). RC STRAIN=C57BL/6J; TISSUE=Heart, Lung, and Thymus; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE. RX PubMed=15752708; DOI=10.1016/j.abb.2005.02.001; RA Choudhary D., Jansson I., Stoilov I., Sarfarazi M., Schenkman J.B.; RT "Expression patterns of mouse and human CYP orthologs (families 1-4) RT during development and in different adult tissues."; RL Arch. Biochem. Biophys. 436:50-61(2005). CC -!- FUNCTION: Catalyzes the hydroxylation of arachidonic acid, CC docosahexaenoic acid and other long chain fatty acids. May CC modulate the arachidonic acid signaling pathway and play a role in CC other fatty acid signaling processes (By similarity). CC -!- CATALYTIC ACTIVITY: RH + reduced flavoprotein + O(2) = ROH + CC oxidized flavoprotein + H(2)O. CC -!- COFACTOR: Heme group (By similarity). CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass CC membrane protein (By similarity). Microsome membrane (By CC similarity). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q9CX98-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9CX98-2; Sequence=VSP_026227, VSP_026228; CC Name=3; CC IsoId=Q9CX98-3; Sequence=VSP_026224, VSP_026225, VSP_026226; CC Note=No experimental confirmation available; CC -!- TISSUE SPECIFICITY: Widely expressed. CC -!- DEVELOPMENTAL STAGE: Expressed at all stages after E7. CC -!- SIMILARITY: Belongs to the cytochrome P450 family. CC -!- SEQUENCE CAUTION: CC Sequence=AK142740; Type=Frameshift; Positions=245; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK018458; BAB31223.1; -; mRNA. DR EMBL; AK041477; BAC30954.1; -; mRNA. DR EMBL; AK142740; -; NOT_ANNOTATED_CDS; mRNA. DR RefSeq; NP_082092.2; NM_027816.3. DR UniGene; Mm.473179; -. DR ProteinModelPortal; Q9CX98; -. DR SMR; Q9CX98; 49-530. DR PhosphoSite; Q9CX98; -. DR PRIDE; Q9CX98; -. DR DNASU; 71519; -. DR Ensembl; ENSMUST00000106337; ENSMUSP00000101944; ENSMUSG00000027983. [Q9CX98-1] DR GeneID; 71519; -. DR KEGG; mmu:71519; -. DR UCSC; uc008rjn.1; mouse. [Q9CX98-1] DR UCSC; uc008rjo.1; mouse. [Q9CX98-2] DR UCSC; uc008rjp.1; mouse. [Q9CX98-3] DR CTD; 113612; -. DR MGI; MGI:1918769; Cyp2u1. DR eggNOG; COG2124; -. DR GeneTree; ENSGT00730000110808; -. DR HOGENOM; HOG000036991; -. DR HOVERGEN; HBG015789; -. DR InParanoid; Q9CX98; -. DR KO; K07422; -. DR OMA; IEEFAYV; -. DR OrthoDB; EOG7RBZ85; -. DR TreeFam; TF352043; -. DR ChiTaRS; CYP2U1; mouse. DR NextBio; 333927; -. DR PRO; PR:Q9CX98; -. DR Bgee; Q9CX98; -. DR Genevestigator; Q9CX98; -. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0070330; F:aromatase activity; IEA:UniProtKB-EC. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR Gene3D; 1.10.630.10; -; 1. DR InterPro; IPR001128; Cyt_P450. DR InterPro; IPR017972; Cyt_P450_CS. DR InterPro; IPR002401; Cyt_P450_E_grp-I. DR InterPro; IPR008069; Cyt_P450_E_grp-I_CYP2D-like. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00463; EP450I. DR PRINTS; PR01686; EP450ICYP2D. DR PRINTS; PR00385; P450. DR SUPFAM; SSF48264; SSF48264; 1. DR PROSITE; PS00086; CYTOCHROME_P450; 1. PE 2: Evidence at transcript level; KW Alternative splicing; Complete proteome; Endoplasmic reticulum; Heme; KW Iron; Membrane; Metal-binding; Microsome; Monooxygenase; NADP; KW Oxidoreductase; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 530 Cytochrome P450 2U1. FT /FTId=PRO_0000291757. FT TRANSMEM 21 41 Helical; (Potential). FT TRANSMEM 99 119 Helical; (Potential). FT TRANSMEM 247 267 Helical; (Potential). FT TRANSMEM 328 348 Helical; (Potential). FT TRANSMEM 481 501 Helical; (Potential). FT METAL 476 476 Iron (heme axial ligand) (By similarity). FT VAR_SEQ 236 270 Missing (in isoform 3). FT /FTId=VSP_026224. FT VAR_SEQ 416 416 V -> A (in isoform 3). FT /FTId=VSP_026225. FT VAR_SEQ 417 530 Missing (in isoform 3). FT /FTId=VSP_026226. FT VAR_SEQ 473 501 KRVCMGEQLAKMELFLMFVSLMQTFTFAL -> QLKLGFNL FT FFTLSLVCVCVCVCVCVYRHV (in isoform 2). FT /FTId=VSP_026227. FT VAR_SEQ 502 530 Missing (in isoform 2). FT /FTId=VSP_026228. SQ SEQUENCE 530 AA; 60578 MW; FCB595EADA88A213 CRC64; MSSLGDQRPA AGEQPGARLH VRATGGALLL CLLAVLLGWV WLRRQRACGI PPGPKPRPLV GNFGHLLVPR FLRPQFWLGS GSQTDTVGQH VYLARMARVY GNIFSFFIGH RLVVVLSDFH SVREALVQQA EVFSDRPRMP LISIMTKEKG IVFAHYGPIW KQQRRFSHST LRHFGLGKLS LEPRIIEEFA YVKEAMQKHG EAPFSPFPII SNAVSNIICS LCFGQRFDYT NKEFKKVLDF MSRGLEICLH SQLFLINICP WFYYLPFGPF KELRQIERDI SCFLKNIIRE HQESLDASNP QDFIDMYLLH MEEEQGASRR SSFDEDYLFY IIGDLFIAGT DTTTNSLLWC LLYMSLNPDV QKKVHEEIER VIGCDRAPSL TDKAQMPYTE ATIMEVQRLS MVVPLAIPHM TSEKTVLQGF TIPKGTVVLI NLWSVHRDPA IWEKPDDFCP HRFLDDQGQL LKRETFIPFG IGKRVCMGEQ LAKMELFLMF VSLMQTFTFA LPEGSEKPVM TGRFGLTLAP HPFNVTISKR // ID CP341_MOUSE Reviewed; 504 AA. AC Q9JMA7; B2RQU5; E9QJT9; DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 2. DT 19-FEB-2014, entry version 107. DE RecName: Full=Cytochrome P450 3A41; DE EC=1.14.14.1; GN Name=Cyp3a41a; Synonyms=Cyp3a41; GN and GN Name=Cyp3a41b; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=ddY; TISSUE=Liver; RX PubMed=10775455; DOI=10.1006/abbi.2000.1747; RA Sakuma T., Takai M., Endo Y., Kuroiwa M., Ohara A., Jarukamjorn K., RA Honma R., Nemoto N.; RT "A novel female-specific member of the CYP3A gene subfamily in the RT mouse liver."; RL Arch. Biochem. Biophys. 377:153-162(2000). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- CATALYTIC ACTIVITY: RH + reduced flavoprotein + O(2) = ROH + CC oxidized flavoprotein + H(2)O. CC -!- COFACTOR: Heme group (By similarity). CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral CC membrane protein (Potential). Microsome membrane; Peripheral CC membrane protein (Potential). CC -!- TISSUE SPECIFICITY: Expressed in liver. Also expressed in the CC kidneys of female mice, with traces in the stomach, ovary, and CC heart of female mice and in the testis of male mice. CC -!- DEVELOPMENTAL STAGE: Detected immediately after birth in the CC livers of animals of both sexes, but increases with age in CC females, whereas it is gradually reduced in males, resulting in CC predominantly female-specific expression in livers. CC -!- SIMILARITY: Belongs to the cytochrome P450 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AB033414; BAA95951.1; -; mRNA. DR EMBL; AC124483; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC166648; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC138083; AAI38084.1; -; mRNA. DR EMBL; BC138084; AAI38085.1; -; mRNA. DR RefSeq; NP_001098629.1; NM_001105159.1. DR RefSeq; NP_059092.2; NM_017396.3. DR UniGene; Mm.379071; -. DR UniGene; Mm.489591; -. DR ProteinModelPortal; Q9JMA7; -. DR SMR; Q9JMA7; 29-498. DR IntAct; Q9JMA7; 3. DR MINT; MINT-4091744; -. DR PhosphoSite; Q9JMA7; -. DR PaxDb; Q9JMA7; -. DR PRIDE; Q9JMA7; -. DR Ensembl; ENSMUST00000075837; ENSMUSP00000075234; ENSMUSG00000075552. DR Ensembl; ENSMUST00000094111; ENSMUSP00000091659; ENSMUSG00000075551. DR GeneID; 100041375; -. DR GeneID; 53973; -. DR KEGG; mmu:100041375; -. DR KEGG; mmu:53973; -. DR UCSC; uc012egw.1; mouse. DR CTD; 100041375; -. DR CTD; 53973; -. DR MGI; MGI:1858451; Cyp3a41a. DR MGI; MGI:3714859; Cyp3a41b. DR eggNOG; COG2124; -. DR GeneTree; ENSGT00730000110610; -. DR HOGENOM; HOG000039127; -. DR HOVERGEN; HBG108567; -. DR InParanoid; B2RQU5; -. DR KO; K07424; -. DR OrthoDB; EOG744TBS; -. DR TreeFam; TF105087; -. DR NextBio; 310861; -. DR PRO; PR:Q9JMA7; -. DR Bgee; Q9JMA7; -. DR Genevestigator; Q9JMA7; -. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0070330; F:aromatase activity; IEA:UniProtKB-EC. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR Gene3D; 1.10.630.10; -; 1. DR InterPro; IPR001128; Cyt_P450. DR InterPro; IPR017972; Cyt_P450_CS. DR InterPro; IPR008072; Cyt_P450_E_CYP3A. DR InterPro; IPR002402; Cyt_P450_E_grp-II. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00464; EP450II. DR PRINTS; PR01689; EP450IICYP3A. DR PRINTS; PR00385; P450. DR SUPFAM; SSF48264; SSF48264; 1. DR PROSITE; PS00086; CYTOCHROME_P450; 1. PE 2: Evidence at transcript level; KW Complete proteome; Endoplasmic reticulum; Heme; Iron; Membrane; KW Metal-binding; Microsome; Monooxygenase; Oxidoreductase; KW Reference proteome. FT CHAIN 1 504 Cytochrome P450 3A41. FT /FTId=PRO_0000051813. FT METAL 443 443 Iron (heme axial ligand) (By similarity). FT CONFLICT 42 42 K -> T (in Ref. 1; BAA95951 and 3; FT AAI38084/AAI38085). SQ SEQUENCE 504 AA; 57987 MW; 1F6455156C073479 CRC64; MNLFSALSLD TWVLLAIILV LLYRYGTRTH GLFKKQGIPG PKPLPFLGTV LNYYKGLWKF DMECYEKYGK TWGLFDGQMP LFVITDPEMI KNVLVKECFS VFTNRREFGP VGIMSKAISI SKDEEWKRYR ALLSPTFTSG KLKEMFPVIE QYGDILVKYL MQEAEKGKPV TMKDVLGAYS IDVITSTSFG VNVDSLNNPE DPFVEKAKGI LRVDFFDPLV FSVVLFPFLT PVYEMLNICM FPKDSIEFFK KFVNRMKESR LDSKQKHRVD FLQLMMNAHN NSKDKDSHKA LSDMEITAQS IVFIFAGYET TSSTLSFTLY CLATHPDIQK KLQEEIDETL PNKAPPTYDT VMEMEYLDMV LNETLRLYPI GNRLERFCKK DVELNGVYIP KGSTVMIPSY ALHHDPQHWP EPEEFQPERF SKENKGSIDP YLYMPFGIGP RNCIGMRFAF MTMKLALTKV MQNFSFQPCQ ETQIPLKLSR QGLLQPEKPI VLKVVPRDVV ITGA // ID CP39A_MOUSE Reviewed; 470 AA. AC Q9JKJ9; DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 19-MAR-2014, entry version 101. DE RecName: Full=24-hydroxycholesterol 7-alpha-hydroxylase; DE EC=1.14.13.99; DE AltName: Full=Cytochrome P450 39A1; DE Short=mCYP39A1; DE AltName: Full=Oxysterol 7-alpha-hydroxylase; GN Name=Cyp39a1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Liver; RX PubMed=10748047; DOI=10.1074/jbc.M001810200; RA Li-Hawkins J., Lund E.G., Bronson A.D., Russell D.W.; RT "Expression cloning of an oxysterol 7alpha-hydroxylase selective for RT 24-hydroxycholesterol."; RL J. Biol. Chem. 275:16543-16549(2000). CC -!- FUNCTION: Involved in the bile acid metabolism. Has a preference CC for 24-hydroxycholesterol, and converts it into a 7-alpha- CC hydroxylated product (By similarity). CC -!- CATALYTIC ACTIVITY: (24R)-cholest-5-ene-3-beta,24-diol + NADPH + CC O(2) = (24R)-cholest-5-ene-3-beta,7-alpha,24-triol + NADP(+) + CC H(2)O. CC -!- COFACTOR: Heme group (By similarity). CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral CC membrane protein. Microsome membrane; Peripheral membrane protein. CC -!- TISSUE SPECIFICITY: Liver specific. Hepatic expression is sexually CC dimorphic (female > male). CC -!- SIMILARITY: Belongs to the cytochrome P450 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF237981; AAF63328.1; -; mRNA. DR RefSeq; NP_061375.1; NM_018887.4. DR UniGene; Mm.17991; -. DR UniGene; Mm.376968; -. DR ProteinModelPortal; Q9JKJ9; -. DR SMR; Q9JKJ9; 24-469. DR IntAct; Q9JKJ9; 1. DR MINT; MINT-4089498; -. DR PaxDb; Q9JKJ9; -. DR PRIDE; Q9JKJ9; -. DR Ensembl; ENSMUST00000170988; ENSMUSP00000130073; ENSMUSG00000023963. DR GeneID; 56050; -. DR KEGG; mmu:56050; -. DR UCSC; uc008cpn.1; mouse. DR CTD; 51302; -. DR MGI; MGI:1927096; Cyp39a1. DR eggNOG; COG2124; -. DR GeneTree; ENSGT00550000074551; -. DR HOGENOM; HOG000290686; -. DR HOVERGEN; HBG106232; -. DR InParanoid; Q9JKJ9; -. DR KO; K07439; -. DR OMA; DRWKEAN; -. DR OrthoDB; EOG7W153H; -. DR TreeFam; TF105090; -. DR BRENDA; 1.14.13.99; 3474. DR NextBio; 311832; -. DR PRO; PR:Q9JKJ9; -. DR ArrayExpress; Q9JKJ9; -. DR Bgee; Q9JKJ9; -. DR Genevestigator; Q9JKJ9; -. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; TAS:UniProtKB. DR GO; GO:0033782; F:24-hydroxycholesterol 7alpha-hydroxylase activity; IEA:UniProtKB-EC. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0008396; F:oxysterol 7-alpha-hydroxylase activity; IDA:UniProtKB. DR GO; GO:0008387; F:steroid 7-alpha-hydroxylase activity; IDA:MGI. DR GO; GO:0006699; P:bile acid biosynthetic process; IDA:UniProtKB. DR GO; GO:0030573; P:bile acid catabolic process; IEA:UniProtKB-KW. DR GO; GO:0006707; P:cholesterol catabolic process; IDA:MGI. DR GO; GO:0007586; P:digestion; TAS:UniProtKB. DR Gene3D; 1.10.630.10; -; 1. DR InterPro; IPR001128; Cyt_P450. DR InterPro; IPR024204; Cyt_P450_CYP7A1-type. DR InterPro; IPR002403; Cyt_P450_E_grp-IV. DR Pfam; PF00067; p450; 1. DR PIRSF; PIRSF000047; Cytochrome_CYPVIIA1; 1. DR PRINTS; PR00465; EP450IV. DR SUPFAM; SSF48264; SSF48264; 1. PE 2: Evidence at transcript level; KW Bile acid catabolism; Complete proteome; Endoplasmic reticulum; Heme; KW Iron; Lipid degradation; Lipid metabolism; Membrane; Metal-binding; KW Microsome; Monooxygenase; NADP; Oxidoreductase; Reference proteome; KW Steroid metabolism. FT CHAIN 1 470 24-hydroxycholesterol 7-alpha- FT hydroxylase. FT /FTId=PRO_0000051993. FT METAL 415 415 Iron (heme axial ligand) (Potential). SQ SEQUENCE 470 AA; 53575 MW; 9F08D3D936C26270 CRC64; MGIMELFSPI AIAVLGSCVL FLFSRLKNLL GPPCIQGWIP WIGAGLEFGK APLEFIEKAR IKYGPVFTIF AMGNRMTFVS EEEGINVLLK SEHVDFESAV QSPVYHTAWI PKNVFSALHE RLYALMKGKM GTFNTHHFTG PLTEELHEQL EGLGTHGTMD LNDFVRYLLY PATLNTLFKK GLFLTDKRTI KEFYQQFKTY DEGFEYGSQL PEWLLRNWSK SKRWLLALFE KNIGNIKAHG SAGHSGTLLQ AILEVVETET RQYSPNYGLV VLWAALANAP PIAFWTLGYI LSHPDIHRTV LESISSVFGT AGKDKIKVSE DDLKKLLIIK WCILESVRLR APGVITRKVV KPVKILNHTV PSGDLLMLSP FWLHRNPKYF PEPESFKPER WKEANLDKYI FLDYFMAFGG GKFQCPGRWF ALLEIQLCII LVLYKYECSL LDPLPKQSSR HLVGVPQPAG KCRIEYKQRA // ID CP3AB_MOUSE Reviewed; 504 AA. AC Q64459; DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 19-FEB-2014, entry version 120. DE RecName: Full=Cytochrome P450 3A11; DE EC=1.14.14.1; DE AltName: Full=CYPIIIA11; DE AltName: Full=Cytochrome P-450IIIAM1; DE AltName: Full=Cytochrome P-450UT; GN Name=Cyp3a11; Synonyms=Cyp3a-11; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=ddY; TISSUE=Liver; RX PubMed=1339292; DOI=10.1016/0167-4781(92)90447-8; RA Yanagimoto T., Itoh S., Muller-Enoch D., Kamataki T.; RT "Mouse liver cytochrome P-450 (P-450IIIAM1): its cDNA cloning and RT inducibility by dexamethasone."; RL Biochim. Biophys. Acta 1130:329-332(1992). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Liver; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP PROTEIN SEQUENCE OF 1-17 AND 22-24. RX PubMed=2402224; RA Bornheim L.M., Correia M.A.; RT "Selective inactivation of mouse liver cytochrome P-450IIIA by RT cannabidiol."; RL Mol. Pharmacol. 38:319-326(1990). CC -!- FUNCTION: Catalyzes erythromycin N-demethylation, nifedipine CC oxidation and testosterone 6 beta-hydroxylation. CC -!- CATALYTIC ACTIVITY: RH + reduced flavoprotein + O(2) = ROH + CC oxidized flavoprotein + H(2)O. CC -!- COFACTOR: Heme group (By similarity). CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral CC membrane protein. Microsome membrane; Peripheral membrane protein. CC -!- TISSUE SPECIFICITY: Highly expressed in liver. CC -!- INDUCTION: By dexamethasone. CC -!- SIMILARITY: Belongs to the cytochrome P450 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X60452; CAA42981.1; -; mRNA. DR EMBL; BC010528; AAH10528.1; -; mRNA. DR PIR; S22334; A60564. DR RefSeq; NP_031844.1; NM_007818.3. DR UniGene; Mm.332844; -. DR ProteinModelPortal; Q64459; -. DR SMR; Q64459; 30-498. DR IntAct; Q64459; 6. DR MINT; MINT-4091753; -. DR STRING; 10090.ENSMUSP00000037665; -. DR ChEMBL; CHEMBL1907984; -. DR PhosphoSite; Q64459; -. DR PaxDb; Q64459; -. DR PRIDE; Q64459; -. DR Ensembl; ENSMUST00000035918; ENSMUSP00000037665; ENSMUSG00000056035. DR GeneID; 13112; -. DR KEGG; mmu:13112; -. DR UCSC; uc009amy.1; mouse. DR CTD; 13112; -. DR MGI; MGI:88609; Cyp3a11. DR eggNOG; COG2124; -. DR GeneTree; ENSGT00730000110610; -. DR HOGENOM; HOG000039127; -. DR HOVERGEN; HBG108567; -. DR InParanoid; Q64459; -. DR KO; K07424; -. DR OMA; EMESHKA; -. DR OrthoDB; EOG744TBS; -. DR TreeFam; TF105087; -. DR NextBio; 283122; -. DR PRO; PR:Q64459; -. DR ArrayExpress; Q64459; -. DR Bgee; Q64459; -. DR Genevestigator; Q64459; -. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0070330; F:aromatase activity; IEA:UniProtKB-EC. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0004497; F:monooxygenase activity; IDA:MGI. DR Gene3D; 1.10.630.10; -; 1. DR InterPro; IPR001128; Cyt_P450. DR InterPro; IPR017972; Cyt_P450_CS. DR InterPro; IPR008072; Cyt_P450_E_CYP3A. DR InterPro; IPR002402; Cyt_P450_E_grp-II. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00464; EP450II. DR PRINTS; PR01689; EP450IICYP3A. DR PRINTS; PR00385; P450. DR SUPFAM; SSF48264; SSF48264; 1. DR PROSITE; PS00086; CYTOCHROME_P450; 1. PE 1: Evidence at protein level; KW Complete proteome; Direct protein sequencing; Endoplasmic reticulum; KW Heme; Iron; Membrane; Metal-binding; Microsome; Monooxygenase; KW Oxidoreductase; Reference proteome. FT CHAIN 1 504 Cytochrome P450 3A11. FT /FTId=PRO_0000051794. FT METAL 443 443 Iron (heme axial ligand) (By similarity). SQ SEQUENCE 504 AA; 57855 MW; E369AF71CE23F180 CRC64; MDLVSALSLE TWVLLAISLV LLYRYGTRKH ELFKKQGIPG PKPLPFLGTV LNYYKGLWKF DMECYKKYGK TWGLFDGQTP LLAVTDPETI KNVLVKECFS VFTNRRDFGP VGIMSKAISI SKDDEWKRYR ALLSPTFTSG KLKEMFPVIE QYGDILVKYL RQKAKKGKPV TMKDVLGAYS MDVITSTSFG VNVDSLNNPE DPFVEKAKKL LRFDFFDPLL FSVVLFPFLT PVYEMLNICM FPKDSIEFFK KFVDRMKESR LDSKQKHRVD FLQLMMNSHN NSKDKVSHKA LSDMEITAQS IIFIFAGYET TSSTLSFTLH SLATHPDIQK KLQDEIDEAL PNKAPPTYDT VMEMEYLDMV LNETLRLYPI ANRLERVCKK DVELNGVYIP KGSTVMIPSY ALHHDPQHWS EPEEFQPERF SKENKGSIDP YVYLPFGNGP RNCLGMRFAL MNMKLALTKI MQNFSFQPCK ETQIPLKLSR QGLLQPEKPI VLKVVPRDAV ITGA // ID CP3AD_MOUSE Reviewed; 503 AA. AC Q64464; DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 19-FEB-2014, entry version 113. DE RecName: Full=Cytochrome P450 3A13; DE EC=1.14.14.1; DE AltName: Full=CYPIIIA13; GN Name=Cyp3a13; Synonyms=Cyp3a-13; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=ddY; TISSUE=Liver; RX PubMed=7803471; DOI=10.1016/0304-4165(94)90069-8; RA Yanagimoto T., Itoh S., Sawada M., Hashimoto H., Kamataki T.; RT "Molecular cloning and functional expression of a mouse cytochrome P- RT 450 (Cyp3a-13): examination of Cyp3a-13 enzyme to activate aflatoxin RT B1 (AFB1)."; RL Biochim. Biophys. Acta 1201:405-410(1994). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Olfactory epithelium; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: Can activate aflatoxin B1 to a genotoxic product. CC -!- CATALYTIC ACTIVITY: RH + reduced flavoprotein + O(2) = ROH + CC oxidized flavoprotein + H(2)O. CC -!- COFACTOR: Heme group (By similarity). CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral CC membrane protein. Microsome membrane; Peripheral membrane protein. CC -!- INDUCTION: P450 can be induced to high levels in liver and other CC tissues by various foreign compounds, including drugs, pesticides, CC and carcinogens. CC -!- SIMILARITY: Belongs to the cytochrome P450 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X63023; CAA44754.1; -; mRNA. DR EMBL; BC046592; AAH46592.1; -; mRNA. DR PIR; S50211; S50211. DR RefSeq; NP_031845.1; NM_007819.4. DR UniGene; Mm.289886; -. DR ProteinModelPortal; Q64464; -. DR SMR; Q64464; 28-497. DR MINT; MINT-1863519; -. DR PhosphoSite; Q64464; -. DR PaxDb; Q64464; -. DR PRIDE; Q64464; -. DR Ensembl; ENSMUST00000031741; ENSMUSP00000031741; ENSMUSG00000029727. DR GeneID; 13113; -. DR KEGG; mmu:13113; -. DR UCSC; uc009aef.2; mouse. DR CTD; 13113; -. DR MGI; MGI:88610; Cyp3a13. DR eggNOG; COG2124; -. DR GeneTree; ENSGT00730000110610; -. DR HOGENOM; HOG000039127; -. DR HOVERGEN; HBG108567; -. DR InParanoid; Q64464; -. DR KO; K07424; -. DR OMA; FYLTHRE; -. DR OrthoDB; EOG744TBS; -. DR TreeFam; TF105087; -. DR NextBio; 283126; -. DR PRO; PR:Q64464; -. DR ArrayExpress; Q64464; -. DR Bgee; Q64464; -. DR Genevestigator; Q64464; -. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0070330; F:aromatase activity; IEA:UniProtKB-EC. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0004497; F:monooxygenase activity; ISS:UniProtKB. DR GO; GO:0010628; P:positive regulation of gene expression; IMP:MGI. DR Gene3D; 1.10.630.10; -; 1. DR InterPro; IPR001128; Cyt_P450. DR InterPro; IPR017972; Cyt_P450_CS. DR InterPro; IPR008072; Cyt_P450_E_CYP3A. DR InterPro; IPR002402; Cyt_P450_E_grp-II. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00464; EP450II. DR PRINTS; PR01689; EP450IICYP3A. DR PRINTS; PR00385; P450. DR SUPFAM; SSF48264; SSF48264; 1. DR PROSITE; PS00086; CYTOCHROME_P450; 1. PE 2: Evidence at transcript level; KW Complete proteome; Endoplasmic reticulum; Heme; Iron; Membrane; KW Metal-binding; Microsome; Monooxygenase; Oxidoreductase; KW Reference proteome. FT CHAIN 1 503 Cytochrome P450 3A13. FT /FTId=PRO_0000051796. FT METAL 442 442 Iron (heme axial ligand) (By similarity). SQ SEQUENCE 503 AA; 57492 MW; 15DDE2606B337FCF CRC64; MDLIPNFSME TWMLLATSLV LLYLYGTHSH GIFKKLGIPG PKPLPFLGTI LAYQKGFWEC DIQCHKKYGK MWGLYDGRQP VLAITDPDII KTVLVKECYS TFTNRRRFGP VGILKKAISI SENEEWKRIR ALLSPTFTSG RLKEMFPIIN QFTDVLVRNM RQGLGEGKPT SMKDIFGAYS MDVITATSFG VNIDSLNNPQ DPFVEKIKKL LKFDIFDPLF LSVTLFPFLT PVFDALNVSL FPRDVISFFT TSVERMKENR MKEKEKQRVD FLQLMINSQN YKTKESHKAL SDVEIVAQSV IFIFAGYETT SSALSFALYL LAIHPDVQKK LQDEIDAALP NKAPATYDTL LQMEYLDMVV NETLRLYPIA GRLERVCKTD VEINGLFIPK GTVVMIPTFA LHKDPKYWPE PEEFRPERFS KKNQDSINPY MYLPFGSGPR NCIGMRFALI NMKVALVRVL QNFTVQPCKE TEIPLKLSKQ GLLQPENPLL LKVVSRDETV SDE // ID CP3AG_MOUSE Reviewed; 504 AA. AC Q64481; E9QP65; DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 2. DT 19-FEB-2014, entry version 111. DE RecName: Full=Cytochrome P450 3A16; DE EC=1.14.14.1; DE AltName: Full=CYPIIIA16; GN Name=Cyp3a16; Synonyms=Cyp3a-16; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=ICR; TISSUE=Liver; RX PubMed=7813478; DOI=10.1111/j.1432-1033.1994.t01-1-00877.x; RA Itoh S., Satoh M., Abe Y., Hashimoto H., Yanagimoto T., Kamataki T.; RT "A novel form of mouse cytochrome P450 3A (Cyp3a-16). Its cDNA cloning RT and expression in fetal liver."; RL Eur. J. Biochem. 226:877-882(1994). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). CC -!- FUNCTION: Cytochromes P450 are a group of heme-thiolate CC monooxygenases. In liver microsomes, this enzyme is involved in an CC NADPH-dependent electron transport pathway. It oxidizes a variety CC of structurally unrelated compounds, including steroids, fatty CC acids, and xenobiotics. CC -!- CATALYTIC ACTIVITY: RH + reduced flavoprotein + O(2) = ROH + CC oxidized flavoprotein + H(2)O. CC -!- COFACTOR: Heme group (By similarity). CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral CC membrane protein. Microsome membrane; Peripheral membrane protein. CC -!- DEVELOPMENTAL STAGE: Fetal- and puberty-specific. CC -!- INDUCTION: P450 can be induced to high levels in liver and other CC tissues by various foreign compounds, including drugs, pesticides, CC and carcinogens. CC -!- SIMILARITY: Belongs to the cytochrome P450 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; D26137; BAA05133.1; -; mRNA. DR EMBL; AC115895; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR PIR; S50892; S50892. DR RefSeq; NP_031846.2; NM_007820.2. DR UniGene; Mm.378905; -. DR ProteinModelPortal; Q64481; -. DR SMR; Q64481; 29-498. DR IntAct; Q64481; 3. DR MINT; MINT-4091767; -. DR PhosphoSite; Q64481; -. DR PaxDb; Q64481; -. DR PRIDE; Q64481; -. DR Ensembl; ENSMUST00000031633; ENSMUSP00000031633; ENSMUSG00000038656. DR GeneID; 13114; -. DR KEGG; mmu:13114; -. DR UCSC; uc009amv.2; mouse. DR CTD; 13114; -. DR MGI; MGI:106099; Cyp3a16. DR eggNOG; COG2124; -. DR GeneTree; ENSGT00730000110610; -. DR HOGENOM; HOG000039127; -. DR HOVERGEN; HBG108567; -. DR InParanoid; Q64481; -. DR KO; K07424; -. DR OrthoDB; EOG7W6WKQ; -. DR TreeFam; TF105087; -. DR NextBio; 283130; -. DR PRO; PR:Q64481; -. DR Bgee; Q64481; -. DR Genevestigator; Q64481; -. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0070330; F:aromatase activity; IEA:UniProtKB-EC. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR Gene3D; 1.10.630.10; -; 1. DR InterPro; IPR001128; Cyt_P450. DR InterPro; IPR017972; Cyt_P450_CS. DR InterPro; IPR008072; Cyt_P450_E_CYP3A. DR InterPro; IPR002402; Cyt_P450_E_grp-II. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00464; EP450II. DR PRINTS; PR01689; EP450IICYP3A. DR PRINTS; PR00385; P450. DR SUPFAM; SSF48264; SSF48264; 1. DR PROSITE; PS00086; CYTOCHROME_P450; 1. PE 2: Evidence at transcript level; KW Complete proteome; Endoplasmic reticulum; Heme; Iron; Membrane; KW Metal-binding; Microsome; Monooxygenase; Oxidoreductase; KW Reference proteome. FT CHAIN 1 504 Cytochrome P450 3A16. FT /FTId=PRO_0000051799. FT METAL 443 443 Iron (heme axial ligand) (By similarity). FT CONFLICT 28 28 C -> Y (in Ref. 1; BAA05133). SQ SEQUENCE 504 AA; 57870 MW; 49C1B9E570DB5BC1 CRC64; MNLFSALSLD TLVLLAIILV LLYRYGTCTH GLFKKQGIPG PKPLPFLGTV LNYYKGLWKF DMECYEKYGK TWGLFDGQIP LFVITDPETI KNVLVKECFS VFTNRQDFFP VGIMSKSISL AKDEEWKRYR ALLSPTFTSG NLKEMFPVIE QYGDILVKYL RQEAEKGKPV AVKDVLGAYS MDVIISTTFG VNIDSLNNPE DPFVENAKKV LRFDYFDPLS LSVALFPFLT PIYEMLNICM FPKDSIEFFK KFVDRMTENR LDSKQKHRVD FIYLMMEAYN KSKDKDSHKA LSEIEITAQS IIFIFAGYET TSSILSFTVY SLATHPDIQK KLQEEIDEAL PNKAPPTYDT VMAMEYLDMV LNETLRLYPI TNRLQRVCKK DVEINGIYIP KGSTVIIPSY VLHHDPQHWP EPEEFQPERF SKENKGSIDP YVYLPFGNGP RNCIGMRFAL MNMKLALIKV LQNFSFQPCK ETQIPLKLSR ELLLQPVKPI VLKVVPRDAV ITGA // ID CP3AP_MOUSE Reviewed; 503 AA. AC O09158; DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1997, sequence version 1. DT 19-FEB-2014, entry version 115. DE RecName: Full=Cytochrome P450 3A25; DE EC=1.14.14.1; DE AltName: Full=CYPIIIA25; GN Name=Cyp3a25; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Mahnke A., Roos P., Hanstein W.G.; RL Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Liver; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: Cytochromes P450 are a group of heme-thiolate CC monooxygenases. In liver microsomes, this enzyme is involved in an CC NADPH-dependent electron transport pathway. It oxidizes a variety CC of structurally unrelated compounds, including steroids, fatty CC acids, and xenobiotics. CC -!- CATALYTIC ACTIVITY: RH + reduced flavoprotein + O(2) = ROH + CC oxidized flavoprotein + H(2)O. CC -!- COFACTOR: Heme group (By similarity). CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral CC membrane protein. Microsome membrane; Peripheral membrane protein. CC -!- INDUCTION: P450 can be induced to high levels in liver and other CC tissues by various foreign compounds, including drugs, pesticides, CC and carcinogens. CC -!- SIMILARITY: Belongs to the cytochrome P450 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; Y11995; CAA72720.1; -; mRNA. DR EMBL; BC028855; AAH28855.1; -; mRNA. DR RefSeq; NP_062766.2; NM_019792.2. DR UniGene; Mm.301900; -. DR UniGene; Mm.384461; -. DR ProteinModelPortal; O09158; -. DR SMR; O09158; 28-497. DR STRING; 10090.ENSMUSP00000065585; -. DR PhosphoSite; O09158; -. DR PaxDb; O09158; -. DR PRIDE; O09158; -. DR Ensembl; ENSMUST00000068317; ENSMUSP00000065585; ENSMUSG00000029630. DR GeneID; 56388; -. DR KEGG; mmu:56388; -. DR UCSC; uc009amz.2; mouse. DR CTD; 56388; -. DR MGI; MGI:1930638; Cyp3a25. DR eggNOG; COG2124; -. DR GeneTree; ENSGT00730000110610; -. DR HOGENOM; HOG000039127; -. DR HOVERGEN; HBG108567; -. DR InParanoid; O09158; -. DR KO; K07424; -. DR OMA; FMKKAIT; -. DR TreeFam; TF105087; -. DR NextBio; 312480; -. DR PRO; PR:O09158; -. DR ArrayExpress; O09158; -. DR Bgee; O09158; -. DR Genevestigator; O09158; -. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0070330; F:aromatase activity; IEA:UniProtKB-EC. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR Gene3D; 1.10.630.10; -; 1. DR InterPro; IPR001128; Cyt_P450. DR InterPro; IPR017972; Cyt_P450_CS. DR InterPro; IPR008072; Cyt_P450_E_CYP3A. DR InterPro; IPR002402; Cyt_P450_E_grp-II. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00464; EP450II. DR PRINTS; PR01689; EP450IICYP3A. DR PRINTS; PR00385; P450. DR SUPFAM; SSF48264; SSF48264; 1. DR PROSITE; PS00086; CYTOCHROME_P450; 1. PE 2: Evidence at transcript level; KW Complete proteome; Endoplasmic reticulum; Heme; Iron; Membrane; KW Metal-binding; Microsome; Monooxygenase; Oxidoreductase; KW Reference proteome. FT CHAIN 1 503 Cytochrome P450 3A25. FT /FTId=PRO_0000051805. FT METAL 442 442 Iron (heme axial ligand) (By similarity). SQ SEQUENCE 503 AA; 58122 MW; 9EE9EAF1746595C8 CRC64; MELIPNLSIE TWVLLVTSLV LFYIYGTYSH GLFKKLGIPG PKPLPLLGTI FNYYDGMWKF DEDCYKKYGK IWGFYEGPQP ILAIMDPEII KIVLVKECYS VFTNRRFFGP VGFMKKAITI SEDEEWKRLR TLLSPTFTSG KLKEMFPIMR QYGDILVRNL RREEEKGEPI SMKDIFGAYS MDVITGTSFG VNVDSLNNPQ DPFVQKAKKI LKFKIFDPFL LSIILFPFLT PIYEMLNFSI FPRDSMNFFK KFVKRMKKER LASNQKNRVD FLQLMMNTQN SKGQESQKAL SDLEMAAQAV IFIFGGYDAT STSISLIMYE LATHPDVQKK LQDEIDRTLP NKAPVTYDAL MDMEYLDMVV NESLRLYPIA IRLERVSKKD VEINGVFIPK GTVVMIPIYP LHRNPEYWPE PQEFCPERFS KENKGNIDPY IYMPFGNGPR NCIGMRFALI SIKLAVIGVL QNFTVQPCEE TQIPLKISRE PIFQPEKPII LKVVSRDKPR TGS // ID CP46A_MOUSE Reviewed; 500 AA. AC Q9WVK8; DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 19-MAR-2014, entry version 117. DE RecName: Full=Cholesterol 24-hydroxylase; DE Short=CH24H; DE EC=1.14.13.98; DE AltName: Full=Cytochrome P450 46A1; GN Name=Cyp46a1; Synonyms=Cyp46; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Liver; RX PubMed=10377398; DOI=10.1073/pnas.96.13.7238; RA Lund E.G., Guileyardo J.M., Russell D.W.; RT "cDNA cloning of cholesterol 24-hydroxylase, a mediator of cholesterol RT homeostasis in the brain."; RL Proc. Natl. Acad. Sci. U.S.A. 96:7238-7243(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Liver; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: Involved in the turnover of cholesterol. It converts CC cholesterol into 24S-hydroxycholesterol and, to a lesser extent, CC 25-hydroxycholesterol. Has also activity with xenobiotic CC compounds. CC -!- CATALYTIC ACTIVITY: Cholesterol + NADPH + O(2) = (24S)-24- CC hydroxycholesterol + NADP(+) + H(2)O. CC -!- COFACTOR: Heme group (By similarity). CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass CC membrane protein. Microsome membrane; Single-pass membrane CC protein. CC -!- TISSUE SPECIFICITY: Expressed in high level in brain (cerebral CC cortex, hippocampus, dentate gyrus and thalamus) and in lower CC levels in testis and liver. Brain's expression increased linearly CC with age. CC -!- SIMILARITY: Belongs to the cytochrome P450 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF094479; AAD41243.1; -; mRNA. DR EMBL; BC018307; AAH18307.1; -; mRNA. DR RefSeq; NP_034140.1; NM_010010.1. DR UniGene; Mm.41911; -. DR ProteinModelPortal; Q9WVK8; -. DR SMR; Q9WVK8; 57-491. DR PhosphoSite; Q9WVK8; -. DR PaxDb; Q9WVK8; -. DR PRIDE; Q9WVK8; -. DR Ensembl; ENSMUST00000021684; ENSMUSP00000021684; ENSMUSG00000021259. DR GeneID; 13116; -. DR KEGG; mmu:13116; -. DR UCSC; uc007ozo.1; mouse. DR CTD; 10858; -. DR MGI; MGI:1341877; Cyp46a1. DR eggNOG; COG2124; -. DR GeneTree; ENSGT00660000095370; -. DR HOGENOM; HOG000290190; -. DR HOVERGEN; HBG102502; -. DR InParanoid; Q9WVK8; -. DR KO; K07440; -. DR OMA; TYFEDPL; -. DR OrthoDB; EOG7CK36N; -. DR TreeFam; TF352037; -. DR BRENDA; 1.14.13.98; 3474. DR NextBio; 283138; -. DR PRO; PR:Q9WVK8; -. DR ArrayExpress; Q9WVK8; -. DR Bgee; Q9WVK8; -. DR Genevestigator; Q9WVK8; -. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0033781; F:cholesterol 24-hydroxylase activity; ISS:UniProtKB. DR GO; GO:0020037; F:heme binding; ISS:UniProtKB. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0006707; P:cholesterol catabolic process; ISS:UniProtKB. DR GO; GO:0006805; P:xenobiotic metabolic process; ISS:UniProtKB. DR Gene3D; 1.10.630.10; -; 1. DR InterPro; IPR001128; Cyt_P450. DR InterPro; IPR017972; Cyt_P450_CS. DR InterPro; IPR002401; Cyt_P450_E_grp-I. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00463; EP450I. DR PRINTS; PR00385; P450. DR SUPFAM; SSF48264; SSF48264; 1. DR PROSITE; PS00086; CYTOCHROME_P450; 1. PE 2: Evidence at transcript level; KW Cholesterol metabolism; Complete proteome; Endoplasmic reticulum; KW Heme; Iron; Lipid metabolism; Membrane; Metal-binding; Microsome; KW Monooxygenase; NADP; Oxidoreductase; Reference proteome; KW Steroid metabolism; Sterol metabolism; Transmembrane; KW Transmembrane helix. FT CHAIN 1 500 Cholesterol 24-hydroxylase. FT /FTId=PRO_0000051995. FT TRANSMEM 3 23 Helical; (Potential). FT COMPBIAS 493 499 Poly-Pro. FT METAL 437 437 Iron (heme axial ligand) (By similarity). SQ SEQUENCE 500 AA; 56814 MW; F0F178FA65820FF2 CRC64; MSPGLLLLGS AVLLAFGLCC TFVHRARSRY EHIPGPPRPS FLLGHLPYFW KKDEDCGRVL QDVFLDWAKK YGPVVRVNVF YKTSVIVTSP ESVKKFLMST KYNKDSKMYR ALQTVFGERL FGQGLVSECD YGRWYKQRKV MDLAFSRSSL VSLMETFNEK AEQLVEILEA KADGQTPVSM QDMLTCATID ILAKAAFGME TSMLLGAQKP LSQAVKVMLE GISASRNTLA KFMPGKRKQL REIRESIRLL RQVGKDWVQR RREALKRGED MPADILTQIL KAEEGAQDDE VLLDNFVTFF IAGHETSANH LAFTVMELSR QPEIVARLQA EVDEVVGSKR HLDYEDLGRL QYLSQVLKES LRLYPPAWGT FRLLEEETLI DGVRVPGNTP LLFSTYVMGR MDTYFEDPLT FNPDRFGPGA PKPRFTYFPF SLGHRSCIGQ QFAQMEVKVV MAKLLQRIEF RLVPGQRFGL QEQATLKPLD PVLCTLRPRG WQPAPPPPPC // ID CP4AA_MOUSE Reviewed; 509 AA. AC O88833; A2A976; Q9DCS5; DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 2. DT 19-FEB-2014, entry version 108. DE RecName: Full=Cytochrome P450 4A10; DE AltName: Full=CYPIVA10; DE AltName: Full=Cytochrome P450-LA-omega 1; DE AltName: Full=Cytochrome P452; DE AltName: Full=Lauric acid omega-hydroxylase; DE EC=1.14.15.3; GN Name=Cyp4a10; Synonyms=Cyp4a-10; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=C57BL/6; TISSUE=Liver; RX PubMed=8031839; RA Henderson C.J., Bammler T., Wolf C.R.; RT "Deduced amino acid sequence of a murine cytochrome P-450 Cyp4a RT protein: developmental and hormonal regulation in liver and kidney."; RL Biochim. Biophys. Acta 1200:182-190(1994). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=ddY; TISSUE=Liver; RA Yasumura N., Ikeda T.; RT "Polymorphism of cyp 4A10 sequence between C57BL/6 and ddY mouse."; RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Kidney; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Kidney; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: Cytochromes P450 are a group of heme-thiolate CC monooxygenases. In liver microsomes, this enzyme is involved in an CC NADPH-dependent electron transport pathway. It oxidizes a variety CC of structurally unrelated compounds, including steroids, fatty CC acids, and xenobiotics. CC -!- CATALYTIC ACTIVITY: Octane + reduced rubredoxin + O(2) = 1-octanol CC + oxidized rubredoxin + H(2)O. CC -!- COFACTOR: Heme group (By similarity). CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral CC membrane protein. Microsome membrane; Peripheral membrane protein. CC -!- SIMILARITY: Belongs to the cytochrome P450 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X69296; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; AB018421; BAA33804.1; -; mRNA. DR EMBL; AK002528; BAB22165.1; -; mRNA. DR EMBL; AL627182; CAM21090.1; -; Genomic_DNA. DR EMBL; BC010747; AAH10747.1; -; mRNA. DR EMBL; BC051049; AAH51049.1; -; mRNA. DR PIR; S47553; S47553. DR RefSeq; NP_034141.3; NM_010011.3. DR UniGene; Mm.10742; -. DR ProteinModelPortal; O88833; -. DR SMR; O88833; 53-503. DR STRING; 10090.ENSMUSP00000061126; -. DR PhosphoSite; O88833; -. DR PaxDb; O88833; -. DR PRIDE; O88833; -. DR Ensembl; ENSMUST00000058785; ENSMUSP00000061126; ENSMUSG00000066072. DR GeneID; 13117; -. DR KEGG; mmu:13117; -. DR UCSC; uc008uex.2; mouse. DR CTD; 13117; -. DR MGI; MGI:88611; Cyp4a10. DR eggNOG; COG2124; -. DR GeneTree; ENSGT00740000115505; -. DR HOGENOM; HOG000233833; -. DR HOVERGEN; HBG000182; -. DR InParanoid; A2A976; -. DR KO; K07425; -. DR OMA; THPDHQQ; -. DR OrthoDB; EOG7CNZFK; -. DR TreeFam; TF105088; -. DR ChiTaRS; Cyp4a10; mouse. DR NextBio; 283142; -. DR PRO; PR:O88833; -. DR ArrayExpress; O88833; -. DR Bgee; O88833; -. DR Genevestigator; O88833; -. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:UniProtKB. DR GO; GO:0018685; F:alkane 1-monooxygenase activity; IEA:UniProtKB-EC. DR GO; GO:0052869; F:arachidonic acid omega-hydroxylase activity; IEA:UniProtKB-EC. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0004497; F:monooxygenase activity; TAS:UniProtKB. DR GO; GO:0006631; P:fatty acid metabolic process; TAS:UniProtKB. DR Gene3D; 1.10.630.10; -; 1. DR InterPro; IPR001128; Cyt_P450. DR InterPro; IPR017972; Cyt_P450_CS. DR InterPro; IPR002401; Cyt_P450_E_grp-I. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00463; EP450I. DR PRINTS; PR00385; P450. DR SUPFAM; SSF48264; SSF48264; 1. DR PROSITE; PS00086; CYTOCHROME_P450; 1. PE 2: Evidence at transcript level; KW Complete proteome; Endoplasmic reticulum; Heme; Iron; Membrane; KW Metal-binding; Microsome; Monooxygenase; Oxidoreductase; KW Reference proteome. FT CHAIN 1 509 Cytochrome P450 4A10. FT /FTId=PRO_0000051815. FT METAL 456 456 Iron (heme axial ligand) (By similarity). FT BINDING 320 320 Heme (covalent; via 1 link) (By FT similarity). FT CONFLICT 62 62 H -> L (in Ref. 1; X69296). FT CONFLICT 64 64 K -> Q (in Ref. 2; BAA33804 and 5; FT AAH10747/AAH51049). FT CONFLICT 69 69 Q -> H (in Ref. 2; BAA33804 and 5; FT AAH10747/AAH51049). FT CONFLICT 234 234 I -> N (in Ref. 1; X69296). SQ SEQUENCE 509 AA; 58330 MW; 94F22CE77BD3EDC0 CRC64; MSVSALSPTR FADSLSGFLQ VASVLGLLLL LVKAVQFYLH RQWLLKAFQQ FPSPPFHWFF GHEKFKGDQE LQEIVSCIEN FPSAFPRWFW GSKAYLTVYD PDYMKVILGR SDPKANGAYR LLAPWIGYGL LLLNGQPWFQ HRRMLTPAFH YDILKPYVKN MADSIRLMLD KWERLADQDS SIEIFQHISL MTLDTVMKCA FSHKGSVQVD GNYRTYLQAI GDLNNLFHSR VRNIFHQNDT IYKLSSNGRL AKQACQLAHD HTDGVIKLRK DQLQDEGELE KIKKKRRLDF LDILLFARME NGDSMSDKDL RAEVDTFMFE GHDTTASGVS WIFYALATHP DHQQRCREEV QSLLGDGSSI TWDHLDQIPY TTMCIKEALR LYPPVPGIVR ELSTSVTFPD GRSLPKGVQV TLSIYGLHHN PKVWPNPEVF DPSRFAPDSP RHSHSFLPFS GGARNCIGKQ FAMSELKVIV ALTLLRFELL PDPTRVPMPL ARLVLKSKNG IYLHLKKLH // ID CP4AE_MOUSE Reviewed; 507 AA. AC O35728; A2A975; Q3UER2; Q5EBH0; DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1998, sequence version 1. DT 19-MAR-2014, entry version 106. DE RecName: Full=Cytochrome P450 4A14; DE AltName: Full=CYPIVA14; DE AltName: Full=Cytochrome P450-LA-omega 3; DE AltName: Full=Lauric acid omega-hydroxylase 3; DE EC=1.14.15.3; DE Flags: Precursor; GN Name=Cyp4a14; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, AND INDUCTION. RC STRAIN=C57BL/6 X CBA; RX PubMed=9271096; RA Heng Y.M., Kuo C.-W.S., Jones P.S., Savory R., Shultz R.M., RA Tomlinson S.R., Gray T.J.B., Bell D.R.; RT "A novel murine P-450 gene, Cyp4a14, is part of a cluster of Cyp4a and RT Cyp4b, but not of CYP4F, genes in mouse and humans."; RL Biochem. J. 325:741-749(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Kidney, and Liver; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Kidney; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: Cytochromes P450 are a group of heme-thiolate CC monooxygenases. In liver microsomes, this enzyme is involved in an CC NADPH-dependent electron transport pathway. It oxidizes a variety CC of structurally unrelated compounds, including steroids, fatty CC acids, and xenobiotics. CC -!- CATALYTIC ACTIVITY: Octane + reduced rubredoxin + O(2) = 1-octanol CC + oxidized rubredoxin + H(2)O. CC -!- COFACTOR: Heme group (By similarity). CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral CC membrane protein. Microsome membrane; Peripheral membrane protein. CC -!- TISSUE SPECIFICITY: Very low level in liver, kidney and spleen. CC -!- INDUCTION: By peroxisome proliferator methylclofenapate; 1000-fold CC in liver, 10-fold in kidney. CC -!- SIMILARITY: Belongs to the cytochrome P450 family. CC -!- SEQUENCE CAUTION: CC Sequence=BC089609; Type=Erroneous termination; Positions=365; Note=Translated as Gln; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; Y11638; CAA72345.1; -; Genomic_DNA. DR EMBL; Y11639; CAA72345.1; JOINED; Genomic_DNA. DR EMBL; Y11640; CAA72345.1; JOINED; Genomic_DNA. DR EMBL; Y11641; CAA72345.1; JOINED; Genomic_DNA. DR EMBL; Y11642; CAA72345.1; JOINED; Genomic_DNA. DR EMBL; AK149392; BAE28849.1; -; mRNA. DR EMBL; AK165452; BAE38193.1; -; mRNA. DR EMBL; AL627182; CAM21089.1; -; Genomic_DNA. DR EMBL; BC089609; -; NOT_ANNOTATED_CDS; mRNA. DR RefSeq; NP_031848.1; NM_007822.2. DR UniGene; Mm.250901; -. DR ProteinModelPortal; O35728; -. DR SMR; O35728; 66-506. DR IntAct; O35728; 1. DR MINT; MINT-4104845; -. DR PhosphoSite; O35728; -. DR PaxDb; O35728; -. DR PRIDE; O35728; -. DR DNASU; 13119; -. DR Ensembl; ENSMUST00000030487; ENSMUSP00000030487; ENSMUSG00000028715. DR GeneID; 13119; -. DR KEGG; mmu:13119; -. DR UCSC; uc008uev.2; mouse. DR CTD; 13119; -. DR MGI; MGI:1096550; Cyp4a14. DR eggNOG; COG2124; -. DR GeneTree; ENSGT00740000115505; -. DR HOGENOM; HOG000233833; -. DR HOVERGEN; HBG000182; -. DR InParanoid; O35728; -. DR KO; K07425; -. DR OrthoDB; EOG7CNZFK; -. DR TreeFam; TF105088; -. DR NextBio; 283150; -. DR PRO; PR:O35728; -. DR Bgee; O35728; -. DR Genevestigator; O35728; -. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0018685; F:alkane 1-monooxygenase activity; IEA:UniProtKB-EC. DR GO; GO:0050544; F:arachidonic acid binding; IEA:Ensembl. DR GO; GO:0008391; F:arachidonic acid monooxygenase activity; IEA:Ensembl. DR GO; GO:0052869; F:arachidonic acid omega-hydroxylase activity; IEA:UniProtKB-EC. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0046456; P:icosanoid biosynthetic process; IEA:Ensembl. DR GO; GO:0001822; P:kidney development; IEA:Ensembl. DR GO; GO:0048252; P:lauric acid metabolic process; IEA:Ensembl. DR GO; GO:0043651; P:linoleic acid metabolic process; IEA:Ensembl. DR GO; GO:0042493; P:response to drug; IEA:Ensembl. DR GO; GO:0009725; P:response to hormone; IEA:Ensembl. DR Gene3D; 1.10.630.10; -; 1. DR InterPro; IPR001128; Cyt_P450. DR InterPro; IPR017972; Cyt_P450_CS. DR InterPro; IPR002401; Cyt_P450_E_grp-I. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00463; EP450I. DR PRINTS; PR00385; P450. DR SUPFAM; SSF48264; SSF48264; 1. DR PROSITE; PS00086; CYTOCHROME_P450; 1. PE 2: Evidence at transcript level; KW Complete proteome; Endoplasmic reticulum; Heme; Iron; Membrane; KW Metal-binding; Microsome; Monooxygenase; Oxidoreductase; KW Reference proteome. FT PROPEP 1 4 Removed in mature form (By similarity). FT /FTId=PRO_0000046058. FT CHAIN 5 507 Cytochrome P450 4A14. FT /FTId=PRO_0000046059. FT METAL 454 454 Iron (heme axial ligand) (By similarity). FT BINDING 318 318 Heme (covalent; via 1 link) (By FT similarity). FT CONFLICT 231 231 N -> D (in Ref. 2; BAE28849). FT CONFLICT 278 278 Q -> R (in Ref. 4; BC089609). FT CONFLICT 401 401 S -> F (in Ref. 4; BC089609). SQ SEQUENCE 507 AA; 58720 MW; EB46205838D4549C CRC64; MGFFLFSPTR YLDGISGFFQ WAFLLSLFLV LFKAVQFYLR RQWLLKTLQH FPCMPSHWLW GHHLKDKELQ QILIWVEKFP SACLQCLSGS NIRVLLYDPD YVKVVLGRSD PKASGIYQFF APWIGYGLLL LNGKKWFQHR RMLTPAFHYD ILKPYVKIMA DSVNIMLDKW EKLDGQDHPL EIFHCVSLMT LDTVMKCAFS YQGSVQLDEN SKLYTKAVED LNNLTFFRLR NAFYKYNIIY NMSSDGRLSH HACQIAHEHT DGVIKMRKSQ LQNEEELQKA RKKRHLDFLD ILLFARMEDR NSLSDEDLRA EVDTFMFEGH DTTASGISWI FYALATHPEH QQRCREEVQS ILGDGTSVTW DHLGQMPYTT MCIKEALRLY PPVISVSREL SSPVTFPDGR SIPKGITATI SIYGLHHNPR FWPNPKVFDP SRFAPDSSHH SHAYLPFSGG SRNCIGKQFA MNELKVAVAL TLLRFELLPD PTRIPVPIAR LVLKSKNGIH LCLKKLR // ID CP4B1_MOUSE Reviewed; 511 AA. AC Q64462; DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 19-MAR-2014, entry version 119. DE RecName: Full=Cytochrome P450 4B1; DE EC=1.14.14.1; DE AltName: Full=CYPIVB1; GN Name=Cyp4b1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE. RC STRAIN=BALB/c; TISSUE=Kidney; RX PubMed=7639529; DOI=10.1006/abbi.1995.1393; RA Imaoka S., Hiroi T., Tamura Y., Yamazaki H., Shimada T., Komori M., RA Degawa M., Funae Y.; RT "Mutagenic activation of 3-methoxy-4-aminoazobenzene by mouse renal RT cytochrome P450 CYP4B1: cloning and characterization of mouse RT CYP4B1."; RL Arch. Biochem. Biophys. 321:255-262(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: Responsible for mutagenic activation of 3-methoxy-4- CC aminoazobenzene (3-MeO-AAB); a potent procarcinogen. Also active CC on 2-aminofluorene and 2-aminoanthracene. CC -!- CATALYTIC ACTIVITY: RH + reduced flavoprotein + O(2) = ROH + CC oxidized flavoprotein + H(2)O. CC -!- COFACTOR: Heme group (By similarity). CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral CC membrane protein. Microsome membrane; Peripheral membrane protein. CC -!- TISSUE SPECIFICITY: Present abundantly in renal microsomes of male CC mice but not in those of female mice. Also present in pulmonary CC microsomes of male and female mice. Not found in liver. CC -!- INDUCTION: P450 can be induced to high levels in liver and other CC tissues by various foreign compounds, including drugs, pesticides, CC and carcinogens. CC -!- SIMILARITY: Belongs to the cytochrome P450 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; D50834; BAA09446.1; -; mRNA. DR EMBL; BC008996; AAH08996.1; -; mRNA. DR PIR; S66472; S66472. DR RefSeq; NP_031849.1; NM_007823.2. DR UniGene; Mm.1840; -. DR ProteinModelPortal; Q64462; -. DR SMR; Q64462; 42-506. DR IntAct; Q64462; 3. DR MINT; MINT-4091779; -. DR STRING; 10090.ENSMUSP00000099768; -. DR PhosphoSite; Q64462; -. DR PaxDb; Q64462; -. DR PRIDE; Q64462; -. DR Ensembl; ENSMUST00000102707; ENSMUSP00000099768; ENSMUSG00000028713. DR GeneID; 13120; -. DR KEGG; mmu:13120; -. DR UCSC; uc008ufc.1; mouse. DR CTD; 1580; -. DR MGI; MGI:103225; Cyp4b1. DR eggNOG; COG2124; -. DR GeneTree; ENSGT00730000110562; -. DR HOGENOM; HOG000233833; -. DR HOVERGEN; HBG000182; -. DR InParanoid; Q64462; -. DR KO; K07426; -. DR OMA; DENGSKL; -. DR OrthoDB; EOG7CNZFK; -. DR TreeFam; TF105088; -. DR NextBio; 283154; -. DR PRO; PR:Q64462; -. DR ArrayExpress; Q64462; -. DR Bgee; Q64462; -. DR Genevestigator; Q64462; -. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0070330; F:aromatase activity; IEA:UniProtKB-EC. DR GO; GO:0008144; F:drug binding; IEA:Ensembl. DR GO; GO:0018585; F:fluorene oxygenase activity; IEA:Ensembl. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0018879; P:biphenyl metabolic process; IEA:Ensembl. DR GO; GO:0042738; P:exogenous drug catabolic process; IEA:Ensembl. DR GO; GO:0018917; P:fluorene metabolic process; IEA:Ensembl. DR Gene3D; 1.10.630.10; -; 1. DR InterPro; IPR001128; Cyt_P450. DR InterPro; IPR017972; Cyt_P450_CS. DR InterPro; IPR002401; Cyt_P450_E_grp-I. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00463; EP450I. DR PRINTS; PR00385; P450. DR SUPFAM; SSF48264; SSF48264; 1. DR PROSITE; PS00086; CYTOCHROME_P450; 1. PE 1: Evidence at protein level; KW Complete proteome; Direct protein sequencing; Endoplasmic reticulum; KW Heme; Iron; Membrane; Metal-binding; Microsome; Monooxygenase; KW Oxidoreductase; Reference proteome. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 511 Cytochrome P450 4B1. FT /FTId=PRO_0000051820. FT METAL 453 453 Iron (heme axial ligand) (By similarity). FT BINDING 315 315 Heme (covalent; via 1 link) (By FT similarity). SQ SEQUENCE 511 AA; 58900 MW; 35463ACDFFE6328B CRC64; MALSFLSPSL SRLGLWASVV ILMVTVLKLL SLLFRRQKLA RALDSFPGPP KHWLFGHALE IQKTGGLDKV VTWTEQFPYA HPLWLGQFIV FLNIYEPDYA KAVYSRGDPK AAYVYDFFLQ WIGKGLLVLE GPKWFQHRKL LTPGFHYDVL KPYVAIFAES TRVMLDKWEK KASENKSFDI FCDVGHMALD TLMKCTFGKG DSGLSHSDNS YYLAVSDLTL LMQQRIDSFQ YHNDFIYWLT PHGRRFLRAC QIAHDHTDHV IRQRKAALQD EKEQKKLQER RHLDFLDILL GARDESGIKL SDADLRAEVD TFMFEGHDTT TSGISWFLYC MALYPMHQQR CREEVREILG DRDSFQWDDL AQMTYLTMCM KECFRLYPPV PQVYRQLSKP VTFVDGRSLP AGSLISLHIY ALHRNSAVWP DPEVFDPLRF SPENMTGRHP FAFMPFSAGP RNCIGQQFAM NEMKVVTALC LLRFEFSPDP SKIPIKVPQL ILRSKNGIHL YLKPLGPGSG K // ID CP4CA_MOUSE Reviewed; 508 AA. AC Q91WL5; A2A973; Q3UNE4; Q6P931; Q8N7N3; DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 2. DT 19-MAR-2014, entry version 105. DE RecName: Full=Cytochrome P450 4A12A; DE EC=1.14.14.1; DE AltName: Full=CYPIVA12; GN Name=Cyp4a12a; Synonyms=Cyp4a12; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Gall bladder; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Kidney, and Liver; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: Cytochromes P450 are a group of heme-thiolate CC monooxygenases. In liver microsomes, this enzyme is involved in an CC NADPH-dependent electron transport pathway. It oxidizes a variety CC of structurally unrelated compounds, including steroids, fatty CC acids, and xenobiotics. CC -!- CATALYTIC ACTIVITY: RH + reduced flavoprotein + O(2) = ROH + CC oxidized flavoprotein + H(2)O. CC -!- COFACTOR: Heme group (By similarity). CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral CC membrane protein. Microsome membrane; Peripheral membrane protein. CC -!- INDUCTION: P450 can be induced to high levels in liver and other CC tissues by various foreign compounds, including drugs, pesticides, CC and carcinogens. CC -!- SIMILARITY: Belongs to the cytochrome P450 family. CC -!- SEQUENCE CAUTION: CC Sequence=BAE25803.1; Type=Frameshift; Positions=492; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK144260; BAE25803.1; ALT_FRAME; mRNA. DR EMBL; AL627227; CAM18400.1; -; Genomic_DNA. DR EMBL; AL627182; CAM18400.1; JOINED; Genomic_DNA. DR EMBL; AL627182; CAM21083.1; -; Genomic_DNA. DR EMBL; AL627227; CAM21083.1; JOINED; Genomic_DNA. DR EMBL; CH466552; EDL30651.1; -; Genomic_DNA. DR EMBL; BC014721; AAH14721.1; -; mRNA. DR EMBL; BC025936; AAH25936.1; -; mRNA. DR EMBL; BC026582; AAH26582.1; -; mRNA. DR EMBL; BC031141; AAH31141.1; -; mRNA. DR EMBL; BC033924; AAH33924.1; -; mRNA. DR RefSeq; NP_803125.2; NM_177406.3. DR UniGene; Mm.276106; -. DR ProteinModelPortal; Q91WL5; -. DR SMR; Q91WL5; 70-508. DR MINT; MINT-1864052; -. DR STRING; 10090.ENSMUSP00000081370; -. DR PhosphoSite; Q91WL5; -. DR PaxDb; Q91WL5; -. DR PRIDE; Q91WL5; -. DR Ensembl; ENSMUST00000084343; ENSMUSP00000081370; ENSMUSG00000066071. DR GeneID; 277753; -. DR KEGG; mmu:277753; -. DR UCSC; uc008uer.1; mouse. DR CTD; 277753; -. DR MGI; MGI:88612; Cyp4a12a. DR eggNOG; COG2124; -. DR GeneTree; ENSGT00740000115505; -. DR HOGENOM; HOG000233833; -. DR HOVERGEN; HBG000182; -. DR InParanoid; A2A973; -. DR KO; K07425; -. DR OMA; ANSACKL; -. DR OrthoDB; EOG7CNZFK; -. DR TreeFam; TF105088; -. DR NextBio; 393827; -. DR PRO; PR:Q91WL5; -. DR ArrayExpress; Q91WL5; -. DR Bgee; Q91WL5; -. DR Genevestigator; Q91WL5; -. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0018685; F:alkane 1-monooxygenase activity; IDA:MGI. DR GO; GO:0070330; F:aromatase activity; IEA:UniProtKB-EC. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0006631; P:fatty acid metabolic process; ISS:UniProtKB. DR Gene3D; 1.10.630.10; -; 1. DR InterPro; IPR001128; Cyt_P450. DR InterPro; IPR017972; Cyt_P450_CS. DR InterPro; IPR002401; Cyt_P450_E_grp-I. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00463; EP450I. DR PRINTS; PR00385; P450. DR SUPFAM; SSF48264; SSF48264; 1. DR PROSITE; PS00086; CYTOCHROME_P450; 1. PE 2: Evidence at transcript level; KW Complete proteome; Endoplasmic reticulum; Heme; Iron; Membrane; KW Metal-binding; Microsome; Monooxygenase; Oxidoreductase; KW Reference proteome. FT CHAIN 1 508 Cytochrome P450 4A12A. FT /FTId=PRO_0000051817. FT METAL 455 455 Iron (heme axial ligand) (By similarity). FT BINDING 319 319 Heme (covalent; via 1 link) (By FT similarity). FT CONFLICT 58 58 W -> C (in Ref. 1; BAE25803). FT CONFLICT 131 131 M -> L (in Ref. 4; AAH14721/AAH25936/ FT AAH26582/AAH31141/AAH33924). FT CONFLICT 288 288 D -> G (in Ref. 1; BAE25803). SQ SEQUENCE 508 AA; 58350 MW; 0F6C78665E78DF4F CRC64; MSASALSSIR FPGSISEYLQ VASVLSLLLL LFKTAQLYLH RQWLLSSTQQ FPSPPSHWLF GHKILKDQDL QDILTRIKNF PSACPQWLWG SKVRIQVYDP DYMKLILGRS DPKANGSYRF LAPWIGRGLL MLDGQTWFQH RRMLTPAFHY DILKPYTEIM ADSVRVMLDK WEQIVGQDST LEIFRHITLM TLDTIMKCAF SHEGSVQLDR KYKSYIQAVE DLNDLVFSRV RNIFHQNDII YRVSSNGCKA NSACKLAHDH TDQVIKSRRI QLQDEEELEK LKKKRRLDFL DILLFARMEN GKSLSDKDLR AEVDTFMFEG HDTTASGISW IFYALATNPE HQQRCRKEIQ SLLGDGTSIT WNDLDKMPYT TMCIKEALRI YPPVPSVSRE LSSPVTFPDG RSLPKGIHVM LSFYGLHHNP TVWPNPEVFD PSRFAPGSSR HSHSFLPFSG GARNCIGKQF AMNELKVAVA LTLLRFELLP DPTRVPIPIP RIVLKSKNGI HLHLKKLQ // ID CP4F3_MOUSE Reviewed; 524 AA. AC Q99N16; E9QLZ3; Q9D8N4; DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 2. DT 19-MAR-2014, entry version 95. DE RecName: Full=Leukotriene-B(4) omega-hydroxylase 2; DE EC=1.14.13.30; DE AltName: Full=CYPIVF3; DE AltName: Full=Cytochrome P450 4F3; DE AltName: Full=Cytochrome P450-LTB-omega; DE AltName: Full=Leukotriene-B(4) 20-monooxygenase 2; GN Name=Cyp4f3; Synonyms=Cyp4f18; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Kidney; RA Antonovic L., Kawashima H., Strobel H.; RT "Protein expression and catalytic activity assessment of mouse 4F RT clones."; RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Pancreas; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Colon; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP FUNCTION, TISSUE SPECIFICITY, AND INDUCTION. RX PubMed=16380383; DOI=10.1074/jbc.M513101200; RA Christmas P., Tolentino K., Primo V., Berry K.Z., Murphy R.C., RA Chen M., Lee D.M., Soberman R.J.; RT "Cytochrome P-450 4F18 is the leukotriene B4 omega-1/omega-2 RT hydroxylase in mouse polymorphonuclear leukocytes: identification as RT the functional orthologue of human polymorphonuclear leukocyte CYP4F3A RT in the down-regulation of responses to LTB4."; RL J. Biol. Chem. 281:7189-7196(2006). CC -!- FUNCTION: Cytochromes P450 are a group of heme-thiolate CC monooxygenases. This enzyme requires molecular oxygen and NADPH CC for the omega-hydroxylation of LTB4, a potent chemoattractant for CC polymorphonuclear leukocytes. CC -!- CATALYTIC ACTIVITY: (6Z,8E,10E,14Z)-(5S,12R)-5,12-dihydroxyicosa- CC 6,8,10,14-tetraenoate + NADPH + O(2) = (6Z,8E,10E,14Z)-(5S,12R)- CC 5,12,20-trihydroxyicosa-6,8,10,14-tetraenoate + NADP(+) + H(2)O. CC -!- COFACTOR: Heme group (By similarity). CC -!- ENZYME REGULATION: Inhibited by carbon monoxide (CO) (By CC similarity). CC -!- PATHWAY: Lipid metabolism; leukotriene B4 degradation. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass CC membrane protein (By similarity). Microsome membrane; Single-pass CC membrane protein (By similarity). CC -!- TISSUE SPECIFICITY: Highest level in polymorphonuclear leukocytes CC and dendritic cells. Detectable in lymph nodes, spleen, bone CC marrow and peripheral blood. Highly expressed in ovary. Very low CC level in liver, kidney, and smooth muscle. CC -!- INDUCTION: Up-regulated in myeloid dendritic cells upon induction CC with LPS in vitro. Down-regulated upon migration of induced cells CC to the lymph node. CC -!- SIMILARITY: Belongs to the cytochrome P450 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF233647; AAK15013.1; -; mRNA. DR EMBL; AK007863; BAB25315.1; -; mRNA. DR EMBL; AC162522; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC013494; AAH13494.1; -; mRNA. DR RefSeq; NP_077764.2; NM_024444.2. DR RefSeq; XP_006509811.1; XM_006509748.1. DR UniGene; Mm.160020; -. DR ProteinModelPortal; Q99N16; -. DR SMR; Q99N16; 96-524. DR STRING; 10090.ENSMUSP00000003574; -. DR PhosphoSite; Q99N16; -. DR PaxDb; Q99N16; -. DR PRIDE; Q99N16; -. DR Ensembl; ENSMUST00000003574; ENSMUSP00000003574; ENSMUSG00000003484. DR GeneID; 72054; -. DR KEGG; mmu:72054; -. DR UCSC; uc009mfe.2; mouse. DR CTD; 72054; -. DR MGI; MGI:1919304; Cyp4f18. DR eggNOG; COG2124; -. DR GeneTree; ENSGT00730000110562; -. DR HOGENOM; HOG000233833; -. DR HOVERGEN; HBG000182; -. DR InParanoid; Q99N16; -. DR KO; K17726; -. DR OMA; RISIFGT; -. DR OrthoDB; EOG7CNZFK; -. DR TreeFam; TF105088; -. DR UniPathway; UPA00883; -. DR NextBio; 335324; -. DR PRO; PR:Q99N16; -. DR Bgee; Q99N16; -. DR Genevestigator; Q99N16; -. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0052871; F:alpha-tocopherol omega-hydroxylase activity; IEA:UniProtKB-EC. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0050051; F:leukotriene-B4 20-monooxygenase activity; IEA:UniProtKB-EC. DR GO; GO:0036101; P:leukotriene B4 catabolic process; IEA:GOC. DR Gene3D; 1.10.630.10; -; 1. DR InterPro; IPR001128; Cyt_P450. DR InterPro; IPR017972; Cyt_P450_CS. DR InterPro; IPR002401; Cyt_P450_E_grp-I. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00463; EP450I. DR PRINTS; PR00385; P450. DR SUPFAM; SSF48264; SSF48264; 1. DR PROSITE; PS00086; CYTOCHROME_P450; 1. PE 2: Evidence at transcript level; KW Complete proteome; Endoplasmic reticulum; Heme; Iron; Membrane; KW Metal-binding; Microsome; Monooxygenase; NADP; Oxidoreductase; KW Reference proteome; Transmembrane; Transmembrane helix. FT CHAIN 1 524 Leukotriene-B(4) omega-hydroxylase 2. FT /FTId=PRO_0000238924. FT TRANSMEM 15 35 Helical; (Potential). FT METAL 468 468 Iron (heme axial ligand) (By similarity). FT CONFLICT 6 6 M -> L (in Ref. 1; AAK15013 and 4; FT AAH13494). FT CONFLICT 37 37 P -> Q (in Ref. 1; AAK15013 and 4; FT AAH13494). FT CONFLICT 142 142 D -> G (in Ref. 2; BAB25315). FT CONFLICT 230 230 T -> A (in Ref. 1; AAK15013 and 4; FT AAH13494). FT CONFLICT 284 284 V -> D (in Ref. 1; AAK15013 and 4; FT AAH13494). SQ SEQUENCE 524 AA; 59843 MW; E97FACEB00CFD7CB CRC64; MSQLSMSWMG LGHTAASPWL LLLLAGASCL LAYILTPIYG VFENSLRLRC FPQPPKRNWI LGHLGLIQSS EEGLLYIQSL VRTFRDACCW WVGPLHPVIR IFHPAFIKPV VLAPALVAPK DTVFYRFLKP WLGDGLLMST GDKWSRHRRM LTPAFHFNIL KPYVKVFNDS TNIMHAKWQR LASKGSAYLN MFEHISLMTL DSLQKCVFSF DSNCQEKPSE YITAILELST LVARRHQRLL LHVDLFYYLT HDGMRFRKAC RLVHDFTDAV IRERRRTLLD QGGVDVLKAK AKAKTLDFID VLLLSKDEHG KALSDEDIRA EADTFMFGGH DTTASGLSWI LYNLARHPEY QERCRQEVRE LLRDREPEEI EWDDLAQLPF LTMCIKESLR LHPPVTAISR CCTQDIVLPD GRVIPKGVIS RISIFGTHHN PAVWPDPEVY DPFRFDADNV KGRSPLAFIP FSAGPRNCIG QTFAMSEMKV ALALTLLRFR VLPDDKEPRR KPELILRAEG GLWLKVEPLS AGAQ // ID CP4FE_MOUSE Reviewed; 524 AA. AC Q9EP75; Q52L93; DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2001, sequence version 1. DT 19-MAR-2014, entry version 103. DE RecName: Full=Leukotriene-B4 omega-hydroxylase 3; DE EC=1.14.13.30; DE AltName: Full=Cyp4f-14; DE AltName: Full=Cytochrome P450 4F14; DE AltName: Full=Cytochrome P450-LTB-omega; DE AltName: Full=Leukotriene-B4 20-monooxygenase 3; GN Name=Cyp4f14; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=C57BL/6; TISSUE=Liver; RA Kikuta Y., Kasyu H., Kusunose E., Kusunose M.; RT "Mouse liver leukotriene B4 omega-hydroxylase."; RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=129/Sv; TISSUE=Brain; RA Antonovic L., Kawashima H., Strobel H.; RT "Protein expression and catalytic activity assessment of mouse 4F RT clones."; RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Cecum, and Liver; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Liver; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: Cytochromes P450 are a group of heme-thiolate CC monooxygenases. This enzyme requires molecular oxygen and NADPH CC for the omega-hydroxylation of LTB4 (By similarity). CC -!- CATALYTIC ACTIVITY: (6Z,8E,10E,14Z)-(5S,12R)-5,12-dihydroxyicosa- CC 6,8,10,14-tetraenoate + NADPH + O(2) = (6Z,8E,10E,14Z)-(5S,12R)- CC 5,12,20-trihydroxyicosa-6,8,10,14-tetraenoate + NADP(+) + H(2)O. CC -!- COFACTOR: Heme group (By similarity). CC -!- PATHWAY: Lipid metabolism; leukotriene B4 degradation. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral CC membrane protein (By similarity). Microsome membrane; Peripheral CC membrane protein (By similarity). CC -!- SIMILARITY: Belongs to the cytochrome P450 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AB037541; BAB12564.1; -; mRNA. DR EMBL; AB037540; BAB12563.1; -; mRNA. DR EMBL; AF233644; AAK15010.1; -; mRNA. DR EMBL; AK005007; BAB23740.1; -; mRNA. DR EMBL; AK018676; BAB31338.1; -; mRNA. DR EMBL; BC011228; AAH11228.1; -; mRNA. DR EMBL; BC094016; AAH94016.1; -; mRNA. DR RefSeq; NP_001191262.1; NM_001204333.1. DR RefSeq; NP_001191263.1; NM_001204334.1. DR RefSeq; NP_001191264.1; NM_001204335.1. DR RefSeq; NP_001191265.1; NM_001204336.1. DR RefSeq; NP_071879.1; NM_022434.2. DR RefSeq; XP_006524845.1; XM_006524782.1. DR RefSeq; XP_006524846.1; XM_006524783.1. DR UniGene; Mm.486449; -. DR ProteinModelPortal; Q9EP75; -. DR SMR; Q9EP75; 97-519. DR IntAct; Q9EP75; 1. DR MINT; MINT-1862770; -. DR STRING; 10090.ENSMUSP00000050478; -. DR PhosphoSite; Q9EP75; -. DR PaxDb; Q9EP75; -. DR PRIDE; Q9EP75; -. DR Ensembl; ENSMUST00000054174; ENSMUSP00000050478; ENSMUSG00000024292. DR Ensembl; ENSMUST00000179434; ENSMUSP00000136139; ENSMUSG00000024292. DR GeneID; 64385; -. DR KEGG; mmu:64385; -. DR UCSC; uc008bxq.2; mouse. DR CTD; 64385; -. DR MGI; MGI:1927669; Cyp4f14. DR eggNOG; COG2124; -. DR GeneTree; ENSGT00730000110562; -. DR HOGENOM; HOG000233833; -. DR HOVERGEN; HBG000182; -. DR InParanoid; Q9EP75; -. DR KO; K17726; -. DR OMA; DKEPRRQ; -. DR OrthoDB; EOG7CNZFK; -. DR TreeFam; TF105088; -. DR UniPathway; UPA00883; -. DR ChiTaRS; Cyp4f14; mouse. DR NextBio; 320067; -. DR PRO; PR:Q9EP75; -. DR ArrayExpress; Q9EP75; -. DR Bgee; Q9EP75; -. DR Genevestigator; Q9EP75; -. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0052871; F:alpha-tocopherol omega-hydroxylase activity; IEA:UniProtKB-EC. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0050051; F:leukotriene-B4 20-monooxygenase activity; IEA:UniProtKB-EC. DR GO; GO:0036101; P:leukotriene B4 catabolic process; IEA:GOC. DR Gene3D; 1.10.630.10; -; 1. DR InterPro; IPR001128; Cyt_P450. DR InterPro; IPR017972; Cyt_P450_CS. DR InterPro; IPR002401; Cyt_P450_E_grp-I. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00463; EP450I. DR PRINTS; PR00385; P450. DR SUPFAM; SSF48264; SSF48264; 1. DR PROSITE; PS00086; CYTOCHROME_P450; 1. PE 2: Evidence at transcript level; KW Complete proteome; Endoplasmic reticulum; Heme; Iron; Membrane; KW Metal-binding; Microsome; Monooxygenase; NADP; Oxidoreductase; KW Reference proteome. FT CHAIN 1 524 Leukotriene-B4 omega-hydroxylase 3. FT /FTId=PRO_0000051858. FT METAL 468 468 Iron (heme axial ligand) (By similarity). FT BINDING 328 328 Heme (covalent; via 1 link) (By FT similarity). SQ SEQUENCE 524 AA; 59800 MW; A89F80E10925E9F4 CRC64; MSQLSLSWLG LGPEVAFPWK TLLLLGASWI LARILIQIYA AYRNYRHLHG FPQPPKRNWL MGHVGMVTPT EQGLKELTRL VGTYPQGFLM WIGPMVPVIT LCHSDIVRSI LNASAAVALK DVIFYSILKP WLGDGLLVSA GDKWSRHRRM LTPAFHFNIL KPYVKIFNDS TNIMHAKWQR LISDGSARLD MFEHVSLMTL DSLQKCVFSF DSNCQEKSSE YIAAILELSA LVAKRHQQPL MFMDLLYNLT PDGMRFRKAC NVVHEFTDAV IRERHRTLPD QGLDDFLKSK AKSKTLDFID VLLLSKDEDG KELSDEDIRA EADTFMFEGH DTTASGLSWI LYNLARHPEY QERCRQEVQE LLRGREPEEI EWDDLAQLPF LTMCIKESLR LHPPVTVISR CCTQDILLPD GRTIPKGIIC LISIFGIHHN PSVWPDPEVY DPFRFDPENI KDSSPLAFIP FSAGPRNCIG QTFAMSEMKV ALALTLLRFR LLPDDKEPRR QPELILRAEG GLWLRVEPLS AGAH // ID CP4V2_MOUSE Reviewed; 525 AA. AC Q9DBW0; DT 02-AUG-2005, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 19-FEB-2014, entry version 99. DE RecName: Full=Cytochrome P450 4V2; DE EC=1.14.13.-; GN Name=Cyp4v2; Synonyms=Cyp4v3; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=C57BL/6; TISSUE=Liver; RA Fujita Y., Kase K., Ohi H.; RT "Mouse mRNA for cytochrome P450, cDNA clone KK-1."; RL Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Lung; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP PROTEIN SEQUENCE OF 472-478, AND MASS SPECTROMETRY. RC STRAIN=OF1; TISSUE=Hippocampus; RA Lubec G., Sunyer B., Chen W.-Q.; RL Submitted (JAN-2009) to UniProtKB. RN [4] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=17242355; DOI=10.1073/pnas.0609836104; RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; RT "Large-scale phosphorylation analysis of mouse liver."; RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). CC -!- FUNCTION: Catalyzes the omega-hydroxylation of medium-chain CC saturated fatty acids such as laurate, myristate and palmitate in CC an NADPH-dependent pathway. The substrate specificity is higher CC for myristate > laurate > palmitate (C14>C16>C12) (By similarity). CC -!- COFACTOR: Heme group (By similarity). CC -!- ENZYME REGULATION: Inhibited by N-hydroxy-N'-(4-n-butyl-2- CC methylphenyl formamidine)(HET0016) (By similarity). CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass CC membrane protein (Potential). CC -!- SIMILARITY: Belongs to the cytochrome P450 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AB056457; BAB33032.1; -; mRNA. DR EMBL; AK004724; BAB23507.1; -; mRNA. DR RefSeq; NP_598730.1; NM_133969.2. DR UniGene; Mm.245297; -. DR ProteinModelPortal; Q9DBW0; -. DR SMR; Q9DBW0; 62-520. DR MINT; MINT-1863146; -. DR STRING; 10090.ENSMUSP00000092966; -. DR PhosphoSite; Q9DBW0; -. DR PaxDb; Q9DBW0; -. DR PRIDE; Q9DBW0; -. DR Ensembl; ENSMUST00000095328; ENSMUSP00000092966; ENSMUSG00000079057. DR GeneID; 102294; -. DR KEGG; mmu:102294; -. DR UCSC; uc009lou.1; mouse. DR CTD; 102294; -. DR MGI; MGI:2142763; Cyp4v3. DR eggNOG; COG2124; -. DR GeneTree; ENSGT00730000110591; -. DR HOVERGEN; HBG000182; -. DR InParanoid; Q9DBW0; -. DR KO; K07427; -. DR OMA; EMIFRRI; -. DR TreeFam; TF105088; -. DR NextBio; 355392; -. DR PRO; PR:Q9DBW0; -. DR ArrayExpress; Q9DBW0; -. DR Bgee; Q9DBW0; -. DR Genevestigator; Q9DBW0; -. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW. DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro. DR GO; GO:0010430; P:fatty acid omega-oxidation; ISS:UniProtKB. DR Gene3D; 1.10.630.10; -; 1. DR InterPro; IPR001128; Cyt_P450. DR InterPro; IPR017972; Cyt_P450_CS. DR InterPro; IPR002401; Cyt_P450_E_grp-I. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00463; EP450I. DR PRINTS; PR00385; P450. DR SUPFAM; SSF48264; SSF48264; 1. DR PROSITE; PS00086; CYTOCHROME_P450; 1. PE 1: Evidence at protein level; KW Complete proteome; Direct protein sequencing; Endoplasmic reticulum; KW Heme; Iron; Membrane; Metal-binding; Monooxygenase; Oxidoreductase; KW Reference proteome; Transmembrane; Transmembrane helix. FT CHAIN 1 525 Cytochrome P450 4V2. FT /FTId=PRO_0000051861. FT TRANSMEM 14 34 Helical; (Potential). FT METAL 467 467 Iron (heme axial ligand) (By similarity). FT BINDING 329 329 Heme (covalent; via 1 link) (By FT similarity). SQ SEQUENCE 525 AA; 60939 MW; 71BB341589BD10A6 CRC64; MLWLWLGLSG QKLLLWGAAS AVSLAGATIL ISIFPMLVSY ARKWQQMRSI PSVARAYPLV GHALYMKPNN AEFFQQLIYY TEEFRHLPII KLWIGPVPLV ALYKAENVEV ILTSSKQIDK SFLYKFLQPW LGLGLLTSTG SKWRTRRKML TPTFHFTILE NFLDVMNEQA NILVNKLEKH VNQEAFNCFF YITLCALDII CETAMGKNIG AQSNNDSEYV RTVYRMSDMI YRRMKMPWLW FDLWYLVFKE GRDHKRGLKC LHTFTNNVIA ERVKERKAEE DWTGAGRGPI PSKNKRKAFL DLLLSVTDEE GNRLSQEDIR EEVDTFMFEG HDTTAAAINW SLYLLGTNPE VQRKVDQELD EVFGRSHRPV TLEDLKKLKY LDCVIKETLR VFPSVPLFAR SLSEDCEVGG YKVTKGTEAI IIPYALHRDP RYFPDPEEFR PERFFPENSQ GRHPYAYVPF SAGPRNCIGQ KFAVMEEKTI LACILRQFWV ESNQKREELG LAGDLILRPN NGIWIKLKRR HEDDP // ID CP4X1_MOUSE Reviewed; 507 AA. AC Q6A152; Q2HJC6; Q8BYS0; DT 06-MAR-2013, integrated into UniProtKB/Swiss-Prot. DT 13-SEP-2004, sequence version 1. DT 19-MAR-2014, entry version 77. DE RecName: Full=Cytochrome P450 4X1; DE EC=1.14.14.1; DE AltName: Full=CYPIVX1; GN Name=Cyp4x1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE RP SPECIFICITY. RC STRAIN=129; TISSUE=Brain; RX PubMed=16478468; DOI=10.1111/j.1742-4658.2006.05119.x; RA Al-Anizy M., Horley N.J., Kuo C.W., Gillett L.C., Laughton C.A., RA Kendall D., Barrett D.A., Parker T., Bell D.R.; RT "Cytochrome P450 Cyp4x1 is a major P450 protein in mouse brain."; RL FEBS J. 273:936-947(2006). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-507. RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 9-507. RC STRAIN=C57BL/6J; TISSUE=Hypothalamus; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). CC -!- CATALYTIC ACTIVITY: RH + reduced flavoprotein + O(2) = ROH + CC oxidized flavoprotein + H(2)O. CC -!- COFACTOR: Heme group (By similarity). CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane (By CC similarity); Single-pass membrane protein (Potential). Microsome CC membrane. CC -!- TISSUE SPECIFICITY: Expressed in brain and aorta. In the brain, CC expressed in the Purkinje cells of the cerebellum, pyramidal CC neurons in the dentate gyrus of the hippocampus, cortical CC forebrain neurons and those of brain stem nuclei (at protein CC level). In addition to neurons, also expressed in cerebral CC vascular endothelial cells (at protein level). Also expressed in CC epithelial cells of the choroid plexus (at protein level). Hardly CC detectable in heart, lung, kidney and spleen. CC -!- SIMILARITY: Belongs to the cytochrome P450 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJ786769; CAH10751.1; -; mRNA. DR EMBL; AL645473; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC113125; AAI13126.1; -; mRNA. DR EMBL; AK038526; BAC30028.1; -; mRNA. DR RefSeq; NP_001003947.1; NM_001003947.1. DR UniGene; Mm.215544; -. DR ProteinModelPortal; Q6A152; -. DR SMR; Q6A152; 44-505. DR STRING; 10090.ENSMUSP00000059545; -. DR PRIDE; Q6A152; -. DR DNASU; 81906; -. DR Ensembl; ENSMUST00000051400; ENSMUSP00000059545; ENSMUSG00000047155. DR GeneID; 81906; -. DR KEGG; mmu:81906; -. DR UCSC; uc008uep.1; mouse. DR CTD; 260293; -. DR MGI; MGI:1932403; Cyp4x1. DR GeneTree; ENSGT00740000115505; -. DR HOGENOM; HOG000233833; -. DR HOVERGEN; HBG000182; -. DR InParanoid; Q6A152; -. DR KO; K07428; -. DR OMA; FQENEME; -. DR TreeFam; TF105088; -. DR NextBio; 350477; -. DR PRO; PR:Q6A152; -. DR ArrayExpress; Q6A152; -. DR Genevestigator; Q6A152; -. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0070330; F:aromatase activity; IEA:UniProtKB-EC. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR Gene3D; 1.10.630.10; -; 1. DR InterPro; IPR001128; Cyt_P450. DR InterPro; IPR017972; Cyt_P450_CS. DR InterPro; IPR002401; Cyt_P450_E_grp-I. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00463; EP450I. DR PRINTS; PR00385; P450. DR SUPFAM; SSF48264; SSF48264; 1. DR PROSITE; PS00086; CYTOCHROME_P450; 1. PE 1: Evidence at protein level; KW Complete proteome; Endoplasmic reticulum; Heme; Iron; Membrane; KW Metal-binding; Microsome; Monooxygenase; Oxidoreductase; KW Reference proteome; Transmembrane; Transmembrane helix. FT CHAIN 1 507 Cytochrome P450 4X1. FT /FTId=PRO_0000421683. FT TRANSMEM 14 34 Helical; (Potential). FT METAL 452 452 Iron (heme axial ligand) (By similarity). FT CONFLICT 9 9 R -> G (in Ref. 4; BAC30028). FT CONFLICT 110 110 M -> T (in Ref. 3; AAI13126). FT CONFLICT 188 188 T -> A (in Ref. 3; AAI13126). FT CONFLICT 327 327 L -> P (in Ref. 3; AAI13126). SQ SEQUENCE 507 AA; 58557 MW; 11A2FAAA650F705A CRC64; MEASWLETRW ARPLHLALVF CLALVLMQAM KLYLRRQRLL RDLSPFPGPP AHWLLGHQKF LQEDNMETLD EIVKKHPCAF PCWVGPFQAF FYIYDPDYAK IFLSRTDPKM QYLHQLLTPC IGRGLLNLDG PRWFQHRCLL TPAFHQDILK PCVDTMAHSV KVMLDKWEKM WTTQETTIEV FEHINLMTLD IIMKCAFGQE TNCQINGTYE SYVKATFELG EIISSRLYNF WHHHDIIFKL SPKGHCFQEL GKVIHQYTEK IIQDRKKILK NQVKQDDTQT SQIFLDIVLS AQAEDERAFS DADLRAEVNT FMWAGHDASA ASISWLLYCL ALNPEHQDRC RTEIRSILGD GSSITWEQLD EMSYTTMCIK ETLRLIPPVP SISRELSKPL TLPDGHSLPA GMTVVLSIWG LHHNPAVWND PKVFDPLRFT KENSDQRHPC AFLPFSSGPR NCIGQQFAML ELKVAIALIL LHFQVAPDLT RPPAFSSHTV LRPKHGIYLH LKKLLEC // ID CP51A_MOUSE Reviewed; 503 AA. AC Q8K0C4; Q8BSQ7; Q9JIP8; Q9JIY3; DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2002, sequence version 1. DT 19-FEB-2014, entry version 108. DE RecName: Full=Lanosterol 14-alpha demethylase; DE Short=LDM; DE EC=1.14.13.70; DE AltName: Full=CYPLI; DE AltName: Full=Cytochrome P450 51A1; DE AltName: Full=Cytochrome P450-14DM; DE Short=Cytochrome P45014DM; DE AltName: Full=Cytochrome P450LI; DE AltName: Full=Sterol 14-alpha demethylase; GN Name=Cyp51a1; Synonyms=Cyp51; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=129/Sv; RX PubMed=10864439; DOI=10.1006/abbi.2000.1859; RA Debeljak N., Horvat S., Vouk K., Lee M., Rozman D.; RT "Characterization of the mouse lanosterol 14alpha-demethylase (CYP51), RT a new member of the evolutionarily most conserved cytochrome P450 RT family."; RL Arch. Biochem. Biophys. 379:37-45(2000). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY. RC STRAIN=129/Sv; RX PubMed=10653123; DOI=10.1007/s004240000070; RA Debeljak N., Horvat S., Komel R., Rozman D.; RT "Molecular cloning and partial characterisation of the mouse Cyp51 RT cDNA."; RL Pflugers Arch. 439:R7-R8(2000). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Embryo, Placenta, Skin, and Testis; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Salivary gland; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: Catalyzes C14-demethylation of lanosterol; it transforms CC lanosterol into 4,4'-dimethyl cholesta-8,14,24-triene-3-beta-ol CC (By similarity). CC -!- CATALYTIC ACTIVITY: A 14-alpha-methylsteroid + 3 O(2) + 3 NADPH = CC a Delta(14)-steroid + formate + 3 NADP(+) + 4 H(2)O. CC -!- COFACTOR: Heme group (By similarity). CC -!- PATHWAY: Steroid biosynthesis; zymosterol biosynthesis; zymosterol CC from lanosterol: step 1/6. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane (Potential). CC Microsome membrane (Potential). CC -!- SIMILARITY: Belongs to the cytochrome P450 family. CC -!- SEQUENCE CAUTION: CC Sequence=AAF73986.1; Type=Erroneous initiation; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF204804; AAF74562.1; -; Genomic_DNA. DR EMBL; AF204796; AAF74562.1; JOINED; Genomic_DNA. DR EMBL; AF204797; AAF74562.1; JOINED; Genomic_DNA. DR EMBL; AF204798; AAF74562.1; JOINED; Genomic_DNA. DR EMBL; AF204799; AAF74562.1; JOINED; Genomic_DNA. DR EMBL; AF204800; AAF74562.1; JOINED; Genomic_DNA. DR EMBL; AF204801; AAF74562.1; JOINED; Genomic_DNA. DR EMBL; AF204802; AAF74562.1; JOINED; Genomic_DNA. DR EMBL; AF204803; AAF74562.1; JOINED; Genomic_DNA. DR EMBL; AF166266; AAF73986.1; ALT_INIT; mRNA. DR EMBL; AK028355; BAC25900.1; -; mRNA. DR EMBL; AK028815; BAC26134.1; -; mRNA. DR EMBL; AK031059; BAC27231.1; -; mRNA. DR EMBL; AK076983; BAC36548.1; -; mRNA. DR EMBL; CH466600; EDL14627.1; -; Genomic_DNA. DR EMBL; BC031813; AAH31813.1; -; mRNA. DR RefSeq; NP_064394.2; NM_020010.2. DR UniGene; Mm.140158; -. DR ProteinModelPortal; Q8K0C4; -. DR SMR; Q8K0C4; 59-502. DR MINT; MINT-1853747; -. DR PhosphoSite; Q8K0C4; -. DR PaxDb; Q8K0C4; -. DR PRIDE; Q8K0C4; -. DR Ensembl; ENSMUST00000001507; ENSMUSP00000001507; ENSMUSG00000001467. DR GeneID; 13121; -. DR KEGG; mmu:13121; -. DR UCSC; uc008wie.1; mouse. DR CTD; 13121; -. DR MGI; MGI:106040; Cyp51. DR eggNOG; COG2124; -. DR GeneTree; ENSGT00660000095370; -. DR HOGENOM; HOG000042780; -. DR InParanoid; Q9JIP8; -. DR KO; K05917; -. DR OMA; MIHTPHN; -. DR OrthoDB; EOG7PZRX3; -. DR TreeFam; TF105091; -. DR UniPathway; UPA00770; UER00754. DR NextBio; 283158; -. DR PRO; PR:Q8K0C4; -. DR ArrayExpress; Q8K0C4; -. DR Bgee; Q8K0C4; -. DR Genevestigator; Q8K0C4; -. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0020037; F:heme binding; ISS:UniProtKB. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0008398; F:sterol 14-demethylase activity; ISS:UniProtKB. DR GO; GO:0006695; P:cholesterol biosynthetic process; TAS:MGI. DR GO; GO:0033488; P:cholesterol biosynthetic process via 24,25-dihydrolanosterol; IEA:Ensembl. DR Gene3D; 1.10.630.10; -; 1. DR InterPro; IPR001128; Cyt_P450. DR InterPro; IPR017972; Cyt_P450_CS. DR InterPro; IPR002403; Cyt_P450_E_grp-IV. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00465; EP450IV. DR PRINTS; PR00385; P450. DR SUPFAM; SSF48264; SSF48264; 1. DR PROSITE; PS00086; CYTOCHROME_P450; 1. PE 2: Evidence at transcript level; KW Cholesterol biosynthesis; Cholesterol metabolism; Complete proteome; KW Endoplasmic reticulum; Heme; Iron; Lipid biosynthesis; KW Lipid metabolism; Membrane; Metal-binding; Microsome; Monooxygenase; KW NADP; Oxidoreductase; Reference proteome; Steroid biosynthesis; KW Steroid metabolism; Sterol biosynthesis; Sterol metabolism; KW Transmembrane; Transmembrane helix. FT CHAIN 1 503 Lanosterol 14-alpha demethylase. FT /FTId=PRO_0000376796. FT TRANSMEM 24 44 Helical; (Potential). FT METAL 449 449 Iron (heme axial ligand) (By similarity). FT CONFLICT 19 19 E -> A (in Ref. 1; AAF74562). FT CONFLICT 98 98 F -> L (in Ref. 1; AAF74562 and 2; FT AAF73986). FT CONFLICT 235 235 T -> A (in Ref. 3; BAC27231). SQ SEQUENCE 503 AA; 56776 MW; 6A4BBA350F1D85C7 CRC64; MVLLGLLQSG GWVLGQAMEQ VTGGNLLSTL LIACAFTLSL VYLFRLAVGH MVQLPAGAKS PPHIYSPIPF LGHAIAFGKS PIEFLENAYE KYGPVFSFTM VGKTFTYLLG SDAAALLFNS KNEDLNAEEV YGRLTTPVFG KGVAYDVPNA IFLEQKKIIK SGLNIAHFKQ YVPIIEKEAK EYFQSWGESG ERNVFEALSE LIILTASHCL HGKEIRSQLN EKVAQLYADL DGGFTHAAWL LPAWLPLPSF RRRDRAHREI KNIFYKAIQK RRLSKEPAED ILQTLLDSTY KDGRPLTDEE ISGMLIGLLL AGQHTSSTTS AWMGFFLAKD KPLQEKCYLE QKAVCGEDLP PLTYDQLKDL NLLDRCIKET LRLRPPIMTM MRMAKTPQTV AGYTIPPGHQ VCVSPTVNQR LKDSWAERLD FNPDRYLQDN PASGEKFAYV PFGAGRHRCV GENFAYVQIK TIWSTMLRLY EFDLINGYFP TVNYTTMIHT PENPVIRYKR RSK // ID CP7A1_MOUSE Reviewed; 503 AA. AC Q64505; Q8BFR7; DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 2. DT 19-MAR-2014, entry version 106. DE RecName: Full=Cholesterol 7-alpha-monooxygenase; DE EC=1.14.13.17; DE AltName: Full=CYPVII; DE AltName: Full=Cholesterol 7-alpha-hydroxylase; DE AltName: Full=Cytochrome P450 7A1; GN Name=Cyp7a1; Synonyms=Cyp7; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=8088795; DOI=10.1006/geno.1994.1250; RA Tzung K.W., Ishimura-Oka K., Kihara S., Oka K., Chan L.; RT "Structure of the mouse cholesterol 7 alpha-hydroxylase gene."; RL Genomics 21:244-247(1994). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Liver; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [4] RP FUNCTION, AND INDUCTION BY FASTING. RX PubMed=14522988; DOI=10.1074/jbc.M309736200; RA Shin D.J., Campos J.A., Gil G., Osborne T.F.; RT "PGC-1alpha activates CYP7A1 and bile acid biosynthesis."; RL J. Biol. Chem. 278:50047-50052(2003). RN [5] RP INDUCTION BY FASTING. RX PubMed=17636037; DOI=10.1210/me.2007-0196; RA Ponugoti B., Fang S., Kemper J.K.; RT "Functional interaction of hepatic nuclear factor-4 and peroxisome RT proliferator-activated receptor-gamma coactivator 1alpha in CYP7A1 RT regulation is inhibited by a key lipogenic activator, sterol RT regulatory element-binding protein-1c."; RL Mol. Endocrinol. 21:2698-2712(2007). CC -!- FUNCTION: Catalyzes a rate-limiting step in cholesterol catabolism CC and bile acid biosynthesis by introducing a hydrophilic moiety at CC position 7 of cholesterol. Important for cholesterol homeostasis. CC -!- CATALYTIC ACTIVITY: Cholesterol + NADPH + O(2) = 7-alpha- CC hydroxycholesterol + NADP(+) + H(2)O. CC -!- COFACTOR: Heme group (By similarity). CC -!- PATHWAY: Lipid metabolism; bile acid biosynthesis. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral CC membrane protein. Microsome membrane; Peripheral membrane protein. CC -!- INDUCTION: Up-regulated by fasting, returns to ground state upon CC feeding. Up-regulated by experimentally induced diabetes. Down- CC regulated by insulin treatment. CC -!- SIMILARITY: Belongs to the cytochrome P450 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L23754; AAA68867.1; -; Genomic_DNA. DR EMBL; AK050020; BAC34033.1; -; mRNA. DR EMBL; AK050210; BAC34123.1; -; mRNA. DR EMBL; AK050220; BAC34131.1; -; mRNA. DR EMBL; AK050260; BAC34150.1; -; mRNA. DR EMBL; AL772306; CAM27235.1; -; Genomic_DNA. DR PIR; A54779; A54779. DR RefSeq; NP_031850.2; NM_007824.2. DR RefSeq; XP_006537666.1; XM_006537603.1. DR UniGene; Mm.57029; -. DR ProteinModelPortal; Q64505; -. DR SMR; Q64505; 25-503. DR ChEMBL; CHEMBL2212; -. DR PhosphoSite; Q64505; -. DR PaxDb; Q64505; -. DR PRIDE; Q64505; -. DR Ensembl; ENSMUST00000029905; ENSMUSP00000029905; ENSMUSG00000028240. DR GeneID; 13122; -. DR KEGG; mmu:13122; -. DR UCSC; uc008rxk.1; mouse. DR CTD; 1581; -. DR MGI; MGI:106091; Cyp7a1. DR eggNOG; COG2124; -. DR GeneTree; ENSGT00550000074551; -. DR HOGENOM; HOG000231026; -. DR HOVERGEN; HBG051100; -. DR InParanoid; Q8BFR7; -. DR KO; K00489; -. DR OMA; FHYTTSA; -. DR OrthoDB; EOG7J9VP6; -. DR TreeFam; TF105090; -. DR UniPathway; UPA00221; -. DR NextBio; 283162; -. DR PRO; PR:Q64505; -. DR Bgee; Q64505; -. DR Genevestigator; Q64505; -. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISS:UniProtKB. DR GO; GO:0008123; F:cholesterol 7-alpha-monooxygenase activity; ISS:UniProtKB. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0006699; P:bile acid biosynthetic process; ISS:UniProtKB. DR GO; GO:0071397; P:cellular response to cholesterol; ISS:UniProtKB. DR GO; GO:0071333; P:cellular response to glucose stimulus; ISS:UniProtKB. DR GO; GO:0006707; P:cholesterol catabolic process; ISS:UniProtKB. DR GO; GO:0042632; P:cholesterol homeostasis; ISS:UniProtKB. DR GO; GO:0070859; P:positive regulation of bile acid biosynthetic process; TAS:BHF-UCL. DR Gene3D; 1.10.630.10; -; 1. DR InterPro; IPR001128; Cyt_P450. DR InterPro; IPR017972; Cyt_P450_CS. DR InterPro; IPR024204; Cyt_P450_CYP7A1-type. DR InterPro; IPR002403; Cyt_P450_E_grp-IV. DR Pfam; PF00067; p450; 1. DR PIRSF; PIRSF000047; Cytochrome_CYPVIIA1; 1. DR PRINTS; PR00465; EP450IV. DR SUPFAM; SSF48264; SSF48264; 1. DR PROSITE; PS00086; CYTOCHROME_P450; 1. PE 2: Evidence at transcript level; KW Cholesterol metabolism; Complete proteome; Endoplasmic reticulum; KW Heme; Iron; Lipid metabolism; Membrane; Metal-binding; Microsome; KW Monooxygenase; NADP; Oxidoreductase; Reference proteome; KW Steroid metabolism; Sterol metabolism. FT CHAIN 1 503 Cholesterol 7-alpha-monooxygenase. FT /FTId=PRO_0000051902. FT METAL 444 444 Iron (heme axial ligand) (By similarity). FT CONFLICT 197 197 S -> T (in Ref. 1; AAA68867). FT CONFLICT 228 228 F -> L (in Ref. 1; AAA68867). FT CONFLICT 318 318 A -> S (in Ref. 1; AAA68867). SQ SEQUENCE 503 AA; 57262 MW; F7F8BC2CDD2C43D1 CRC64; MMSISLIWGI AVVVSCCIWF IIGIRRRKVG EPPLDNGLIP YLGCALKFGS NPLEFLRAKQ RKHGHVFTCK LMGKYVHFIT NSLSYHKVLC HGKYFDWKKF HYTTSAKAFG HRSIDPSDGN TTENINKTFN KTLQGDALCS LSEAMMQNLQ SVMRPPGLPK SKSAVWVTEG MYAFCYRVMF EAGYLTLFGK DISKTDSQRA FIQNNLDSFK QFDQVFPALV AGVPIHLFKT AHKARERLAE SLKHKNLYMR DQVSELIRLR MFLNDTLSTF DDMEKAKTHL VILWASQANT IPATFWSLFQ MIRSPEAMKA ASEEVNGALQ SAGQELSSGG NAIYLDQEQL NNLPVLDSII KEALRLSSAS LNIRTAKEDF TLHLEDGSYN IRKDDIIALY PQLMHLDPEI YPDPLTFKYD RYLDESGKAK TTFYRNGNKL KYFYMPFGSG ATICPGRLFA VQEIKQFLIL MLSYFELELV ESHTKCPPLD QSRAGLGILP PLNDIEFKYK LKH // ID CP7B1_MOUSE Reviewed; 507 AA. AC Q60991; Q9CZ39; DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 2. DT 19-MAR-2014, entry version 108. DE RecName: Full=25-hydroxycholesterol 7-alpha-hydroxylase; DE EC=1.14.13.100; DE AltName: Full=Cytochrome P450 7B1; DE AltName: Full=Hippocampal transcript 1 protein; DE Short=HCT-1; DE AltName: Full=Oxysterol 7-alpha-hydroxylase; GN Name=Cyp7b1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Brain, and Liver; RX PubMed=8530364; DOI=10.1074/jbc.270.50.29739; RA Stapleton G., Steel M., Richardson M., Mason J.O., Rose K.A., RA Morris R.G., Lathe R.; RT "A novel cytochrome P450 expressed primarily in brain."; RL J. Biol. Chem. 270:29739-29745(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Embryo; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). CC -!- CATALYTIC ACTIVITY: Cholest-5-ene-3-beta,25-diol + NADPH + O(2) = CC cholest-5-ene-3-beta,7-alpha,25-triol + NADP(+) + H(2)O. CC -!- CATALYTIC ACTIVITY: Cholest-5-ene-3-beta,27-diol + NADPH + O(2) = CC cholest-5-ene-3-beta,7-alpha,27-triol + NADP(+) + H(2)O. CC -!- COFACTOR: Heme group (By similarity). CC -!- PATHWAY: Lipid metabolism; bile acid biosynthesis. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral CC membrane protein. Microsome membrane; Peripheral membrane protein. CC -!- TISSUE SPECIFICITY: Highly expressed in brain; also expressed in CC liver and kidney. CC -!- SIMILARITY: Belongs to the cytochrome P450 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U36993; AAA92615.1; -; mRNA. DR EMBL; AK013034; BAB28613.1; -; mRNA. DR RefSeq; NP_031851.3; NM_007825.4. DR RefSeq; XP_006535446.1; XM_006535383.1. DR UniGene; Mm.316000; -. DR ProteinModelPortal; Q60991; -. DR SMR; Q60991; 37-503. DR MINT; MINT-1864111; -. DR STRING; 10090.ENSMUSP00000037487; -. DR PhosphoSite; Q60991; -. DR PaxDb; Q60991; -. DR PRIDE; Q60991; -. DR Ensembl; ENSMUST00000035625; ENSMUSP00000037487; ENSMUSG00000039519. DR GeneID; 13123; -. DR KEGG; mmu:13123; -. DR UCSC; uc008orm.2; mouse. DR CTD; 9420; -. DR MGI; MGI:104978; Cyp7b1. DR eggNOG; COG2124; -. DR GeneTree; ENSGT00550000074551; -. DR HOGENOM; HOG000231026; -. DR HOVERGEN; HBG051100; -. DR InParanoid; Q9CZ39; -. DR KO; K07430; -. DR OMA; QYQLVIK; -. DR OrthoDB; EOG7J9VP6; -. DR TreeFam; TF105090; -. DR BRENDA; 1.14.13.100; 3474. DR UniPathway; UPA00221; -. DR NextBio; 283166; -. DR PRO; PR:Q60991; -. DR Bgee; Q60991; -. DR Genevestigator; Q60991; -. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; TAS:UniProtKB. DR GO; GO:0033783; F:25-hydroxycholesterol 7alpha-hydroxylase activity; IEA:UniProtKB-EC. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0008396; F:oxysterol 7-alpha-hydroxylase activity; IDA:UniProtKB. DR GO; GO:0006699; P:bile acid biosynthetic process; IDA:UniProtKB. DR GO; GO:0008203; P:cholesterol metabolic process; IEA:UniProtKB-KW. DR GO; GO:0007586; P:digestion; TAS:UniProtKB. DR GO; GO:0033147; P:negative regulation of intracellular estrogen receptor signaling pathway; IMP:MGI. DR GO; GO:0050679; P:positive regulation of epithelial cell proliferation; IMP:MGI. DR GO; GO:0060740; P:prostate gland epithelium morphogenesis; IMP:MGI. DR Gene3D; 1.10.630.10; -; 1. DR InterPro; IPR001128; Cyt_P450. DR InterPro; IPR024204; Cyt_P450_CYP7A1-type. DR InterPro; IPR002403; Cyt_P450_E_grp-IV. DR Pfam; PF00067; p450; 1. DR PIRSF; PIRSF000047; Cytochrome_CYPVIIA1; 1. DR PRINTS; PR00465; EP450IV. DR SUPFAM; SSF48264; SSF48264; 1. PE 2: Evidence at transcript level; KW Cholesterol metabolism; Complete proteome; Endoplasmic reticulum; KW Heme; Iron; Lipid metabolism; Membrane; Metal-binding; Microsome; KW Monooxygenase; NADP; Oxidoreductase; Reference proteome; KW Steroid metabolism; Sterol metabolism. FT CHAIN 1 507 25-hydroxycholesterol 7-alpha- FT hydroxylase. FT /FTId=PRO_0000051907. FT METAL 447 447 Iron (heme axial ligand) (By similarity). FT CONFLICT 265 265 R -> S (in Ref. 1; AAA92615). FT CONFLICT 278 278 P -> S (in Ref. 1; AAA92615). FT CONFLICT 432 432 K -> R (in Ref. 1; AAA92615). FT CONFLICT 463 463 M -> E (in Ref. 1; AAA92615). SQ SEQUENCE 507 AA; 58470 MW; 628A0D3270C04DA4 CRC64; MQGATTLDAA SPGPLALLGL LFAATLLLSA LFLLTRRTRR PREPPLIKGW LPYLGMALKF FKDPLTFLKT LQRQHGDTFT VFLVGKYITF VLNPFQYQYV TKNPKQLSFQ KFSSRLSAKA FSVKKLLTDD DLNEDVHRAY LLLQGKPLDA LLETMIQEVK ELFESQLLKI TDWNTERIFA FCGSLVFEIT FATLYGKILA GNKKQIISEL RDDFFKFDDM FPYLVSDIPI QLLRNEESMQ KKIIKCLTSE KVAQMQGQSK IVQERQDLLK RYYRHDDPEI GAHHLGFLWA SLANTIPAMF WAMYYILRHP EAMEALRDEI DSFLQSTGQK KGPGISVHFT REQLDSLVCL ESTILEVLRL CSYSSIIREV QEDMNLSLES KSFSLRKGDF VALFPPLIHN DPEIFDAPKE FRFDRFIEDG KKKSTFFKGG KKLKTYVMPF GLGTSKCPGR YFAVNEMKLL LIMLLTYFDL EIIDRKPIGL NHSRMFLGIQ HPDSAVSFRY KAKSWRS // ID CP8B1_MOUSE Reviewed; 500 AA. AC O88962; Q9R217; DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1998, sequence version 1. DT 19-FEB-2014, entry version 115. DE RecName: Full=7-alpha-hydroxycholest-4-en-3-one 12-alpha-hydroxylase; DE EC=1.14.13.95; DE AltName: Full=7-alpha-hydroxy-4-cholesten-3-one 12-alpha-hydroxylase; DE AltName: Full=CYPVIIIB1; DE AltName: Full=Cytochrome P450 8B1; DE AltName: Full=Sterol 12-alpha-hydroxylase; GN Name=Cyp8b1; Synonyms=Cyp12; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND VARIANT LYS-242. RC STRAIN=129/SvJ, and BALB/c; TISSUE=Liver; RX PubMed=10051404; DOI=10.1006/geno.1998.5606; RA Gaafvels M., Olin M., Chowdhary B.P., Raudsepp T., Andersson U., RA Persson B., Jansson M., Bjoerkhem I., Eggertsen G.; RT "Structure and chromosomal assignment of the sterol 12alpha- RT hydroxylase gene (CYP8B1) in human and mouse: eukaryotic cytochrome P- RT 450 gene devoid of introns."; RL Genomics 56:184-196(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Liver; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: Involved in bile acid synthesis and is responsible for CC the conversion of 7 alpha-hydroxy-4-cholesten-3-one into 7 alpha, CC 12 alpha-dihydroxy-4-cholesten-3-one. Responsible for the balance CC between formation of cholic acid and chenodeoxycholic acid. Has a CC rather broad substrate specificity including a number of 7-alpha- CC hydroxylated C27 steroids. CC -!- CATALYTIC ACTIVITY: 7-alpha-hydroxycholest-4-en-3-one + NADPH + CC O(2) = 7-alpha,12-alpha-dihydroxycholest-4-en-3-one + NADP(+) + CC H(2)O. CC -!- COFACTOR: Heme group (By similarity). CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass CC membrane protein. Microsome membrane; Single-pass membrane CC protein. CC -!- TISSUE SPECIFICITY: Expressed in liver. CC -!- SIMILARITY: Belongs to the cytochrome P450 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF090317; AAC63036.1; -; mRNA. DR EMBL; AF090319; AAD19876.1; -; Genomic_DNA. DR EMBL; BC010973; AAH10973.1; -; mRNA. DR EMBL; BC010974; AAH10974.1; -; mRNA. DR EMBL; BC049969; AAH49969.1; -; mRNA. DR RefSeq; NP_034142.3; NM_010012.3. DR UniGene; Mm.20889; -. DR ProteinModelPortal; O88962; -. DR SMR; O88962; 25-498. DR MINT; MINT-1865660; -. DR STRING; 10090.ENSMUSP00000052989; -. DR PhosphoSite; O88962; -. DR PaxDb; O88962; -. DR PRIDE; O88962; -. DR Ensembl; ENSMUST00000062474; ENSMUSP00000052989; ENSMUSG00000050445. DR GeneID; 13124; -. DR KEGG; mmu:13124; -. DR UCSC; uc009sef.2; mouse. DR CTD; 1582; -. DR MGI; MGI:1338044; Cyp8b1. DR eggNOG; COG2124; -. DR GeneTree; ENSGT00550000074551; -. DR HOGENOM; HOG000231026; -. DR HOVERGEN; HBG051100; -. DR InParanoid; O88962; -. DR KO; K07431; -. DR OrthoDB; EOG7J9VP6; -. DR TreeFam; TF105090; -. DR NextBio; 283170; -. DR PRO; PR:O88962; -. DR Bgee; O88962; -. DR Genevestigator; O88962; -. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0033778; F:7alpha-hydroxycholest-4-en-3-one 12alpha-hydroxylase activity; IEA:UniProtKB-EC. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0008397; F:sterol 12-alpha-hydroxylase activity; IEA:Ensembl. DR Gene3D; 1.10.630.10; -; 1. DR InterPro; IPR001128; Cyt_P450. DR InterPro; IPR024204; Cyt_P450_CYP7A1-type. DR InterPro; IPR002403; Cyt_P450_E_grp-IV. DR Pfam; PF00067; p450; 1. DR PIRSF; PIRSF000047; Cytochrome_CYPVIIA1; 1. DR PRINTS; PR00465; EP450IV. DR SUPFAM; SSF48264; SSF48264; 1. PE 2: Evidence at transcript level; KW Complete proteome; Endoplasmic reticulum; Heme; Iron; Membrane; KW Metal-binding; Microsome; Monooxygenase; NADP; Oxidoreductase; KW Polymorphism; Reference proteome; Transmembrane; Transmembrane helix. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 500 7-alpha-hydroxycholest-4-en-3-one 12- FT alpha-hydroxylase. FT /FTId=PRO_0000051914. FT TRANSMEM 4 24 Helical; (Potential). FT METAL 439 439 Iron (heme axial ligand) (By similarity). FT VARIANT 242 242 E -> K (in strain: 129/SvJ). SQ SEQUENCE 500 AA; 57706 MW; D6902755B4AD141A CRC64; MTLWCTVLGA LLTVVGCLCL SLLLRHRRPW EPPLDKGFVP WLGHSMAFRK NMFEFLKGMR AKHGDVFTVQ LGGQYFTFVM DPLSFGPIIK NTEKALDFQS YAKELVLKVF GYQSVDGDHR MIHLASTKHL MGQGLEELNQ AMLDSLSLVM LGPKGSSLGA SSWCEDGLFH FCYRILFKAG FLSLFGYTKD KQQDLDEADE LFRKFRRFDF LFPRFVYSLL GPREWVEVSQ LQRLFHQRLS VEQNLEKDGI SCWLGYMLQF LREQGIASSM QDKFNFMMLW ASQGNTGPTC FWVLLFLLKH QDAMKAVREE ATRVMGKARL EAKKSFTFTP SALKHTPVLD SVMEESLRLC ATPTLLRVVQ EDYVLKMASG QEYQIRRGDK VALFPYLSVH MDPDIHPEPT AFKYDRFLNP DGTRKVDFYK SGKKIHHYSM PWGSGVSKCP GRFFALSEMK TFVLLMIMYF DFKLVDPDIP VPPIDPRRWG FGTSQPSHEV RFLYRLKPVQ // ID CRYL1_MOUSE Reviewed; 319 AA. AC Q99KP3; Q542R9; Q8R4W7; DT 24-OCT-2001, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 19-FEB-2014, entry version 102. DE RecName: Full=Lambda-crystallin homolog; DE EC=1.1.1.45; DE AltName: Full=L-gulonate 3-dehydrogenase; DE Short=Gul3DH; GN Name=Cryl1; Synonyms=Cry; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY. RX PubMed=12527201; DOI=10.1016/S0378-1119(02)01095-8; RA Chen J., Yu L., Li D., Gao Q., Wang J., Huang X., Bi G., Wu H., RA Zhao S.; RT "Human CRYL1, a novel enzyme-crystallin overexpressed in liver and RT kidney and downregulated in 58% of liver cancer tissues from 60 RT Chinese patients, and four new homologs from other mammalians."; RL Gene 302:103-113(2003). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Brain cortex; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Mammary gland; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- CATALYTIC ACTIVITY: L-gulonate + NAD(+) = 3-dehydro-L-gulonate + CC NADH. CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- TISSUE SPECIFICITY: Widely expressed, with highest levels in CC liver. Undetectable in skeletal muscle. CC -!- SIMILARITY: Belongs to the 3-hydroxyacyl-CoA dehydrogenase family. CC -!- SEQUENCE CAUTION: CC Sequence=AAM13398.1; Type=Frameshift; Positions=227; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF351609; AAM13398.1; ALT_FRAME; mRNA. DR EMBL; AK043569; BAC31583.1; -; mRNA. DR EMBL; AK080625; BAC37964.1; -; mRNA. DR EMBL; AK135834; BAE22682.1; -; mRNA. DR EMBL; BC004074; AAH04074.1; -; mRNA. DR EMBL; BC027064; AAH27064.1; -; mRNA. DR RefSeq; NP_084280.2; NM_030004.3. DR UniGene; Mm.25539; -. DR ProteinModelPortal; Q99KP3; -. DR SMR; Q99KP3; 7-316. DR IntAct; Q99KP3; 2. DR MINT; MINT-4092037; -. DR PhosphoSite; Q99KP3; -. DR REPRODUCTION-2DPAGE; Q99KP3; -. DR PaxDb; Q99KP3; -. DR PRIDE; Q99KP3; -. DR Ensembl; ENSMUST00000022517; ENSMUSP00000022517; ENSMUSG00000021947. DR GeneID; 68631; -. DR KEGG; mmu:68631; -. DR UCSC; uc007ucz.1; mouse. DR CTD; 51084; -. DR MGI; MGI:1915881; Cryl1. DR eggNOG; COG1250; -. DR GeneTree; ENSGT00390000007182; -. DR HOGENOM; HOG000141499; -. DR HOVERGEN; HBG051126; -. DR InParanoid; Q99KP3; -. DR KO; K13247; -. DR OMA; SWAMVFA; -. DR OrthoDB; EOG7XPZ65; -. DR TreeFam; TF313501; -. DR NextBio; 327590; -. DR PRO; PR:Q99KP3; -. DR ArrayExpress; Q99KP3; -. DR Bgee; Q99KP3; -. DR CleanEx; MM_CRYL1; -. DR Genevestigator; Q99KP3; -. DR GO; GO:0005829; C:cytosol; ISS:UniProtKB. DR GO; GO:0003857; F:3-hydroxyacyl-CoA dehydrogenase activity; IEA:InterPro. DR GO; GO:0050104; F:L-gulonate 3-dehydrogenase activity; ISS:UniProtKB. DR GO; GO:0070403; F:NAD+ binding; ISS:UniProtKB. DR GO; GO:0006631; P:fatty acid metabolic process; IEA:InterPro. DR Gene3D; 1.10.1040.10; -; 1. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR022694; 3-OHacyl-CoA_DH. DR InterPro; IPR006180; 3-OHacyl-CoA_DH_CS. DR InterPro; IPR006176; 3-OHacyl-CoA_DH_NAD-bd. DR InterPro; IPR006108; 3HC_DH_C. DR InterPro; IPR008927; 6-PGluconate_DH_C-like. DR InterPro; IPR013328; DH_multihelical. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Pfam; PF00725; 3HCDH; 1. DR Pfam; PF02737; 3HCDH_N; 1. DR PIRSF; PIRSF000105; HCDH; 1. DR SUPFAM; SSF48179; SSF48179; 1. DR PROSITE; PS00067; 3HCDH; 1. PE 2: Evidence at transcript level; KW Complete proteome; Cytoplasm; NAD; Oxidoreductase; Reference proteome. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 319 Lambda-crystallin homolog. FT /FTId=PRO_0000109321. FT NP_BIND 16 17 NAD (By similarity). FT BINDING 36 36 NAD (By similarity). FT BINDING 97 97 NAD (By similarity). FT BINDING 102 102 NAD (By similarity). SQ SEQUENCE 319 AA; 35209 MW; 590EC278F5C83A9D CRC64; MASPAAGGVV IVGSGLIGRS WAMLFASGGF KVKLYDIEQQ QITDALENIR KEMKSLEQSG SLKGSLSAER QLSLISGCGN LAEAVEGAVH IQECVPENLE LKKKIFAQLD RIVDDRVILS SSSSCLLPSK LFSGLAHVKQ CIVAHPVNPP YYVPLVELVP HPETAPATMD RTYALMKKIG QSPVRVLKEI DGFVLNRLQY AVISEAWRLV EEEIVSPSDL DLVMSDGLGM RYAFIGPLET MHLNAEGVIS YCERYSEGMK HVLSTFGPVP EFSGATVERV SEDMCMKVPD DPEHLAARRQ WRDDCLMKLS ILKYQMQPK // ID CRYM_MOUSE Reviewed; 313 AA. AC O54983; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1998, sequence version 1. DT 19-FEB-2014, entry version 86. DE RecName: Full=Ketimine reductase mu-crystallin; DE EC=1.5.1.25; DE AltName: Full=NADP-regulated thyroid-hormone-binding protein; GN Name=Crym; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=FVB/N; TISSUE=Brain; RA Sperbeck S.J., Segovia L., Wistow G.J.; RL Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6; TISSUE=Retina; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP PROTEIN SEQUENCE OF 4-18; 37-47; 119-128 AND 176-185, AND MASS RP SPECTROMETRY. RC STRAIN=C57BL/6; TISSUE=Brain; RA Lubec G., Kang S.U.; RL Submitted (APR-2007) to UniProtKB. CC -!- FUNCTION: Specifically catalyzes the reduction of imine bonds in CC brain substrates that may include cystathionine ketimine (CysK) CC and lanthionine ketimine (LK). Binds thyroid hormone which is a CC strong reversible inhibitor. Presumably involved in the regulation CC of the free intracellular concentration of triiodothyronine and CC access to its nuclear receptors (By similarity). CC -!- CATALYTIC ACTIVITY: Thiomorpholine 3-carboxylate + NAD(P)(+) = CC 3,4-dehydro-thiomorpholine-3-carboxylate + NAD(P)H. CC -!- COFACTOR: NAD or NADP (By similarity). CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the ornithine cyclodeaminase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF039391; AAB94770.1; -; mRNA. DR EMBL; BC045159; AAH45159.1; -; mRNA. DR RefSeq; NP_057878.1; NM_016669.1. DR UniGene; Mm.9114; -. DR ProteinModelPortal; O54983; -. DR SMR; O54983; 3-312. DR IntAct; O54983; 3. DR MINT; MINT-4092055; -. DR STRING; 10090.ENSMUSP00000033198; -. DR PhosphoSite; O54983; -. DR PaxDb; O54983; -. DR PRIDE; O54983; -. DR Ensembl; ENSMUST00000033198; ENSMUSP00000033198; ENSMUSG00000030905. DR GeneID; 12971; -. DR KEGG; mmu:12971; -. DR UCSC; uc009jmk.1; mouse. DR CTD; 1428; -. DR MGI; MGI:102675; Crym. DR eggNOG; COG2423; -. DR HOGENOM; HOG000137263; -. DR HOVERGEN; HBG005408; -. DR InParanoid; O54983; -. DR OMA; KHRGYLG; -. DR OrthoDB; EOG7S7SFB; -. DR TreeFam; TF105309; -. DR ChiTaRS; CRYM; mouse. DR NextBio; 282732; -. DR PRO; PR:O54983; -. DR ArrayExpress; O54983; -. DR Bgee; O54983; -. DR CleanEx; MM_CRYM; -. DR Genevestigator; O54983; -. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR GO; GO:0005634; C:nucleus; IDA:MGI. DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl. DR GO; GO:0042562; F:hormone binding; IMP:MGI. DR GO; GO:0050661; F:NADP binding; IEA:Ensembl. DR GO; GO:0047127; F:thiomorpholine-carboxylate dehydrogenase activity; IEA:UniProtKB-EC. DR GO; GO:0070324; F:thyroid hormone binding; IEA:Ensembl. DR GO; GO:0003714; F:transcription corepressor activity; IEA:Ensembl. DR GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IEA:Ensembl. DR GO; GO:0007605; P:sensory perception of sound; IEA:Ensembl. DR GO; GO:0042403; P:thyroid hormone metabolic process; IMP:MGI. DR GO; GO:0070327; P:thyroid hormone transport; IEA:Ensembl. DR Gene3D; 3.30.1780.10; -; 1. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR003462; ODC_Mu_crystall. DR InterPro; IPR023401; ODC_N. DR Pfam; PF02423; OCD_Mu_crystall; 1. DR PIRSF; PIRSF001439; CryM; 1. PE 1: Evidence at protein level; KW Complete proteome; Cytoplasm; Direct protein sequencing; NAD; NADP; KW Oxidoreductase; Reference proteome. FT CHAIN 1 313 Ketimine reductase mu-crystallin. FT /FTId=PRO_0000200679. FT NP_BIND 142 147 NADP (By similarity). FT BINDING 167 167 NADP (By similarity). FT BINDING 168 168 NADP (By similarity). SQ SEQUENCE 313 AA; 33523 MW; 0898EDA9E2D34C83 CRC64; MKRAPAFLSA EEVQDHLRSS SLLIPPLEAA LANFSKGPDG GVMQPVRTVV PVAKHRGFLG VMPAYSAAED ALTTKLVTFY EGHSNTAVPS HQASVLLFDP SNGSLLAVMD GNVITAKRTA AVSAIATKLL KPPGSDVLCI LGAGVQAYSH YEIFTEQFSF KEVRMWNRTR ENAEKFASTV QGDVRVCSSV QEAVTGADVI ITVTMATEPI LFGEWVKPGA HINAVGASRP DWRELDDELM RQAVLYVDSR EAALKESGDV LLSGADIFAE LGEVISGAKP AHCEKTTVFK SLGMAVEDLV AAKLVYDSWS SGK // ID CTBP1_MOUSE Reviewed; 441 AA. AC O88712; Q3TAT1; Q3TDL5; Q3TUM5; Q91WI6; Q91YX3; Q9QYG2; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2007, sequence version 2. DT 19-MAR-2014, entry version 128. DE RecName: Full=C-terminal-binding protein 1; DE Short=CtBP1; DE EC=1.1.1.-; GN Name=Ctbp1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND SUBCELLULAR RP LOCATION. RX PubMed=10369679; DOI=10.1093/emboj/18.12.3392; RA Criqui-Filipe P., Ducret C., Maira S.-M., Wasylyk B.; RT "Net, a negative Ras-switchable TCF, contains a second inhibition RT domain, the CID, that mediates repression through interactions with RT CtBP and de-acetylation."; RL EMBO J. 18:3392-3403(1999). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, RP AND DEVELOPMENTAL STAGE. RC STRAIN=ICR; RX PubMed=10567582; RA Furusawa T., Moribe H., Kondoh H., Higashi Y.; RT "Identification of CtBP1 and CtBP2 as corepressors of zinc finger- RT homeodomain factor deltaEF1."; RL Mol. Cell. Biol. 19:8581-8590(1999). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3). RC STRAIN=C57BL/6J, and NOD; TISSUE=Spleen; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC STRAIN=129, FVB/N, and FVB/N-3; RC TISSUE=Mammary tumor, and Salivary gland; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP PROTEIN SEQUENCE OF 98-108 AND 286-305, AND MASS SPECTROMETRY. RC STRAIN=C57BL/6; TISSUE=Brain, and Hippocampus; RA Lubec G., Klug S., Kang S.U.; RL Submitted (APR-2007) to UniProtKB. RN [6] RP INTERACTION WITH HDAC4; HDAC5 AND HDAC9. RX PubMed=11022042; DOI=10.1074/jbc.M007364200; RA Zhang C.L., McKinsey T.A., Lu J.R., Olson E.N.; RT "Association of COOH-terminal-binding protein (CtBP) and MEF2- RT interacting transcription repressor (MITR) contributes to RT transcriptional repression of the MEF2 transcription factor."; RL J. Biol. Chem. 276:35-39(2001). RN [7] RP INTERACTION WITH HIPK2. RX PubMed=14567915; DOI=10.1016/S0092-8674(03)00802-X; RA Zhang Q., Yoshimatsu Y., Hildebrand J., Frisch S.M., Goodman R.H.; RT "Homeodomain interacting protein kinase 2 promotes apoptosis by RT downregulating the transcriptional corepressor CtBP."; RL Cell 115:177-186(2003). RN [8] RP INTERACTION WITH NRIP1. RX PubMed=14736873; DOI=10.1074/jbc.M313906200; RA Christian M., Tullet J.M.A., Parker M.G.; RT "Characterization of four autonomous repression domains in the RT corepressor receptor interacting protein 140."; RL J. Biol. Chem. 279:15645-15651(2004). RN [9] RP INTERACTION WITH FOXP1 AND FOXP2. RX PubMed=14701752; DOI=10.1128/MCB.24.2.809-822.2004; RA Li S., Weidenfeld J., Morrisey E.E.; RT "Transcriptional and DNA binding activity of the Foxp1/2/4 family is RT modulated by heterotypic and homotypic protein interactions."; RL Mol. Cell. Biol. 24:809-822(2004). RN [10] RP INTERACTION WITH GLIS2, FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=16326862; DOI=10.1093/nar/gki985; RA Kim S.-C., Kim Y.-S., Jetten A.M.; RT "Kruppel-like zinc finger protein Gli-similar 2 (Glis2) represses RT transcription through interaction with C-terminal binding protein 1 RT (CtBP1)."; RL Nucleic Acids Res. 33:6805-6815(2005). RN [11] RP INTERACTION WITH WIZ. RX PubMed=16702210; DOI=10.1074/jbc.M603087200; RA Ueda J., Tachibana M., Ikura T., Shinkai Y.; RT "Zinc finger protein Wiz links G9a/GLP histone methyltransferases to RT the co-repressor molecule CtBP."; RL J. Biol. Chem. 281:20120-20128(2006). RN [12] RP FUNCTION, INTERACTION WITH PRDM16, AND SUBCELLULAR LOCATION. RX PubMed=18483224; DOI=10.1101/gad.1666108; RA Kajimura S., Seale P., Tomaru T., Erdjument-Bromage H., Cooper M.P., RA Ruas J.L., Chin S., Tempst P., Lazar M.A., Spiegelman B.M.; RT "Regulation of the brown and white fat gene programs through a RT PRDM16/CtBP transcriptional complex."; RL Genes Dev. 22:1397-1409(2008). RN [13] RP FUNCTION, AND INTERACTION WITH SATB1. RX PubMed=19103759; DOI=10.1128/MCB.00822-08; RA Purbey P.K., Singh S., Notani D., Kumar P.P., Limaye A.S., Galande S.; RT "Acetylation-dependent interaction of SATB1 and CtBP1 mediates RT transcriptional repression by SATB1."; RL Mol. Cell. Biol. 29:1321-1337(2009). CC -!- FUNCTION: Corepressor targeting diverse transcription regulators CC such as GLIS2 or BCL6. Has dehydrogenase activity. Involved in CC controlling the equilibrium between tubular and stacked structures CC in the Golgi complex. Functions in brown adipose tissue (BAT) CC differentiation. CC -!- COFACTOR: NAD. Cofactor binding induces a conformation change (By CC similarity). CC -!- SUBUNIT: Homo- or heterodimer. Heterodimer with CTBP2. Interacts CC with ELK3 (via its PXDLS motif). Interacts with RBBP8 (via its CC PXDLS motif). Interacts with PNN, MECOM, ZNF366 and ZFHX1B. CC Interaction with SATB1 (non-acetylated form); the interaction CC stabilizes its attachment to DNA and promotes transcription CC repression. Interacts with PRDM16; the interaction represses white CC adipose tissue (WAT)-specific genes expression. Interacts with CC GLIS2, HIPK2, FOXP1, FOXP2, HDAC4, HDAC5, HDAC9, NRIP1, WIZ and CC ZNF217. Interacts with BCL6; the interaction is required for BCL6 CC transcriptional autoinhibition and inhibition of some BCL6 target CC genes. CC -!- INTERACTION: CC Q14526:HIC1 (xeno); NbExp=10; IntAct=EBI-604547, EBI-2507362; CC Q64318:Zeb1; NbExp=4; IntAct=EBI-604547, EBI-8560245; CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=O88712-1; Sequence=Displayed; CC Name=2; CC IsoId=O88712-2; Sequence=VSP_024738; CC Name=3; CC IsoId=O88712-3; Sequence=VSP_024737; CC Note=No experimental confirmation available; CC -!- TISSUE SPECIFICITY: Expressed in a wide range of adult tissues. CC -!- DEVELOPMENTAL STAGE: Expressed throughout the developmental CC stages. CC -!- PTM: ADP-ribosylated; when cells are exposed to brefeldin A (By CC similarity). CC -!- PTM: The level of phosphorylation appears to be regulated during CC the cell cycle. Phosphorylation by HIPK2 on Ser-423 induces CC proteasomal degradation (By similarity). CC -!- PTM: Sumoylation on Lys-429 is promoted by the E3 SUMO-protein CC ligase CBX4 (By similarity). CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid CC dehydrogenase family. CC -!- SEQUENCE CAUTION: CC Sequence=BAE41586.1; Type=Erroneous initiation; Note=Translation N-terminally extended; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJ010483; CAA09219.1; -; mRNA. DR EMBL; AB033122; BAA85180.1; -; mRNA. DR EMBL; AK133816; BAE21859.1; -; mRNA. DR EMBL; AK160658; BAE35946.1; -; mRNA. DR EMBL; AK165276; BAE38115.1; -; mRNA. DR EMBL; AK170133; BAE41586.1; ALT_INIT; mRNA. DR EMBL; AK171650; BAE42587.1; -; mRNA. DR EMBL; BC013702; AAH13702.1; -; mRNA. DR EMBL; BC015071; AAH15071.1; -; mRNA. DR EMBL; BC042425; AAH42425.1; -; mRNA. DR RefSeq; NP_001185788.1; NM_001198859.1. DR RefSeq; NP_001185789.1; NM_001198860.1. DR RefSeq; NP_001185790.1; NM_001198861.1. DR RefSeq; NP_038530.1; NM_013502.3. DR RefSeq; XP_006503773.1; XM_006503710.1. DR UniGene; Mm.7286; -. DR ProteinModelPortal; O88712; -. DR SMR; O88712; 26-356. DR BioGrid; 198961; 13. DR DIP; DIP-33907N; -. DR IntAct; O88712; 10. DR MINT; MINT-146962; -. DR PhosphoSite; O88712; -. DR PaxDb; O88712; -. DR PRIDE; O88712; -. DR Ensembl; ENSMUST00000079746; ENSMUSP00000078682; ENSMUSG00000037373. [O88712-1] DR GeneID; 13016; -. DR KEGG; mmu:13016; -. DR UCSC; uc008xaj.2; mouse. [O88712-1] DR UCSC; uc008xak.2; mouse. [O88712-2] DR CTD; 1487; -. DR MGI; MGI:1201685; Ctbp1. DR eggNOG; COG0111; -. DR GeneTree; ENSGT00530000063021; -. DR HOVERGEN; HBG001898; -. DR InParanoid; O88712; -. DR KO; K04496; -. DR OMA; DRDHPSD; -. DR OrthoDB; EOG761BT9; -. DR TreeFam; TF313593; -. DR ChiTaRS; CTBP1; mouse. DR NextBio; 282870; -. DR PRO; PR:O88712; -. DR Bgee; O88712; -. DR CleanEx; MM_CTBP1; -. DR Genevestigator; O88712; -. DR GO; GO:0005829; C:cytosol; IEA:Ensembl. DR GO; GO:0005667; C:transcription factor complex; IDA:MGI. DR GO; GO:0017053; C:transcriptional repressor complex; IDA:UniProtKB. DR GO; GO:0051287; F:NAD binding; ISS:UniProtKB. DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro. DR GO; GO:0001106; F:RNA polymerase II transcription corepressor activity; IEA:Ensembl. DR GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; IDA:MGI. DR GO; GO:0007030; P:Golgi organization; IEA:Ensembl. DR GO; GO:0090241; P:negative regulation of histone H4 acetylation; IEA:Ensembl. DR GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IMP:MGI. DR GO; GO:0031065; P:positive regulation of histone deacetylation; IEA:Ensembl. DR GO; GO:0051726; P:regulation of cell cycle; IEA:Ensembl. DR GO; GO:0034401; P:regulation of transcription by chromatin organization; IEA:Ensembl. DR GO; GO:0006366; P:transcription from RNA polymerase II promoter; IEA:GOC. DR GO; GO:0050872; P:white fat cell differentiation; IDA:UniProtKB. DR Gene3D; 3.40.50.720; -; 2. DR InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom. DR InterPro; IPR006140; D-isomer_2_OHA_DH_NAD-bd. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Pfam; PF00389; 2-Hacid_dh; 1. DR Pfam; PF02826; 2-Hacid_dh_C; 1. DR PROSITE; PS00065; D_2_HYDROXYACID_DH_1; 1. DR PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1. PE 1: Evidence at protein level; KW ADP-ribosylation; Alternative splicing; Complete proteome; Cytoplasm; KW Differentiation; Direct protein sequencing; Isopeptide bond; NAD; KW Nucleus; Oxidoreductase; Phosphoprotein; Reference proteome; KW Repressor; Transcription; Transcription regulation; Ubl conjugation. FT CHAIN 1 441 C-terminal-binding protein 1. FT /FTId=PRO_0000076042. FT NP_BIND 180 185 NAD (By similarity). FT NP_BIND 237 243 NAD (By similarity). FT NP_BIND 264 266 NAD (By similarity). FT NP_BIND 315 318 NAD (By similarity). FT REGION 1 70 Interaction with GLIS2 1. FT REGION 288 360 Interaction with GLIS2 2. FT ACT_SITE 266 266 By similarity. FT ACT_SITE 295 295 By similarity. FT ACT_SITE 315 315 Proton donor (By similarity). FT BINDING 100 100 NAD (By similarity). FT BINDING 204 204 NAD (By similarity). FT BINDING 290 290 NAD (By similarity). FT MOD_RES 300 300 Phosphoserine (By similarity). FT MOD_RES 423 423 Phosphoserine (By similarity). FT CROSSLNK 429 429 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO) (By FT similarity). FT VAR_SEQ 1 74 Missing (in isoform 3). FT /FTId=VSP_024737. FT VAR_SEQ 1 13 MGSSHLLNKGLPL -> MS (in isoform 2). FT /FTId=VSP_024738. FT CONFLICT 55 55 D -> G (in Ref. 3; BAE41586/BAE42587). FT CONFLICT 108 108 K -> R (in Ref. 3; BAE35946). FT CONFLICT 380 380 Missing (in Ref. 1; CAA09219 and 3; FT BAE35946). SQ SEQUENCE 441 AA; 47745 MW; 2105CC8D69D915F4 CRC64; MGSSHLLNKG LPLGVRPPIM NGPMHPRPLV ALLDGRDCTV EMPILKDVAT VAFCDAQSTQ EIHEKVLNEA VGALMYHTIT LTREDLEKFK ALRIIVRIGS GFDNIDIKSA GDLGIAVCNV PAASVEETAD STLCHILNLY RRTTWLHQAL REGTRVQSVE QIREVASGAA RIRGETLGII GLGRVGQAVA LRAKAFGFNV LFYDPYLSDG IERALGLQRV STLQDLLFHS DCVTLHCGLN EHNHHLINDF TVKQMRQGAF LVNTARGGLV DEKALAQALK EGRIRGAALD VHESEPFSFS QGPLKDAPNL ICTPHAAWYS EQASIEMREE AAREIRRAIT GRIPDSLKNC VNKDHLTAAT HWASMDPAVV HPELNGAAYS RYPPGVVSVA PTGIPAAVEG IVPSAMSLSH GLPPVAHPPH APSPGQTVKP EADRDHTSDQ L // ID CY24B_MOUSE Reviewed; 570 AA. AC Q61093; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 19-MAR-2014, entry version 109. DE RecName: Full=Cytochrome b-245 heavy chain; DE EC=1.-.-.-; DE AltName: Full=CGD91-phox; DE AltName: Full=Cytochrome b(558) subunit beta; DE Short=Cytochrome b558 subunit beta; DE AltName: Full=Heme-binding membrane glycoprotein gp91phox; DE AltName: Full=Neutrophil cytochrome b 91 kDa polypeptide; DE AltName: Full=gp91-1; DE AltName: Full=gp91-phox; DE AltName: Full=p22 phagocyte B-cytochrome; GN Name=Cybb; Synonyms=Cgd; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=8634451; RA Bjorgvinsdottir H., Zhen L., Dinauer M.C.; RT "Cloning of murine gp91phox cDNA and functional expression in a human RT X-linked chronic granulomatous disease cell line."; RL Blood 87:2005-2010(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=NMRI; TISSUE=Mammary gland; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: Critical component of the membrane-bound oxidase of CC phagocytes that generates superoxide. It is the terminal component CC of a respiratory chain that transfers single electrons from CC cytoplasmic NADPH across the plasma membrane to molecular oxygen CC on the exterior. Also functions as a voltage-gated proton channel CC that mediates the H(+) currents of resting phagocytes. CC -!- COFACTOR: FAD (Probable). CC -!- SUBUNIT: Composed of a heavy chain (beta) and a light chain CC (alpha). Component of an NADPH oxidase complex composed of a CC heterodimer formed by the membrane proteins CYBA and CYBB and the CC cytosolic subunits NCF1, NCF2 and NCF4. Interacts with NCF1. CC Interacts with calprotectin (S100A8/9) (By similarity). CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. CC -!- PTM: Glycosylated. CC -!- PTM: Phosphorylated on Ser and Thr residues (By similarity). CC -!- SIMILARITY: Contains 1 FAD-binding FR-type domain. CC -!- SIMILARITY: Contains 1 ferric oxidoreductase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U43384; AAB05997.1; -; mRNA. DR EMBL; BC071229; AAH71229.1; -; mRNA. DR RefSeq; NP_031833.3; NM_007807.5. DR RefSeq; XP_006527628.1; XM_006527565.1. DR UniGene; Mm.200362; -. DR ProteinModelPortal; Q61093; -. DR SMR; Q61093; 385-570. DR IntAct; Q61093; 3. DR PeroxiBase; 5957; MmNOx02. DR PhosphoSite; Q61093; -. DR PaxDb; Q61093; -. DR PRIDE; Q61093; -. DR Ensembl; ENSMUST00000015484; ENSMUSP00000015484; ENSMUSG00000015340. DR GeneID; 13058; -. DR KEGG; mmu:13058; -. DR UCSC; uc009spv.2; mouse. DR CTD; 1536; -. DR MGI; MGI:88574; Cybb. DR eggNOG; NOG287712; -. DR GeneTree; ENSGT00550000074350; -. DR HOGENOM; HOG000216669; -. DR HOVERGEN; HBG003760; -. DR InParanoid; Q61093; -. DR KO; K08008; -. DR OMA; ERNNANF; -. DR OrthoDB; EOG71P299; -. DR TreeFam; TF105354; -. DR ChiTaRS; CYBB; mouse. DR NextBio; 282986; -. DR PRO; PR:Q61093; -. DR ArrayExpress; Q61093; -. DR Bgee; Q61093; -. DR CleanEx; MM_CYBB; -. DR Genevestigator; Q61093; -. DR GO; GO:0030425; C:dendrite; IEA:Ensembl. DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR GO; GO:0043020; C:NADPH oxidase complex; IEA:Ensembl. DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl. DR GO; GO:0005886; C:plasma membrane; IDA:MGI. DR GO; GO:0005791; C:rough endoplasmic reticulum; IEA:Ensembl. DR GO; GO:0009055; F:electron carrier activity; IEA:Ensembl. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:Ensembl. DR GO; GO:0020037; F:heme binding; IEA:Ensembl. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW. DR GO; GO:0005244; F:voltage-gated ion channel activity; IEA:UniProtKB-KW. DR GO; GO:0050665; P:hydrogen peroxide biosynthetic process; IMP:MGI. DR GO; GO:0034220; P:ion transmembrane transport; IEA:GOC. DR GO; GO:0042493; P:response to drug; IEA:Ensembl. DR GO; GO:0007584; P:response to nutrient; IEA:Ensembl. DR GO; GO:0042554; P:superoxide anion generation; IEA:Ensembl. DR InterPro; IPR000778; Cyt_b245_heavy_chain. DR InterPro; IPR013112; FAD-bd_8. DR InterPro; IPR017927; Fd_Rdtase_FAD-bd. DR InterPro; IPR013130; Fe3_Rdtase_TM_dom. DR InterPro; IPR013121; Fe_red_NAD-bd_6. DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl. DR Pfam; PF08022; FAD_binding_8; 1. DR Pfam; PF01794; Ferric_reduct; 1. DR Pfam; PF08030; NAD_binding_6; 1. DR PRINTS; PR00466; GP91PHOX. DR SUPFAM; SSF63380; SSF63380; 1. DR PROSITE; PS51384; FAD_FR; 1. PE 2: Evidence at transcript level; KW Cell membrane; Complete proteome; Electron transport; FAD; KW Flavoprotein; Glycoprotein; Heme; Ion channel; Ion transport; Iron; KW Membrane; Metal-binding; NADP; Oxidoreductase; Phosphoprotein; KW Reference proteome; Transmembrane; Transmembrane helix; Transport; KW Voltage-gated channel. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 570 Cytochrome b-245 heavy chain. FT /FTId=PRO_0000210146. FT TOPO_DOM 2 8 Cytoplasmic (Potential). FT TRANSMEM 9 29 Helical; (Potential). FT TOPO_DOM 30 48 Extracellular (Potential). FT TRANSMEM 49 69 Helical; (Potential). FT TOPO_DOM 70 102 Cytoplasmic (Potential). FT TRANSMEM 103 123 Helical; (Potential). FT TOPO_DOM 124 169 Extracellular (Potential). FT TRANSMEM 170 190 Helical; (Potential). FT TOPO_DOM 191 200 Cytoplasmic (Potential). FT TRANSMEM 201 221 Helical; (Potential). FT TOPO_DOM 222 261 Extracellular (Potential). FT TRANSMEM 262 282 Helical; (Potential). FT TOPO_DOM 283 570 Cytoplasmic (Potential). FT DOMAIN 54 286 Ferric oxidoreductase. FT DOMAIN 287 397 FAD-binding FR-type. FT NP_BIND 338 344 FAD (Potential). FT METAL 101 101 Iron (heme axial ligand) (Probable). FT METAL 115 115 Iron (heme axial ligand) (Probable). FT METAL 209 209 Iron (heme axial ligand) (Probable). FT METAL 222 222 Iron (heme axial ligand) (Probable). FT CARBOHYD 40 40 N-linked (GlcNAc...) (Potential). SQ SEQUENCE 570 AA; 65305 MW; 8816274E3D253DFA CRC64; MGNWAVNEGL SIFVILVWLG LNVFLFINYY KVYDDGPKYN YTRKLLGSAL ALARAPAACL NFNCMLILLP VCRNLLSFLR GSSACCSTRI RRQLDRNLTF HKMVAWMIAL HTAIHTIAHL FNVEWCVNAR VGISDRYSIA LSDIGDNENE EYLNFAREKI KNPEGGLYVA VTRLAGITGI VITLCLILII TSSTKTIRRS YFEVFWYTHH LFVIFFIGLA IHGAERIVRG QTAESLEEHN LDICADKIEE WGKIKECPVP KFAGNPPMTW KWIVGPMFLY LCERLVRFWR SQQKVVITKV VTHPFKTIEL QMKKKGFKME VGQYIFVKCP KVSKLEWHPF TLTSAPEEDF FSIHIRIVGD WTEGLFNACG CDKQEFQDAW KLPKIAVDGP FGTASEDVFS YEVVMLVGAG IGVTPFASIL KSVWYKYCDN ATSLKLKKIY FYWLCRDTHA FEWFADLLQL LETQMQERNN ANFLSYNIYL TGWDESQANH FAVHHDEEKD VITGLKQKTL YGRPNWDNEF KTIASEHPNT TIGVFLCGPE ALAETLSKQS ISNSESGPRG VHFIFNKENF // ID CY250_MOUSE Reviewed; 490 AA. AC Q91X77; E9QPJ0; Q6XVG3; Q80X43; DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 2. DT 19-MAR-2014, entry version 94. DE RecName: Full=Cytochrome P450 2C50; DE EC=1.14.14.1; DE AltName: Full=CYPIIC50; GN Name=Cyp2c50; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE RP SPECIFICITY (ISOFORM 1). RC STRAIN=C57BL/6; TISSUE=Heart; RX PubMed=15102943; DOI=10.1124/mol.65.5.1148; RA Wang H., Zhao Y., Bradbury J.A., Graves J.P., Foley J., RA Blaisdell J.A., Goldstein J.A., Zeldin D.C.; RT "Cloning, expression, and characterization of three new mouse RT cytochrome p450 enzymes and partial characterization of their fatty RT acid oxidation activities."; RL Mol. Pharmacol. 65:1148-1158(2004). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC STRAIN=FVB/N; TISSUE=Liver; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP PROTEIN SEQUENCE OF 100-116, AND MASS SPECTROMETRY. RC STRAIN=OF1; TISSUE=Hippocampus; RA Lubec G., Sunyer B., Chen W.-Q.; RL Submitted (JAN-2009) to UniProtKB. CC -!- FUNCTION: Metabolizes arachidonic acid to several midchain and CC omega-terminal hydroxyeicosatetraenoic acids (HETE). CC -!- CATALYTIC ACTIVITY: RH + reduced flavoprotein + O(2) = ROH + CC oxidized flavoprotein + H(2)O. CC -!- COFACTOR: Heme group (By similarity). CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral CC membrane protein. Microsome membrane; Peripheral membrane protein. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q91X77-1; Sequence=Displayed; CC Name=2; CC IsoId=Q91X77-2; Sequence=VSP_052374; CC Note=No experimental confirmation available; CC -!- TISSUE SPECIFICITY: Expressed in heart and liver. CC -!- INDUCTION: P450 can be induced to high levels in liver and other CC tissues by various foreign compounds, including drugs, pesticides, CC and carcinogens. CC -!- SIMILARITY: Belongs to the cytochrome P450 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AY206873; AAO52736.1; -; mRNA. DR EMBL; AC148014; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC011222; AAH11222.1; -; mRNA. DR EMBL; BC051050; AAH51050.1; -; mRNA. DR RefSeq; NP_001161347.1; NM_001167875.1. DR RefSeq; NP_598905.2; NM_134144.2. DR UniGene; Mm.474575; -. DR ProteinModelPortal; Q91X77; -. DR SMR; Q91X77; 30-489. DR PhosphoSite; Q91X77; -. DR PaxDb; Q91X77; -. DR PRIDE; Q91X77; -. DR Ensembl; ENSMUST00000068094; ENSMUSP00000068039; ENSMUSG00000054827. [Q91X77-2] DR Ensembl; ENSMUST00000080171; ENSMUSP00000079065; ENSMUSG00000054827. [Q91X77-1] DR GeneID; 107141; -. DR KEGG; mmu:107141; -. DR UCSC; uc008hki.2; mouse. [Q91X77-1] DR UCSC; uc012blo.1; mouse. [Q91X77-2] DR CTD; 107141; -. DR MGI; MGI:2147497; Cyp2c50. DR eggNOG; COG2124; -. DR GeneTree; ENSGT00680000099783; -. DR HOGENOM; HOG000036992; -. DR HOVERGEN; HBG015789; -. DR InParanoid; Q91X77; -. DR KO; K07413; -. DR OrthoDB; EOG7RBZ85; -. DR TreeFam; TF352043; -. DR NextBio; 358582; -. DR PRO; PR:Q91X77; -. DR Bgee; Q91X77; -. DR Genevestigator; Q91X77; -. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0070330; F:aromatase activity; IEA:UniProtKB-EC. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR Gene3D; 1.10.630.10; -; 1. DR InterPro; IPR001128; Cyt_P450. DR InterPro; IPR017972; Cyt_P450_CS. DR InterPro; IPR002401; Cyt_P450_E_grp-I. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00463; EP450I. DR PRINTS; PR00385; P450. DR SUPFAM; SSF48264; SSF48264; 1. DR PROSITE; PS00086; CYTOCHROME_P450; 1. PE 1: Evidence at protein level; KW Alternative splicing; Complete proteome; Direct protein sequencing; KW Endoplasmic reticulum; Heme; Iron; Membrane; Metal-binding; Microsome; KW Monooxygenase; Oxidoreductase; Reference proteome. FT CHAIN 1 490 Cytochrome P450 2C50. FT /FTId=PRO_0000282957. FT METAL 435 435 Iron (heme axial ligand) (By similarity). FT VAR_SEQ 215 273 Missing (in isoform 2). FT /FTId=VSP_052374. FT CONFLICT 71 71 R -> N (in Ref. 3; AAH51050/AAH11222). FT CONFLICT 275 275 N -> D (in Ref. 3; AAH11222). FT CONFLICT 336 336 R -> S (in Ref. 3; AAH51050/AAH11222). FT CONFLICT 344 344 H -> R (in Ref. 3; AAH51050/AAH11222). FT CONFLICT 458 458 L -> Q (in Ref. 1; AAO52736). SQ SEQUENCE 490 AA; 55765 MW; 6C66FA7482AB3F78 CRC64; MDPILVLVFT LSCLFLLSLW RQSSERGKLP PGPTPLPIIG NILQINVKDI CQSFTNLSKV YGPVYTLYLG RKPTVVLHGY EAVKEALVDH GEEFAGRGRL PVFDKATNGM GIIFSKGNVW KNTRRFSLTT LRNLGMGKRS IEDRVQEEAR CLVEELRKTN GSPCDPTFIL GCAPCNVICS IIFQDRFDYK DRDFLNLMEK LNEITKIMST PWLQVCNTFP VLLDYCPGSH NKVFKNYACI KNFLLEKIKE HEESLDVTIP RDFIDYFLIN GGQENGNYPL KNRLEHLAIT VTDLFSAGTE TTSTTLRYAL LLLLKYPHVT AKVQEEIEHV IGKHRRPCMQ DRSHMPYTDA MIHEVQRFID LVPNSLPHEV TCDIKFRNYF IPKGTNVITS LSSVLRDSKE FPNPEKFDPG HFLDENGKFK KSDYFMPFST GKRICAGEGL ARMELFLFLT SILQNFNLKP LVHPKDIDVT PMLIGLASVP PAFQLCFIPS // ID CYAC3_MOUSE Reviewed; 242 AA. AC Q6P1H1; Q3TVE2; Q3V3G2; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 19-MAR-2014, entry version 75. DE RecName: Full=Cytochrome b ascorbate-dependent protein 3; DE EC=1.-.-.-; DE AltName: Full=Cytochrome b561 family member A3; DE AltName: Full=Lysosomal cytochrome b; DE Short=LCytb; GN Name=Cyb561a3; Synonyms=Cybasc3, Lcytb; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3). RC STRAIN=C57BL/6J, and NOD; RC TISSUE=Amnion, Aorta, Egg, Spleen, Thymus, Tongue, and Vein; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC STRAIN=C57BL/6; TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP SUBCELLULAR LOCATION, GLYCOSYLATION, TISSUE SPECIFICITY, AND RP DEVELOPMENTAL STAGE. RX PubMed=16996694; DOI=10.1016/j.bbagen.2006.07.019; RA Zhang D.-L., Su D., Berczi A., Vargas A., Asard H.; RT "An ascorbate-reducible cytochrome b561 is localized in macrophage RT lysosomes."; RL Biochim. Biophys. Acta 1760:1903-1913(2006). RN [4] RP FUNCTION, ENZYME ACTIVITY, AND MUTAGENESIS OF PHE-44; TYR-66; ARG-67; RP HIS-83; SER-115; HIS-117; TRP-119; GLN-131; ARG-149; HIS-156 AND RP GLU-196. RX PubMed=16911521; DOI=10.1111/j.1742-4658.2006.05381.x; RA Su D., Asard H.; RT "Three mammalian cytochromes b561 are ascorbate-dependent RT ferrireductases."; RL FEBS J. 273:3722-3734(2006). CC -!- FUNCTION: Ferric-chelate reductase that reduces Fe(3+) to Fe(2+) CC before its transport from the endosome to the cytoplasm. Probably CC uses ascorbate as electron donor. CC -!- COFACTOR: Binds 2 heme groups non-covalently (By similarity). CC -!- SUBCELLULAR LOCATION: Late endosome membrane; Multi-pass membrane CC protein. Lysosome membrane; Multi-pass membrane protein. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q6P1H1-1; Sequence=Displayed; CC Name=2; CC IsoId=Q6P1H1-2; Sequence=VSP_030398; CC Note=No experimental confirmation available; CC Name=3; CC IsoId=Q6P1H1-3; Sequence=VSP_030399; CC Note=No experimental confirmation available; CC -!- TISSUE SPECIFICITY: Present in lung, spleen, thymus and testis. CC Present at low level in brain, heart, liver and kidney. Expressed CC in the alveolar macrophages of the lung, in the white pulp of the CC spleen, widespread in the thymus, and in the Sertoli cells of the CC testis (at protein level). CC -!- DEVELOPMENTAL STAGE: At 17.5 dpc, it is primarily expressed in CC lung, spleen, thymus, testis, placenta, small intestine and CC stomach. CC -!- PTM: N-glycosylated. CC -!- SIMILARITY: Contains 1 cytochrome b561 domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK040692; BAE20585.1; -; mRNA. DR EMBL; AK139533; BAE24053.1; -; mRNA. DR EMBL; AK160179; BAE35677.1; -; mRNA. DR EMBL; AK168841; BAE40664.1; -; mRNA. DR EMBL; AK169729; BAE41333.1; -; mRNA. DR EMBL; AK170911; BAE42109.1; -; mRNA. DR EMBL; AK172638; BAE43109.1; -; mRNA. DR EMBL; BC065078; AAH65078.1; -; mRNA. DR RefSeq; NP_001268993.1; NM_001282064.1. DR RefSeq; NP_001268994.1; NM_001282065.1. DR RefSeq; NP_001268996.1; NM_001282067.1. DR RefSeq; NP_958739.1; NM_201351.2. DR RefSeq; XP_006527003.1; XM_006526940.1. DR UniGene; Mm.252701; -. DR ProteinModelPortal; Q6P1H1; -. DR TCDB; 5.B.2.1.5; the eukaryotic cytochrome b561 (cytb561) family. DR PRIDE; Q6P1H1; -. DR Ensembl; ENSMUST00000168445; ENSMUSP00000130680; ENSMUSG00000034445. [Q6P1H1-1] DR GeneID; 225912; -. DR KEGG; mmu:225912; -. DR UCSC; uc008gqg.1; mouse. [Q6P1H1-1] DR UCSC; uc008gqi.1; mouse. [Q6P1H1-2] DR CTD; 220002; -. DR MGI; MGI:2686925; Cyb561a3. DR eggNOG; NOG327154; -. DR GeneTree; ENSGT00390000010986; -. DR HOGENOM; HOG000231043; -. DR HOVERGEN; HBG054164; -. DR KO; K16295; -. DR OMA; MAVGWFY; -. DR OrthoDB; EOG7SJD5W; -. DR TreeFam; TF314222; -. DR NextBio; 377877; -. DR PRO; PR:Q6P1H1; -. DR Bgee; Q6P1H1; -. DR CleanEx; MM_CYBASC3; -. DR Genevestigator; Q6P1H1; -. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0031902; C:late endosome membrane; IDA:UniProtKB. DR GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW. DR InterPro; IPR028836; Cyb561a3. DR InterPro; IPR006593; Cyt_b561/ferric_Rdtase_TM. DR InterPro; IPR004877; Cyt_b561_euk. DR PANTHER; PTHR10106:SF2; PTHR10106:SF2; 1. DR Pfam; PF03188; Cytochrom_B561; 1. DR SMART; SM00665; B561; 1. DR PROSITE; PS50939; CYTOCHROME_B561; 1. PE 1: Evidence at protein level; KW Alternative splicing; Complete proteome; Electron transport; Endosome; KW Glycoprotein; Heme; Iron; Lysosome; Membrane; Metal-binding; KW Oxidoreductase; Reference proteome; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1 242 Cytochrome b ascorbate-dependent protein FT 3. FT /FTId=PRO_0000314839. FT TRANSMEM 5 25 Helical; Name=1; (Potential). FT TRANSMEM 41 61 Helical; Name=2; (Potential). FT TRANSMEM 82 102 Helical; Name=3; (Potential). FT TRANSMEM 120 140 Helical; Name=4; (Potential). FT TRANSMEM 155 175 Helical; Name=5; (Potential). FT TRANSMEM 203 223 Helical; Name=6; (Potential). FT DOMAIN 12 219 Cytochrome b561. FT METAL 47 47 Iron (heme axial ligand) (Probable). FT METAL 83 83 Iron (heme axial ligand) (Probable). FT METAL 87 87 Iron (heme axial ligand) (Potential). FT METAL 105 105 Iron (heme axial ligand) (Potential). FT METAL 117 117 Iron (heme axial ligand) (Probable). FT METAL 156 156 Iron (heme axial ligand) (Probable). FT VAR_SEQ 236 242 PLLHDRE -> LLLQLLPGSRPFPVTYMPVPLR (in FT isoform 2). FT /FTId=VSP_030398. FT VAR_SEQ 236 242 PLLHDRE -> DGTCGWRLSPSALMWSPGWNVRMAEDFV FT (in isoform 3). FT /FTId=VSP_030399. FT MUTAGEN 44 44 F->A: Induces a 45% reduction in enzyme FT activity. FT MUTAGEN 47 47 H->A: Abolishes enzyme activity. FT MUTAGEN 66 66 Y->A: Almost abolishes enzyme activity. FT MUTAGEN 67 67 R->A: Almost abolishes enzyme activity. FT MUTAGEN 83 83 H->A: Abolishes enzyme activity. FT MUTAGEN 115 115 S->A: Induces a 50% reduction in enzyme FT activity. FT MUTAGEN 117 117 H->A: Abolishes enzyme activity. FT MUTAGEN 119 119 W->A: Induces a 83% reduction in enzyme FT activity. FT MUTAGEN 131 131 Q->A: Induces a 55% reduction in enzyme FT activity. FT MUTAGEN 149 149 R->A: Induces a 75% reduction in enzyme FT activity. FT MUTAGEN 156 156 H->A: Abolishes enzyme activity. FT MUTAGEN 196 196 E->A: Induces a 77% reduction in enzyme FT activity. SQ SEQUENCE 242 AA; 27086 MW; 675709EC97741761 CRC64; MASGWFYLSC MVLGSLGSMC ILFTAYWMQY WRGGFAWDGT VLMFNWHPVL MVAGMVVLYG AASLVYRLPS SWVGPRLPWK VLHAALHLLA FTCTVVGLIA VFRFHNHSRI AHLYSLHSWL GITTVVLFAC QWFLGFAVFL LPWASQWLRS LLKPLHVFFG ACILSLSITS VISGINEKLF FVLKNATKPY SSLPGEAVFA NSTGLLVVAF GLLVLYVLLA SSWKRPDPGA LTDRQPLLHD RE // ID CYBR1_MOUSE Reviewed; 290 AA. AC Q925G2; A2AUU8; Q9D7U1; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 15-JAN-2008, sequence version 2. DT 19-MAR-2014, entry version 73. DE RecName: Full=Cytochrome b reductase 1; DE EC=1.-.-.-; DE AltName: Full=Duodenal cytochrome b; GN Name=Cybrd1; Synonyms=Dcytb; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR RP LOCATION, TISSUE SPECIFICITY, AND INDUCTION. RX PubMed=11230685; DOI=10.1126/science.1057206; RA McKie A.T., Barrow D., Latunde-Dada G.O., Rolfs A., Sager G., RA Mudaly E., Mudaly M., Richardson C., Barlow D., Bomford A., RA Peters T.J., Raja K.B., Shirali S., Hediger M.A., Farzaneh F., RA Simpson R.J.; RT "An iron-regulated ferric reductase associated with the absorption of RT dietary iron."; RL Science 291:1755-1759(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC STRAIN=C57BL/6J; TISSUE=Skin, and Stomach; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [4] RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION. RX PubMed=12547225; DOI=10.1006/bcmd.2002.0574; RA Latunde-Dada G.O., Van der Westhuizen J., Vulpe C.D., Anderson G.J., RA Simpson R.J., McKie A.T.; RT "Molecular and functional roles of duodenal cytochrome B (Dcytb) in RT iron metabolism."; RL Blood Cells Mol. Dis. 29:356-360(2002). RN [5] RP INDUCTION. RX PubMed=12377801; DOI=10.1136/gut.51.5.648; RA Dupic F., Fruchon S., Bensaid M., Loreal O., Brissot P., Borot N., RA Roth M.P., Coppin H.; RT "Duodenal mRNA expression of iron related genes in response to iron RT loading and iron deficiency in four strains of mice."; RL Gut 51:648-653(2002). RN [6] RP INDUCTION. RX PubMed=12704390; DOI=10.1038/ng1152; RA Muckenthaler M., Roy C.N., Custodio A.O., Minana B., deGraaf J., RA Montross L.K., Andrews N.C., Hentze M.W.; RT "Regulatory defects in liver and intestine implicate abnormal hepcidin RT and Cybrd1 expression in mouse hemochromatosis."; RL Nat. Genet. 34:102-107(2003). RN [7] RP DISRUPTION PHENOTYPE. RX PubMed=15961514; DOI=10.1182/blood-2005-02-0716; RA Gunshin H., Starr C.N., Direnzo C., Fleming M.D., Jin J., Greer E.L., RA Sellers V.M., Galica S.M., Andrews N.C.; RT "Cybrd1 (duodenal cytochrome b) is not necessary for dietary iron RT absorption in mice."; RL Blood 106:2879-2883(2005). RN [8] RP COMMENT ON PUBMED:15961514. RX PubMed=16326980; DOI=10.1182/blood-2005-07-2923; RA Frazer D.M., Wilkins S.J., Vulpe C.D., Anderson G.J.; RT "The role of duodenal cytochrome b in intestinal iron absorption RT remains unclear."; RL Blood 106:4413-4413(2005). CC -!- FUNCTION: Ferric-chelate reductase that reduces Fe(3+) to Fe(2+). CC Present at the brush border of duodenal enterocytes where it CC probably reduces dietary Fe(3+) thereby facilitating its transport CC into the mucosal cells. Uses ascorbate as electron donor. May be CC involved in extracellular ascorbate recycling in erythrocyte CC membranes. May also act as a ferrireductase in airway epithelial CC cells. CC -!- COFACTOR: Binds 2 heme groups non-covalently (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q925G2-1; Sequence=Displayed; CC Name=2; CC IsoId=Q925G2-2; Sequence=VSP_030396, VSP_030397; CC -!- TISSUE SPECIFICITY: Highly expressed in the brush-border membrane CC of duodenal enterocytes (at protein level). Also expressed in CC liver and spleen. CC -!- INDUCTION: By iron deficiency. Up-regulated in duodenal mucosa of CC mice lacking transferrin or Hfe (at protein level). CC -!- DISRUPTION PHENOTYPE: Mice are normal and do not display iron CC stores defects, even in the setting of iron deficiency. These CC results, reported by PubMed:15961514, suggest that Cybrd1 is not CC an essential component of intestinal iron apparatus. However, CC according to PubMed:16326980, no direct measurements of iron CC absorption were made by PubMed:15961514, suggesting that final CC conclusions can be drawn only when direct iron absorption studies CC are carried out or mice are maintained on a diet containing ferric CC iron only. CC -!- SIMILARITY: Contains 1 cytochrome b561 domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF354666; AAK50909.1; -; mRNA. DR EMBL; AK008849; BAB25928.1; -; mRNA. DR EMBL; AK029112; BAC26304.1; -; mRNA. DR EMBL; AL929228; CAM22157.1; -; Genomic_DNA. DR RefSeq; NP_082869.2; NM_028593.2. DR UniGene; Mm.45435; -. DR ProteinModelPortal; Q925G2; -. DR PRIDE; Q925G2; -. DR Ensembl; ENSMUST00000028403; ENSMUSP00000028403; ENSMUSG00000027015. [Q925G2-1] DR GeneID; 73649; -. DR KEGG; mmu:73649; -. DR UCSC; uc008kaf.2; mouse. [Q925G2-1] DR CTD; 79901; -. DR MGI; MGI:2654575; Cybrd1. DR eggNOG; NOG259716; -. DR GeneTree; ENSGT00390000010986; -. DR HOGENOM; HOG000231043; -. DR HOVERGEN; HBG054164; -. DR InParanoid; Q925G2; -. DR KO; K08370; -. DR OMA; MEGYRGF; -. DR OrthoDB; EOG7SJD5W; -. DR TreeFam; TF314222; -. DR NextBio; 338709; -. DR PRO; PR:Q925G2; -. DR ArrayExpress; Q925G2; -. DR Bgee; Q925G2; -. DR CleanEx; MM_CYBRD1; -. DR Genevestigator; Q925G2; -. DR GO; GO:0031526; C:brush border membrane; IDA:MGI. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0000293; F:ferric-chelate reductase activity; IEA:Ensembl. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0010039; P:response to iron ion; IDA:MGI. DR InterPro; IPR028838; Cybrd1. DR InterPro; IPR006593; Cyt_b561/ferric_Rdtase_TM. DR InterPro; IPR004877; Cyt_b561_euk. DR PANTHER; PTHR10106:SF1; PTHR10106:SF1; 1. DR Pfam; PF03188; Cytochrom_B561; 1. DR SMART; SM00665; B561; 1. DR PROSITE; PS50939; CYTOCHROME_B561; 1. PE 1: Evidence at protein level; KW Alternative splicing; Complete proteome; Electron transport; KW Glycoprotein; Heme; Iron; Membrane; Metal-binding; Oxidoreductase; KW Phosphoprotein; Reference proteome; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1 290 Cytochrome b reductase 1. FT /FTId=PRO_0000314831. FT TRANSMEM 12 32 Helical; Name=1; (Potential). FT TRANSMEM 49 69 Helical; Name=2; (Potential). FT TRANSMEM 85 105 Helical; Name=3; (Potential). FT TRANSMEM 127 147 Helical; Name=4; (Potential). FT TRANSMEM 158 178 Helical; Name=5; (Potential). FT TRANSMEM 199 219 Helical; Name=6; (Potential). FT DOMAIN 15 220 Cytochrome b561. FT METAL 50 50 Iron (heme axial ligand) (Potential). FT METAL 86 86 Iron (heme axial ligand) (Potential). FT METAL 108 108 Iron (heme axial ligand) (Potential). FT METAL 120 120 Iron (heme axial ligand) (Potential). FT METAL 159 159 Iron (heme axial ligand) (Potential). FT MOD_RES 289 289 Phosphothreonine (By similarity). FT CARBOHYD 41 41 N-linked (GlcNAc...) (Potential). FT VAR_SEQ 243 244 EC -> D (in isoform 2). FT /FTId=VSP_030396. FT VAR_SEQ 261 263 Missing (in isoform 2). FT /FTId=VSP_030397. FT CONFLICT 188 188 H -> R (in Ref. 1; AAK50909). SQ SEQUENCE 290 AA; 31844 MW; F5098086F0EA937E CRC64; MAMEGYRGFL GLLVSALLVG FLSVIFVLIW VLHFREGLGW NGSGLEFNWH PVLAVTGFVF IQGIAIIVYR LPWTWKCSKL LMKSIHAGLN AVAAILAIIS VVAVFEYHNV QKVPHMYSLH SWVGLTALIL YIQQLVVGFF VFLLPWAPPS LRAIVMPIHV YSGLLLFGTV IATVLMGVTE KLFFVLKHPS YHSFPPEGVF TNTLGLLILV FGALIFWIVT RPQWKRPREP GSVPLQLNGG NAECRMEGAI AISSAHSMDA ADPADAESSS EGAARKRTLG LADSGQRSTM // ID D2HDH_MOUSE Reviewed; 535 AA. AC Q8CIM3; E9QLL1; Q149H0; Q3TDF5; Q8BU06; DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot. DT 03-OCT-2012, sequence version 3. DT 19-MAR-2014, entry version 81. DE RecName: Full=D-2-hydroxyglutarate dehydrogenase, mitochondrial; DE EC=1.1.99.-; DE Flags: Precursor; GN Name=D2hgdh; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=NOD; TISSUE=Thymus; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Czech II; TISSUE=Mammary tumor; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-115, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., RA Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). CC -!- FUNCTION: Catalyzes the oxidation of D-2-hydroxyglutarate to CC alpha-ketoglutarate (By similarity). CC -!- CATALYTIC ACTIVITY: (R)-2-hydroxyglutarate + acceptor = 2- CC oxoglutarate + reduced acceptor. CC -!- COFACTOR: FAD (Potential). CC -!- ENZYME REGULATION: Activated by zinc and cobalt (By similarity). CC -!- SUBCELLULAR LOCATION: Mitochondrion (By similarity). CC -!- SIMILARITY: Belongs to the FAD-binding oxidoreductase/transferase CC type 4 family. CC -!- SIMILARITY: Contains 1 FAD-binding PCMH-type domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK088200; BAC40205.1; -; mRNA. DR EMBL; AK170226; BAE41647.1; -; mRNA. DR EMBL; AC167139; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC023277; AAH23277.1; -; mRNA. DR EMBL; BC117794; AAI17795.1; -; mRNA. DR RefSeq; NP_849213.2; NM_178882.3. DR UniGene; Mm.383401; -. DR ProteinModelPortal; Q8CIM3; -. DR SMR; Q8CIM3; 75-531. DR PhosphoSite; Q8CIM3; -. DR PaxDb; Q8CIM3; -. DR PRIDE; Q8CIM3; -. DR Ensembl; ENSMUST00000097633; ENSMUSP00000095235; ENSMUSG00000073609. DR GeneID; 98314; -. DR KEGG; mmu:98314; -. DR CTD; 728294; -. DR MGI; MGI:2138209; D2hgdh. DR eggNOG; COG0277; -. DR GeneTree; ENSGT00550000075086; -. DR HOGENOM; HOG000230997; -. DR HOVERGEN; HBG079809; -. DR InParanoid; Q149H0; -. DR TreeFam; TF323342; -. DR NextBio; 353414; -. DR PRO; PR:Q8CIM3; -. DR ArrayExpress; Q8CIM3; -. DR CleanEx; MM_D2HGDH; -. DR Genevestigator; Q8CIM3; -. DR GO; GO:0005739; C:mitochondrion; ISS:HGNC. DR GO; GO:0051990; F:(R)-2-hydroxyglutarate dehydrogenase activity; ISS:HGNC. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. DR GO; GO:0008762; F:UDP-N-acetylmuramate dehydrogenase activity; IEA:InterPro. DR GO; GO:0044267; P:cellular protein metabolic process; ISS:HGNC. DR GO; GO:0032025; P:response to cobalt ion; ISS:HGNC. DR GO; GO:0010042; P:response to manganese ion; ISS:HGNC. DR GO; GO:0010043; P:response to zinc ion; ISS:HGNC. DR Gene3D; 1.10.45.10; -; 1. DR Gene3D; 3.30.43.10; -; 1. DR Gene3D; 3.30.465.10; -; 1. DR InterPro; IPR016169; CO_DH_flavot_FAD-bd_sub2. DR InterPro; IPR016166; FAD-bd_2. DR InterPro; IPR016167; FAD-bd_2_sub1. DR InterPro; IPR016164; FAD-linked_Oxase-like_C. DR InterPro; IPR004113; FAD-linked_oxidase_C. DR InterPro; IPR006094; Oxid_FAD_bind_N. DR InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2. DR Pfam; PF02913; FAD-oxidase_C; 1. DR Pfam; PF01565; FAD_binding_4; 1. DR SUPFAM; SSF55103; SSF55103; 1. DR SUPFAM; SSF56176; SSF56176; 1. DR PROSITE; PS51387; FAD_PCMH; 1. PE 1: Evidence at protein level; KW Complete proteome; FAD; Flavoprotein; Mitochondrion; Oxidoreductase; KW Reference proteome; Transit peptide. FT TRANSIT 1 50 Mitochondrion (Potential). FT CHAIN 51 535 D-2-hydroxyglutarate dehydrogenase, FT mitochondrial. FT /FTId=PRO_0000231675. FT DOMAIN 110 289 FAD-binding PCMH-type. FT MOD_RES 115 115 N6-succinyllysine. FT CONFLICT 56 56 G -> S (in Ref. 3; AAH23277). FT CONFLICT 451 451 D -> G (in Ref. 1; BAE41647). FT CONFLICT 522 522 E -> K (in Ref. 1; BAE41647/BAC40205 and FT 3; AAH23277/AAI17795). SQ SEQUENCE 535 AA; 58576 MW; 1056007386DE4043 CRC64; MVLPLVSRWS ARVLWASPGW RRTYTQRACV GLKRLGCPRG VYSPLAHRAY SVVAGGPEVT LTPERYPVQR LPFSTVSEED LAAFECIIPG RVITDPEQLQ TCNVDWLKTV RGCSKVLLRP QTSEEVSQIL RHCYKRNLAV NPQGGNTGMV GGSVPVFDEV ILSTALMNQV ISFHDVSGIL VCQAGCVLEE LSRYVQERDF IMPLDLGAKG SCHIGGNVAT NAGGLRFLRY GSLRGTVLGL EVVLADGTIL NCLTSLRKDN TGYDLKQMFI GSEGTLGVIT AVSIVCPPRP KAVNVAFLGC PGFAEVLQTF RTCRGMLGEI LSAFEFMDTE CMQLVGQHLQ LTNPVQESPF YVLVETSGSS AGHDAEKLTN VLEQVLNSGL VTDGTMATDQ RKVQMLWALR ERITEALSRD GYVFKYDLSL PVERLYDLVI DLRTRLGPRA KHVVGYGHLG DGNLHLNVTA EAFSRELLGA LEPYVYAWTA EQRGSVSAEH GLGFKKKDVL GYSKPPVAVT LMQQLKAMLD PEGILNPYKT LPAQA // ID D39U1_MOUSE Reviewed; 308 AA. AC Q5M8N4; Q3V467; Q8BWX0; DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-2005, sequence version 1. DT 19-MAR-2014, entry version 78. DE RecName: Full=Epimerase family protein SDR39U1; DE EC=1.1.1.-; DE AltName: Full=Short-chain dehydrogenase/reductase family 39U member 1; GN Name=Sdr39u1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC STRAIN=C57BL/6J; TISSUE=Spinal cord, and Tongue; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Kidney; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: Putative NADP-dependent oxidoreductase (By similarity). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q5M8N4-1; Sequence=Displayed; CC Name=2; CC IsoId=Q5M8N4-2; Sequence=VSP_023504; CC -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase CC family. SDR39U1 subfamily. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK009339; BAE43214.1; -; mRNA. DR EMBL; AK049709; BAC33886.1; -; mRNA. DR EMBL; BC087941; AAH87941.1; -; mRNA. DR RefSeq; NP_001076444.1; NM_001082975.1. DR UniGene; Mm.486218; -. DR ProteinModelPortal; Q5M8N4; -. DR SMR; Q5M8N4; 1-291. DR STRING; 10090.ENSMUSP00000050096; -. DR PhosphoSite; Q5M8N4; -. DR PaxDb; Q5M8N4; -. DR PRIDE; Q5M8N4; -. DR Ensembl; ENSMUST00000111325; ENSMUSP00000106957; ENSMUSG00000022223. [Q5M8N4-2] DR GeneID; 654795; -. DR KEGG; mmu:654795; -. DR UCSC; uc007ubc.1; mouse. [Q5M8N4-1] DR CTD; 56948; -. DR MGI; MGI:1916876; Sdr39u1. DR eggNOG; COG1090; -. DR GeneTree; ENSGT00390000000337; -. DR HOGENOM; HOG000029190; -. DR InParanoid; Q5M8N4; -. DR KO; K07071; -. DR OMA; YMPWIHI; -. DR OrthoDB; EOG7XH6QF; -. DR TreeFam; TF324783; -. DR NextBio; 425717; -. DR PRO; PR:Q5M8N4; -. DR Bgee; Q5M8N4; -. DR CleanEx; MM_2310014G06RIK; -. DR Genevestigator; Q5M8N4; -. DR GO; GO:0050662; F:coenzyme binding; IEA:InterPro. DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW. DR GO; GO:0044237; P:cellular metabolic process; IEA:InterPro. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR013549; DUF1731_C. DR InterPro; IPR001509; Epimerase_deHydtase. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR010099; Sugar_nucleotide_Epase_put. DR PANTHER; PTHR11092; PTHR11092; 1. DR Pfam; PF08338; DUF1731; 1. DR Pfam; PF01370; Epimerase; 1. DR TIGRFAMs; TIGR01777; yfcH; 1. PE 2: Evidence at transcript level; KW Alternative splicing; Complete proteome; NADP; Oxidoreductase; KW Reference proteome. FT CHAIN 1 308 Epimerase family protein SDR39U1. FT /FTId=PRO_0000279749. FT NP_BIND 9 12 NADP (By similarity). FT NP_BIND 31 32 NADP (By similarity). FT NP_BIND 58 62 NADP (By similarity). FT BINDING 82 82 NADP (By similarity). FT VAR_SEQ 294 308 Missing (in isoform 2). FT /FTId=VSP_023504. FT CONFLICT 132 132 F -> S (in Ref. 1; BAE43214). SQ SEQUENCE 308 AA; 32995 MW; 8F4F087F669738C2 CRC64; MRVLVGGGTG FIGTAVTQLL RGRGHEVKLV SRQPGPGRIT WSELSESGLP LCDVVINLAG ENILNPLRRW NETFQKEVLT SRLDTTHLLA KAITETAHPP QAWILVTGVA YYQPSLTKEY DEDSPGGNFD FFSNLVTKWE AAARLPGEST RQVVVRSGVV LGRGGGAISH MLLPFRLGLG GPIGSGRQFF PWIHIGDLAG ILNYALEANH VQGVLNGVAP ASTTTNAEFA QALGAALGRP AFIPVPSTVV RAVFGERAIM LLEGQKVVPR RTLATGYQYS FPELRAALKD VVACSRTLRS GSGDDPCT // ID D42E1_MOUSE Reviewed; 394 AA. AC Q9D665; Q8VCV0; DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 19-MAR-2014, entry version 90. DE RecName: Full=Short-chain dehydrogenase/reductase family 42E member 1; DE EC=1.1.1.-; GN Name=Sdr42e1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Skin; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Mammary tumor; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein CC (Potential). CC -!- SIMILARITY: Belongs to the 3-beta-HSD family. CC -!- SEQUENCE CAUTION: CC Sequence=AAH18550.1; Type=Erroneous initiation; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK014586; BAB29446.1; -; mRNA. DR EMBL; BC018550; AAH18550.1; ALT_INIT; mRNA. DR EMBL; BC038819; AAH38819.1; -; mRNA. DR RefSeq; NP_083001.1; NM_028725.3. DR RefSeq; XP_006531471.1; XM_006531408.1. DR RefSeq; XP_006531472.1; XM_006531409.1. DR UniGene; Mm.296302; -. DR ProteinModelPortal; Q9D665; -. DR SMR; Q9D665; 6-242. DR PhosphoSite; Q9D665; -. DR PaxDb; Q9D665; -. DR PRIDE; Q9D665; -. DR Ensembl; ENSMUST00000037955; ENSMUSP00000044457; ENSMUSG00000034308. DR Ensembl; ENSMUST00000173522; ENSMUSP00000133782; ENSMUSG00000034308. DR GeneID; 74032; -. DR KEGG; mmu:74032; -. DR UCSC; uc009npd.1; mouse. DR CTD; 93517; -. DR MGI; MGI:1921282; Sdr42e1. DR eggNOG; COG0451; -. DR GeneTree; ENSGT00550000074557; -. DR HOGENOM; HOG000168007; -. DR InParanoid; Q9D665; -. DR OMA; NVTCVFH; -. DR OrthoDB; EOG77M8NP; -. DR TreeFam; TF313574; -. DR NextBio; 339586; -. DR PRO; PR:Q9D665; -. DR ArrayExpress; Q9D665; -. DR Bgee; Q9D665; -. DR Genevestigator; Q9D665; -. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0003854; F:3-beta-hydroxy-delta5-steroid dehydrogenase activity; IEA:InterPro. DR GO; GO:0006694; P:steroid biosynthetic process; IEA:InterPro. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR002225; 3Beta_OHSteriod_DH/Estase. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Pfam; PF01073; 3Beta_HSD; 1. PE 2: Evidence at transcript level; KW Complete proteome; Membrane; NAD; Oxidoreductase; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 394 Short-chain dehydrogenase/reductase FT family 42E member 1. FT /FTId=PRO_0000331756. FT TRANSMEM 283 303 Helical; (Potential). FT TRANSMEM 367 387 Helical; (Potential). FT ACT_SITE 153 153 Proton acceptor (By similarity). FT BINDING 157 157 NAD (By similarity). SQ SEQUENCE 394 AA; 43894 MW; B1FB024CED5D1D15 CRC64; MDSPRFPEET VLITGGGGYF GFRLGCALNQ KGARVILFDI TQPAQNLPEG IKFVCGDIRC LADVETAFQD AEKVACVFHV ASYGMSGREQ LNKTQIEEVN VGGTENILRA CLERGVPRLV YTSTFNVIFG GQVIRNGDES LPYLPLHLHP DHYSRTKSIA EKKVLEANGL AFKQGDGILR TCAIRPAGIY GAGEQRHLPR IVSYIERGLF RFVYGDPQSL VEFVHVDNLA KAHILASEAL KADKGHVASG QPYFISDGRP VNNFEFFRPL VEGLGYTFPS TRLPLTLIYC LAFLVEMTHF IVGRLYNFQP FLTRTEVYKT GVTHYFSLEK AKKELGFEPQ PFDLQEVVEW FKAHGHGRGA AGQDSEFMLW DGILILLLAL SVLTWILPST TLSI // ID DCXR_MOUSE Reviewed; 244 AA. AC Q91X52; Q3U5L5; Q9D129; Q9D8W1; DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot. DT 19-JUL-2004, sequence version 2. DT 19-FEB-2014, entry version 98. DE RecName: Full=L-xylulose reductase; DE Short=XR; DE EC=1.1.1.10; DE AltName: Full=Dicarbonyl/L-xylulose reductase; GN Name=Dcxr; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], ENZYME ACTIVITY, SUBCELLULAR LOCATION, AND RP TISSUE SPECIFICITY. RC STRAIN=C57BL/6; TISSUE=Kidney; RX PubMed=11882650; DOI=10.1074/jbc.M110703200; RA Nakagawa J., Ishikura S., Asami J., Isaji T., Usami N., Hara A., RA Sakurai T., Tsuritani K., Oda K., Takahashi M., Yoshimoto M., RA Otsuka N., Kitamura K.; RT "Molecular characterization of mammalian dicarbonyl/L-xylulose RT reductase and its localization in kidney."; RL J. Biol. Chem. 277:17883-17891(2002). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Bone marrow, Embryo, and Pancreas; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Salivary gland; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: Catalyzes the NADPH-dependent reduction of several CC pentoses, tetroses, trioses, alpha-dicarbonyl compounds and L- CC xylulose. Participates in the uronate cycle of glucose metabolism. CC May play a role in the water absorption and cellular CC osmoregulation in the proximal renal tubules by producing xylitol, CC an osmolyte, thereby preventing osmolytic stress from occurring in CC the renal tubules. CC -!- CATALYTIC ACTIVITY: Xylitol + NADP(+) = L-xylulose + NADPH. CC -!- SUBUNIT: Homotetramer. CC -!- SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein (By CC similarity). Apical cell membrane; Peripheral membrane protein. CC Note=Probably recruited to membranes via an interaction with CC phosphatidylinositol (By similarity). In kidney, it is localized CC in the brush border membranes of proximal tubular cells. CC -!- TISSUE SPECIFICITY: Highly expressed in kidney, liver and CC epididymis. Expressed at intermediate level in lung. Weakly or not CC expressed in brain, heart, spleen and testis. CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases CC (SDR) family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; D89656; BAB88678.1; -; mRNA. DR EMBL; AK004023; BAB23131.1; -; mRNA. DR EMBL; AK007627; BAB25146.1; -; mRNA. DR EMBL; AK153521; BAE32063.1; -; mRNA. DR EMBL; BC012247; AAH12247.1; -; mRNA. DR RefSeq; NP_080704.2; NM_026428.2. DR UniGene; Mm.231091; -. DR ProteinModelPortal; Q91X52; -. DR SMR; Q91X52; 1-243. DR IntAct; Q91X52; 2. DR MINT; MINT-1869627; -. DR PhosphoSite; Q91X52; -. DR REPRODUCTION-2DPAGE; Q91X52; -. DR PaxDb; Q91X52; -. DR PRIDE; Q91X52; -. DR Ensembl; ENSMUST00000026144; ENSMUSP00000026144; ENSMUSG00000039450. DR GeneID; 67880; -. DR KEGG; mmu:67880; -. DR UCSC; uc007muh.1; mouse. DR CTD; 51181; -. DR MGI; MGI:1915130; Dcxr. DR eggNOG; COG1028; -. DR GeneTree; ENSGT00740000115208; -. DR HOVERGEN; HBG105069; -. DR InParanoid; Q91X52; -. DR KO; K03331; -. DR OMA; QRAITNH; -. DR TreeFam; TF313841; -. DR BRENDA; 1.1.1.10; 3474. DR SABIO-RK; Q91X52; -. DR NextBio; 325821; -. DR PRO; PR:Q91X52; -. DR ArrayExpress; Q91X52; -. DR Bgee; Q91X52; -. DR CleanEx; MM_DCXR; -. DR Genevestigator; Q91X52; -. DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005903; C:brush border; IDA:MGI. DR GO; GO:0005881; C:cytoplasmic microtubule; ISS:UniProtKB. DR GO; GO:0005902; C:microvillus; IDA:MGI. DR GO; GO:0050038; F:L-xylulose reductase (NADP+) activity; IDA:UniProtKB. DR GO; GO:0016655; F:oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor; IEA:Ensembl. DR GO; GO:0042732; P:D-xylose metabolic process; IEA:UniProtKB-KW. DR GO; GO:0006006; P:glucose metabolic process; IDA:UniProtKB. DR GO; GO:0006739; P:NADP metabolic process; IDA:MGI. DR GO; GO:0051289; P:protein homotetramerization; IDA:UniProtKB. DR GO; GO:0005997; P:xylulose metabolic process; IDA:MGI. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR002198; DH_sc/Rdtase_SDR. DR InterPro; IPR002347; Glc/ribitol_DH. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR020904; Sc_DH/Rdtase_CS. DR PRINTS; PR00081; GDHRDH. DR PRINTS; PR00080; SDRFAMILY. DR PROSITE; PS00061; ADH_SHORT; 1. PE 2: Evidence at transcript level; KW Acetylation; Carbohydrate metabolism; Cell membrane; KW Complete proteome; Glucose metabolism; Membrane; NADP; Oxidoreductase; KW Reference proteome; Xylose metabolism. FT CHAIN 1 244 L-xylulose reductase. FT /FTId=PRO_0000054556. FT NP_BIND 11 39 NADP (By similarity). FT ACT_SITE 149 149 Proton acceptor (By similarity). FT ACT_SITE 153 153 By similarity. FT BINDING 136 136 Substrate (By similarity). FT MOD_RES 1 1 N-acetylmethionine (By similarity). FT CONFLICT 127 127 V -> N (in Ref. 3; AAH12247). FT CONFLICT 133 135 NVS -> KKY (in Ref. 3; AAH12247). FT CONFLICT 157 158 DM -> FL (in Ref. 3; AAH12247). FT CONFLICT 162 162 M -> R (in Ref. 3; AAH12247). FT CONFLICT 172 172 I -> S (in Ref. 3; AAH12247). FT CONFLICT 184 184 T -> R (in Ref. 3; AAH12247). FT CONFLICT 202 203 DR -> ES (in Ref. 3; AAH12247). FT CONFLICT 224 224 S -> G (in Ref. 2; BAB23131). SQ SEQUENCE 244 AA; 25746 MW; 9701111544053820 CRC64; MDLGLAGRRA LVTGAGKGIG RSTVLALKAA GAQVVAVSRT REDLDDLVRE CPGVEPVCVD LADWEATEQA LSNVGPVDLL VNNAAVALLQ PFLEVTKEAC DTSFNVNLRA VIQVSQIVAK GMIARGVPGA IVNVSSQASQ RALTNHTVYC STKGALDMLT KMMALELGPH KIRVNAVNPT VVMTPMGRTN WSDPHKAKAM LDRIPLGKFA EVENVVDTIL FLLSNRSGMT TGSTLPVDGG FLAT // ID DECR2_MOUSE Reviewed; 292 AA. AC Q9WV68; DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 19-MAR-2014, entry version 99. DE RecName: Full=Peroxisomal 2,4-dienoyl-CoA reductase; DE EC=1.3.1.34; DE AltName: Full=2,4-dienoyl-CoA reductase 2; GN Name=Decr2; Synonyms=Pdcr; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], ENZYME ACTIVITY, SUBCELLULAR LOCATION, AND RP BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=10464321; DOI=10.1074/jbc.274.36.25814; RA Geisbrecht B.V., Liang X., Morrell J.C., Schulz H., Gould S.J.; RT "The mouse gene PDCR encodes a peroxisomal delta(2), delta(4)-dienoyl- RT CoA reductase."; RL J. Biol. Chem. 274:25814-25820(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Liver; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-64, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23576753; DOI=10.1073/pnas.1302961110; RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., RA Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.; RT "Label-free quantitative proteomics of the lysine acetylome in RT mitochondria identifies substrates of SIRT3 in metabolic pathways."; RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013). CC -!- FUNCTION: Auxiliary enzyme of beta-oxidation. Participates in the CC degradation of unsaturated fatty enoyl-CoA esters having double CC bonds in both even- and odd-numbered positions in peroxisome. CC Catalyzes the NADP-dependent reduction of 2,4-dienoyl-CoA to yield CC trans-3-enoyl-CoA. Has activity towards short and medium chain CC 2,4-dienoyl-CoAs, but also towards 2,4,7,10,13,16,19- CC docosaheptaenoyl-CoA, suggesting that it does not constitute a CC rate limiting step in the peroxisomal degradation of CC docosahexaenoic acid. CC -!- CATALYTIC ACTIVITY: Trans-2,3-didehydroacyl-CoA + NADP(+) = CC trans,trans-2,3,4,5-tetradehydroacyl-CoA + NADPH. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=108 uM for 2,4-hexadienoyl-CoA; CC KM=6 uM for 2,4-decadienoyl-CoA; CC KM=155 uM for 2,4,7,10,13,16,19-docosaheptaenoyl-CoA; CC Vmax=8 nmol/min/mg enzyme with 2,4-hexadienoyl-CoA as substrate; CC Vmax=20 nmol/min/mg enzyme with 2,4-decadienoyl-CoA as CC substrate; CC Vmax=5 nmol/min/mg enzyme with 2,4,7,10,13,16,19- CC docosaheptaenoyl-CoA as substrate; CC -!- SUBUNIT: Monomer, dimer and oligomer (By similarity). CC -!- SUBCELLULAR LOCATION: Peroxisome. CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases CC (SDR) family. 2,4-dienoyl-CoA reductase subfamily. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF155575; AAD38196.1; -; mRNA. DR EMBL; BC021865; AAH21865.1; -; mRNA. DR RefSeq; NP_036063.1; NM_011933.2. DR UniGene; Mm.292869; -. DR ProteinModelPortal; Q9WV68; -. DR SMR; Q9WV68; 3-278. DR IntAct; Q9WV68; 2. DR MINT; MINT-1870221; -. DR PhosphoSite; Q9WV68; -. DR PaxDb; Q9WV68; -. DR PRIDE; Q9WV68; -. DR DNASU; 26378; -. DR Ensembl; ENSMUST00000040907; ENSMUSP00000045621; ENSMUSG00000036775. DR GeneID; 26378; -. DR KEGG; mmu:26378; -. DR UCSC; uc008bdg.1; mouse. DR CTD; 26063; -. DR MGI; MGI:1347059; Decr2. DR eggNOG; COG1028; -. DR GeneTree; ENSGT00740000115347; -. DR HOVERGEN; HBG100327; -. DR InParanoid; Q9WV68; -. DR KO; K13237; -. DR OMA; YPDYLLD; -. DR OrthoDB; EOG789CBR; -. DR TreeFam; TF315256; -. DR NextBio; 304285; -. DR PRO; PR:Q9WV68; -. DR ArrayExpress; Q9WV68; -. DR Bgee; Q9WV68; -. DR CleanEx; MM_DECR2; -. DR Genevestigator; Q9WV68; -. DR GO; GO:0005778; C:peroxisomal membrane; IEA:Ensembl. DR GO; GO:0008670; F:2,4-dienoyl-CoA reductase (NADPH) activity; ISS:UniProtKB. DR GO; GO:0019166; F:trans-2-enoyl-CoA reductase (NADPH) activity; IEA:Ensembl. DR GO; GO:0006636; P:unsaturated fatty acid biosynthetic process; ISS:UniProtKB. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR002347; Glc/ribitol_DH. DR InterPro; IPR016040; NAD(P)-bd_dom. DR PRINTS; PR00081; GDHRDH. PE 1: Evidence at protein level; KW Acetylation; Complete proteome; Fatty acid metabolism; KW Lipid metabolism; NADP; Oxidoreductase; Peroxisome; KW Reference proteome. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 292 Peroxisomal 2,4-dienoyl-CoA reductase. FT /FTId=PRO_0000054560. FT NP_BIND 35 40 NADP (By similarity). FT NP_BIND 60 64 NADP (By similarity). FT NP_BIND 208 214 NADP (By similarity). FT REGION 126 128 Substrate binding (By similarity). FT MOTIF 290 292 Microbody targeting signal (By FT similarity). FT BINDING 60 60 Substrate (By similarity). FT BINDING 86 86 NADP (By similarity). FT BINDING 88 88 Substrate (By similarity). FT BINDING 118 118 Substrate (By similarity). FT BINDING 182 182 NADP (By similarity). FT BINDING 219 219 Substrate (By similarity). FT MOD_RES 2 2 N-acetylalanine (By similarity). FT MOD_RES 64 64 N6-acetyllysine. FT MOD_RES 151 151 N6-acetyllysine (By similarity). FT MOD_RES 291 291 N6-acetyllysine (By similarity). SQ SEQUENCE 292 AA; 31300 MW; E25ED366830CC6AB CRC64; MAQPPPDVEG DDCLPEYHHL FCPDLLQDKV AFITGGGSGI GFRIAEIFMR HGCHTVIVGR SLQKVTTAAK KLVAATGKRC LPLSMDVRVP PEVMTAVDQA LQEFGKINIL INCAAGNFLC PASALSFNAF KTVVDIDTIG TFNVSSVLYK KFFRDHGGVI VNITATLSMR GQVLQLHAGA AKAAVDAMTR HLAVEWGPQN IRVNSLAPGA ISGTEGLRRL RGSNASSKLK HFSNPIPRLG TKTEIAHSVL YLASPLASYV SGIVLVVDGG SWMTFPNGIK QLLEFESFSA KL // ID DECR_MOUSE Reviewed; 335 AA. AC Q9CQ62; Q9DCI7; DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 19-MAR-2014, entry version 98. DE RecName: Full=2,4-dienoyl-CoA reductase, mitochondrial; DE EC=1.3.1.34; DE AltName: Full=2,4-dienoyl-CoA reductase [NADPH]; DE Short=4-enoyl-CoA reductase [NADPH]; DE Flags: Precursor; GN Name=Decr1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Lung, and Testis; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Eye; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-106, SUCCINYLATION [LARGE RP SCALE ANALYSIS] AT LYS-42; LYS-49; LYS-73; LYS-97; LYS-106; LYS-244; RP LYS-260 AND LYS-319, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE RP SCALE ANALYSIS]. RC TISSUE=Embryonic fibroblast, and Liver; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., RA Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). RN [4] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-42; LYS-49; LYS-97; LYS-106; RP LYS-244; LYS-260; LYS-315 AND LYS-319, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23576753; DOI=10.1073/pnas.1302961110; RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., RA Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.; RT "Label-free quantitative proteomics of the lysine acetylome in RT mitochondria identifies substrates of SIRT3 in metabolic pathways."; RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013). CC -!- FUNCTION: Auxiliary enzyme of beta-oxidation. It participates in CC the metabolism of unsaturated fatty enoyl-CoA esters having double CC bonds in both even- and odd-numbered positions. Catalyzes the CC NADP-dependent reduction of 2,4-dienoyl-CoA to yield trans-3- CC enoyl-CoA (By similarity). CC -!- CATALYTIC ACTIVITY: Trans-2,3-didehydroacyl-CoA + NADP(+) = CC trans,trans-2,3,4,5-tetradehydroacyl-CoA + NADPH. CC -!- SUBUNIT: Homotetramer (By similarity). CC -!- SUBCELLULAR LOCATION: Mitochondrion (By similarity). CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases CC (SDR) family. 2,4-dienoyl-CoA reductase subfamily. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK002756; BAB22333.1; -; mRNA. DR EMBL; AK004725; BAB23508.1; -; mRNA. DR EMBL; AK015692; BAB29933.1; -; mRNA. DR EMBL; BC046972; AAH46972.1; -; mRNA. DR RefSeq; NP_080448.1; NM_026172.3. DR UniGene; Mm.393293; -. DR ProteinModelPortal; Q9CQ62; -. DR SMR; Q9CQ62; 37-328. DR IntAct; Q9CQ62; 4. DR MINT; MINT-1860375; -. DR PhosphoSite; Q9CQ62; -. DR PaxDb; Q9CQ62; -. DR PRIDE; Q9CQ62; -. DR Ensembl; ENSMUST00000029877; ENSMUSP00000029877; ENSMUSG00000028223. DR GeneID; 67460; -. DR KEGG; mmu:67460; -. DR UCSC; uc008sbm.1; mouse. DR CTD; 1666; -. DR MGI; MGI:1914710; Decr1. DR eggNOG; COG1028; -. DR GeneTree; ENSGT00740000115347; -. DR HOVERGEN; HBG005465; -. DR InParanoid; Q9CQ62; -. DR KO; K13236; -. DR OMA; NCTLAFG; -. DR OrthoDB; EOG7KH9K9; -. DR TreeFam; TF315256; -. DR NextBio; 324642; -. DR PRO; PR:Q9CQ62; -. DR ArrayExpress; Q9CQ62; -. DR Bgee; Q9CQ62; -. DR CleanEx; MM_DECR1; -. DR Genevestigator; Q9CQ62; -. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR GO; GO:0005634; C:nucleus; IEA:Ensembl. DR GO; GO:0008670; F:2,4-dienoyl-CoA reductase (NADPH) activity; ISS:UniProtKB. DR GO; GO:0070402; F:NADPH binding; IEA:Ensembl. DR GO; GO:0006635; P:fatty acid beta-oxidation; ISS:UniProtKB. DR GO; GO:0051289; P:protein homotetramerization; IEA:Ensembl. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR002347; Glc/ribitol_DH. DR InterPro; IPR016040; NAD(P)-bd_dom. DR PRINTS; PR00081; GDHRDH. PE 1: Evidence at protein level; KW Acetylation; Complete proteome; Fatty acid metabolism; KW Lipid metabolism; Mitochondrion; NADP; Oxidoreductase; KW Reference proteome; Transit peptide. FT TRANSIT 1 34 Mitochondrion (By similarity). FT CHAIN 35 335 2,4-dienoyl-CoA reductase, mitochondrial. FT /FTId=PRO_0000031966. FT NP_BIND 66 71 NADP (By similarity). FT NP_BIND 240 243 NADP (By similarity). FT ACT_SITE 199 199 Proton acceptor (Potential). FT BINDING 91 91 NADP (By similarity). FT BINDING 91 91 Substrate (By similarity). FT BINDING 117 117 NADP (By similarity). FT BINDING 119 119 Substrate (By similarity). FT BINDING 149 149 Substrate (By similarity). FT BINDING 214 214 NADP (By similarity). FT BINDING 251 251 Substrate (By similarity). FT MOD_RES 42 42 N6-acetyllysine; alternate. FT MOD_RES 42 42 N6-succinyllysine; alternate. FT MOD_RES 49 49 N6-acetyllysine; alternate. FT MOD_RES 49 49 N6-succinyllysine; alternate. FT MOD_RES 73 73 N6-succinyllysine. FT MOD_RES 97 97 N6-acetyllysine; alternate. FT MOD_RES 97 97 N6-succinyllysine; alternate. FT MOD_RES 106 106 N6-acetyllysine; alternate. FT MOD_RES 106 106 N6-succinyllysine; alternate. FT MOD_RES 244 244 N6-acetyllysine; alternate. FT MOD_RES 244 244 N6-succinyllysine; alternate. FT MOD_RES 260 260 N6-acetyllysine; alternate. FT MOD_RES 260 260 N6-succinyllysine; alternate. FT MOD_RES 315 315 N6-acetyllysine. FT MOD_RES 319 319 N6-acetyllysine; alternate. FT MOD_RES 319 319 N6-succinyllysine; alternate. FT CONFLICT 203 203 G -> V (in Ref. 1; BAB22333). SQ SEQUENCE 335 AA; 36214 MW; C064AC03F818E25A CRC64; MALLGRAFFA GVSRLPCDPG PQRFFSFGTK TLYQSKDAPQ SKFFQPVLKP MLPPDAFQGK VAFITGGGTG LGKAMTTFLS TLGAQCVIAS RNIDVLKATA EEISSKTGNK VHAIRCDVRD PDMVHNTVLE LIKVAGHPDV VINNAAGNFI SPSERLTPNG WKTITDIVLN GTAYVTLEIG KQLIKAQKGA AFLAITTIYA ESGSGFVMPS SSAKSGVEAM NKSLAAEWGR YGMRFNIIQP GPIKTKGAFS RLDPTGRFEK EMIDRIPCGR LGTMEELANL ATFLCSDYAS WINGAVIRFD GGEEVFLSGE FNSLKKVTKE EWDIIEGLIR KTKGS // ID DEGS1_MOUSE Reviewed; 323 AA. AC O09005; Q8R4H3; DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1997, sequence version 1. DT 19-FEB-2014, entry version 101. DE RecName: Full=Sphingolipid delta(4)-desaturase DES1; DE EC=1.14.-.-; DE AltName: Full=Degenerative spermatocyte homolog 1; GN Name=Degs1; Synonyms=Degs, Des1, Mdes; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY. RC STRAIN=ddY; TISSUE=Testis; RX PubMed=9227906; DOI=10.1046/j.1440-169X.1997.00015.x; RA Endo K., Matsuda Y., Kobayashi S.; RT "Mdes, a mouse homolog of the Drosophila degenerative spermatocyte RT gene is expressed during mouse spermatogenesis."; RL Dev. Growth Differ. 39:399-403(1997). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION. RC STRAIN=C57BL/6; TISSUE=Kidney; RX PubMed=11937514; DOI=10.1074/jbc.M202947200; RA Ternes P., Franke S., Zaehringer U., Sperling P., Heinz E.; RT "Identification and characterization of a sphingolipid delta 4- RT desaturase family."; RL J. Biol. Chem. 277:25512-25518(2002). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; RC TISSUE=Bone marrow macrophage, Egg, Kidney, Ovary, and Uterus; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Mammary tumor; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: Has sphingolipid-delta-4-desaturase activity. Converts CC D-erythro-sphinganine to D-erythro-sphingosine (E-sphing-4-enine). CC -!- SUBCELLULAR LOCATION: Mitochondrion. Endoplasmic reticulum CC membrane; Multi-pass membrane protein (By similarity). CC -!- TISSUE SPECIFICITY: Detected in testis. Detected in pachytene CC spermatocytes and round spermatids. CC -!- PTM: Myristoylation can target the enzyme to the mitochondria CC leading to an increase in ceramide levels (By similarity). CC -!- SIMILARITY: Belongs to the fatty acid desaturase family. DEGS CC subfamily. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; Y08460; CAA69714.1; -; mRNA. DR EMBL; AF466376; AAM12532.1; -; mRNA. DR EMBL; AK002617; BAB22233.1; -; mRNA. DR EMBL; AK077257; BAC36713.1; -; mRNA. DR EMBL; AK149811; BAE29098.1; -; mRNA. DR EMBL; AK163404; BAE37337.1; -; mRNA. DR EMBL; BC003751; AAH03751.1; -; mRNA. DR RefSeq; NP_031879.1; NM_007853.4. DR UniGene; Mm.29648; -. DR ProteinModelPortal; O09005; -. DR STRING; 10090.ENSMUSP00000048519; -. DR PhosphoSite; O09005; -. DR PaxDb; O09005; -. DR PRIDE; O09005; -. DR Ensembl; ENSMUST00000035295; ENSMUSP00000048519; ENSMUSG00000038633. DR GeneID; 13244; -. DR KEGG; mmu:13244; -. DR UCSC; uc007dxw.1; mouse. DR CTD; 8560; -. DR MGI; MGI:1097711; Degs1. DR eggNOG; NOG321008; -. DR GeneTree; ENSGT00390000013448; -. DR HOGENOM; HOG000188299; -. DR HOVERGEN; HBG052775; -. DR InParanoid; O09005; -. DR KO; K04712; -. DR OMA; HNSAFGH; -. DR OrthoDB; EOG7WDN2X; -. DR TreeFam; TF313582; -. DR NextBio; 283464; -. DR PRO; PR:O09005; -. DR ArrayExpress; O09005; -. DR Bgee; O09005; -. DR CleanEx; MM_DEGS1; -. DR Genevestigator; O09005; -. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell. DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro. DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW. DR InterPro; IPR005804; Fatty_acid_desaturase-1. DR InterPro; IPR011388; Sphingolipid_d4-desaturase. DR InterPro; IPR013866; Sphingolipid_d4-desaturase_N. DR Pfam; PF00487; FA_desaturase; 1. DR Pfam; PF08557; Lipid_DES; 1. DR PIRSF; PIRSF017228; Sphnglp_dlt4_des; 1. PE 2: Evidence at transcript level; KW Complete proteome; Endoplasmic reticulum; Fatty acid biosynthesis; KW Fatty acid metabolism; Lipid biosynthesis; Lipid metabolism; KW Lipoprotein; Membrane; Mitochondrion; Myristate; Oxidoreductase; KW Phosphoprotein; Reference proteome; Transmembrane; KW Transmembrane helix. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 323 Sphingolipid delta(4)-desaturase DES1. FT /FTId=PRO_0000312729. FT TRANSMEM 41 61 Helical; (Potential). FT TRANSMEM 68 88 Helical; (Potential). FT TRANSMEM 104 124 Helical; (Potential). FT TRANSMEM 152 172 Helical; (Potential). FT TRANSMEM 184 204 Helical; (Potential). FT TRANSMEM 209 229 Helical; (Potential). FT MOD_RES 307 307 Phosphoserine (By similarity). FT LIPID 2 2 N-myristoyl glycine (By similarity). FT CONFLICT 203 203 V -> A (in Ref. 2; AAM12532). SQ SEQUENCE 323 AA; 38241 MW; C1840C24E6FF29E0 CRC64; MGSRVSREEF EWVYTDQPHA ARRKEILAKY PEIKSLMKPD HNLIWIVAMM LLVQLASFYL VKDLDWKWVI FWSYVFGSCL NHSMTLAIHE ISHNFPFGHH KALWNRWFGM FANLSLGVPY SISFKRYHMD HHRYLGADKI DVDIPTDFEG WFFCTTFRKF VWVILQPLFY AFRPLFINPK PITYLEIINT VIQITFDIII YYVFGVKSLV YMLAATLLGL GLHPISGHFI AEHYMFLKGH ETYSYYGPLN LLTFNVGYHN EHHDFPNVPG KNLPMVRKIA SEYYDDLPHY NSWIKVLYDF VTDDTISPYS RMKRPPKGNE ILE // ID DEGS2_MOUSE Reviewed; 323 AA. AC Q8R2F2; Q3TR85; Q78JJ1; DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2002, sequence version 1. DT 19-MAR-2014, entry version 90. DE RecName: Full=Sphingolipid delta(4)-desaturase/C4-hydroxylase DES2; DE EC=1.-.-.-; DE EC=1.14.-.-; DE AltName: Full=Degenerative spermatocyte homolog 2; GN Name=Degs2; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND PATHWAY. RC STRAIN=FVB/N; RX PubMed=11937514; DOI=10.1074/jbc.M202947200; RA Ternes P., Franke S., Zaehringer U., Sperling P., Heinz E.; RT "Identification and characterization of a sphingolipid delta 4- RT desaturase family."; RL J. Biol. Chem. 277:25512-25518(2002). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC STRAIN=C57BL/6J; TISSUE=Thymus; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC STRAIN=FVB/N; TISSUE=Colon; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE SPECIFICITY. RX PubMed=14731113; DOI=10.1042/BJ20031425; RA Omae F., Miyazaki M., Enomoto A., Suzuki M., Suzuki Y., Suzuki A.; RT "DES2 protein is responsible for phytoceramide biosynthesis in the RT mouse small intestine."; RL Biochem. J. 379:687-695(2004). RN [5] RP REGION REQUIRED FOR HYDROLASE ACTIVITY. RX PubMed=15474011; DOI=10.1016/j.febslet.2004.08.060; RA Omae F., Miyazaki M., Enomoto A., Suzuki A.; RT "Identification of an essential sequence for dihydroceramide C-4 RT hydroxylase activity of mouse DES2."; RL FEBS Lett. 576:63-67(2004). RN [6] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=16571104; DOI=10.1042/BJ20051938; RA Enomoto A., Omae F., Miyazaki M., Kozutsumi Y., Yubisui T., Suzuki A.; RT "Dihydroceramide:sphinganine C-4-hydroxylation requires Des2 RT hydroxylase and the membrane form of cytochrome b5."; RL Biochem. J. 397:289-295(2006). CC -!- FUNCTION: Bifunctional enzyme which acts as both a sphingolipid CC delta(4)-desaturase and a sphingolipid C4-hydroxylase. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC pH dependence: CC Optimum pH is 7.0-8.0; CC -!- PATHWAY: Membrane lipid metabolism; sphingolipid biosynthesis. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass CC membrane protein (Probable). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q8R2F2-1; Sequence=Displayed; CC Name=2; CC IsoId=Q8R2F2-2; Sequence=VSP_052629; CC Note=No experimental confirmation available; CC -!- TISSUE SPECIFICITY: Highly expressed in intestinal crypt cells and CC adjacent epithelial cells (at protein level). CC -!- SIMILARITY: Belongs to the fatty acid desaturase family. DEGS CC subfamily. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF466377; AAM12533.1; -; mRNA. DR EMBL; AK162979; BAE37145.1; -; mRNA. DR EMBL; BC016427; AAH16427.2; -; mRNA. DR RefSeq; NP_001164473.1; NM_001171002.1. DR RefSeq; NP_081575.2; NM_027299.5. DR UniGene; Mm.207605; -. DR PhosphoSite; Q8R2F2; -. DR PRIDE; Q8R2F2; -. DR Ensembl; ENSMUST00000021691; ENSMUSP00000021691; ENSMUSG00000021263. [Q8R2F2-1] DR Ensembl; ENSMUST00000167978; ENSMUSP00000125891; ENSMUSG00000021263. [Q8R2F2-2] DR GeneID; 70059; -. DR KEGG; mmu:70059; -. DR UCSC; uc007pab.2; mouse. [Q8R2F2-1] DR UCSC; uc011yrv.1; mouse. [Q8R2F2-2] DR CTD; 123099; -. DR MGI; MGI:1917309; Degs2. DR eggNOG; NOG321008; -. DR GeneTree; ENSGT00390000013448; -. DR HOGENOM; HOG000188299; -. DR HOVERGEN; HBG052775; -. DR InParanoid; Q8R2F2; -. DR KO; K04712; -. DR OMA; DFFWTYT; -. DR OrthoDB; EOG7WDN2X; -. DR TreeFam; TF313582; -. DR UniPathway; UPA00786; -. DR NextBio; 330915; -. DR PRO; PR:Q8R2F2; -. DR Bgee; Q8R2F2; -. DR Genevestigator; Q8R2F2; -. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro. DR GO; GO:0042284; F:sphingolipid delta-4 desaturase activity; IGI:MGI. DR GO; GO:0000170; F:sphingosine hydroxylase activity; IDA:MGI. DR GO; GO:0046513; P:ceramide biosynthetic process; IDA:MGI. DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro. DR GO; GO:0006667; P:sphinganine metabolic process; IDA:MGI. DR GO; GO:0030148; P:sphingolipid biosynthetic process; IEA:UniProtKB-UniPathway. DR InterPro; IPR005804; Fatty_acid_desaturase-1. DR InterPro; IPR011388; Sphingolipid_d4-desaturase. DR InterPro; IPR013866; Sphingolipid_d4-desaturase_N. DR Pfam; PF00487; FA_desaturase; 1. DR Pfam; PF08557; Lipid_DES; 1. DR PIRSF; PIRSF017228; Sphnglp_dlt4_des; 1. PE 1: Evidence at protein level; KW Alternative splicing; Complete proteome; Endoplasmic reticulum; KW Lipid biosynthesis; Lipid metabolism; Lipoprotein; Membrane; KW Myristate; Oxidoreductase; Reference proteome; Transmembrane; KW Transmembrane helix. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 323 Sphingolipid delta(4)-desaturase/C4- FT hydroxylase DES2. FT /FTId=PRO_0000312817. FT TRANSMEM 41 61 Helical; (Potential). FT TRANSMEM 68 88 Helical; (Potential). FT TRANSMEM 210 231 Helical; (Potential). FT REGION 95 99 Required for C4-hydroxylase activity. FT LIPID 2 2 N-myristoyl glycine (By similarity). FT VAR_SEQ 276 323 VRKIAPEYYDHLPQHHSWVKVLWDFVFEDSMGPYSRVKRKC FT KLAKDHL -> DDWNPVRRDVL (in isoform 2). FT /FTId=VSP_052629. FT CONFLICT 88 88 I -> T (in Ref. 2; BAE37145). SQ SEQUENCE 323 AA; 37491 MW; E5B63884E45B5E16 CRC64; MGNSAARSDF EWVYSDQPHT QRRKEMLAKY PAIKALMRPD PHIKWTVSGM VLVQVLACWL VRGLSWRWLL FWAYAFGGCI NHSLTLAIHD ISHNTAFGTS CVSRNRWFAI FANLPIGLPY ATSFKKYHVD HHRYLGGDGL DVDIPTNFEG WFFCTPARKL LWLVLQPFFY SLRPLCVNPK VVTRMEILNA LVQLAFDVTI FALWGIKPIV YLLGSSLLGL GLHPISGHFV AEHYMFLKGH ETYSYYGPLN WITFNVGYHM EHHDFPSIPG YYLPLVRKIA PEYYDHLPQH HSWVKVLWDF VFEDSMGPYS RVKRKCKLAK DHL // ID DHB11_MOUSE Reviewed; 298 AA. AC Q9EQ06; Q3U2P6; Q8BR33; Q8C7S0; DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2001, sequence version 1. DT 19-MAR-2014, entry version 105. DE RecName: Full=Estradiol 17-beta-dehydrogenase 11; DE EC=1.1.1.62; DE AltName: Full=17-beta-hydroxysteroid dehydrogenase 11; DE Short=17-beta-HSD 11; DE Short=17bHSD11; DE Short=17betaHSD11; DE AltName: Full=17-beta-hydroxysteroid dehydrogenase XI; DE Short=17-beta-HSD XI; DE Short=17betaHSDXI; DE AltName: Full=Dehydrogenase/reductase SDR family member 8; DE Flags: Precursor; GN Name=Hsd17b11; Synonyms=Dhrs8, Pan1b; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND ENZYME ACTIVITY IN VITRO. RC STRAIN=NIH Swiss; RX PubMed=11165019; DOI=10.1016/S0303-7207(00)00417-2; RA Brereton P., Suzuki T., Sasano H., Li K., Duarte C., Obeyesekere V., RA Haeseleer F., Palczewski K., Smith I., Komesaroff P., Krozowski Z.; RT "Pan1b (17betaHSD11)-enzymatic activity and distribution in the RT lung."; RL Mol. Cell. Endocrinol. 171:111-117(2001). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC STRAIN=BALB/c; RA Chen W., Napoli J.; RL Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC STRAIN=C57BL/6J, and NOD; RC TISSUE=Corpora quadrigemina, Dendritic cell, Embryonic stem cell, and RC Inner ear; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC STRAIN=FVB/N; TISSUE=Mammary gland; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP POSSIBLE SUBCELLULAR LOCATION. RX PubMed=12697717; DOI=10.1210/en.2002-221030; RA Chai Z., Brereton P., Suzuki T., Sasano H., Obeyesekere V., Escher G., RA Saffery R., Fuller P., Enriquez C., Krozowski Z.; RT "17 beta-hydroxysteroid dehydrogenase type XI localizes to human RT steroidogenic cells."; RL Endocrinology 144:2084-2091(2003). CC -!- FUNCTION: Can convert androstan-3-alpha,17-beta-diol (3-alpha- CC diol) to androsterone in vitro, suggesting that it may participate CC in androgen metabolism during steroidogenesis. May act by CC metabolizing compounds that stimulate steroid synthesis and/or by CC generating metabolites that inhibit it. Has no activity toward CC DHEA (dehydroepiandrosterone), or A-dione (4-androste-3,17-dione), CC and only a slight activity toward testosterone to A-dione. CC -!- CATALYTIC ACTIVITY: 17-beta-estradiol + NAD(P)(+) = estrone + CC NAD(P)H. CC -!- SUBCELLULAR LOCATION: Secreted (Potential). Cytoplasm. CC Note=According to PubMed:12697717 it is cytoplasmic. However, the CC relevance of such result remains unclear. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9EQ06-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9EQ06-2; Sequence=VSP_015013, VSP_015014; CC Note=No experimental confirmation available; CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases CC (SDR) family. 17-beta-HSD 3 subfamily. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF304306; AAG41413.1; -; mRNA. DR EMBL; AY053570; AAL14859.1; -; mRNA. DR EMBL; AK049355; BAC33704.1; -; mRNA. DR EMBL; AK154803; BAE32840.1; -; mRNA. DR EMBL; AK155174; BAE33094.1; -; mRNA. DR EMBL; AK155202; BAE33115.1; -; mRNA. DR EMBL; AK155327; BAE33194.1; -; mRNA. DR EMBL; AK158327; BAE34459.1; -; mRNA. DR EMBL; AK170939; BAE42129.1; -; mRNA. DR EMBL; BC038340; AAH38340.1; -; mRNA. DR RefSeq; NP_444492.1; NM_053262.3. DR UniGene; Mm.46019; -. DR ProteinModelPortal; Q9EQ06; -. DR SMR; Q9EQ06; 30-273. DR IntAct; Q9EQ06; 3. DR MINT; MINT-1862554; -. DR PhosphoSite; Q9EQ06; -. DR PaxDb; Q9EQ06; -. DR PRIDE; Q9EQ06; -. DR DNASU; 114664; -. DR Ensembl; ENSMUST00000031251; ENSMUSP00000031251; ENSMUSG00000029311. [Q9EQ06-1] DR Ensembl; ENSMUST00000119025; ENSMUSP00000113455; ENSMUSG00000029311. [Q9EQ06-2] DR GeneID; 114664; -. DR KEGG; mmu:114664; -. DR UCSC; uc008yjy.1; mouse. [Q9EQ06-1] DR CTD; 51170; -. DR MGI; MGI:2149821; Hsd17b11. DR eggNOG; COG1028; -. DR GeneTree; ENSGT00540000069900; -. DR HOVERGEN; HBG051352; -. DR InParanoid; Q9EQ06; -. DR OMA; FLLAYXL; -. DR OrthoDB; EOG7Z3F50; -. DR TreeFam; TF312837; -. DR NextBio; 368648; -. DR PRO; PR:Q9EQ06; -. DR Bgee; Q9EQ06; -. DR CleanEx; MM_HSD17B11; -. DR Genevestigator; Q9EQ06; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0005811; C:lipid particle; IEA:Ensembl. DR GO; GO:0004303; F:estradiol 17-beta-dehydrogenase activity; IEA:UniProtKB-EC. DR GO; GO:0006710; P:androgen catabolic process; IEA:Ensembl. DR GO; GO:0006694; P:steroid biosynthetic process; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR002198; DH_sc/Rdtase_SDR. DR InterPro; IPR002347; Glc/ribitol_DH. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Pfam; PF00106; adh_short; 1. DR PIRSF; PIRSF000126; 11-beta-HSD1; 1. DR PRINTS; PR00081; GDHRDH. DR PRINTS; PR00080; SDRFAMILY. PE 2: Evidence at transcript level; KW Alternative splicing; Complete proteome; Cytoplasm; KW Lipid biosynthesis; Lipid metabolism; NADP; Oxidoreductase; KW Reference proteome; Secreted; Signal; Steroid biosynthesis. FT SIGNAL 1 21 Potential. FT CHAIN 22 298 Estradiol 17-beta-dehydrogenase 11. FT /FTId=PRO_0000031971. FT NP_BIND 40 64 NADP (By similarity). FT ACT_SITE 185 185 Proton acceptor (By similarity). FT BINDING 172 172 Substrate (By similarity). FT VAR_SEQ 232 232 N -> K (in isoform 2). FT /FTId=VSP_015013. FT VAR_SEQ 233 298 Missing (in isoform 2). FT /FTId=VSP_015014. SQ SEQUENCE 298 AA; 32881 MW; 8ED9279FFBF20EA1 CRC64; MKYLLDLILL LPLLIVFSIE SLVKLFIPKK KKSVAGEIVL ITGAGHGIGR LTAYEFAKLN TKLVLWDINK NGIEETAAKC RKLGAQAHPF VVDCSQREEI YSAAKKVKEE VGDVSILVNN AGVVYTADLF ATQDPQIEKT FEVNVLAHFW TTKAFLPVMM KNNHGHIVTV ASAAGHTVVP FLLAYCSSKF AAVGFHRALT DELAALGRTG VRTSCLCPNF INTGFIKNPS TNLGPTLEPE EVVEHLMHGI LTEKQMIFVP SSIALLTVLE RIVPERFLQV LKHRINVKFD AVVGYKDK // ID DHB1_MOUSE Reviewed; 344 AA. AC P51656; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 19-FEB-2014, entry version 106. DE RecName: Full=Estradiol 17-beta-dehydrogenase 1; DE EC=1.1.1.62; DE AltName: Full=17-beta-hydroxysteroid dehydrogenase type 1; DE Short=17-beta-HSD 1; GN Name=Hsd17b1; Synonyms=Edh17b1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Ovary; RX PubMed=8612620; DOI=10.1111/j.1432-1033.1996.00482.x; RA Nokelainen P., Puranen T., Peltoketo H., Orava M., Vihko P., Vihko R.; RT "Molecular cloning of mouse 17 beta-hydroxysteroid dehydrogenase type RT 1 and characterization of enzyme activity."; RL Eur. J. Biochem. 236:482-490(1996). CC -!- FUNCTION: Favors the reduction of estrogens and androgens. Uses CC preferentially NADH. CC -!- CATALYTIC ACTIVITY: 17-beta-estradiol + NAD(P)(+) = estrone + CC NAD(P)H. CC -!- PATHWAY: Steroid biosynthesis; estrogen biosynthesis. CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases CC (SDR) family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X89627; CAA61770.1; -; mRNA. DR PIR; S62652; S62652. DR RefSeq; NP_034605.1; NM_010475.1. DR UniGene; Mm.188939; -. DR ProteinModelPortal; P51656; -. DR SMR; P51656; 4-284. DR ChEMBL; CHEMBL1914269; -. DR PRIDE; P51656; -. DR Ensembl; ENSMUST00000019445; ENSMUSP00000019445; ENSMUSG00000019301. DR GeneID; 15485; -. DR KEGG; mmu:15485; -. DR UCSC; uc007lnb.1; mouse. DR CTD; 3292; -. DR MGI; MGI:105077; Hsd17b1. DR eggNOG; COG1028; -. DR HOVERGEN; HBG014077; -. DR InParanoid; P51656; -. DR KO; K00044; -. DR OMA; AMHRAVF; -. DR OrthoDB; EOG76T9RW; -. DR TreeFam; TF105451; -. DR UniPathway; UPA00769; -. DR NextBio; 288346; -. DR PRO; PR:P51656; -. DR ArrayExpress; P51656; -. DR Bgee; P51656; -. DR CleanEx; MM_HSD17B1; -. DR Genevestigator; P51656; -. DR GO; GO:0005829; C:cytosol; IEA:Ensembl. DR GO; GO:0004303; F:estradiol 17-beta-dehydrogenase activity; IEA:UniProtKB-EC. DR GO; GO:0060348; P:bone development; IEA:Ensembl. DR GO; GO:0071248; P:cellular response to metal ion; IEA:Ensembl. DR GO; GO:0006703; P:estrogen biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0061370; P:testosterone biosynthetic process; IEA:Ensembl. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR011348; 17beta_DH. DR InterPro; IPR002198; DH_sc/Rdtase_SDR. DR InterPro; IPR002347; Glc/ribitol_DH. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR020904; Sc_DH/Rdtase_CS. DR Pfam; PF00106; adh_short; 1. DR PIRSF; PIRSF000095; 17beta-HSD; 1. DR PRINTS; PR00081; GDHRDH. DR PRINTS; PR00080; SDRFAMILY. DR PROSITE; PS00061; ADH_SHORT; 1. PE 2: Evidence at transcript level; KW Complete proteome; Cytoplasm; Lipid biosynthesis; Lipid metabolism; KW NAD; Oxidoreductase; Reference proteome; Steroid biosynthesis. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 344 Estradiol 17-beta-dehydrogenase 1. FT /FTId=PRO_0000054568. FT NP_BIND 3 32 NAD (By similarity). FT ACT_SITE 156 156 Proton acceptor (By similarity). FT BINDING 143 143 Substrate (By similarity). SQ SEQUENCE 344 AA; 36785 MW; 0335C473F453C14A CRC64; MDPTVVLITG CSSGIGMHLA VRLASDRSQS FKVYATLRDL KAQGPLLEAA RTQGCPPGSL EILELDVRDS KSVAAAQACV TEGRVDVLVC NAGRGLFGPL EAHELNAVGA VLDVNVLGTI RMLQAFLPDM KRRHSGRVLV TASVGGLMGL PFHEVYCASK FALEGLCESL AILLPLFGVH VSLIECGAVH TAFYEKLVGG PGGALERADA QTRHLFAHYL RGYEQALSEA QDPEEVTELF LTAMRAPQPA LRYFSTNRFL PLARMRTEDP SGSSYVAAMH QEAFSNLQTQ ENAKAGAQVP GVSDTASSAL ICLPECAIPR VASELGWSAS DKPGQDNSCY QQKI // ID DHB2_MOUSE Reviewed; 381 AA. AC P51658; O08898; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 2. DT 19-FEB-2014, entry version 117. DE RecName: Full=Estradiol 17-beta-dehydrogenase 2; DE EC=1.1.1.62; DE AltName: Full=17-beta-hydroxysteroid dehydrogenase type 2; DE Short=17-beta-HSD 2; DE AltName: Full=Testosterone 17-beta-dehydrogenase; DE EC=1.1.1.239; GN Name=Hsd17b2; Synonyms=Edh17b2; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=BALB/c; TISSUE=Liver; RX PubMed=9224647; RA Mustonen M.; RT "Cloning of mouse 17beta-hydroxysteroid dehydrogenase type 2, and RT analysing expression of the mRNAs for types 1, 2, 3, 4 and 5 in mouse RT embryos and adult tissues."; RL Biochem. J. 325:199-205(1997). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-358. RC STRAIN=BALB/c; RA Stoffel W., Weiss B.; RL Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Capable of catalyzing the interconversion of CC testosterone and androstenedione, as well as estradiol and CC estrone. Also has 20-alpha-HSD activity. Uses NADH while EDH17B3 CC uses NADPH (By similarity). CC -!- CATALYTIC ACTIVITY: 17-beta-estradiol + NAD(P)(+) = estrone + CC NAD(P)H. CC -!- CATALYTIC ACTIVITY: Testosterone + NAD(+) = androstenedione + CC NADH. CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane CC protein (Potential). CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases CC (SDR) family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; Y09517; CAA70706.1; -; mRNA. DR EMBL; X95685; CAA64982.1; -; mRNA. DR RefSeq; NP_032316.2; NM_008290.2. DR UniGene; Mm.276466; -. DR ProteinModelPortal; P51658; -. DR SMR; P51658; 83-324. DR MINT; MINT-1864098; -. DR STRING; 10090.ENSMUSP00000034304; -. DR ChEMBL; CHEMBL1914270; -. DR PhosphoSite; P51658; -. DR PaxDb; P51658; -. DR PRIDE; P51658; -. DR Ensembl; ENSMUST00000034304; ENSMUSP00000034304; ENSMUSG00000031844. DR GeneID; 15486; -. DR KEGG; mmu:15486; -. DR UCSC; uc009npf.1; mouse. DR CTD; 3294; -. DR MGI; MGI:1096386; Hsd17b2. DR eggNOG; COG1028; -. DR GeneTree; ENSGT00650000093222; -. DR HOVERGEN; HBG005482; -. DR InParanoid; P51658; -. DR KO; K13368; -. DR OMA; QEDYGQD; -. DR OrthoDB; EOG7FXZZX; -. DR TreeFam; TF325617; -. DR NextBio; 288350; -. DR PRO; PR:P51658; -. DR ArrayExpress; P51658; -. DR Bgee; P51658; -. DR CleanEx; MM_HSD17B2; -. DR Genevestigator; P51658; -. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004303; F:estradiol 17-beta-dehydrogenase activity; IEA:UniProtKB-EC. DR GO; GO:0047035; F:testosterone dehydrogenase (NAD+) activity; IEA:UniProtKB-EC. DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI. DR GO; GO:0001890; P:placenta development; IMP:MGI. DR GO; GO:0032526; P:response to retinoic acid; IEA:Ensembl. DR GO; GO:0006694; P:steroid biosynthetic process; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR002198; DH_sc/Rdtase_SDR. DR InterPro; IPR002347; Glc/ribitol_DH. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR020904; Sc_DH/Rdtase_CS. DR Pfam; PF00106; adh_short; 1. DR PRINTS; PR00081; GDHRDH. DR PRINTS; PR00080; SDRFAMILY. DR PROSITE; PS00061; ADH_SHORT; 1. PE 2: Evidence at transcript level; KW Complete proteome; Lipid biosynthesis; Lipid metabolism; Membrane; KW NAD; Oxidoreductase; Reference proteome; Signal-anchor; KW Steroid biosynthesis; Transmembrane; Transmembrane helix. FT CHAIN 1 381 Estradiol 17-beta-dehydrogenase 2. FT /FTId=PRO_0000054571. FT TRANSMEM 4 24 Helical; Signal-anchor for type II FT membrane protein; (Potential). FT NP_BIND 83 112 NAD (By similarity). FT ACT_SITE 233 233 Proton acceptor (By similarity). FT BINDING 220 220 Substrate (By similarity). FT CONFLICT 36 37 QA -> RP (in Ref. 2; CAA64982). SQ SEQUENCE 381 AA; 41836 MW; 74A62797947E6086 CRC64; MSPFASESAW LCLAAAAVLG GTLLCGCRSG RQLRSQAVCL AGLWGGACLL SLSLLCTLFL LSVACFLLLY MSSSDQDLLP VDQKAVLVTG ADSGFGHGLA KHLDKLGFTV FAGVLDKEGP GAEELRKHCS ERLSVLQMDV TKPEQIKDAH SKVTEKIQDK GLWAVVNNAG VFHLPIDGEL IPMSIYRKCM AVNFFGTVEV TKAFLPLLRK SKGRLVNVSS MGGTVPLQMT SAYAATKAAL TMFSTIIRQE LDKWGVKVVT IKPGGFKTNI TGSQDIWDKM EKEILDHFSK DIQENYGQDY VHTQKLIIPT LKERSNPDIT PVLRDIQHAI SARNPSSFYY PGRMAYLWVC LAAYCPTSLL DYVIKKGFYP QPTPRALRTV H // ID DHB3_MOUSE Reviewed; 305 AA. AC P70385; G3UWF9; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 03-OCT-2012, sequence version 2. DT 19-FEB-2014, entry version 101. DE RecName: Full=Testosterone 17-beta-dehydrogenase 3; DE EC=1.1.1.64; DE AltName: Full=17-beta-hydroxysteroid dehydrogenase type 3; DE Short=17-beta-HSD 3; DE AltName: Full=Testicular 17-beta-hydroxysteroid dehydrogenase; GN Name=Hsd17b3; Synonyms=Edh17b3; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Testis; RX PubMed=9182854; DOI=10.1016/S0960-0760(96)00165-3; RA Sha J.A., Dudley K., Rajapaksha W.R.A.K.J.S., O'Shaughnessy P.J.; RT "Sequence of mouse 17beta-hydroxysteroid dehydrogenase type 3 cDNA and RT tissue distribution of the type 1 and type 3 isoform mRNAs."; RL J. Steroid Biochem. Mol. Biol. 60:19-24(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP PROTEIN SEQUENCE OF 81-90, AND MASS SPECTROMETRY. RC STRAIN=OF1; TISSUE=Hippocampus; RA Lubec G., Sunyer B., Chen W.-Q.; RL Submitted (JAN-2009) to UniProtKB. CC -!- FUNCTION: Favors the reduction of androstenedione to testosterone. CC Uses NADPH while the two other EDH17B enzymes use NADH (By CC similarity). CC -!- CATALYTIC ACTIVITY: Testosterone + NADP(+) = androst-4-ene-3,17- CC dione + NADPH. CC -!- PATHWAY: Hormone biosynthesis; testosterone biosynthesis. CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases CC (SDR) family. 17-beta-HSD 3 subfamily. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U66827; AAB06793.1; -; mRNA. DR EMBL; CT009717; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH466631; EDL16224.1; -; Genomic_DNA. DR RefSeq; NP_032317.2; NM_008291.3. DR UniGene; Mm.5109; -. DR ProteinModelPortal; P70385; -. DR SMR; P70385; 43-290. DR STRING; 10090.ENSMUSP00000044217; -. DR BindingDB; P70385; -. DR ChEMBL; CHEMBL1932905; -. DR PhosphoSite; P70385; -. DR PRIDE; P70385; -. DR DNASU; 15487; -. DR Ensembl; ENSMUST00000039832; ENSMUSP00000044217; ENSMUSG00000033122. DR Ensembl; ENSMUST00000166224; ENSMUSP00000132011; ENSMUSG00000033122. DR GeneID; 15487; -. DR KEGG; mmu:15487; -. DR UCSC; uc007qyf.1; mouse. DR CTD; 3293; -. DR MGI; MGI:107177; Hsd17b3. DR eggNOG; COG0300; -. DR GeneTree; ENSGT00390000010069; -. DR HOGENOM; HOG000039237; -. DR HOVERGEN; HBG005478; -. DR InParanoid; P70385; -. DR KO; K10207; -. DR OMA; SMGQWAX; -. DR OrthoDB; EOG7CZK63; -. DR TreeFam; TF314591; -. DR UniPathway; UPA00367; -. DR NextBio; 288354; -. DR PRO; PR:P70385; -. DR CleanEx; MM_HSD17B3; -. DR Genevestigator; P70385; -. DR GO; GO:0047045; F:testosterone 17-beta-dehydrogenase (NADP+) activity; IEA:UniProtKB-EC. DR GO; GO:0061370; P:testosterone biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR002198; DH_sc/Rdtase_SDR. DR InterPro; IPR002347; Glc/ribitol_DH. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR020904; Sc_DH/Rdtase_CS. DR Pfam; PF00106; adh_short; 1. DR PIRSF; PIRSF000126; 11-beta-HSD1; 1. DR PRINTS; PR00081; GDHRDH. DR PRINTS; PR00080; SDRFAMILY. DR PROSITE; PS00061; ADH_SHORT; 1. PE 1: Evidence at protein level; KW Complete proteome; Direct protein sequencing; Lipid biosynthesis; KW Lipid metabolism; NADP; Oxidoreductase; Reference proteome; KW Steroid biosynthesis. FT CHAIN 1 305 Testosterone 17-beta-dehydrogenase 3. FT /FTId=PRO_0000054574. FT NP_BIND 44 73 NADP (By similarity). FT ACT_SITE 194 194 Proton acceptor (By similarity). FT BINDING 181 181 Substrate (By similarity). FT CONFLICT 95 95 C -> G (in Ref. 1; AAB06793). FT CONFLICT 121 121 I -> N (in Ref. 1; AAB06793). FT CONFLICT 142 142 T -> S (in Ref. 1; AAB06793). SQ SEQUENCE 305 AA; 34330 MW; 8EA9966B2777064D CRC64; MEKLFIAAGL FVGLVCLVKC MRFSQHLFLR FCKALPSSFL RSMGQWAVIT GAGDGIGKAY SFELARHGLN VVLISRTLEK LQTIAEEIER TTGSCVKIVQ ADFTREDIYD HIKEHLEGLE IGILVNNVGM LPSFFPSHFL STSGESQNLI HCNITSVVKM TQLVLKHMES RRKGLILNIS SGAALRPWPL YSLYSASKAF VYTFSKALSV EYRDKGIIIQ VLTPYSISTP MTKYLNNKMT KTADEFVKES LKYVTIGAES CGCLAHEIIA IILNRIPSRI FYSSTAQRFL LTRYSDYLKR NISNR // ID DHB12_MOUSE Reviewed; 312 AA. AC O70503; Q3TID1; Q3U7V9; Q542N3; Q8CI39; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1998, sequence version 1. DT 19-MAR-2014, entry version 119. DE RecName: Full=Estradiol 17-beta-dehydrogenase 12; DE EC=1.1.1.62; DE AltName: Full=17-beta-hydroxysteroid dehydrogenase 12; DE Short=17-beta-HSD 12; DE AltName: Full=3-ketoacyl-CoA reductase; DE Short=KAR; DE EC=1.3.1.-; DE AltName: Full=KIK-I; GN Name=Hsd17b12; Synonyms=Kik1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC STRAIN=BALB/c; TISSUE=Liver; RA Gambotto A., Pagliano O., Robbins P., Deleo A.; RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC STRAIN=BALB/c, C57BL/6J, and NOD; RC TISSUE=Bone marrow, Cerebellum, Colon, Head, Lung, and Thymus; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC STRAIN=FVB/N-3; TISSUE=Mammary tumor; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP TISSUE SPECIFICITY. RX PubMed=12482854; DOI=10.1074/jbc.M211684200; RA Moon Y.-A., Horton J.D.; RT "Identification of two mammalian reductases involved in the two-carbon RT fatty acyl elongation cascade."; RL J. Biol. Chem. 278:7335-7343(2003). CC -!- FUNCTION: Catalyzes the transformation of estrone (E1) into CC estradiol (E2), suggesting a central role in estrogen formation. CC Its strong expression in ovary and mammary gland suggest that it CC may constitute the major enzyme responsible for the conversion of CC E1 to E2 in females. Also has 3-ketoacyl-CoA reductase activity, CC reducing both long chain 3-ketoacyl-CoAs and long chain fatty CC acyl-CoAs, suggesting a role in long fatty acid elongation (By CC similarity). CC -!- CATALYTIC ACTIVITY: 17-beta-estradiol + NAD(P)(+) = estrone + CC NAD(P)H. CC -!- PATHWAY: Steroid biosynthesis; estrogen biosynthesis. CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass CC membrane protein (By similarity). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=O70503-1; Sequence=Displayed; CC Name=2; CC IsoId=O70503-2; Sequence=VSP_020255; CC Note=No experimental confirmation available; CC -!- TISSUE SPECIFICITY: Expressed in most tissues tested. CC -!- DOMAIN: The di-lysine motif confers endoplasmic reticulum CC localization for type I membrane proteins (By similarity). CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases CC (SDR) family. 17-beta-HSD 3 subfamily. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF064635; AAC16885.1; -; mRNA. DR EMBL; AK078841; BAC37418.1; -; mRNA. DR EMBL; AK081869; BAC38354.1; -; mRNA. DR EMBL; AK082715; BAC38583.1; -; mRNA. DR EMBL; AK088521; BAC40401.1; -; mRNA. DR EMBL; AK150849; BAE29906.1; -; mRNA. DR EMBL; AK152489; BAE31260.1; -; mRNA. DR EMBL; AK166027; BAE38530.1; -; mRNA. DR EMBL; AK167908; BAE39915.1; -; mRNA. DR EMBL; BC037620; AAH37620.1; -; mRNA. DR RefSeq; NP_062631.1; NM_019657.4. DR UniGene; Mm.22505; -. DR ProteinModelPortal; O70503; -. DR SMR; O70503; 49-295. DR BioGrid; 207914; 8. DR IntAct; O70503; 5. DR MINT; MINT-1863669; -. DR PhosphoSite; O70503; -. DR PaxDb; O70503; -. DR PRIDE; O70503; -. DR Ensembl; ENSMUST00000028619; ENSMUSP00000028619; ENSMUSG00000027195. [O70503-1] DR GeneID; 56348; -. DR KEGG; mmu:56348; -. DR UCSC; uc008lgp.1; mouse. [O70503-1] DR CTD; 51144; -. DR MGI; MGI:1926967; Hsd17b12. DR eggNOG; COG0300; -. DR HOGENOM; HOG000039237; -. DR HOVERGEN; HBG005478; -. DR InParanoid; O70503; -. DR KO; K10251; -. DR OMA; QWSTSLG; -. DR OrthoDB; EOG7CZK63; -. DR TreeFam; TF314591; -. DR UniPathway; UPA00094; -. DR UniPathway; UPA00769; -. DR ChiTaRS; HSD17B12; mouse. DR NextBio; 312340; -. DR PRO; PR:O70503; -. DR ArrayExpress; O70503; -. DR Bgee; O70503; -. DR CleanEx; MM_HSD17B12; -. DR Genevestigator; O70503; -. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0031012; C:extracellular matrix; IDA:MGI. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005518; F:collagen binding; IDA:MGI. DR GO; GO:0004303; F:estradiol 17-beta-dehydrogenase activity; IEA:UniProtKB-EC. DR GO; GO:0001968; F:fibronectin binding; IDA:MGI. DR GO; GO:0008201; F:heparin binding; IDA:MGI. DR GO; GO:0006703; P:estrogen biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0030198; P:extracellular matrix organization; IDA:MGI. DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0010811; P:positive regulation of cell-substrate adhesion; IDA:MGI. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR002198; DH_sc/Rdtase_SDR. DR InterPro; IPR002347; Glc/ribitol_DH. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR020904; Sc_DH/Rdtase_CS. DR Pfam; PF00106; adh_short; 1. DR PIRSF; PIRSF000126; 11-beta-HSD1; 1. DR PRINTS; PR00081; GDHRDH. DR PRINTS; PR00080; SDRFAMILY. DR PROSITE; PS00061; ADH_SHORT; 1. PE 2: Evidence at transcript level; KW Alternative splicing; Complete proteome; Endoplasmic reticulum; KW Lipid biosynthesis; Lipid metabolism; Membrane; NADP; Oxidoreductase; KW Reference proteome; Steroid biosynthesis; Transmembrane; KW Transmembrane helix. FT CHAIN 1 312 Estradiol 17-beta-dehydrogenase 12. FT /FTId=PRO_0000054576. FT TRANSMEM 4 24 Helical; (Potential). FT TRANSMEM 182 202 Helical; (Potential). FT TRANSMEM 269 285 Helical; (Potential). FT NP_BIND 50 79 NADP (By similarity). FT MOTIF 308 312 Di-lysine motif (By similarity). FT ACT_SITE 202 202 Proton acceptor (By similarity). FT BINDING 189 189 Substrate (By similarity). FT VAR_SEQ 1 135 Missing (in isoform 2). FT /FTId=VSP_020255. FT CONFLICT 2 2 E -> V (in Ref. 2; BAE39915). FT CONFLICT 256 256 V -> M (in Ref. 2; BAE29906/BAE31260). SQ SEQUENCE 312 AA; 34742 MW; 7D255188FA1F8DDB CRC64; MECAPPAAGF LYWVGASTIA YLALRASYSL FRAFQVWCVG NEALVGPRLG EWAVVTGGTD GIGKAYAEEL AKRGMKIVLI SRSQDKLNQV SNNIKEKFNV ETRTIAVDFS LDDIYDKIKT GLSGLEIGVL VNNVGMSYEY PEYFLEIPDL DNTIKKLINI NVLSVCKVTR LVLPGMVERS KGVILNISSA SGMLPVPLLT IYSATKAFVD FFSQCLHEEY KSKGIFVQSV MPYLVATKLA KIQKPTLDKP SAETFVKSAI KTVGLQTRTT GYVIHSLMGS INSIMPRWMY FKIIMGFSKS LRNRYLKKRK KN // ID DHB5_MOUSE Reviewed; 323 AA. AC P70694; DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 19-FEB-2014, entry version 109. DE RecName: Full=Estradiol 17 beta-dehydrogenase 5; DE EC=1.1.1.-; DE AltName: Full=17-beta-HSD 5; GN Name=Akr1c6; Synonyms=Hsd17b5; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF N-TERMINUS, AND RP PARTIAL PROTEIN SEQUENCE. RC STRAIN=BALB/c; TISSUE=Liver; RX PubMed=7737980; DOI=10.1074/jbc.270.18.10461; RA Deyashiki Y., Ohshima K., Nakanishi M., Sato K., Matsuura K., Hara A.; RT "Molecular cloning and characterization of mouse estradiol 17 beta- RT dehydrogenase (A-specific), a member of the aldoketoreductase RT family."; RL J. Biol. Chem. 270:10461-10467(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND TISSUE SPECIFICITY. RC STRAIN=BALB/c; TISSUE=Leukocyte; RX PubMed=10500239; DOI=10.1016/S0167-4781(99)00106-2; RA Rheault P., Charbonneau A., Luu-The V.; RT "Structure and activity of the murine type 5 17beta-hydroxysteroid RT dehydrogenase gene."; RL Biochim. Biophys. Acta 1447:17-24(1999). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Liver; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: Active toward androgens, estrogens, and xenobiotic CC substrates. Also exhibits low 20 alpha-HSD activity. Shows a- CC stereospecificity in hydrogen transfer between cofactors and CC substrates (A-specific). Preferentially catalyzes the reduction of CC 4-androstenedione, 5-alpha-androstane-3,17-dione, androsterone and CC dehydroepiandrosterone to testosterone, dihydrotestosterone, 5- CC alpha-androstane-3-alpha,17-beta-diol and 5-androstene-3-beta,17- CC beta-diol, respectively. CC -!- SUBUNIT: Monomer. CC -!- TISSUE SPECIFICITY: Mainly found in liver. Also expressed weakly CC in kidney. CC -!- PTM: Three forms are detected, probably due to post-translational CC modifications. CC -!- SIMILARITY: Belongs to the aldo/keto reductase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; D45850; BAA08285.1; -; mRNA. DR EMBL; AF110414; AAD41250.1; -; Genomic_DNA. DR EMBL; AF110408; AAD41250.1; JOINED; Genomic_DNA. DR EMBL; AF110409; AAD41250.1; JOINED; Genomic_DNA. DR EMBL; AF110410; AAD41250.1; JOINED; Genomic_DNA. DR EMBL; AF110411; AAD41250.1; JOINED; Genomic_DNA. DR EMBL; AF110412; AAD41250.1; JOINED; Genomic_DNA. DR EMBL; AF110413; AAD41250.1; JOINED; Genomic_DNA. DR EMBL; BC056643; AAH56643.1; -; mRNA. DR PIR; A56424; A56424. DR RefSeq; NP_085114.1; NM_030611.3. DR UniGene; Mm.196666; -. DR ProteinModelPortal; P70694; -. DR SMR; P70694; 2-323. DR IntAct; P70694; 3. DR MINT; MINT-1866293; -. DR STRING; 10090.ENSMUSP00000021630; -. DR PhosphoSite; P70694; -. DR SWISS-2DPAGE; P70694; -. DR PaxDb; P70694; -. DR PRIDE; P70694; -. DR Ensembl; ENSMUST00000021630; ENSMUSP00000021630; ENSMUSG00000021210. DR GeneID; 83702; -. DR KEGG; mmu:83702; -. DR UCSC; uc007pjo.1; mouse. DR CTD; 83702; -. DR MGI; MGI:1933427; Akr1c6. DR eggNOG; COG0656; -. DR HOGENOM; HOG000250272; -. DR HOVERGEN; HBG000020; -. DR InParanoid; P70694; -. DR OMA; RIASNID; -. DR OrthoDB; EOG70KGQF; -. DR TreeFam; TF106492; -. DR NextBio; 350738; -. DR PRO; PR:P70694; -. DR ArrayExpress; P70694; -. DR Bgee; P70694; -. DR CleanEx; MM_AKR1C6; -. DR Genevestigator; P70694; -. DR GO; GO:0004033; F:aldo-keto reductase (NADP) activity; IDA:MGI. DR GO; GO:0004303; F:estradiol 17-beta-dehydrogenase activity; IDA:MGI. DR GO; GO:0006694; P:steroid biosynthetic process; IDA:MGI. DR Gene3D; 3.20.20.100; -; 1. DR InterPro; IPR001395; Aldo/ket_red. DR InterPro; IPR018170; Aldo/ket_reductase_CS. DR InterPro; IPR020471; Aldo/keto_reductase_subgr. DR InterPro; IPR023210; NADP_OxRdtase_dom. DR PANTHER; PTHR11732; PTHR11732; 1. DR Pfam; PF00248; Aldo_ket_red; 1. DR PIRSF; PIRSF000097; AKR; 1. DR PRINTS; PR00069; ALDKETRDTASE. DR SUPFAM; SSF51430; SSF51430; 1. DR PROSITE; PS00798; ALDOKETO_REDUCTASE_1; 1. DR PROSITE; PS00062; ALDOKETO_REDUCTASE_2; 1. DR PROSITE; PS00063; ALDOKETO_REDUCTASE_3; 1. PE 1: Evidence at protein level; KW Complete proteome; Direct protein sequencing; Lipid biosynthesis; KW Lipid metabolism; NADP; Oxidoreductase; Reference proteome; KW Steroid biosynthesis. FT CHAIN 1 323 Estradiol 17 beta-dehydrogenase 5. FT /FTId=PRO_0000124652. FT NP_BIND 20 24 NADP (By similarity). FT NP_BIND 166 167 NADP (By similarity). FT NP_BIND 216 221 NADP (By similarity). FT NP_BIND 270 280 NADP (By similarity). FT ACT_SITE 55 55 Proton donor (By similarity). FT BINDING 50 50 NADP (By similarity). FT BINDING 117 117 Substrate (By similarity). FT BINDING 190 190 NADP (By similarity). FT SITE 84 84 Lowers pKa of active site Tyr (By FT similarity). SQ SEQUENCE 323 AA; 37048 MW; 7A1B195E3074D36D CRC64; MDSKQQTVRL SDGHFIPILG FGTYAPQEVP KSKATEATKI AIDAGFRHID SASMYQNEKE VGLAIRSKIA DGTVKREDIF YTSKVWCTFH RPELVRVCLE QSLKQLQLDY VDLYLIHFPM AMKPGENYLP KDENGKLIYD AVDICDTWEA MEKCKDAGLA KSIGVSNFNR RQLEKILKKP GLKYKPVCNQ VECHPYLNQG KLLDFCRSKD IVLVAYSALG SHREKQWVDQ SSPVLLDNPV LGSMAKKYNR TPALIALRYQ LQRGVVVLAK SFSEKRIKEN MQVFEFQLTS EDMKVLDDLN KNIRYISGSS FKDHPDFPFW DEY // ID DHB4_MOUSE Reviewed; 735 AA. AC P51660; Q9DBM3; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 19-MAR-2014, entry version 122. DE RecName: Full=Peroxisomal multifunctional enzyme type 2; DE Short=MFE-2; DE AltName: Full=17-beta-hydroxysteroid dehydrogenase 4; DE Short=17-beta-HSD 4; DE AltName: Full=D-bifunctional protein; DE Short=DBP; DE AltName: Full=Multifunctional protein 2; DE Short=MPF-2; DE Contains: DE RecName: Full=(3R)-hydroxyacyl-CoA dehydrogenase; DE EC=1.1.1.n12; DE Contains: DE RecName: Full=Enoyl-CoA hydratase 2; DE EC=4.2.1.107; DE EC=4.2.1.119; DE AltName: Full=3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholest-24-enoyl-CoA hydratase; GN Name=Hsd17b4; Synonyms=Edh17b4; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=8547180; DOI=10.1016/0960-0760(95)00204-9; RA Normand T., Husen B., Leenders F., Pelczar H., Baert J.-L., Begue A., RA Flourens A.C., Adamski J., de Launoit Y.; RT "Molecular characterization of mouse 17 beta-hydroxysteroid RT dehydrogenase IV."; RL J. Steroid Biochem. Mol. Biol. 55:541-548(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J, and NOD; TISSUE=Amnion, Liver, and Thymus; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Colon; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-308, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=17242355; DOI=10.1073/pnas.0609836104; RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; RT "Large-scale phosphorylation analysis of mouse liver."; RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). RN [5] RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-46; LYS-57; LYS-68; RP LYS-84; LYS-275; LYS-355; LYS-423; LYS-578; LYS-662 AND LYS-724, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., RA Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). RN [6] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-46; LYS-564 AND LYS-706, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23576753; DOI=10.1073/pnas.1302961110; RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., RA Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.; RT "Label-free quantitative proteomics of the lysine acetylome in RT mitochondria identifies substrates of SIRT3 in metabolic pathways."; RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013). CC -!- FUNCTION: Bifunctional enzyme acting on the peroxisomal beta- CC oxidation pathway for fatty acids. Catalyzes the formation of 3- CC ketoacyl-CoA intermediates from both straight-chain and 2-methyl- CC branched-chain fatty acids (By similarity). CC -!- CATALYTIC ACTIVITY: (R)-3-hydroxyacyl-CoA + NAD(+) = 3-oxoacyl-CoA CC + NADH. CC -!- CATALYTIC ACTIVITY: (24R,25R)-3-alpha,7-alpha,12-alpha,24- CC tetrahydroxy-5-beta-cholestanoyl-CoA = (24E)-3-alpha,7-alpha,12- CC alpha-trihydroxy-5-beta-cholest-24-enoyl-CoA + H(2)O. CC -!- CATALYTIC ACTIVITY: (3R)-3-hydroxyacyl-CoA = (2E)-2-enoyl-CoA + CC H(2)O. CC -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation. CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SUBCELLULAR LOCATION: Peroxisome (By similarity). CC -!- TISSUE SPECIFICITY: Present in many tissues with highest CC concentrations in liver and kidney. CC -!- MISCELLANEOUS: The protein is found both as a full length peptide CC and in a cleaved version (By similarity). CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases CC (SDR) family. CC -!- SIMILARITY: Contains 1 MaoC-like domain. CC -!- SIMILARITY: Contains 1 SCP2 domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X89998; CAA62015.1; -; mRNA. DR EMBL; AK004866; BAB23627.1; -; mRNA. DR EMBL; AK088381; BAC40317.1; -; mRNA. DR EMBL; AK166801; BAE39029.1; -; mRNA. DR EMBL; AK167060; BAE39222.1; -; mRNA. DR EMBL; AK169077; BAE40862.1; -; mRNA. DR EMBL; BC022175; AAH22175.1; -; mRNA. DR RefSeq; NP_032318.2; NM_008292.4. DR UniGene; Mm.277857; -. DR ProteinModelPortal; P51660; -. DR SMR; P51660; 3-303, 322-604, 621-735. DR IntAct; P51660; 5. DR MINT; MINT-2512164; -. DR PhosphoSite; P51660; -. DR PaxDb; P51660; -. DR PRIDE; P51660; -. DR Ensembl; ENSMUST00000025385; ENSMUSP00000025385; ENSMUSG00000024507. DR GeneID; 15488; -. DR KEGG; mmu:15488; -. DR UCSC; uc008eww.2; mouse. DR CTD; 3295; -. DR MGI; MGI:105089; Hsd17b4. DR eggNOG; COG1028; -. DR GeneTree; ENSGT00530000062928; -. DR HOGENOM; HOG000170895; -. DR HOVERGEN; HBG002174; -. DR InParanoid; P51660; -. DR KO; K12405; -. DR OMA; LVTEMWK; -. DR OrthoDB; EOG7RBZ7V; -. DR TreeFam; TF105656; -. DR UniPathway; UPA00659; -. DR ChiTaRS; HSD17B4; mouse. DR NextBio; 288358; -. DR PRO; PR:P51660; -. DR Bgee; P51660; -. DR CleanEx; MM_HSD17B4; -. DR Genevestigator; P51660; -. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR GO; GO:0005778; C:peroxisomal membrane; IEA:Ensembl. DR GO; GO:0005777; C:peroxisome; IDA:MGI. DR GO; GO:0044594; F:17-beta-hydroxysteroid dehydrogenase (NAD+) activity; IEA:Ensembl. DR GO; GO:0003857; F:3-hydroxyacyl-CoA dehydrogenase activity; IEA:Ensembl. DR GO; GO:0033989; F:3alpha,7alpha,12alpha-trihydroxy-5beta-cholest-24-enoyl-CoA hydratase activity; IEA:UniProtKB-EC. DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW. DR GO; GO:0016508; F:long-chain-enoyl-CoA hydratase activity; IEA:Ensembl. DR GO; GO:0032934; F:sterol binding; IEA:InterPro. DR GO; GO:0008209; P:androgen metabolic process; IEA:Ensembl. DR GO; GO:0008210; P:estrogen metabolic process; IEA:Ensembl. DR GO; GO:0006635; P:fatty acid beta-oxidation; IMP:MGI. DR GO; GO:0036112; P:medium-chain fatty-acyl-CoA metabolic process; IEA:Ensembl. DR GO; GO:0060009; P:Sertoli cell development; IMP:MGI. DR GO; GO:0000038; P:very long-chain fatty acid metabolic process; IMP:MGI. DR GO; GO:0036111; P:very long-chain fatty-acyl-CoA metabolic process; IEA:Ensembl. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR002198; DH_sc/Rdtase_SDR. DR InterPro; IPR002347; Glc/ribitol_DH. DR InterPro; IPR002539; MaoC_dom. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR020904; Sc_DH/Rdtase_CS. DR InterPro; IPR003033; SCP2_sterol-bd_dom. DR Pfam; PF00106; adh_short; 1. DR Pfam; PF01575; MaoC_dehydratas; 1. DR Pfam; PF02036; SCP2; 1. DR PRINTS; PR00081; GDHRDH. DR PRINTS; PR00080; SDRFAMILY. DR SUPFAM; SSF55718; SSF55718; 1. DR PROSITE; PS00061; ADH_SHORT; 1. PE 1: Evidence at protein level; KW Acetylation; Complete proteome; Fatty acid metabolism; Isomerase; KW Lipid metabolism; Lyase; NAD; Oxidoreductase; Peroxisome; KW Phosphoprotein; Reference proteome. FT CHAIN 1 735 Peroxisomal multifunctional enzyme type FT 2. FT /FTId=PRO_0000054584. FT CHAIN 1 311 (3R)-hydroxyacyl-CoA dehydrogenase. FT /FTId=PRO_0000400084. FT CHAIN 312 735 Enoyl-CoA hydratase 2. FT /FTId=PRO_0000400085. FT DOMAIN 483 599 MaoC-like. FT DOMAIN 623 735 SCP2. FT NP_BIND 13 37 NAD (By similarity). FT NP_BIND 75 76 NAD (By similarity). FT NP_BIND 164 168 NAD (By similarity). FT NP_BIND 196 199 NAD (By similarity). FT REGION 1 305 (3R)-hydroxyacyl-CoA dehydrogenase. FT REGION 321 621 Enoyl-CoA hydratase 2. FT REGION 405 406 (3R)-3-hydroxydecanoyl-CoA binding (By FT similarity). FT REGION 509 514 (3R)-3-hydroxydecanoyl-CoA binding (By FT similarity). FT MOTIF 733 735 Microbody targeting signal (Potential). FT ACT_SITE 164 164 Proton acceptor (By similarity). FT BINDING 21 21 NAD; via amide nitrogen (By similarity). FT BINDING 40 40 NAD (By similarity). FT BINDING 99 99 NAD; via carbonyl oxygen (By similarity). FT BINDING 151 151 Substrate (By similarity). FT BINDING 434 434 (3R)-3-hydroxydecanoyl-CoA (By FT similarity). FT BINDING 532 532 (3R)-3-hydroxydecanoyl-CoA; via amide FT nitrogen (By similarity). FT BINDING 562 562 (3R)-3-hydroxydecanoyl-CoA; via carbonyl FT oxygen (By similarity). FT BINDING 705 705 Substrate (By similarity). FT BINDING 723 723 Substrate (By similarity). FT MOD_RES 46 46 N6-acetyllysine; alternate. FT MOD_RES 46 46 N6-succinyllysine; alternate. FT MOD_RES 57 57 N6-succinyllysine. FT MOD_RES 68 68 N6-succinyllysine. FT MOD_RES 84 84 N6-succinyllysine. FT MOD_RES 275 275 N6-succinyllysine. FT MOD_RES 304 304 Phosphoserine (By similarity). FT MOD_RES 308 308 Phosphoserine. FT MOD_RES 355 355 N6-succinyllysine. FT MOD_RES 423 423 N6-succinyllysine. FT MOD_RES 564 564 N6-acetyllysine. FT MOD_RES 578 578 N6-succinyllysine. FT MOD_RES 662 662 N6-succinyllysine. FT MOD_RES 668 668 N6-acetyllysine (By similarity). FT MOD_RES 706 706 N6-acetyllysine. FT MOD_RES 724 724 N6-succinyllysine. FT CONFLICT 17 17 A -> P (in Ref. 1; CAA62015). FT CONFLICT 417 417 P -> L (in Ref. 1; CAA62015). SQ SEQUENCE 735 AA; 79482 MW; AD7804FE93EB9BA8 CRC64; MASPLRFDGR VVLVTGAGGG LGRAYALAFA ERGALVIVND LGGDFKGIGK GSSAADKVVA EIRRKGGKAV ANYDSVEAGE KLVKTALDTF GRIDVVVNNA GILRDRSFSR ISDEDWDIIH RVHLRGSFQV TRAAWDHMKK QNYGRILMTS SASGIYGNFG QANYSAAKLG ILGLCNTLAI EGRKNNIHCN TIAPNAGSRM TETVLPEDLV EALKPEYVAP LVLWLCHESC EENGGLFEVG AGWIGKLRWE RTLGAIVRKR NQPMTPEAVR DNWEKICDFS NASKPQTIQE STGGIVEVLH KVDSEGISPN RTSHAAPAAT SGFVGAVGHK LPSFSSSYTE LQSIMYALGV GASVKNPKDL KFVYEGSADF SCLPTFGVIV AQKSMMNGGL AEVPGLSFNF AKALHGEQYL ELYKPLPRSG ELKCEAVIAD ILDKGSGVVI VMDVYSYSGK ELICYNQFSV FVVGSGGFGG KRTSEKLKAA VAVPNRPPDA VLRDATSLNQ AALYRLSGDW NPLHIDPDFA SVAGFEKPIL HGLCTFGFSA RHVLQQFADN DVSRFKAIKV RFAKPVYPGQ TLQTEMWKEG NRIHFQTKVH ETGDVVISNA YVDLVPASGV STQTPSEGGE LQSALVFGEI GRRLKSVGRE VVKKANAVFE WHITKGGTVA AKWTIDLKSG SGEVYQGPAK GSADVTIIIS DEDFMEVVFG KLDPQKAFFS GRLKARGNIM LSQKLQMILK DYAKL // ID DHB7_MOUSE Reviewed; 334 AA. AC O88736; Q8K5C9; Q921L1; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1998, sequence version 1. DT 19-MAR-2014, entry version 116. DE RecName: Full=3-keto-steroid reductase; DE EC=1.1.1.270; DE AltName: Full=17-beta-hydroxysteroid dehydrogenase 7; DE Short=17-beta-HSD 7; DE AltName: Full=Estradiol 17-beta-dehydrogenase 7; DE EC=1.1.1.62; GN Name=Hsd17b7; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=BALB/c; TISSUE=Mammary gland; RX PubMed=9658408; DOI=10.1210/me.12.7.1048; RA Nokelainen P., Peltoketo H., Vihko R., Vihko P.; RT "Expression cloning of a novel estrogenic mouse 17 beta-hydroxysteroid RT dehydrogenase/17-ketosteroid reductase (m17HSD7), previously described RT as a prolactin receptor-associated protein (PRAP) in rat."; RL Mol. Endocrinol. 12:1048-1059(1998). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Nokelainen P., Vihko P.; RT "Characterization of mouse 17beta-hydroxysteroid dehydrogenase type 7 RT gene."; RL Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Liver, and Placenta; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Mammary tumor; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP NUCLEOTIDE SEQUENCE OF 1-301. RA Ohnesorg T., Adamski J.; RT "Characterization of mouse gene for 17-beta-hydroxysteroid RT dehydrogenase type 7."; RL Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Responsible for the reduction of the keto group on the CC C-3 of sterols. CC -!- CATALYTIC ACTIVITY: A 3-beta-hydroxysteroid + NADP(+) = a 3- CC oxosteroid + NADPH. CC -!- CATALYTIC ACTIVITY: 17-beta-estradiol + NAD(P)(+) = estrone + CC NAD(P)H. CC -!- PATHWAY: Steroid biosynthesis; estrogen biosynthesis. CC -!- PATHWAY: Steroid biosynthesis; zymosterol biosynthesis; zymosterol CC from lanosterol: step 5/6. CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein. CC -!- TISSUE SPECIFICITY: Most abundant in ovaries of pregnant animals. CC Present also in nonpregnant animals in ovaries, mammary gland, CC liver, kidney and testis. CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases CC (SDR) family. ERG27 subfamily. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; Y15733; CAA75742.1; -; mRNA. DR EMBL; AJ291459; CAC88119.1; -; Genomic_DNA. DR EMBL; AJ291460; CAC88119.1; JOINED; Genomic_DNA. DR EMBL; AJ291461; CAC88119.1; JOINED; Genomic_DNA. DR EMBL; AJ291463; CAC88119.1; JOINED; Genomic_DNA. DR EMBL; AJ291465; CAC88119.1; JOINED; Genomic_DNA. DR EMBL; AJ291466; CAC88119.1; JOINED; Genomic_DNA. DR EMBL; AJ291464; CAC88119.1; JOINED; Genomic_DNA. DR EMBL; AJ291462; CAC88119.1; JOINED; Genomic_DNA. DR EMBL; AK028380; BAC25918.1; -; mRNA. DR EMBL; AK050211; BAC34124.1; -; mRNA. DR EMBL; BC011464; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; AF367475; AAM21211.1; -; Genomic_DNA. DR RefSeq; NP_034606.3; NM_010476.3. DR UniGene; Mm.12882; -. DR ProteinModelPortal; O88736; -. DR SMR; O88736; 2-321. DR BioGrid; 200436; 1. DR IntAct; O88736; 1. DR MINT; MINT-1862744; -. DR PhosphoSite; O88736; -. DR PaxDb; O88736; -. DR PRIDE; O88736; -. DR Ensembl; ENSMUST00000027989; ENSMUSP00000027989; ENSMUSG00000026675. DR GeneID; 15490; -. DR KEGG; mmu:15490; -. DR UCSC; uc007dlp.1; mouse. DR CTD; 51478; -. DR MGI; MGI:1330808; Hsd17b7. DR eggNOG; COG1028; -. DR GeneTree; ENSGT00390000013340; -. DR HOGENOM; HOG000253921; -. DR HOVERGEN; HBG058236; -. DR KO; K13373; -. DR OMA; CHSDNPS; -. DR OrthoDB; EOG7S4X6D; -. DR TreeFam; TF105433; -. DR UniPathway; UPA00769; -. DR UniPathway; UPA00770; UER00758. DR NextBio; 288362; -. DR PRO; PR:O88736; -. DR ArrayExpress; O88736; -. DR Bgee; O88736; -. DR CleanEx; MM_HSD17B7; -. DR Genevestigator; O88736; -. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0000253; F:3-keto sterol reductase activity; IDA:MGI. DR GO; GO:0004303; F:estradiol 17-beta-dehydrogenase activity; IEA:UniProtKB-EC. DR GO; GO:0006695; P:cholesterol biosynthetic process; IDA:MGI. DR GO; GO:0006703; P:estrogen biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR002198; DH_sc/Rdtase_SDR. DR InterPro; IPR002347; Glc/ribitol_DH. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Pfam; PF00106; adh_short; 1. DR PRINTS; PR00081; GDHRDH. PE 2: Evidence at transcript level; KW Cell membrane; Complete proteome; Glycoprotein; Lipid biosynthesis; KW Lipid metabolism; Membrane; NAD; NADP; Oxidoreductase; KW Reference proteome; Steroid biosynthesis; Transmembrane; KW Transmembrane helix. FT CHAIN 1 334 3-keto-steroid reductase. FT /FTId=PRO_0000054587. FT TOPO_DOM 1 229 Extracellular (Potential). FT TRANSMEM 230 250 Helical; (Potential). FT TOPO_DOM 251 334 Cytoplasmic (Potential). FT NP_BIND 8 15 NAD (Potential). FT ACT_SITE 193 193 Proton acceptor (By similarity). FT BINDING 171 171 Substrate (By similarity). FT CARBOHYD 37 37 N-linked (GlcNAc...) (Potential). FT CARBOHYD 127 127 N-linked (GlcNAc...) (Potential). FT CARBOHYD 178 178 N-linked (GlcNAc...) (Potential). FT CARBOHYD 229 229 N-linked (GlcNAc...) (Potential). FT CONFLICT 160 160 A -> V (in Ref. 2; CAC88119 and 4; FT BC011464). SQ SEQUENCE 334 AA; 37317 MW; E05F0716465BC160 CRC64; MRKVVLITGA SSGIGLALCG RLLAEDDDLH LCLACRNLSK ARAVRDTLLA SHPSAEVSIV QMDVSSLQSV VRGAEEVKQK FQRLDYLYLN AGILPNPQFN LKAFFCGIFS RNVIHMFTTA EGILTQNDSV TADGLQEVFE TNLFGHFILI RELEPLLCHA DNPSQLIWTS SRNAKKANFS LEDIQHSKGP EPYSSSKYAT DLLNVALNRN FNQKGLYSSV MCPGVVMTNM TYGILPPFIW TLLLPIMWLL RFFVNALTVT PYNGAEALVW LFHQKPESLN PLTKYASATS GFGTNYVTGQ KMDIDEDTAE KFYEVLLELE KRVRTTVQKS DHPS // ID DHC24_MOUSE Reviewed; 516 AA. AC Q8VCH6; Q6ZQK9; Q91ZD0; Q9CU63; DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2002, sequence version 1. DT 19-FEB-2014, entry version 87. DE RecName: Full=Delta(24)-sterol reductase; DE EC=1.3.1.72; DE AltName: Full=24-dehydrocholesterol reductase; DE AltName: Full=3-beta-hydroxysterol delta-24-reductase; DE Flags: Precursor; GN Name=Dhcr24; Synonyms=Kiaa0018; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=11519011; DOI=10.1086/323473; RA Waterham H.R., Koster J., Romeijn G.J., Hennekam R.C.M., Vreken P., RA Andersson H.C., FitzPatrick D.R., Kelley R.I., Wanders R.J.A.; RT "Mutations in the 3beta-hydroxysterol delta24-reductase gene cause RT desmosterolosis, an autosomal recessive disorder of cholesterol RT biosynthesis."; RL Am. J. Hum. Genet. 69:685-694(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Fetal brain; RX PubMed=14621295; DOI=10.1093/dnares/10.4.167; RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., RA Saga Y., Nagase T., Ohara O., Koga H.; RT "Prediction of the coding sequences of mouse homologues of KIAA gene: RT III. The complete nucleotide sequences of 500 mouse KIAA-homologous RT cDNAs identified by screening of terminal sequences of cDNA clones RT randomly sampled from size-fractionated libraries."; RL DNA Res. 10:167-180(2003). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Liver; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 38-516. RC STRAIN=C57BL/6J; TISSUE=Thymus; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). CC -!- FUNCTION: Catalyzes the reduction of the delta-24 double bond of CC sterol intermediates (By similarity). CC -!- CATALYTIC ACTIVITY: 5-alpha-cholest-7-en-3-beta-ol + NADP(+) = 5- CC alpha-cholesta-7,24-dien-3-beta-ol + NADPH. CC -!- COFACTOR: FAD (By similarity). CC -!- PATHWAY: Steroid biosynthesis; cholesterol biosynthesis. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass CC membrane protein (By similarity). Golgi apparatus membrane; CC Single-pass membrane protein (By similarity). CC -!- SIMILARITY: Belongs to the FAD-binding oxidoreductase/transferase CC type 4 family. CC -!- SIMILARITY: Contains 1 FAD-binding PCMH-type domain. CC -!- SEQUENCE CAUTION: CC Sequence=BAC97846.1; Type=Erroneous initiation; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AY039762; AAK72106.1; -; mRNA. DR EMBL; AK129036; BAC97846.1; ALT_INIT; mRNA. DR EMBL; AL929585; CAM27475.1; -; Genomic_DNA. DR EMBL; BX511043; CAM27475.1; JOINED; Genomic_DNA. DR EMBL; BC019797; AAH19797.1; -; mRNA. DR EMBL; AK017937; BAB31012.1; -; mRNA. DR RefSeq; NP_444502.2; NM_053272.2. DR UniGene; Mm.133370; -. DR ProteinModelPortal; Q8VCH6; -. DR SMR; Q8VCH6; 115-286. DR MINT; MINT-1858806; -. DR PhosphoSite; Q8VCH6; -. DR PaxDb; Q8VCH6; -. DR PRIDE; Q8VCH6; -. DR Ensembl; ENSMUST00000047973; ENSMUSP00000038063; ENSMUSG00000034926. DR GeneID; 74754; -. DR KEGG; mmu:74754; -. DR UCSC; uc008tyl.1; mouse. DR CTD; 1718; -. DR MGI; MGI:1922004; Dhcr24. DR eggNOG; COG0277; -. DR GeneTree; ENSGT00390000008338; -. DR HOGENOM; HOG000243421; -. DR HOVERGEN; HBG051349; -. DR InParanoid; Q8VCH6; -. DR KO; K09828; -. DR OMA; GLEAICE; -. DR OrthoDB; EOG7H7920; -. DR TreeFam; TF313170; -. DR UniPathway; UPA00063; -. DR ChiTaRS; DHCR24; mouse. DR NextBio; 341564; -. DR PRO; PR:Q8VCH6; -. DR Bgee; Q8VCH6; -. DR CleanEx; MM_DHCR24; -. DR Genevestigator; Q8VCH6; -. DR GO; GO:0005856; C:cytoskeleton; IEA:Ensembl. DR GO; GO:0005829; C:cytosol; IEA:Ensembl. DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005634; C:nucleus; ISS:UniProtKB. DR GO; GO:0050614; F:delta24-sterol reductase activity; IEA:UniProtKB-EC. DR GO; GO:0019899; F:enzyme binding; ISS:UniProtKB. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. DR GO; GO:0016628; F:oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor; ISO:MGI. DR GO; GO:0042605; F:peptide antigen binding; ISS:UniProtKB. DR GO; GO:0008762; F:UDP-N-acetylmuramate dehydrogenase activity; IEA:InterPro. DR GO; GO:0042987; P:amyloid precursor protein catabolic process; IMP:MGI. DR GO; GO:0006695; P:cholesterol biosynthetic process; IMP:UniProtKB. DR GO; GO:0030539; P:male genitalia development; IMP:MGI. DR GO; GO:0061024; P:membrane organization; IMP:MGI. DR GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB. DR GO; GO:0008285; P:negative regulation of cell proliferation; IEA:Ensembl. DR GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; ISS:UniProtKB. DR GO; GO:0031639; P:plasminogen activation; IMP:MGI. DR GO; GO:0008104; P:protein localization; IMP:MGI. DR GO; GO:0007265; P:Ras protein signal transduction; IEA:Ensembl. DR GO; GO:0009725; P:response to hormone; IEA:Ensembl. DR GO; GO:0006979; P:response to oxidative stress; ISS:UniProtKB. DR GO; GO:0043588; P:skin development; IMP:UniProtKB. DR GO; GO:0009888; P:tissue development; ISS:UniProtKB. DR Gene3D; 3.30.465.10; -; 1. DR InterPro; IPR016169; CO_DH_flavot_FAD-bd_sub2. DR InterPro; IPR016166; FAD-bd_2. DR InterPro; IPR006094; Oxid_FAD_bind_N. DR Pfam; PF01565; FAD_binding_4; 1. DR SUPFAM; SSF56176; SSF56176; 1. DR PROSITE; PS51387; FAD_PCMH; 1. PE 2: Evidence at transcript level; KW Cholesterol biosynthesis; Cholesterol metabolism; Complete proteome; KW Endoplasmic reticulum; FAD; Flavoprotein; Golgi apparatus; KW Lipid biosynthesis; Lipid metabolism; Membrane; NADP; Oxidoreductase; KW Reference proteome; Signal; Steroid biosynthesis; Steroid metabolism; KW Sterol biosynthesis; Sterol metabolism; Transmembrane; KW Transmembrane helix. FT SIGNAL 1 22 Potential. FT CHAIN 23 516 Delta(24)-sterol reductase. FT /FTId=PRO_0000320300. FT TOPO_DOM 23 31 Lumenal (Potential). FT TRANSMEM 32 52 Helical; (Potential). FT TOPO_DOM 53 516 Cytoplasmic (Potential). FT DOMAIN 58 234 FAD-binding PCMH-type. FT NP_BIND 163 175 FAD (Potential). FT SITE 122 123 Cleavage; by caspase (Potential). FT SITE 383 384 Cleavage; by caspase (Potential). FT CONFLICT 61 62 SS -> TN (in Ref. 5; BAB31012). FT CONFLICT 68 71 EQRV -> NXPL (in Ref. 5; BAB31012). FT CONFLICT 94 94 R -> P (in Ref. 5; BAB31012). FT CONFLICT 278 278 V -> VAV (in Ref. 1; AAK72106). FT CONFLICT 290 290 P -> S (in Ref. 1; AAK72106). SQ SEQUENCE 516 AA; 60112 MW; 7F41D598539E86E4 CRC64; MEPAVSLAVC ALLFLLWVRV KGLEFVLIHQ RWVFVCLFLL PLSLIFDIYY YVRAWVVFKL SSAPRLHEQR VRDIQKQVRE WKEQGSKTFM CTGRPGWLTV SLRVGKYKKT HKNIMINLMD ILEVDTKKQI VRVEPLVSMG QVTALLNSIG WTLPVLPELD DLTVGGLIMG TGIESSSHKY GLFQHICTAY ELILADGSFV RCTPSENSDL FYAVPWSCGT LGFLVAAEIR IIPAKKYVKL RFEPVRGLEA ICEKFTRESQ RLENHFVEGL LYSLDEAVIM TGVMTDDVEP SKLNSIGSYY KPWFFKHVEN YLKTNREGLE YIPLRHYYHR HTRSIFWELQ DIIPFGNNPI FRYLFGWMVP PKISLLKLTQ GETLRKLYEQ HHVVQDMLVP MKCMSQALHT FQNDIHVYPI WLCPFILPSQ PGLVHPKGDE AELYVDIGAY GEPRVKHFEA RSCMRQLEKF VRSVHGFQML YADCYMNREE FWEMFDGSLY HKLRKQLGCQ DAFPEVYDKI CKAARH // ID DHB8_MOUSE Reviewed; 259 AA. AC P50171; Q5M9K0; Q60958; Q60959; Q9Z1W2; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 20-APR-2010, sequence version 2. DT 19-MAR-2014, entry version 122. DE RecName: Full=Estradiol 17-beta-dehydrogenase 8; DE EC=1.1.1.62; DE AltName: Full=17-beta-hydroxysteroid dehydrogenase 8; DE Short=17-beta-HSD 8; DE AltName: Full=3-oxoacyl-[acyl-carrier-protein] reductase; DE EC=1.1.1.-; DE AltName: Full=Protein Ke6; DE Short=Ke-6; DE AltName: Full=Testosterone 17-beta-dehydrogenase 8; DE EC=1.1.1.239; GN Name=Hsd17b8; Synonyms=H2-Ke6, Hke6; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=DBA/2J; TISSUE=Kidney; RX PubMed=8441417; RA Aziz N., Maxwell M.M., St Jacques B., Brenner B.M.; RT "Downregulation of Ke 6, a novel gene encoded within the major RT histocompatibility complex, in murine polycystic kidney disease."; RL Mol. Cell. Biol. 13:1847-1853(1993). RN [2] RP ERRATUM. RA Aziz N., Maxwell M.M., St Jacques B., Brenner B.M.; RL Mol. Cell. Biol. 13:6614-6614(1993). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=C57BL/6; RX PubMed=7559658; DOI=10.1074/jbc.270.42.25213; RA Maxwell M.M., Nearing J., Aziz N.; RT "Ke 6 gene. Sequence and organization and aberrant regulation in RT murine polycystic kidney disease."; RL J. Biol. Chem. 270:25213-25219(1995). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=129/SvJ; RA Rowen L., Qin S., Madan A., Loretz C., James R., Dors M., Mix L., RA Hall J., Lasky S., Hood L.; RT "Sequence of the mouse major histocomaptibility locus class II RT region."; RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SHORT). RC TISSUE=Kidney; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=9712896; DOI=10.1074/jbc.273.35.22664; RA Fomitcheva J., Baker M.E., Anderson E., Lee G.Y., Aziz N.; RT "Characterization of Ke 6, a new 17beta-hydroxysteroid dehydrogenase, RT and its expression in gonadal tissues."; RL J. Biol. Chem. 273:22664-22671(1998). RN [7] RP SUBCELLULAR LOCATION. RX PubMed=15923359; DOI=10.1369/jhc.5A6692.2005; RA Pelletier G., Luu-The V., Li S., Labrie F.; RT "Localization of type 8 17beta-hydroxysteroid dehydrogenase mRNA in RT mouse tissues as studied by in situ hybridization."; RL J. Histochem. Cytochem. 53:1257-1271(2005). RN [8] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain; RX PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200; RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., RA Burlingame A.L.; RT "Comprehensive identification of phosphorylation sites in postsynaptic RT density preparations."; RL Mol. Cell. Proteomics 5:914-922(2006). RN [9] RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-158 AND LYS-171, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., RA Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). RN [10] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-66, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23576753; DOI=10.1073/pnas.1302961110; RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., RA Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.; RT "Label-free quantitative proteomics of the lysine acetylome in RT mitochondria identifies substrates of SIRT3 in metabolic pathways."; RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013). CC -!- FUNCTION: NAD-dependent 17-beta-hydroxysteroid dehydrogenase with CC highest activity towards estradiol. Has very low activity towards CC testosterone (By similarity). The heteroteramer with CBR4 has CC NADH-dependent 3-ketoacyl-acyl carrier protein reductase activity. CC May play a role in biosynthesis of fatty acids in mitochondria (By CC similarity). CC -!- CATALYTIC ACTIVITY: 17-beta-estradiol + NAD(P)(+) = estrone + CC NAD(P)H. CC -!- CATALYTIC ACTIVITY: Testosterone + NAD(+) = androstenedione + CC NADH. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=0.110 uM for estradiol; CC KM=0.422 uM for testosterone; CC KM=0.368 uM for estrone; CC KM=0.360 uM for dihydrotestosterone; CC Vmax=0.405 nmol/min/mg enzyme for estradiol as substrate; CC Vmax=0.123 nmol/min/mg enzyme for testosterone as substrate; CC Vmax=0.186 nmol/min/mg enzyme for estrone as substrate; CC Vmax=0.081 nmol/min/mg enzyme for dihydrotestosterone as CC substrate; CC -!- PATHWAY: Steroid biosynthesis; estrogen biosynthesis. CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis. CC -!- SUBUNIT: Heterotetramer with CBR4; contains two molecules of CC HSD17B8 and CBR4 (By similarity). CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix (By similarity). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=Short; CC IsoId=P50171-1; Sequence=Displayed; CC Name=Long; CC IsoId=P50171-2; Sequence=VSP_006030; CC -!- TISSUE SPECIFICITY: Kidney, liver, testis, ovary, oviduct, uterus, CC mammary gland, vagina, prostate, clitoral gland and moderately in CC spleen, heart, dorsal skin, brain and lung. CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases CC (SDR) family. CC -!- SEQUENCE CAUTION: CC Sequence=AAC69902.1; Type=Erroneous gene model prediction; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U34072; AAC53573.1; -; Genomic_DNA. DR EMBL; U34072; AAC53574.1; -; Genomic_DNA. DR EMBL; AF100956; AAC69902.1; ALT_SEQ; Genomic_DNA. DR EMBL; BC086927; AAH86927.1; -; mRNA. DR PIR; A48154; A48154. DR RefSeq; NP_038571.2; NM_013543.2. DR UniGene; Mm.275452; -. DR ProteinModelPortal; P50171; -. DR SMR; P50171; 6-258. DR IntAct; P50171; 1. DR MINT; MINT-1861146; -. DR PhosphoSite; P50171; -. DR REPRODUCTION-2DPAGE; P50171; -. DR PaxDb; P50171; -. DR PRIDE; P50171; -. DR Ensembl; ENSMUST00000045467; ENSMUSP00000038069; ENSMUSG00000073422. [P50171-1] DR GeneID; 14979; -. DR KEGG; mmu:14979; -. DR UCSC; uc008cat.2; mouse. [P50171-1] DR CTD; 14979; -. DR MGI; MGI:95911; H2-Ke6. DR eggNOG; COG1028; -. DR GeneTree; ENSGT00710000106273; -. DR HOVERGEN; HBG002145; -. DR KO; K13370; -. DR OMA; HMSEEDW; -. DR OrthoDB; EOG73Z2VD; -. DR TreeFam; TF313099; -. DR UniPathway; UPA00094; -. DR UniPathway; UPA00769; -. DR NextBio; 287352; -. DR PRO; PR:P50171; -. DR ArrayExpress; P50171; -. DR Bgee; P50171; -. DR CleanEx; MM_H2-KE6; -. DR Genevestigator; P50171; -. DR GO; GO:0005740; C:mitochondrial envelope; IDA:MGI. DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; IDA:MGI. DR GO; GO:0003857; F:3-hydroxyacyl-CoA dehydrogenase activity; IEA:Ensembl. DR GO; GO:0004303; F:estradiol 17-beta-dehydrogenase activity; ISS:UniProtKB. DR GO; GO:0047035; F:testosterone dehydrogenase (NAD+) activity; IDA:MGI. DR GO; GO:0008209; P:androgen metabolic process; IDA:MGI. DR GO; GO:0006703; P:estrogen biosynthetic process; ISS:UniProtKB. DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR002198; DH_sc/Rdtase_SDR. DR InterPro; IPR002347; Glc/ribitol_DH. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR020904; Sc_DH/Rdtase_CS. DR Pfam; PF00106; adh_short; 1. DR PRINTS; PR00081; GDHRDH. DR PRINTS; PR00080; SDRFAMILY. DR PROSITE; PS00061; ADH_SHORT; 1. PE 1: Evidence at protein level; KW Acetylation; Alternative splicing; Complete proteome; KW Fatty acid biosynthesis; Fatty acid metabolism; Lipid biosynthesis; KW Lipid metabolism; Mitochondrion; NAD; Oxidoreductase; KW Reference proteome; Steroid biosynthesis. FT CHAIN 1 259 Estradiol 17-beta-dehydrogenase 8. FT /FTId=PRO_0000054599. FT NP_BIND 13 21 NAD (By similarity). FT NP_BIND 40 41 NAD (By similarity). FT NP_BIND 72 74 NAD (By similarity). FT NP_BIND 167 171 NAD (By similarity). FT NP_BIND 200 202 NAD (By similarity). FT ACT_SITE 167 167 Proton acceptor (By similarity). FT BINDING 154 154 Substrate (By similarity). FT MOD_RES 66 66 N6-acetyllysine. FT MOD_RES 158 158 N6-succinyllysine. FT MOD_RES 171 171 N6-succinyllysine. FT VAR_SEQ 256 259 GLFM -> MRPSWGGGQENRTQVVMRK (in isoform FT Long). FT /FTId=VSP_006030. FT CONFLICT 229 229 E -> EG (in Ref. 1; AAC53573/AAC53574). SQ SEQUENCE 259 AA; 26588 MW; C4704F02B63C275F CRC64; MASQLRLRSA LALVTGAGSG IGRAISVRLA AEGAAVAACD LDGAAAQDTV RLLGSPGSED GAPRGKHAAF QADVSQGPAA RRLLEEVQAC FSRPPSVVVS CAGITRDEFL LHMSEEDWDR VIAVNLKGTF LVTQAAAQAL VSSGGRGSII NISSIIGKVG NIGQTNYASS KAGVIGLTQT AARELGRHGI RCNSVLPGFI ATPMTQKMPE KVKDKVTAMI PLGHMGDPED VADVVAFLAS EDSGYITGAS VEVSGGLFM // ID DHCR7_MOUSE Reviewed; 471 AA. AC O88455; DT 31-JAN-2002, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1998, sequence version 1. DT 19-MAR-2014, entry version 103. DE RecName: Full=7-dehydrocholesterol reductase; DE Short=7-DHC reductase; DE EC=1.3.1.21; DE AltName: Full=Sterol Delta(7)-reductase; GN Name=Dhcr7; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=C57BL/6J; RX PubMed=9653161; DOI=10.1073/pnas.95.14.8181; RA Fitzky B.U., Witsch-Baumgartner M., Erdel M., Lee J.N., Paik Y.-K., RA Glossmann H., Utermann G., Moebius F.F.; RT "Mutations in the delta7-sterol reductase gene in patients with the RT Smith-Lemli-Opitz syndrome."; RL Proc. Natl. Acad. Sci. U.S.A. 95:8181-8186(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: Production of cholesterol by reduction of C7-C8 double CC bond of 7-dehydrocholesterol (7-DHC). CC -!- CATALYTIC ACTIVITY: Cholesterol + NADP(+) = cholesta-5,7-dien-3- CC beta-ol + NADPH. CC -!- PATHWAY: Steroid biosynthesis; cholesterol biosynthesis. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass CC membrane protein. CC -!- SIMILARITY: Belongs to the ERG4/ERG24 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF057368; AAC40164.1; -; mRNA. DR EMBL; BC006854; AAH06854.1; -; mRNA. DR RefSeq; NP_031882.1; NM_007856.2. DR RefSeq; XP_006508541.1; XM_006508478.1. DR RefSeq; XP_006508542.1; XM_006508479.1. DR RefSeq; XP_006508543.1; XM_006508480.1. DR RefSeq; XP_006508544.1; XM_006508481.1. DR UniGene; Mm.249342; -. DR ProteinModelPortal; O88455; -. DR PhosphoSite; O88455; -. DR PaxDb; O88455; -. DR PRIDE; O88455; -. DR Ensembl; ENSMUST00000073878; ENSMUSP00000073541; ENSMUSG00000058454. DR Ensembl; ENSMUST00000124340; ENSMUSP00000117659; ENSMUSG00000058454. DR Ensembl; ENSMUST00000141916; ENSMUSP00000121782; ENSMUSG00000058454. DR GeneID; 13360; -. DR KEGG; mmu:13360; -. DR UCSC; uc009kqc.1; mouse. DR CTD; 1717; -. DR MGI; MGI:1298378; Dhcr7. DR eggNOG; NOG72042; -. DR GeneTree; ENSGT00390000000417; -. DR HOGENOM; HOG000193296; -. DR HOVERGEN; HBG007825; -. DR InParanoid; O88455; -. DR KO; K00213; -. DR OMA; TFAMIKG; -. DR TreeFam; TF101180; -. DR UniPathway; UPA00063; -. DR NextBio; 283692; -. DR PRO; PR:O88455; -. DR ArrayExpress; O88455; -. DR Bgee; O88455; -. DR CleanEx; MM_DHCR7; -. DR Genevestigator; O88455; -. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005640; C:nuclear outer membrane; IEA:Ensembl. DR GO; GO:0047598; F:7-dehydrocholesterol reductase activity; IDA:MGI. DR GO; GO:0001568; P:blood vessel development; IMP:MGI. DR GO; GO:0030154; P:cell differentiation; IMP:MGI. DR GO; GO:0006695; P:cholesterol biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0030324; P:lung development; IMP:MGI. DR GO; GO:0035264; P:multicellular organism growth; IMP:MGI. DR GO; GO:0009791; P:post-embryonic development; IMP:MGI. DR GO; GO:0042127; P:regulation of cell proliferation; IMP:MGI. DR GO; GO:0045540; P:regulation of cholesterol biosynthetic process; IEA:Ensembl. DR GO; GO:0016126; P:sterol biosynthetic process; IMP:MGI. DR InterPro; IPR001171; Ergosterol_biosynth_ERG4_ERG24. DR InterPro; IPR018083; Sterol_reductase_CS. DR Pfam; PF01222; ERG4_ERG24; 1. DR PROSITE; PS01017; STEROL_REDUCT_1; 1. DR PROSITE; PS01018; STEROL_REDUCT_2; 1. PE 2: Evidence at transcript level; KW Cholesterol biosynthesis; Cholesterol metabolism; Complete proteome; KW Endoplasmic reticulum; Lipid biosynthesis; Lipid metabolism; Membrane; KW NADP; Oxidoreductase; Phosphoprotein; Reference proteome; KW Steroid biosynthesis; Steroid metabolism; Sterol biosynthesis; KW Sterol metabolism; Transmembrane; Transmembrane helix. FT CHAIN 1 471 7-dehydrocholesterol reductase. FT /FTId=PRO_0000207503. FT TRANSMEM 36 56 Helical; (Potential). FT TRANSMEM 95 115 Helical; (Potential). FT TRANSMEM 144 164 Helical; (Potential). FT TRANSMEM 173 193 Helical; (Potential). FT TRANSMEM 233 253 Helical; (Potential). FT TRANSMEM 262 282 Helical; (Potential). FT TRANSMEM 302 322 Helical; (Potential). FT TRANSMEM 327 347 Helical; (Potential). FT TRANSMEM 416 436 Helical; (Potential). FT MOD_RES 14 14 Phosphoserine (By similarity). SQ SEQUENCE 471 AA; 53919 MW; 6B1BC356CC539290 CRC64; MASKSQHNAP KVKSPNGKAG SQGQWGRAWE VDWFSLASII FLLLFAPFIV YYFIMACDQY SCSLTAPALD IATGHASLAD IWAKTPPVTA KAAQLYALWV SFQVLLYSWL PDFCHRFLPG YVGGVQEGAI TPAGVVNKYE VNGLQAWLIT HILWFVNAYL LSWFSPTIIF DNWIPLLWCA NILGYAVSTF AMIKGYLFPT SAEDCKFTGN FFYNYMMGIE FNPRIGKWFD FKLFFNGRPG IVAWTLINLS FAAKQQELYG HVTNSMILVN VLQAIYVLDF FWNETWYLKT IDICHDHFGW YLGWGDCVWL PYLYTLQGLY LVYHPVQLST PNALGILLLG LVGYYIFRMT NHQKDLFRRT DGRCLIWGKK PKAIECSYTS ADGLKHHSKL LVSGFWGVAR HFNYTGDLMG SLAYCLACGG GHLLPYFYII YMTILLTHRC LRDEHRCANK YGRDWERYTA AVPYRLLPGI F // ID DHDH_MOUSE Reviewed; 333 AA. AC Q9DBB8; Q14B09; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 19-FEB-2014, entry version 85. DE RecName: Full=Trans-1,2-dihydrobenzene-1,2-diol dehydrogenase; DE EC=1.3.1.20; DE AltName: Full=D-xylose 1-dehydrogenase; DE AltName: Full=D-xylose-NADP dehydrogenase; DE EC=1.1.1.179; DE AltName: Full=Dimeric dihydrodiol dehydrogenase; GN Name=Dhdh; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J, and NOD; TISSUE=Liver; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- CATALYTIC ACTIVITY: Trans-1,2-dihydrobenzene-1,2-diol + NADP(+) = CC catechol + NADPH. CC -!- CATALYTIC ACTIVITY: D-xylose + NADP(+) = D-xylono-1,5-lactone + CC NADPH. CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SIMILARITY: Belongs to the Gfo/Idh/MocA family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK005050; BAB23776.1; -; mRNA. DR EMBL; AK154452; BAE32596.1; -; mRNA. DR EMBL; BC116414; AAI16415.1; -; mRNA. DR RefSeq; NP_082179.1; NM_027903.3. DR UniGene; Mm.34208; -. DR ProteinModelPortal; Q9DBB8; -. DR SMR; Q9DBB8; 2-331. DR IntAct; Q9DBB8; 2. DR MINT; MINT-1869308; -. DR PaxDb; Q9DBB8; -. DR PRIDE; Q9DBB8; -. DR Ensembl; ENSMUST00000011526; ENSMUSP00000011526; ENSMUSG00000011382. DR GeneID; 71755; -. DR KEGG; mmu:71755; -. DR UCSC; uc009gvj.1; mouse. DR CTD; 27294; -. DR MGI; MGI:1919005; Dhdh. DR eggNOG; COG0673; -. DR GeneTree; ENSGT00390000007946; -. DR HOVERGEN; HBG105348; -. DR InParanoid; Q9DBB8; -. DR KO; K00078; -. DR OMA; KGMYWEA; -. DR OrthoDB; EOG78D7KF; -. DR TreeFam; TF324504; -. DR NextBio; 334417; -. DR PRO; PR:Q9DBB8; -. DR Bgee; Q9DBB8; -. DR CleanEx; MM_DHDH; -. DR Genevestigator; Q9DBB8; -. DR GO; GO:0047837; F:D-xylose 1-dehydrogenase (NADP+) activity; IDA:MGI. DR GO; GO:0047115; F:trans-1,2-dihydrobenzene-1,2-diol dehydrogenase activity; IEA:UniProtKB-EC. DR GO; GO:0042843; P:D-xylose catabolic process; IDA:MGI. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR000683; Oxidoreductase_N. DR InterPro; IPR004104; OxRdtase_C. DR Pfam; PF01408; GFO_IDH_MocA; 1. DR Pfam; PF02894; GFO_IDH_MocA_C; 1. PE 2: Evidence at transcript level; KW Complete proteome; NADP; Oxidoreductase; Reference proteome. FT CHAIN 1 333 Trans-1,2-dihydrobenzene-1,2-diol FT dehydrogenase. FT /FTId=PRO_0000315364. FT SITE 71 71 May play an important role in coenzyme FT binding (By similarity). FT SITE 79 79 May play an important role in coenzyme FT binding (By similarity). FT SITE 97 97 May play an important role in coenzyme FT binding (By similarity). FT SITE 176 176 May play an important role for the FT adaptation of the alcohol substrate into FT the binding site (By similarity). FT SITE 180 180 May play an important role in catalytic FT activity (By similarity). FT CONFLICT 115 115 S -> F (in Ref. 2; AAI16415). SQ SEQUENCE 333 AA; 36301 MW; 24CCCB8DB0423074 CRC64; MALRWGIVSA GLIANDFTTV LSSLPSSEHQ VVAVAARDLN RAEEFAQKFN IPKAYGSYEE LAKDPNVEVA YIATQHPQHK PAVLLCLAAG KAVLCEKPMG VNAAEVREMV AKARSQGVFL MEAIWSRFFP AMEALREVLV QGTIGDLRVA RAEFGFDLSH IPRATDWNQA GGGLLDLGIY CVQFLSMIFG AQKPEKISAV GRIHETGVDD TVSVLLQYPG GVHGSFTCSI SSNLPNTAYV SGTKGMAQIQ KLWAPTELVV NGERKEFPPP VLGKDYNFVN GSCMLYEANH VRECLRKGLK ESPVVPLAES ELLAEILEEA RKAIGVTFPQ DKR // ID DHB13_MOUSE Reviewed; 304 AA. AC Q8VCR2; A8Y5N6; Q8CIU2; DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot. DT 03-OCT-2012, sequence version 2. DT 19-MAR-2014, entry version 92. DE RecName: Full=17-beta-hydroxysteroid dehydrogenase 13; DE Short=17-beta-HSD 13; DE EC=1.1.-.-; DE AltName: Full=Alcohol dehydrogenase PAN1B-like; DE AltName: Full=Short-chain dehydrogenase/reductase 9; DE Flags: Precursor; GN Name=Hsd17b13; Synonyms=Scdr9; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RC STRAIN=BALB/c; RA Oliver P.L., Isaacs A.M., Davies K.E.; RL Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC STRAIN=FVB/N; TISSUE=Liver; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=17242355; DOI=10.1073/pnas.0609836104; RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; RT "Large-scale phosphorylation analysis of mouse liver."; RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). RN [6] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-79, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23576753; DOI=10.1073/pnas.1302961110; RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., RA Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.; RT "Label-free quantitative proteomics of the lysine acetylome in RT mitochondria identifies substrates of SIRT3 in metabolic pathways."; RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013). CC -!- SUBCELLULAR LOCATION: Secreted (Potential). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q8VCR2-1; Sequence=Displayed; CC Name=2; CC IsoId=Q8VCR2-2; Sequence=VSP_015861; CC Note=No experimental confirmation available; CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases CC (SDR) family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AY101768; AAM51176.1; -; mRNA. DR EMBL; AL714024; CAP19303.1; -; Genomic_DNA. DR EMBL; CH466529; EDL20237.1; -; Genomic_DNA. DR EMBL; BC019427; AAH19427.1; -; mRNA. DR RefSeq; NP_001156958.1; NM_001163486.1. DR RefSeq; NP_932147.2; NM_198030.2. DR UniGene; Mm.284944; -. DR ProteinModelPortal; Q8VCR2; -. DR SMR; Q8VCR2; 30-271. DR IntAct; Q8VCR2; 1. DR MINT; MINT-1862503; -. DR STRING; 10090.ENSMUSP00000046772; -. DR PhosphoSite; Q8VCR2; -. DR PaxDb; Q8VCR2; -. DR PRIDE; Q8VCR2; -. DR Ensembl; ENSMUST00000048118; ENSMUSP00000046772; ENSMUSG00000034528. [Q8VCR2-1] DR Ensembl; ENSMUST00000112803; ENSMUSP00000108422; ENSMUSG00000034528. [Q8VCR2-2] DR GeneID; 243168; -. DR KEGG; mmu:243168; -. DR UCSC; uc008yjw.2; mouse. DR CTD; 345275; -. DR MGI; MGI:2140804; Hsd17b13. DR eggNOG; COG1028; -. DR GeneTree; ENSGT00540000069900; -. DR HOVERGEN; HBG051352; -. DR InParanoid; Q8VCR2; -. DR OMA; KLFIPRR; -. DR OrthoDB; EOG7Z3F50; -. DR TreeFam; TF312837; -. DR NextBio; 385661; -. DR PRO; PR:Q8VCR2; -. DR ArrayExpress; Q8VCR2; -. DR CleanEx; MM_HSD17B13; -. DR Genevestigator; Q8VCR2; -. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR002198; DH_sc/Rdtase_SDR. DR InterPro; IPR002347; Glc/ribitol_DH. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Pfam; PF00106; adh_short; 1. DR PIRSF; PIRSF000126; 11-beta-HSD1; 1. DR PRINTS; PR00081; GDHRDH. DR PRINTS; PR00080; SDRFAMILY. PE 1: Evidence at protein level; KW Acetylation; Alternative splicing; Complete proteome; NAD; KW Oxidoreductase; Reference proteome; Secreted; Signal. FT SIGNAL 1 19 Potential. FT CHAIN 20 304 17-beta-hydroxysteroid dehydrogenase 13. FT /FTId=PRO_0000042584. FT NP_BIND 40 67 NAD (By similarity). FT ACT_SITE 185 185 Proton acceptor (By similarity). FT BINDING 172 172 Substrate (By similarity). FT BINDING 189 189 NAD (By similarity). FT MOD_RES 79 79 N6-acetyllysine. FT VAR_SEQ 272 304 GPGFSSKHPHGGSQQPVTPIPGDLTPSSDFLKH -> FLPE FT RALKAISRIQNIQFEAIVGHKTKMK (in isoform 2). FT /FTId=VSP_015861. FT CONFLICT 212 212 Q -> K (in Ref. 4; AAH19427). FT CONFLICT 266 266 S -> F (in Ref. 4; AAH19427). SQ SEQUENCE 304 AA; 33458 MW; 91D3A09C56024F01 CRC64; MNLILEFLLL VGVIIYSYLE SLVKFFIPRR RKSVTGQTVL ITGAGHGIGR LTAYEFAKQK SRLVLWDINK RGVEETADKC RKLGAVVHVF VVDCSNRAEI YNSVDQVKRE VGDVEIVVNN AGAIYPADLL SAKDEEITKT FEVNILGHFW IIKALLPSML RRNSGHIVTV ASVCGHGVIP YLIPYCSSKF AAVGFHRALT AELDTLGKTG IQTSCLCPVF VNTGFTKNPS TRLWPVLEPE EVARSLINGI LTNKKMIFVP SYINISLILE KGPGFSSKHP HGGSQQPVTP IPGDLTPSSD FLKH // ID DHE3_MOUSE Reviewed; 558 AA. AC P26443; Q8C273; DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1992, sequence version 1. DT 19-MAR-2014, entry version 129. DE RecName: Full=Glutamate dehydrogenase 1, mitochondrial; DE Short=GDH 1; DE EC=1.4.1.3; DE Flags: Precursor; GN Name=Glud1; Synonyms=Glud; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=BALB/c; TISSUE=Brain; RX PubMed=1711373; DOI=10.1016/0167-4781(91)90017-G; RA Tzimagiorgis G., Moschonas N.K.; RT "Molecular cloning, structure and expression analysis of a full-length RT mouse brain glutamate dehydrogenase cDNA."; RL Biochim. Biophys. Acta 1089:250-253(1991). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Olfactory bulb; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6; TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP PROTEIN SEQUENCE OF 61-76; 108-123; 125-136; 152-183; 192-200; RP 212-231; 275-318; 327-346; 353-363; 366-386; 400-420; 461-476; RP 481-496; 504-516; 528-545 AND 549-558. RC STRAIN=C57BL/6, and OF1; TISSUE=Brain, and Hippocampus; RA Lubec G., Klug S., Kang S.U., Sunyer B., Chen W.-Q.; RL Submitted (JAN-2009) to UniProtKB. RN [5] RP ADP-RIBOSYLATION. RX PubMed=16959573; DOI=10.1016/j.cell.2006.06.057; RA Haigis M.C., Mostoslavsky R., Haigis K.M., Fahie K., RA Christodoulou D.C., Murphy A.J., Valenzuela D.M., Yancopoulos G.D., RA Karow M., Blander G., Wolberger C., Prolla T.A., Weindruch R., RA Alt F.W., Guarente L.; RT "SIRT4 inhibits glutamate dehydrogenase and opposes the effects of RT calorie restriction in pancreatic beta cells."; RL Cell 126:941-954(2006). RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79 AND SER-128, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=17242355; DOI=10.1073/pnas.0609836104; RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; RT "Large-scale phosphorylation analysis of mouse liver."; RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-135, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain; RX PubMed=18034455; DOI=10.1021/pr0701254; RA Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.; RT "Large-scale identification and evolution indexing of tyrosine RT phosphorylation sites from murine brain."; RL J. Proteome Res. 7:311-318(2008). RN [8] RP FUNCTION, AND ADP-RIBOSYLATION. RX PubMed=23663782; DOI=10.1016/j.cell.2013.04.023; RA Csibi A., Fendt S.M., Li C., Poulogiannis G., Choo A.Y., Chapski D.J., RA Jeong S.M., Dempsey J.M., Parkhitko A., Morrison T., Henske E.P., RA Haigis M.C., Cantley L.C., Stephanopoulos G., Yu J., Blenis J.; RT "The mTORC1 pathway stimulates glutamine metabolism and cell RT proliferation by repressing SIRT4."; RL Cell 153:840-854(2013). RN [9] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-84; LYS-503; LYS-527 AND RP LYS-545, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-68; LYS-84; RP LYS-162; LYS-183; LYS-191; LYS-200; LYS-346; LYS-352; LYS-363; RP LYS-365; LYS-390; LYS-477; LYS-480; LYS-503; LYS-527 AND LYS-545, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic fibroblast, and Liver; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., RA Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). RN [10] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-84; LYS-90; LYS-110; RP LYS-162; LYS-171; LYS-187; LYS-191; LYS-211; LYS-326; LYS-346; RP LYS-352; LYS-363; LYS-365; LYS-390; LYS-399; LYS-415; LYS-457; RP LYS-477; LYS-480; LYS-503; LYS-527; LYS-545 AND LYS-548, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23576753; DOI=10.1073/pnas.1302961110; RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., RA Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.; RT "Label-free quantitative proteomics of the lysine acetylome in RT mitochondria identifies substrates of SIRT3 in metabolic pathways."; RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013). CC -!- FUNCTION: Mitochondrial glutamate dehydrogenase that converts L- CC glutamate into alpha-ketoglutarate. Plays a key role in glutamine CC anaplerosis by producing alpha-ketoglutarate, an important CC intermediate in the tricarboxylic acid cycle. May be involved in CC learning and memory reactions by increasing the turnover of the CC excitatory neurotransmitter glutamate. CC -!- CATALYTIC ACTIVITY: L-glutamate + H(2)O + NAD(P)(+) = 2- CC oxoglutarate + NH(3) + NAD(P)H. CC -!- ENZYME REGULATION: Subject to allosteric regulation. Activated by CC ADP. Inhibited by GTP and ATP. ADP can occupy the NADH binding CC site and activate the enzyme (By similarity). CC -!- SUBUNIT: Homohexamer. CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix. CC -!- PTM: Acetylation of Lys-84 is observed in liver mitochondria from CC fasted mice but not from fed mice. CC -!- PTM: ADP-ribosylated by SIRT4, leading to inactivate glutamate CC dehydrogenase activity. Stoichiometry shows that ADP-ribosylation CC occurs in one subunit per catalytically active homohexamer. CC -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X57024; CAA40341.1; -; mRNA. DR EMBL; AK089152; BAC40767.1; -; mRNA. DR EMBL; BC052724; AAH52724.1; -; mRNA. DR EMBL; BC057347; AAH57347.1; -; mRNA. DR PIR; S16239; S16239. DR RefSeq; NP_032159.1; NM_008133.4. DR UniGene; Mm.10600; -. DR ProteinModelPortal; P26443; -. DR SMR; P26443; 63-558. DR BioGrid; 199956; 4. DR IntAct; P26443; 9. DR MINT; MINT-1839447; -. DR PhosphoSite; P26443; -. DR REPRODUCTION-2DPAGE; P26443; -. DR SWISS-2DPAGE; P26443; -. DR UCD-2DPAGE; P26443; -. DR PaxDb; P26443; -. DR PRIDE; P26443; -. DR Ensembl; ENSMUST00000022322; ENSMUSP00000022322; ENSMUSG00000021794. DR GeneID; 14661; -. DR KEGG; mmu:14661; -. DR UCSC; uc007tas.2; mouse. DR CTD; 2746; -. DR MGI; MGI:95753; Glud1. DR eggNOG; COG0334; -. DR GeneTree; ENSGT00390000000854; -. DR HOGENOM; HOG000243801; -. DR HOVERGEN; HBG005479; -. DR InParanoid; P26443; -. DR KO; K00261; -. DR OMA; SGLEYTM; -. DR OrthoDB; EOG73NG50; -. DR TreeFam; TF313945; -. DR ChiTaRS; GLUD1; mouse. DR NextBio; 286534; -. DR PRO; PR:P26443; -. DR ArrayExpress; P26443; -. DR Bgee; P26443; -. DR Genevestigator; P26443; -. DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:MGI. DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004352; F:glutamate dehydrogenase (NAD+) activity; IEA:Ensembl. DR GO; GO:0004353; F:glutamate dehydrogenase [NAD(P)+] activity; IDA:UniProtKB. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0006541; P:glutamine metabolic process; IMP:UniProtKB. DR GO; GO:0007616; P:long-term memory; IEA:Ensembl. DR GO; GO:0032024; P:positive regulation of insulin secretion; IGI:MGI. DR GO; GO:0010044; P:response to aluminum ion; IEA:Ensembl. DR GO; GO:0072350; P:tricarboxylic acid metabolic process; IMP:UniProtKB. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR006095; Glu/Leu/Phe/Val_DH. DR InterPro; IPR006096; Glu/Leu/Phe/Val_DH_C. DR InterPro; IPR006097; Glu/Leu/Phe/Val_DH_dimer_dom. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Pfam; PF00208; ELFV_dehydrog; 1. DR Pfam; PF02812; ELFV_dehydrog_N; 1. DR PRINTS; PR00082; GLFDHDRGNASE. DR SMART; SM00839; ELFV_dehydrog; 1. DR PROSITE; PS00074; GLFV_DEHYDROGENASE; 1. PE 1: Evidence at protein level; KW Acetylation; ADP-ribosylation; ATP-binding; Complete proteome; KW Direct protein sequencing; GTP-binding; Mitochondrion; NADP; KW Nucleotide-binding; Oxidoreductase; Phosphoprotein; KW Reference proteome; Transit peptide. FT TRANSIT 1 53 Mitochondrion. FT CHAIN 54 558 Glutamate dehydrogenase 1, mitochondrial. FT /FTId=PRO_0000007212. FT NP_BIND 141 143 NAD (By similarity). FT ACT_SITE 183 183 By similarity. FT BINDING 147 147 Substrate (By similarity). FT BINDING 171 171 Substrate (By similarity). FT BINDING 176 176 NAD (By similarity). FT BINDING 252 252 NAD (By similarity). FT BINDING 266 266 GTP (By similarity). FT BINDING 270 270 GTP (By similarity). FT BINDING 319 319 GTP (By similarity). FT BINDING 322 322 GTP (By similarity). FT BINDING 438 438 Substrate (By similarity). FT BINDING 444 444 NAD (By similarity). FT BINDING 450 450 ADP (By similarity). FT BINDING 516 516 ADP (By similarity). FT MOD_RES 68 68 N6-succinyllysine. FT MOD_RES 79 79 Phosphoserine. FT MOD_RES 84 84 N6-acetyllysine; alternate. FT MOD_RES 84 84 N6-succinyllysine; alternate. FT MOD_RES 90 90 N6-acetyllysine. FT MOD_RES 110 110 N6-acetyllysine; alternate. FT MOD_RES 110 110 N6-succinyllysine; alternate (By FT similarity). FT MOD_RES 128 128 Phosphoserine. FT MOD_RES 135 135 Phosphotyrosine. FT MOD_RES 162 162 N6-acetyllysine; alternate. FT MOD_RES 162 162 N6-succinyllysine; alternate. FT MOD_RES 171 171 N6-acetyllysine. FT MOD_RES 172 172 ADP-ribosylcysteine (By similarity). FT MOD_RES 183 183 N6-acetyllysine; alternate (By FT similarity). FT MOD_RES 183 183 N6-succinyllysine; alternate. FT MOD_RES 187 187 N6-acetyllysine. FT MOD_RES 191 191 N6-acetyllysine; alternate. FT MOD_RES 191 191 N6-succinyllysine; alternate. FT MOD_RES 200 200 N6-succinyllysine. FT MOD_RES 211 211 N6-acetyllysine. FT MOD_RES 326 326 N6-acetyllysine. FT MOD_RES 346 346 N6-acetyllysine; alternate. FT MOD_RES 346 346 N6-succinyllysine; alternate. FT MOD_RES 352 352 N6-acetyllysine; alternate. FT MOD_RES 352 352 N6-succinyllysine; alternate. FT MOD_RES 363 363 N6-acetyllysine; alternate. FT MOD_RES 363 363 N6-succinyllysine; alternate. FT MOD_RES 365 365 N6-acetyllysine; alternate. FT MOD_RES 365 365 N6-succinyllysine; alternate. FT MOD_RES 386 386 N6-acetyllysine (By similarity). FT MOD_RES 390 390 N6-acetyllysine; alternate. FT MOD_RES 390 390 N6-succinyllysine; alternate. FT MOD_RES 399 399 N6-acetyllysine. FT MOD_RES 415 415 N6-acetyllysine; alternate. FT MOD_RES 415 415 N6-succinyllysine; alternate (By FT similarity). FT MOD_RES 457 457 N6-acetyllysine; alternate. FT MOD_RES 457 457 N6-malonyllysine; alternate (By FT similarity). FT MOD_RES 457 457 N6-succinyllysine; alternate (By FT similarity). FT MOD_RES 477 477 N6-acetyllysine; alternate. FT MOD_RES 477 477 N6-succinyllysine; alternate. FT MOD_RES 480 480 N6-acetyllysine; alternate. FT MOD_RES 480 480 N6-succinyllysine; alternate. FT MOD_RES 503 503 N6-acetyllysine; alternate. FT MOD_RES 503 503 N6-malonyllysine; alternate (By FT similarity). FT MOD_RES 503 503 N6-succinyllysine; alternate. FT MOD_RES 527 527 N6-acetyllysine; alternate. FT MOD_RES 527 527 N6-malonyllysine; alternate (By FT similarity). FT MOD_RES 527 527 N6-succinyllysine; alternate. FT MOD_RES 545 545 N6-acetyllysine; alternate. FT MOD_RES 545 545 N6-succinyllysine; alternate. FT MOD_RES 548 548 N6-acetyllysine. FT CONFLICT 495 495 D -> G (in Ref. 2; BAC40767). SQ SEQUENCE 558 AA; 61337 MW; 92738AA5A133838A CRC64; MYRRLGEALL LSRAGPAALG SAAADSAALL GWARGQPSAA PQPGLTPVAR RHYSEAAADR EDDPNFFKMV EGFFDRGASI VEDKLVEDLK TRESEEQKRN RVRGILRIIK PCNHVLSLSF PIRRDDGSWE VIEGYRAQHS QHRTPCKGGI RYSTDVSVDE VKALASLMTY KCAVVDVPFG GAKAGVKINP KNYTDNELEK ITRRFTMELA KKGFIGPGID VPAPDMSTGE REMSWIADTY ASTIGHYDIN AHACVTGKPI SQGGIHGRIS ATGRGVFHGI ENFINEASYM SILGMTPGFG DKTFVVQGFG NVGLHSMRYL HRFGAKCVGV GESDGSIWNP DGIDPKELED FKLQHGSILG FPKAKVYEGS ILEADCDILI PAASEKQLTK SNAPRVKAKI IAEGANGPTT PEADKIFLER NIMVIPDLYL NAGGVTVSYF EWLKNLNHVS YGRLTFKYER DSNYHLLMSV QESLERKFGK HGGTIPVVPT AEFQDRISGA SEKDIVHSGL AYTMERSARQ IMRTAMKYNL GLDLRTAAYV NAIEKVFKVY NEAGVTFT // ID DHI1_MOUSE Reviewed; 292 AA. AC P50172; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 19-FEB-2014, entry version 120. DE RecName: Full=Corticosteroid 11-beta-dehydrogenase isozyme 1; DE EC=1.1.1.146; DE AltName: Full=11-beta-hydroxysteroid dehydrogenase 1; DE Short=11-DH; DE Short=11-beta-HSD1; DE AltName: Full=11beta-HSD1A; GN Name=Hsd11b1; Synonyms=Hsd11; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=C57BL/6 X CBA; TISSUE=Liver; RX PubMed=7873449; DOI=10.1016/0960-0760(94)00159-J; RA Rajan V., Chapman K.E., Lyons V., Jamieson P., Mullins J.J., RA Edwards C.R., Seckl J.R.; RT "Cloning, sequencing and tissue-distribution of mouse 11 beta- RT hydroxysteroid dehydrogenase-1 cDNA."; RL J. Steroid Biochem. Mol. Biol. 52:141-147(1995). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=BALB/c; TISSUE=Liver; RX PubMed=7851387; DOI=10.1111/j.1432-1033.1995.tb20377.x; RA Oppermann U.C.T., Netter K.J., Maser E.; RT "Cloning and primary structure of murine 11 beta-hydroxysteroid RT dehydrogenase/microsomal carbonyl reductase."; RL Eur. J. Biochem. 227:202-208(1995). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-10. RX PubMed=8973338; DOI=10.1016/S0378-1119(96)00490-8; RA Voice M.W., Seckl J.R., Chapman K.E.; RT "The sequence of 5' flanking DNA from the mouse 11 beta-hydroxysteroid RT dehydrogenase type 1 gene and analysis of putative transcription RT factor binding sites."; RL Gene 181:233-235(1996). RN [4] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 24-291 IN COMPLEXES WITH NADP RP AND CORTICOSTERONE, AND SUBUNIT. RX PubMed=15865440; DOI=10.1021/bi047599q; RA Zhang J., Osslund T.D., Plant M.H., Clogston C.L., Nybo R.E., RA Xiong F., Delaney J.M., Jordan S.R.; RT "Crystal structure of murine 11 beta-hydroxysteroid dehydrogenase 1: RT an important therapeutic target for diabetes."; RL Biochemistry 44:6948-6957(2005). CC -!- FUNCTION: Catalyzes reversibly the conversion of cortisol to the CC inactive metabolite cortisone. CC -!- CATALYTIC ACTIVITY: An 11-beta-hydroxysteroid + NADP(+) = an 11- CC oxosteroid + NADPH. CC -!- SUBUNIT: Homodimer. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass CC type II membrane protein. CC -!- TISSUE SPECIFICITY: Widely expressed. Highest expression in liver. CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases CC (SDR) family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; S75207; AAB33601.1; -; mRNA. DR EMBL; X83202; CAA58209.1; -; mRNA. DR EMBL; X92186; CAA63096.1; -; Genomic_DNA. DR PIR; I56604; I56604. DR RefSeq; NP_001038216.1; NM_001044751.1. DR RefSeq; NP_032314.2; NM_008288.2. DR UniGene; Mm.28328; -. DR PDB; 1Y5M; X-ray; 2.30 A; A/B=24-291. DR PDB; 1Y5R; X-ray; 3.00 A; A/B=24-290. DR PDB; 3GMD; X-ray; 2.28 A; A/B/C/D/E/F/G/H=26-289. DR PDBsum; 1Y5M; -. DR PDBsum; 1Y5R; -. DR PDBsum; 3GMD; -. DR ProteinModelPortal; P50172; -. DR SMR; P50172; 25-289. DR IntAct; P50172; 7. DR MINT; MINT-1863132; -. DR BindingDB; P50172; -. DR ChEMBL; CHEMBL3910; -. DR PhosphoSite; P50172; -. DR PaxDb; P50172; -. DR PRIDE; P50172; -. DR Ensembl; ENSMUST00000016338; ENSMUSP00000016338; ENSMUSG00000016194. DR Ensembl; ENSMUST00000161737; ENSMUSP00000125620; ENSMUSG00000016194. DR GeneID; 15483; -. DR KEGG; mmu:15483; -. DR UCSC; uc007eef.1; mouse. DR CTD; 3290; -. DR MGI; MGI:103562; Hsd11b1. DR eggNOG; COG1028; -. DR HOGENOM; HOG000010276; -. DR HOVERGEN; HBG005481; -. DR InParanoid; P50172; -. DR KO; K15680; -. DR OMA; GLFMAYY; -. DR OrthoDB; EOG7353X9; -. DR TreeFam; TF329114; -. DR BRENDA; 1.1.1.146; 3474. DR EvolutionaryTrace; P50172; -. DR NextBio; 288336; -. DR PRO; PR:P50172; -. DR ArrayExpress; P50172; -. DR Bgee; P50172; -. DR CleanEx; MM_HSD11B1; -. DR Genevestigator; P50172; -. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0070524; F:11-beta-hydroxysteroid dehydrogenase (NADP+) activity; IEA:UniProtKB-EC. DR GO; GO:0003845; F:11-beta-hydroxysteroid dehydrogenase [NAD(P)] activity; IDA:MGI. DR GO; GO:0030324; P:lung development; IMP:MGI. DR GO; GO:0008202; P:steroid metabolic process; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR002198; DH_sc/Rdtase_SDR. DR InterPro; IPR002347; Glc/ribitol_DH. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR020904; Sc_DH/Rdtase_CS. DR Pfam; PF00106; adh_short; 1. DR PRINTS; PR00081; GDHRDH. DR PROSITE; PS00061; ADH_SHORT; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Endoplasmic reticulum; Glycoprotein; KW Lipid metabolism; Membrane; NADP; Oxidoreductase; Reference proteome; KW Signal-anchor; Steroid metabolism; Transmembrane; Transmembrane helix. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 292 Corticosteroid 11-beta-dehydrogenase FT isozyme 1. FT /FTId=PRO_0000054621. FT TOPO_DOM 2 7 Cytoplasmic (Potential). FT TRANSMEM 8 24 Helical; Signal-anchor for type II FT membrane protein; (Potential). FT TOPO_DOM 25 292 Lumenal (Potential). FT NP_BIND 41 67 NADP. FT NP_BIND 92 93 NADP. FT NP_BIND 119 121 NADP. FT NP_BIND 183 187 NADP. FT NP_BIND 216 222 NADP. FT ACT_SITE 183 183 Proton acceptor. FT BINDING 170 170 Substrate. FT CARBOHYD 162 162 N-linked (GlcNAc...) (Potential). FT CARBOHYD 207 207 N-linked (GlcNAc...) (Potential). FT CONFLICT 15 15 F -> S (in Ref. 2; CAA58209). FT CONFLICT 232 232 N -> D (in Ref. 2; CAA58209). FT CONFLICT 234 234 Q -> L (in Ref. 2; CAA58209). FT CONFLICT 261 261 S -> L (in Ref. 2; CAA58209). FT HELIX 29 32 FT STRAND 36 41 FT HELIX 45 57 FT STRAND 60 66 FT HELIX 68 81 FT STRAND 84 90 FT HELIX 96 110 FT STRAND 114 118 FT HELIX 133 143 FT HELIX 145 161 FT STRAND 164 170 FT HELIX 171 173 FT HELIX 181 203 FT STRAND 209 215 FT HELIX 221 227 FT TURN 228 230 FT HELIX 238 251 FT STRAND 254 258 FT HELIX 264 267 FT HELIX 271 279 FT HELIX 280 283 FT HELIX 286 288 SQ SEQUENCE 292 AA; 32364 MW; ADE42B11D82DD6CD CRC64; MAVMKNYLLP ILVLFLAYYY YSTNEEFRPE MLQGKKVIVT GASKGIGREM AYHLSKMGAH VVLTARSEEG LQKVVSRCLE LGAASAHYIA GTMEDMTFAE QFIVKAGKLM GGLDMLILNH ITQTSLSLFH DDIHSVRRVM EVNFLSYVVM STAALPMLKQ SNGSIAVISS LAGKMTQPMI APYSASKFAL DGFFSTIRTE LYITKVNVSI TLCVLGLIDT ETAMKEISGI INAQASPKEE CALEIIKGTA LRKSEVYYDK SPLTPILLGN PGRKIMEFFS LRYYNKDMFV SN // ID DHI2_MOUSE Reviewed; 386 AA. AC P51661; Q91WK3; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 30-APR-2003, sequence version 2. DT 19-MAR-2014, entry version 111. DE RecName: Full=Corticosteroid 11-beta-dehydrogenase isozyme 2; DE EC=1.1.1.-; DE AltName: Full=11-beta-hydroxysteroid dehydrogenase type 2; DE Short=11-DH2; DE Short=11-beta-HSD2; DE AltName: Full=NAD-dependent 11-beta-hydroxysteroid dehydrogenase; GN Name=Hsd11b2; Synonyms=Hsd11k; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=129/Sv; RX PubMed=7664690; DOI=10.1210/en.136.10.4693; RA Cole T.J.; RT "Cloning of the mouse 11 beta-hydroxysteroid dehydrogenase type 2 RT gene: tissue specific expression and localization in distal convoluted RT tubules and collecting ducts of the kidney."; RL Endocrinology 136:4693-4696(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Kidney; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: Catalyzes the conversion of cortisol to the inactive CC metabolite cortisone. Modulates intracellular glucocorticoid CC levels, thus protecting the nonselective mineralocorticoid CC receptor from occupation by glucocorticoids. CC -!- CATALYTIC ACTIVITY: An 11-beta-hydroxysteroid + NAD(+) = an 11- CC oxosteroid + NADH. CC -!- ENZYME REGULATION: Inhibited by glycyrrhetinic acid, carbenoloxone CC and 11-alpha-OH-progesterone (By similarity). CC -!- SUBUNIT: Interacts with ligand-free cytoplasmic NR3C2 (By CC similarity). CC -!- SUBCELLULAR LOCATION: Microsome. Endoplasmic reticulum CC (Potential). CC -!- TISSUE SPECIFICITY: Highly expressed in kidney. Also found in CC colon and small intestine. Not expressed in the adrenal gland. CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases CC (SDR) family. CC -!- SEQUENCE CAUTION: CC Sequence=CAA62219.1; Type=Frameshift; Positions=383; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; S79554; AAC60711.1; ALT_FRAME; Genomic_DNA. DR EMBL; S79550; AAC60711.1; JOINED; Genomic_DNA. DR EMBL; S79551; AAC60711.1; JOINED; Genomic_DNA. DR EMBL; S79552; AAC60711.1; JOINED; Genomic_DNA. DR EMBL; S79553; AAC60711.1; JOINED; Genomic_DNA. DR EMBL; X90646; CAA62218.1; -; Genomic_DNA. DR EMBL; X90647; CAA62219.1; ALT_FRAME; Genomic_DNA. DR EMBL; BC014753; AAH14753.1; -; mRNA. DR PIR; S60188; S60188. DR RefSeq; NP_032315.2; NM_008289.2. DR UniGene; Mm.5079; -. DR ProteinModelPortal; P51661; -. DR SMR; P51661; 3-339. DR IntAct; P51661; 3. DR MINT; MINT-4093038; -. DR BindingDB; P51661; -. DR ChEMBL; CHEMBL3490; -. DR PhosphoSite; P51661; -. DR PaxDb; P51661; -. DR PRIDE; P51661; -. DR Ensembl; ENSMUST00000034363; ENSMUSP00000034363; ENSMUSG00000031891. DR GeneID; 15484; -. DR KEGG; mmu:15484; -. DR UCSC; uc009nde.1; mouse. DR CTD; 3291; -. DR MGI; MGI:104720; Hsd11b2. DR eggNOG; COG1028; -. DR GeneTree; ENSGT00650000093222; -. DR HOVERGEN; HBG005482; -. DR InParanoid; P51661; -. DR KO; K00071; -. DR OMA; RSCMEVN; -. DR OrthoDB; EOG7FXZZX; -. DR TreeFam; TF325617; -. DR BRENDA; 1.1.1.146; 3474. DR NextBio; 288342; -. DR PRO; PR:P51661; -. DR ArrayExpress; P51661; -. DR Bgee; P51661; -. DR CleanEx; MM_HSD11B2; -. DR Genevestigator; P51661; -. DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell. DR GO; GO:0003845; F:11-beta-hydroxysteroid dehydrogenase [NAD(P)] activity; IEA:Ensembl. DR GO; GO:0051287; F:NAD binding; IEA:Ensembl. DR GO; GO:0005496; F:steroid binding; IEA:Ensembl. DR GO; GO:0007565; P:female pregnancy; IEA:Ensembl. DR GO; GO:0008211; P:glucocorticoid metabolic process; IEA:Ensembl. DR GO; GO:0002017; P:regulation of blood volume by renal aldosterone; IEA:Ensembl. DR GO; GO:0042493; P:response to drug; IEA:Ensembl. DR GO; GO:0032094; P:response to food; IEA:Ensembl. DR GO; GO:0051384; P:response to glucocorticoid; IEA:Ensembl. DR GO; GO:0001666; P:response to hypoxia; IEA:Ensembl. DR GO; GO:0032868; P:response to insulin; IEA:Ensembl. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR002198; DH_sc/Rdtase_SDR. DR InterPro; IPR002347; Glc/ribitol_DH. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR020904; Sc_DH/Rdtase_CS. DR Pfam; PF00106; adh_short; 1. DR PRINTS; PR00081; GDHRDH. DR PROSITE; PS00061; ADH_SHORT; 1. PE 2: Evidence at transcript level; KW Complete proteome; Endoplasmic reticulum; Microsome; NAD; KW Oxidoreductase; Reference proteome. FT CHAIN 1 386 Corticosteroid 11-beta-dehydrogenase FT isozyme 2. FT /FTId=PRO_0000054628. FT NP_BIND 82 111 NAD (By similarity). FT ACT_SITE 232 232 Proton acceptor (By similarity). FT BINDING 219 219 Substrate (By similarity). FT CONFLICT 49 49 Q -> L (in Ref. 1; AAC60711/CAA62218). FT CONFLICT 52 52 L -> M (in Ref. 1; AAC60711/CAA62218). FT CONFLICT 178 178 E -> G (in Ref. 1; AAC60711/CAA62218). FT CONFLICT 216 216 T -> P (in Ref. 1; AAC60711/CAA62218). FT CONFLICT 265 265 F -> S (in Ref. 1; AAC60711/CAA62218). FT CONFLICT 268 268 D -> A (in Ref. 1; AAC60711/CAA62218). FT CONFLICT 297 297 E -> A (in Ref. 1; AAC60711/CAA62218). SQ SEQUENCE 386 AA; 42187 MW; 687FD253568487AB CRC64; MERWPWPSGG AWLLVAARAL LQLLRSDLRL GRPLLAALAL LAALDWLCQR LLPPPAALVV LAGAGWIALS RLARPPRLPV ATRAVLITGC DTGFGKETAK KLDAMGFTVL ATVLDLNSPG ALELRDLCSP RLKLLQMDLT KAEDISRVLE ITKAHTASTG LWGLVNNAGL NIVVADVELS PVATFRKCME VNFFGALELT KGLLPLLRHS RGRIVTVGSP AGDMPYPCLA AYGTSKAAIA LLMDTFGCEL LPWGIKVSII KPGCFKTDAV TNVNLWEKRK QLLLANIPRE LLQAYGEDYI EHVHGQFLNS LRMALPDLSP VVDAIIDALL AAQPRSRYYP GRGLGLMYFI HHYLPEGLRR CFLQNFFINH LLPRALRPGQ HGPAPA // ID DHPR_MOUSE Reviewed; 241 AA. AC Q8BVI4; Q3TT09; Q9D0K4; DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot. DT 12-APR-2005, sequence version 2. DT 19-MAR-2014, entry version 93. DE RecName: Full=Dihydropteridine reductase; DE EC=1.5.1.34; DE AltName: Full=HDHPR; DE AltName: Full=Quinoid dihydropteridine reductase; GN Name=Qdpr; Synonyms=Dhpr; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Medulla oblongata; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Mammary tumor; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP PROTEIN SEQUENCE OF 77-93; 125-135; 165-188 AND 218-233, AND MASS RP SPECTROMETRY. RC STRAIN=C57BL/6; TISSUE=Brain, and Hippocampus; RA Lubec G., Klug S., Kang S.U.; RL Submitted (APR-2007) to UniProtKB. RN [4] RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-70; LYS-76; LYS-93 AND RP LYS-99, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Liver; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., RA Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). CC -!- FUNCTION: The product of this enzyme, tetrahydrobiopterin (BH-4), CC is an essential cofactor for phenylalanine, tyrosine, and CC tryptophan hydroxylases (By similarity). CC -!- CATALYTIC ACTIVITY: A 5,6,7,8-tetrahydropteridine + NAD(P)(+) = a CC 6,7-dihydropteridine + NAD(P)H. CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases CC (SDR) family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK011351; BAB27559.1; -; mRNA. DR EMBL; AK078123; BAC37135.1; -; mRNA. DR EMBL; AK159107; BAE34823.1; -; mRNA. DR EMBL; AK161660; BAE36516.1; -; mRNA. DR EMBL; AK166694; BAE38951.1; -; mRNA. DR EMBL; BC002107; AAH02107.1; -; mRNA. DR RefSeq; NP_077198.1; NM_024236.2. DR UniGene; Mm.30204; -. DR ProteinModelPortal; Q8BVI4; -. DR SMR; Q8BVI4; 6-241. DR IntAct; Q8BVI4; 5. DR MINT; MINT-2513757; -. DR STRING; 10090.ENSMUSP00000015950; -. DR PhosphoSite; Q8BVI4; -. DR REPRODUCTION-2DPAGE; Q8BVI4; -. DR PaxDb; Q8BVI4; -. DR PRIDE; Q8BVI4; -. DR Ensembl; ENSMUST00000015950; ENSMUSP00000015950; ENSMUSG00000015806. DR GeneID; 110391; -. DR KEGG; mmu:110391; -. DR UCSC; uc008xix.2; mouse. DR CTD; 5860; -. DR MGI; MGI:97836; Qdpr. DR eggNOG; COG1028; -. DR GeneTree; ENSGT00390000000470; -. DR HOGENOM; HOG000232194; -. DR HOVERGEN; HBG001000; -. DR InParanoid; Q8BVI4; -. DR KO; K00357; -. DR OMA; SDLMWKQ; -. DR OrthoDB; EOG7060RV; -. DR TreeFam; TF105932; -. DR NextBio; 363915; -. DR PRO; PR:Q8BVI4; -. DR ArrayExpress; Q8BVI4; -. DR Bgee; Q8BVI4; -. DR CleanEx; MM_QDPR; -. DR Genevestigator; Q8BVI4; -. DR GO; GO:0005829; C:cytosol; IEA:Ensembl. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR GO; GO:0043005; C:neuron projection; IEA:Ensembl. DR GO; GO:0004155; F:6,7-dihydropteridine reductase activity; ISS:UniProtKB. DR GO; GO:0070404; F:NADH binding; IEA:Ensembl. DR GO; GO:0070402; F:NADPH binding; IEA:Ensembl. DR GO; GO:0035690; P:cellular response to drug; IEA:Ensembl. DR GO; GO:0006559; P:L-phenylalanine catabolic process; IEA:Ensembl. DR GO; GO:0001889; P:liver development; IEA:Ensembl. DR GO; GO:0010044; P:response to aluminum ion; IEA:Ensembl. DR GO; GO:0033762; P:response to glucagon; IEA:Ensembl. DR GO; GO:0010288; P:response to lead ion; IEA:Ensembl. DR GO; GO:0006729; P:tetrahydrobiopterin biosynthetic process; ISS:UniProtKB. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR002198; DH_sc/Rdtase_SDR. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR020904; Sc_DH/Rdtase_CS. DR Pfam; PF00106; adh_short; 1. DR PROSITE; PS00061; ADH_SHORT; 1. PE 1: Evidence at protein level; KW Complete proteome; Direct protein sequencing; NADP; Oxidoreductase; KW Reference proteome; Tetrahydrobiopterin biosynthesis. FT CHAIN 1 241 Dihydropteridine reductase. FT /FTId=PRO_0000054637. FT NP_BIND 11 35 NADP (By similarity). FT ACT_SITE 147 147 Proton acceptor (By similarity). FT MOD_RES 70 70 N6-succinyllysine. FT MOD_RES 76 76 N6-succinyllysine. FT MOD_RES 93 93 N6-succinyllysine. FT MOD_RES 99 99 N6-succinyllysine. FT CONFLICT 167 167 G -> D (in Ref. 1; BAC37135). SQ SEQUENCE 241 AA; 25570 MW; 2ED25295D38C494B CRC64; MAASGEARRV LVYGGRGALG SRCVQAFRAR NWWVASIDVV ENEEASASVV VKMTDSFTEQ ADQVTADVGK LLGDQKVDAI LCVAGGWAGG NAKSKSLFKN CDMMWKQSMW TSTISSHLAT KHLKEGGLLT LAGAKAALDG TPGMIGYGMA KGAVHQLCQS LAGKNSGMPP GAAAIAVLPV TLDTPMNRKS MPEADFSSWT PLEFLVETFH DWITGNKRPN SGSLIQVVTT DGKTELTPAY F // ID DHR11_MOUSE Reviewed; 260 AA. AC Q3U0B3; Q5SXB3; Q8R249; DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2005, sequence version 1. DT 19-FEB-2014, entry version 80. DE RecName: Full=Dehydrogenase/reductase SDR family member 11; DE EC=1.-.-.-; DE Flags: Precursor; GN Name=Dhrs11; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=NOD; TISSUE=Spleen; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Colon; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- SUBUNIT: Homotetramer. CC -!- SUBCELLULAR LOCATION: Secreted (Potential). CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases CC (SDR) family. CC -!- CAUTION: It is uncertain whether Met-1 or Met-6 is the initiator. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK157041; BAE33942.1; -; mRNA. DR EMBL; AL596083; CAI24984.2; -; Genomic_DNA. DR EMBL; BC022224; AAH22224.2; -; mRNA. DR RefSeq; NP_808232.2; NM_177564.5. DR UniGene; Mm.192213; -. DR ProteinModelPortal; Q3U0B3; -. DR SMR; Q3U0B3; 3-256. DR PhosphoSite; Q3U0B3; -. DR PaxDb; Q3U0B3; -. DR PRIDE; Q3U0B3; -. DR Ensembl; ENSMUST00000047560; ENSMUSP00000043467; ENSMUSG00000034449. DR GeneID; 192970; -. DR KEGG; mmu:192970; -. DR UCSC; uc007kqs.2; mouse. DR CTD; 79154; -. DR MGI; MGI:2652816; Dhrs11. DR eggNOG; COG4221; -. DR GeneTree; ENSGT00730000110967; -. DR HOVERGEN; HBG105262; -. DR InParanoid; Q3U0B3; -. DR OMA; CGHRVPP; -. DR OrthoDB; EOG74XS69; -. DR TreeFam; TF324174; -. DR NextBio; 371394; -. DR PRO; PR:Q3U0B3; -. DR ArrayExpress; Q3U0B3; -. DR Bgee; Q3U0B3; -. DR CleanEx; MM_BC022224; -. DR Genevestigator; Q3U0B3; -. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR002198; DH_sc/Rdtase_SDR. DR InterPro; IPR002347; Glc/ribitol_DH. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Pfam; PF00106; adh_short; 1. DR PRINTS; PR00081; GDHRDH. DR PRINTS; PR00080; SDRFAMILY. PE 2: Evidence at transcript level; KW Complete proteome; NADP; Oxidoreductase; Reference proteome; Secreted; KW Signal. FT SIGNAL 1 30 Potential. FT CHAIN 31 260 Dehydrogenase/reductase SDR family member FT 11. FT /FTId=PRO_0000045491. FT NP_BIND 69 71 NADP (By similarity). FT NP_BIND 166 170 NADP (By similarity). FT NP_BIND 198 208 NADP (By similarity). FT ACT_SITE 166 166 Proton acceptor (By similarity). FT BINDING 151 151 Substrate (By similarity). SQ SEQUENCE 260 AA; 28274 MW; D26E6B4F4877EB86 CRC64; MTRAGMERWR DRLALVTGAS GGIGAAVARA LVQQGLKVVG CARTVGNIEE LAAECKSAGY PGTLIPYRCD LSNEEDILSM FSAVRSQHSG VDICINNAGM ARPDTLLSGS TSGWKDMFNV NVLALSICTR EAYQSMKERN IDDGHIININ SMCGHRVPPQ SVIHFYSATK YAVTALTEGL RQELLEAQTH IRATCISPGL VETQFAFKLH DKDPGEAAAT YEHIKCLRPE DVAEAVIYVL STPPHVQVGD IQMRPTEQVT // ID DHR13_MOUSE Reviewed; 376 AA. AC Q5SS80; Q14BH2; Q8BMX8; DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot. DT 21-DEC-2004, sequence version 1. DT 19-MAR-2014, entry version 73. DE RecName: Full=Dehydrogenase/reductase SDR family member 13; DE EC=1.1.-.-; DE Flags: Precursor; GN Name=Dhrs13; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC STRAIN=C57BL/6J; TISSUE=Embryo; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: Putative oxidoreductase (Potential). CC -!- SUBCELLULAR LOCATION: Secreted (Potential). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q5SS80-1; Sequence=Displayed; CC Name=2; CC IsoId=Q5SS80-2; Sequence=VSP_029641; CC Note=No experimental confirmation available; CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases CC (SDR) family. CC -!- SEQUENCE CAUTION: CC Sequence=BAC25347.1; Type=Frameshift; Positions=254, 256, 270, 290; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK011939; BAC25347.1; ALT_FRAME; mRNA. DR EMBL; AL669840; CAI25703.1; -; Genomic_DNA. DR EMBL; BC115881; AAI15882.1; -; mRNA. DR RefSeq; NP_899109.2; NM_183286.2. DR UniGene; Mm.390342; -. DR ProteinModelPortal; Q5SS80; -. DR SMR; Q5SS80; 31-315. DR PhosphoSite; Q5SS80; -. DR PaxDb; Q5SS80; -. DR PRIDE; Q5SS80; -. DR Ensembl; ENSMUST00000021187; ENSMUSP00000021187; ENSMUSG00000020834. [Q5SS80-1] DR GeneID; 70451; -. DR KEGG; mmu:70451; -. DR UCSC; uc007khu.1; mouse. [Q5SS80-1] DR CTD; 147015; -. DR MGI; MGI:1917701; Dhrs13. DR eggNOG; COG1028; -. DR GeneTree; ENSGT00570000078948; -. DR HOVERGEN; HBG078800; -. DR InParanoid; Q5SS80; -. DR KO; K11169; -. DR OMA; CGRTRET; -. DR OrthoDB; EOG73Z2TK; -. DR TreeFam; TF105429; -. DR NextBio; 331649; -. DR PRO; PR:Q5SS80; -. DR ArrayExpress; Q5SS80; -. DR Bgee; Q5SS80; -. DR CleanEx; MM_DHRS13; -. DR Genevestigator; Q5SS80; -. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR002198; DH_sc/Rdtase_SDR. DR InterPro; IPR002347; Glc/ribitol_DH. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Pfam; PF00106; adh_short; 1. DR PRINTS; PR00081; GDHRDH. PE 2: Evidence at transcript level; KW Alternative splicing; Complete proteome; NAD; NADP; Oxidoreductase; KW Reference proteome; Secreted; Signal. FT SIGNAL 1 25 Potential. FT CHAIN 26 376 Dehydrogenase/reductase SDR family member FT 13. FT /FTId=PRO_0000311921. FT NP_BIND 43 49 NAD or NADP (By similarity). FT COMPBIAS 317 330 Asp/Glu-rich. FT ACT_SITE 197 197 Proton acceptor (By similarity). FT BINDING 170 170 Substrate (Potential). FT VAR_SEQ 1 91 Missing (in isoform 2). FT /FTId=VSP_029641. FT CONFLICT 240 240 P -> R (in Ref. 1; BAC25347). SQ SEQUENCE 376 AA; 40745 MW; B4C77A8058948865 CRC64; MEMLLLGAGL LLGAYVLVYY NLVKAPSCGG IGSLRGRTVV VTGANSGIGK MTALELARRG ARVVLACRSR ERGEAAAFDL RQESGNNEVI FMALDLASLA SVQAFATAFL SSEPRLDVLI HNAGISSCGR TRETFNLLLR VNHVGPFLLT HLLLPRLRSC APSRVVIVSS AAHRRGRLDF TRLDCPVVGW QQELRAYADS KLANVLFARE LATQLEGTGV TCYAAHPGPV NSELFLRHLP GWLRPILRPL AWLVLRAPQG GAQTPLYCAL QEGIEPLSGR YFANCHVEEV SPAARDDQAA QRLWKATKKL AGLAPGDDDD DPDEEPEPED PRAPSSQSAP SPEKTTVSGP SHSYQGSQDL SKLTQRRIQV KDEPTP // ID DHRS1_MOUSE Reviewed; 313 AA. AC Q99L04; Q3THW0; Q9D148; DT 10-OCT-2003, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 19-MAR-2014, entry version 91. DE RecName: Full=Dehydrogenase/reductase SDR family member 1; DE EC=1.1.-.-; GN Name=Dhrs1; Synonyms=D14ertd484e; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J, and DBA/2; TISSUE=Embryo; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Mammary tumor; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases CC (SDR) family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK003958; BAB23093.1; -; mRNA. DR EMBL; AK146317; BAE27072.1; -; mRNA. DR EMBL; AK168115; BAE40086.1; -; mRNA. DR EMBL; AK168147; BAE40112.1; -; mRNA. DR EMBL; BC003930; AAH03930.1; -; mRNA. DR RefSeq; NP_081095.2; NM_026819.3. DR RefSeq; XP_006519322.1; XM_006519259.1. DR UniGene; Mm.21623; -. DR ProteinModelPortal; Q99L04; -. DR SMR; Q99L04; 3-262. DR IntAct; Q99L04; 1. DR MINT; MINT-1863592; -. DR PhosphoSite; Q99L04; -. DR PaxDb; Q99L04; -. DR PRIDE; Q99L04; -. DR DNASU; 52585; -. DR Ensembl; ENSMUST00000002403; ENSMUSP00000002403; ENSMUSG00000002332. DR GeneID; 52585; -. DR KEGG; mmu:52585; -. DR UCSC; uc007uan.2; mouse. DR CTD; 115817; -. DR MGI; MGI:1196314; Dhrs1. DR eggNOG; COG1028; -. DR GeneTree; ENSGT00720000108845; -. DR HOVERGEN; HBG051351; -. DR InParanoid; Q99L04; -. DR KO; K11163; -. DR OMA; QVDREQQ; -. DR OrthoDB; EOG72ZCFC; -. DR TreeFam; TF314146; -. DR NextBio; 309171; -. DR PRO; PR:Q99L04; -. DR Bgee; Q99L04; -. DR CleanEx; MM_DHRS1; -. DR Genevestigator; Q99L04; -. DR GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl. DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:MGI. DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR002198; DH_sc/Rdtase_SDR. DR InterPro; IPR002347; Glc/ribitol_DH. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Pfam; PF00106; adh_short; 1. DR PRINTS; PR00081; GDHRDH. PE 2: Evidence at transcript level; KW Complete proteome; Oxidoreductase; Reference proteome. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 313 Dehydrogenase/reductase SDR family member FT 1. FT /FTId=PRO_0000054641. FT ACT_SITE 163 163 Proton acceptor (By similarity). FT BINDING 151 151 Substrate (By similarity). FT CONFLICT 194 194 G -> R (in Ref. 1; BAB23093). FT CONFLICT 304 304 W -> L (in Ref. 1; BAB23093). SQ SEQUENCE 313 AA; 34005 MW; 60E05BD7911BDC0C CRC64; MVAPMKGQVC VVTGASRGIG RGIALQLCKA GATVYITGRH LDTLRATAQE AQSLGGRCVP VVCDSSQESE VKSLFEQVDR EQKGRLDVLV NNAYAGVQAI LNTTNKSFWE VPASIWDDIN NVGLRGHYLC SVYGARLMVP AGKGLIVIVS SPGGLQHMFN VPYGVGKAAC DRLAADCAHE LRRHGVSYVS LWPGLVQTEM VKEFMAKEDT PEDPLFKKMK PDFSSAESPE MSGKCVVALA TDPNILNLSG KVLPSCDLAR RYGLKDIDGR PVKDYFSLGY ALSQVSSLGW LNSFLPGFLR VPKWVVTLYN SKF // ID DHRS7_MOUSE Reviewed; 338 AA. AC Q9CXR1; DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot. DT 29-AUG-2003, sequence version 2. DT 19-MAR-2014, entry version 99. DE RecName: Full=Dehydrogenase/reductase SDR family member 7; DE EC=1.1.-.-; DE AltName: Full=Retinal short-chain dehydrogenase/reductase 4; DE Short=retSDR4; DE Flags: Precursor; GN Name=Dhrs7; Synonyms=Retsdr4; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Embryonic head; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Mammary tumor; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases CC (SDR) family. CC -!- SEQUENCE CAUTION: CC Sequence=AAH16189.1; Type=Erroneous initiation; CC Sequence=BAB29156.1; Type=Frameshift; Positions=11, 15; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK014100; BAB29156.1; ALT_FRAME; mRNA. DR EMBL; BC016189; AAH16189.1; ALT_INIT; mRNA. DR RefSeq; NP_079798.2; NM_025522.5. DR UniGene; Mm.289653; -. DR ProteinModelPortal; Q9CXR1; -. DR SMR; Q9CXR1; 46-310. DR IntAct; Q9CXR1; 1. DR MINT; MINT-4093056; -. DR STRING; 10090.ENSMUSP00000021512; -. DR PhosphoSite; Q9CXR1; -. DR PaxDb; Q9CXR1; -. DR PRIDE; Q9CXR1; -. DR Ensembl; ENSMUST00000021512; ENSMUSP00000021512; ENSMUSG00000021094. DR GeneID; 66375; -. DR KEGG; mmu:66375; -. DR UCSC; uc007nvs.2; mouse. DR CTD; 51635; -. DR MGI; MGI:1913625; Dhrs7. DR eggNOG; COG0300; -. DR GeneTree; ENSGT00740000115336; -. DR HOVERGEN; HBG054346; -. DR InParanoid; Q9CXR1; -. DR KO; K11165; -. DR OMA; MSWELLL; -. DR OrthoDB; EOG7W6WM5; -. DR TreeFam; TF354276; -. DR NextBio; 321485; -. DR Bgee; Q9CXR1; -. DR CleanEx; MM_DHRS7; -. DR Genevestigator; Q9CXR1; -. DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR002198; DH_sc/Rdtase_SDR. DR InterPro; IPR002347; Glc/ribitol_DH. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR020904; Sc_DH/Rdtase_CS. DR Pfam; PF00106; adh_short; 1. DR PIRSF; PIRSF000126; 11-beta-HSD1; 1. DR PRINTS; PR00081; GDHRDH. DR PRINTS; PR00080; SDRFAMILY. DR PROSITE; PS00061; ADH_SHORT; 1. PE 2: Evidence at transcript level; KW Complete proteome; NAD; Oxidoreductase; Reference proteome; Signal. FT SIGNAL 1 28 Potential. FT CHAIN 29 338 Dehydrogenase/reductase SDR family member FT 7. FT /FTId=PRO_0000031969. FT NP_BIND 54 78 NAD (By similarity). FT ACT_SITE 203 203 Proton acceptor (By similarity). FT BINDING 190 190 Substrate (By similarity). FT CONFLICT 10 10 L -> R (in Ref. 1). SQ SEQUENCE 338 AA; 38167 MW; 5D12F0117BD1070D CRC64; MSWELLLWLL ALCALILPLV QLLRFLRADA DLTLLWAEWQ GRRPEWELTD MVVWVTGASS GIGEELAFQL SKLGVSLVLS ARRAQELERV KRRCLENGNL KEKDILVLPL DLTDTSSHEA ATKAVLQEFG KIDILVNNGG RSQRSLVLET NLDVFKELIN LNYIGTVSLT KCVLPHMIER KQGKIVTVNS IAGIASVSLS SGYCASKHAL RGFFNALHSE LGQYPGITFC NVYPGPVQSD IVKNAFTEEV TKSMRNNIDQ SYKMPTSRCV RLMLISMAND LKEVWISDHP VLLGAYIWQY MPTWAAWLNC KLGKERIQNF KNNLDPDLPY KFLKAKKD // ID DHRS4_MOUSE Reviewed; 279 AA. AC Q99LB2; G3X8V7; Q9EQU4; DT 10-OCT-2003, integrated into UniProtKB/Swiss-Prot. DT 03-OCT-2012, sequence version 3. DT 19-MAR-2014, entry version 101. DE RecName: Full=Dehydrogenase/reductase SDR family member 4; DE EC=1.1.1.184; DE AltName: Full=NADPH-dependent carbonyl reductase/NADP-retinol dehydrogenase; DE Short=CR; DE Short=PHCR; DE AltName: Full=NADPH-dependent retinol dehydrogenase/reductase; DE Short=NDRD; DE Short=mouNRDR; DE AltName: Full=Peroxisomal short-chain alcohol dehydrogenase; DE Short=PSCD; GN Name=Dhrs4; Synonyms=D14Ucla2; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=C57BL/6; TISSUE=Liver; RA Furukawa A., Ohnishi T., Huang D., Araki N., Ichikawa Y.; RT "cDNA cloning and characterization of peroxisomal short-chain RT dehydrogenase / reductase that reduce all-trans retinal to retinol."; RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Mammary tumor; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-93; LYS-217; LYS-228 AND RP LYS-235, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Liver; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., RA Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). RN [6] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-93; LYS-106 AND LYS-217, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23576753; DOI=10.1073/pnas.1302961110; RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., RA Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.; RT "Label-free quantitative proteomics of the lysine acetylome in RT mitochondria identifies substrates of SIRT3 in metabolic pathways."; RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013). CC -!- FUNCTION: Reduces all-trans-retinal and 9-cis retinal. Can also CC catalyze the oxidation of all-trans-retinol with NADP as co- CC factor, but with much lower efficiency. Reduces alkyl phenyl CC ketones and alpha-dicarbonyl compounds with aromatic rings, such CC as pyrimidine-4-aldehyde, 3-benzoylpyridine, 4-benzoylpyridine, CC menadione and 4-hexanoylpyridine. Has no activity towards CC aliphatic aldehydes and ketones (By similarity). CC -!- CATALYTIC ACTIVITY: R-CHOH-R' + NADP(+) = R-CO-R' + NADPH. CC -!- SUBUNIT: Homotetramer (By similarity). CC -!- SUBCELLULAR LOCATION: Peroxisome (By similarity). CC -!- MISCELLANEOUS: Inhibited by kaempferol, quercetin, genistein and CC myristic acid (By similarity). CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases CC (SDR) family. CC -!- SEQUENCE CAUTION: CC Sequence=AAH03484.1; Type=Erroneous initiation; Note=Translation N-terminally extended; CC Sequence=BAB18776.1; Type=Erroneous initiation; Note=Translation N-terminally extended; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AB045132; BAB18776.1; ALT_INIT; mRNA. DR EMBL; AC159002; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH466535; EDL36299.1; -; Genomic_DNA. DR EMBL; BC003484; AAH03484.1; ALT_INIT; mRNA. DR EMBL; BC054361; AAH54361.1; -; mRNA. DR RefSeq; NP_001033027.2; NM_001037938.2. DR UniGene; Mm.27427; -. DR ProteinModelPortal; Q99LB2; -. DR SMR; Q99LB2; 26-279. DR IntAct; Q99LB2; 5. DR MINT; MINT-1861432; -. DR PhosphoSite; Q99LB2; -. DR PaxDb; Q99LB2; -. DR PRIDE; Q99LB2; -. DR Ensembl; ENSMUST00000022821; ENSMUSP00000022821; ENSMUSG00000022210. DR GeneID; 28200; -. DR KEGG; mmu:28200; -. DR UCSC; uc007tym.2; mouse. DR CTD; 10901; -. DR MGI; MGI:90169; Dhrs4. DR eggNOG; COG1028; -. DR GeneTree; ENSGT00740000115208; -. DR HOVERGEN; HBG105779; -. DR InParanoid; Q99LB2; -. DR KO; K11147; -. DR OMA; SHSFMAI; -. DR OrthoDB; EOG73Z2VD; -. DR TreeFam; TF315405; -. DR NextBio; 306800; -. DR PRO; PR:Q99LB2; -. DR ArrayExpress; Q99LB2; -. DR CleanEx; MM_DHRS4; -. DR Genevestigator; Q99LB2; -. DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB. DR GO; GO:0005777; C:peroxisome; IDA:MGI. DR GO; GO:0004090; F:carbonyl reductase (NADPH) activity; IEA:UniProtKB-EC. DR GO; GO:0001758; F:retinal dehydrogenase activity; IDA:MGI. DR GO; GO:0042574; P:retinal metabolic process; IDA:MGI. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR002198; DH_sc/Rdtase_SDR. DR InterPro; IPR002347; Glc/ribitol_DH. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR020904; Sc_DH/Rdtase_CS. DR PRINTS; PR00081; GDHRDH. DR PRINTS; PR00080; SDRFAMILY. DR PROSITE; PS00061; ADH_SHORT; 1. PE 1: Evidence at protein level; KW Acetylation; Complete proteome; NADP; Oxidoreductase; Peroxisome; KW Reference proteome. FT CHAIN 1 279 Dehydrogenase/reductase SDR family member FT 4. FT /FTId=PRO_0000054648. FT NP_BIND 37 61 NADP (By similarity). FT MOTIF 277 279 Microbody targeting signal. FT ACT_SITE 183 183 Proton acceptor (By similarity). FT BINDING 170 170 Substrate (By similarity). FT MOD_RES 93 93 N6-acetyllysine; alternate. FT MOD_RES 93 93 N6-succinyllysine; alternate. FT MOD_RES 106 106 N6-acetyllysine. FT MOD_RES 217 217 N6-acetyllysine; alternate. FT MOD_RES 217 217 N6-succinyllysine; alternate. FT MOD_RES 228 228 N6-succinyllysine. FT MOD_RES 235 235 N6-succinyllysine. FT CONFLICT 109 109 Q -> R (in Ref. 4; AAH03484/AAH54361). SQ SEQUENCE 279 AA; 29885 MW; 985668BDE2935072 CRC64; MQKAGRLLGG WTQAWMSVRM ASSGLTRRNP LSNKVALVTA STDGIGFAIA RRLAEDGAHV VVSSRKQQNV DRAVATLQGE GLSVTGIVCH VGKAEDREKL ITTALKRHQG IDILVSNAAV NPFFGNLMDV TEEVWDKVLS INVTATAMMI KAVVPEMEKR GGGSVVIVGS VAGFTRFPSL GPYNVSKTAL LGLTKNFAAE LAPKNIRVNC LAPGLIKTRF SSVLWEEKAR EDFIKEAMQI RRLGKPEDCA GIVSFLCSED ASYINGETVV VGGGTPSRL // ID DHRS3_MOUSE Reviewed; 302 AA. AC O88876; Q3UAD1; Q91WR0; Q91XC3; Q922A6; DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot. DT 10-MAY-2004, sequence version 2. DT 19-MAR-2014, entry version 110. DE RecName: Full=Short-chain dehydrogenase/reductase 3; DE EC=1.1.1.300; DE AltName: Full=Retinal short-chain dehydrogenase/reductase 1; DE Short=retSDR1; GN Name=Dhrs3; Synonyms=Rsdr1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Retina; RX PubMed=9705317; DOI=10.1074/jbc.273.34.21790; RA Haeseleer F., Huang J., Lebioda L., Saari J.C., Palczewski K.; RT "Molecular characterization of a novel short-chain RT dehydrogenase/reductase that reduces all-trans-retinal."; RL J. Biol. Chem. 273:21790-21799(1998). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY. RC TISSUE=Mesenchymal cell; RX PubMed=9853961; RX DOI=10.1002/(SICI)1097-0177(199812)213:4<398::AID-AJA5>3.3.CO;2-K; RA Baechner D., Ahrens M., Schroeder D., Hoffmann A., Lauber J., RA Betat N., Steinert P., Flohe L., Gross G.; RT "Bmp-2 downstream targets in mesenchymal development identified by RT subtractive cloning from recombinant mesenchymal progenitors RT (C3H10T1/2)."; RL Dev. Dyn. 213:398-411(1998). RN [3] RP NUCLEOTIDE SEQUENCE (ISOFORM 1). RC TISSUE=Retina; RA Haeseleer F., Palczewski K.; RT "Structure of retinal short-chain dehydrogenase/reductase retSDR1 RT gene."; RL Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC STRAIN=C57BL/6J; TISSUE=Bone marrow, and Mesonephros; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Colon, Kidney, and Mammary gland; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: Catalyzes the reduction of all-trans-retinal to all- CC trans-retinol in the presence of NADPH (By similarity). CC -!- CATALYTIC ACTIVITY: All-trans-retinol + NADP(+) = all-trans- CC retinal + NADPH. CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein CC (Potential). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=O88876-1; Sequence=Displayed; CC Name=2; CC IsoId=O88876-2; Sequence=VSP_050734, VSP_050735; CC Note=No experimental confirmation available; CC -!- TISSUE SPECIFICITY: In the embryo, expressed in developing CC osteogenic and chondrogenic tissues of vertebra, rib, tooth and CC limb bud. CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases CC (SDR) family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF061743; AAC63265.1; -; mRNA. DR EMBL; X95281; CAA64602.1; -; mRNA. DR EMBL; AF179241; AAD55403.1; -; Genomic_DNA. DR EMBL; AF179238; AAD55403.1; JOINED; Genomic_DNA. DR EMBL; AF179239; AAD55403.1; JOINED; Genomic_DNA. DR EMBL; AF179240; AAD55403.1; JOINED; Genomic_DNA. DR EMBL; AK032958; BAC28098.1; -; mRNA. DR EMBL; AK151419; BAE30384.1; -; mRNA. DR EMBL; BC008980; AAH08980.1; -; mRNA. DR EMBL; BC010972; AAH10972.1; -; mRNA. DR EMBL; BC013540; AAH13540.1; -; mRNA. DR RefSeq; NP_001165895.1; NM_001172424.1. DR RefSeq; NP_035433.1; NM_011303.6. DR UniGene; Mm.14063; -. DR ProteinModelPortal; O88876; -. DR SMR; O88876; 34-290. DR PhosphoSite; O88876; -. DR PaxDb; O88876; -. DR PRIDE; O88876; -. DR DNASU; 20148; -. DR Ensembl; ENSMUST00000105744; ENSMUSP00000101370; ENSMUSG00000066026. [O88876-2] DR Ensembl; ENSMUST00000154208; ENSMUSP00000122552; ENSMUSG00000066026. [O88876-1] DR GeneID; 20148; -. DR KEGG; mmu:20148; -. DR UCSC; uc008vrn.2; mouse. [O88876-1] DR CTD; 9249; -. DR MGI; MGI:1315215; Dhrs3. DR eggNOG; COG1028; -. DR GeneTree; ENSGT00540000069900; -. DR HOVERGEN; HBG051352; -. DR InParanoid; O88876; -. DR KO; K11146; -. DR OMA; WTMHALI; -. DR OrthoDB; EOG7Z3F50; -. DR TreeFam; TF312837; -. DR NextBio; 297657; -. DR PRO; PR:O88876; -. DR ArrayExpress; O88876; -. DR Bgee; O88876; -. DR CleanEx; MM_DHRS3; -. DR Genevestigator; O88876; -. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0052650; F:NADP-retinol dehydrogenase activity; IEA:UniProtKB-EC. DR GO; GO:0042572; P:retinol metabolic process; IEA:GOC. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR002198; DH_sc/Rdtase_SDR. DR InterPro; IPR002347; Glc/ribitol_DH. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Pfam; PF00106; adh_short; 1. DR PIRSF; PIRSF000126; 11-beta-HSD1; 1. DR PRINTS; PR00081; GDHRDH. DR PRINTS; PR00080; SDRFAMILY. PE 2: Evidence at transcript level; KW Alternative splicing; Complete proteome; Membrane; NADP; KW Oxidoreductase; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 302 Short-chain dehydrogenase/reductase 3. FT /FTId=PRO_0000054645. FT TRANSMEM 9 29 Helical; (Potential). FT TRANSMEM 170 190 Helical; (Potential). FT TRANSMEM 195 215 Helical; (Potential). FT TRANSMEM 258 278 Helical; (Potential). FT ACT_SITE 188 188 Proton acceptor (By similarity). FT BINDING 175 175 Substrate (By similarity). FT VAR_SEQ 1 26 Missing (in isoform 2). FT /FTId=VSP_050734. FT VAR_SEQ 114 153 Missing (in isoform 2). FT /FTId=VSP_050735. FT CONFLICT 68 68 L -> F (in Ref. 5; AAH10972). FT CONFLICT 234 234 F -> L (in Ref. 1 and 3). SQ SEQUENCE 302 AA; 33652 MW; E530F36877C3C610 CRC64; MVWKWLGALV VFPLQMIYLV TKAAVGMVLP PKLRDLSRES VLITGGGRGI GRHLAREFAE RGARKIVLWG RTEKCLKETT EEIRQMGTEC HYFICDVGNR EEVYQMAKAV REKVGDITIL VNNAAVVHGK SLMDSDDDAL LKSQHVNTLG QFWTTKAFLP RMLELQNGHI VCLNSVLALS AIPGAIDYCT SKASAFAFME SLTLGLLDCP GVSATTVLPF HTSTEMFQGM RVRFPNLFPP LKPETVARRT VDAVQQNQAL LLLPWTMNIL IILKSILPQA ALEEIHRFSG TYTCMNTFKG RT // ID DHRSX_MOUSE Reviewed; 335 AA. AC Q8VBZ0; B2RRV9; Q3TZW6; DT 03-JUL-2003, integrated into UniProtKB/Swiss-Prot. DT 09-JAN-2007, sequence version 2. DT 19-MAR-2014, entry version 82. DE RecName: Full=Dehydrogenase/reductase SDR family member on chromosome X homolog; DE EC=1.1.-.-; DE AltName: Full=DHRSXY; DE AltName: Full=SCAD family protein; DE Flags: Precursor; GN Name=Dhrsx; Synonyms=Pscad; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=NOD; TISSUE=Spleen; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-280. RC STRAIN=FVB/N; TISSUE=Embryo; RX PubMed=11731500; DOI=10.1101/gr.197001; RA Gianfrancesco F., Sanges R., Esposito T., Tempesta S., Rao E., RA Rappold G., Archidiacono N., Graves J.A.M., Forabosco A., D'Urso M.; RT "Differential divergence of three human pseudoautosomal genes and RT their mouse homologs: implications for sex chromosome evolution."; RL Genome Res. 11:2095-2100(2001). CC -!- MISCELLANEOUS: Autosomal gene, which is the ortholog of human CC DHRSX, located at the termini of the long and short arms of the X CC and Y chromosomes. CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases CC (SDR) family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK157461; BAE34091.1; -; mRNA. DR EMBL; BC138597; AAI38598.1; -; mRNA. DR EMBL; BC138599; AAI38600.1; -; mRNA. DR EMBL; AJ296079; CAC82539.1; -; mRNA. DR UniGene; Mm.305345; -. DR ProteinModelPortal; Q8VBZ0; -. DR SMR; Q8VBZ0; 2-327. DR PaxDb; Q8VBZ0; -. DR PRIDE; Q8VBZ0; -. DR UCSC; uc009vdc.1; mouse. DR MGI; MGI:2181510; Dhrsx. DR eggNOG; COG1028; -. DR HOVERGEN; HBG078800; -. DR InParanoid; B2RRV9; -. DR PRO; PR:Q8VBZ0; -. DR CleanEx; MM_DHRSX; -. DR Genevestigator; Q8VBZ0; -. DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR002198; DH_sc/Rdtase_SDR. DR InterPro; IPR002347; Glc/ribitol_DH. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR020904; Sc_DH/Rdtase_CS. DR Pfam; PF00106; adh_short; 1. DR PRINTS; PR00081; GDHRDH. DR PROSITE; PS00061; ADH_SHORT; 1. PE 2: Evidence at transcript level; KW Complete proteome; Oxidoreductase; Reference proteome; Signal. FT SIGNAL 1 23 Potential. FT CHAIN 24 335 Dehydrogenase/reductase SDR family member FT on chromosome X homolog. FT /FTId=PRO_0000031975. FT NP_BIND 47 71 NAD or NADP (By similarity). FT COMPBIAS 157 163 Poly-Leu. FT ACT_SITE 208 208 Proton acceptor (By similarity). FT BINDING 183 183 Substrate (By similarity). FT CONFLICT 131 131 G -> A (in Ref. 3; CAC82539). FT CONFLICT 186 186 H -> Q (in Ref. 3; CAC82539). FT CONFLICT 247 247 L -> M (in Ref. 3; CAC82539). SQ SEQUENCE 335 AA; 35957 MW; A191AC1BA9065F85 CRC64; MSTLRALRAV LCVYAVGIAV ALAQLLRRLR GDFRPPVLPP QPGRVAIVTG ATAGIGRSTA RQLARLGMCV VVAGNDEHRG QEVVSSIRAE MGSDRAHFLP LDLASLASVR GFARDFQALG LPLHLLVNNA GVMLEPRAET EDGFERHLGV NFLGHFLLTL LLLPALRASG AEGRGSRVVT VGSATHYVGT VDMADLHGRH AYSPYAAYAQ SKLALALFAL QLQRILDARG DPVTSNMADP GVVDTELYRH AGWVLRTAKR FLGWLVFKSP EEGAWTLVYA AAAPELEGVG GRYLRDEAEA EPLGTARDQE LQRRLWAEGL RLTGAGGGDS DGVAW // ID DHRS9_MOUSE Reviewed; 319 AA. AC Q58NB6; Q8BGC7; DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot. DT 25-OCT-2005, sequence version 2. DT 19-MAR-2014, entry version 82. DE RecName: Full=Dehydrogenase/reductase SDR family member 9; DE EC=1.1.-.-; DE AltName: Full=3-alpha hydroxysteroid dehydrogenase; DE Short=3-alpha-HSD; DE AltName: Full=Short-chain dehydrogenase/reductase retSDR8; DE Flags: Precursor; GN Name=Dhrs9; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Eye; RX PubMed=10800688; DOI=10.1016/S0076-6879(00)16736-9; RA Haeseleer F., Palczewski K.; RT "Short-chain dehydrogenases/reductases in retina."; RL Methods Enzymol. 316:372-383(2000). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=BALB/c; TISSUE=Uterus; RA Plumley H.C., Rexer B.N., Li X.-H., Ong D.E.; RT "Mouse homolog of rat epithelial retinol dehydrogenase."; RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Adipose tissue, and Liver; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). CC -!- FUNCTION: 3-alpha-hydroxysteroid dehydrogenase that converts 3- CC alpha-tetrahydroprogesterone (allopregnanolone) to CC dihydroxyprogesterone and 3-alpha-androstanediol to CC dihydroxyprogesterone. May play a role in the biosynthesis of CC retinoic acid from retinaldehyde, but seems to have low activity CC with retinoids. Can utilize both NADH and NADPH (By similarity). CC -!- SUBUNIT: Homotetramer (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Microsome CC membrane (By similarity). Endoplasmic reticulum membrane (By CC similarity). Note=Associated with microsomal membranes (By CC similarity). CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases CC (SDR) family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF361479; AAN75755.1; -; mRNA. DR EMBL; AK050180; BAC34110.1; -; mRNA. DR EMBL; AK080914; BAC38075.1; -; mRNA. DR EMBL; AY936479; AAX33670.1; -; mRNA. DR RefSeq; NP_780721.1; NM_175512.2. DR UniGene; Mm.211655; -. DR ProteinModelPortal; Q58NB6; -. DR SMR; Q58NB6; 26-285. DR IntAct; Q58NB6; 1. DR MINT; MINT-4110286; -. DR PhosphoSite; Q58NB6; -. DR PaxDb; Q58NB6; -. DR PRIDE; Q58NB6; -. DR Ensembl; ENSMUST00000063690; ENSMUSP00000069631; ENSMUSG00000027068. DR GeneID; 241452; -. DR KEGG; mmu:241452; -. DR UCSC; uc008jyb.1; mouse. DR CTD; 10170; -. DR MGI; MGI:2442798; Dhrs9. DR eggNOG; COG1028; -. DR GeneTree; ENSGT00650000093222; -. DR HOVERGEN; HBG005482; -. DR InParanoid; Q58NB6; -. DR KO; K11149; -. DR OMA; FLCAFLW; -. DR OrthoDB; EOG7FXZZX; -. DR TreeFam; TF325617; -. DR NextBio; 385011; -. DR PRO; PR:Q58NB6; -. DR ArrayExpress; Q58NB6; -. DR Bgee; Q58NB6; -. DR CleanEx; MM_DHRS9; -. DR Genevestigator; Q58NB6; -. DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; ISS:UniProtKB. DR GO; GO:0004022; F:alcohol dehydrogenase (NAD) activity; ISS:UniProtKB. DR GO; GO:0004745; F:retinol dehydrogenase activity; ISS:UniProtKB. DR GO; GO:0047035; F:testosterone dehydrogenase (NAD+) activity; ISS:UniProtKB. DR GO; GO:0042904; P:9-cis-retinoic acid biosynthetic process; ISS:UniProtKB. DR GO; GO:0008209; P:androgen metabolic process; IEA:Ensembl. DR GO; GO:0042448; P:progesterone metabolic process; IEA:Ensembl. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR002198; DH_sc/Rdtase_SDR. DR InterPro; IPR002347; Glc/ribitol_DH. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Pfam; PF00106; adh_short; 1. DR PRINTS; PR00081; GDHRDH. DR PRINTS; PR00080; SDRFAMILY. PE 2: Evidence at transcript level; KW Complete proteome; Cytoplasm; Endoplasmic reticulum; Membrane; KW Microsome; NAD; NADP; Oxidoreductase; Reference proteome; Signal. FT SIGNAL 1 20 Potential. FT CHAIN 21 319 Dehydrogenase/reductase SDR family member FT 9. FT /FTId=PRO_0000042618. FT NP_BIND 34 58 NAD (By similarity). FT ACT_SITE 176 176 Proton acceptor (By similarity). FT BINDING 83 83 NAD (By similarity). FT BINDING 164 164 Substrate (By similarity). FT BINDING 180 180 NAD (By similarity). FT CONFLICT 3 5 FWL -> LWV (in Ref. 2; AAX33670). FT CONFLICT 292 292 I -> L (in Ref. 2; AAX33670). FT CONFLICT 317 317 K -> Q (in Ref. 2; AAX33670). SQ SEQUENCE 319 AA; 35242 MW; A8111F84ED57BB19 CRC64; MLFWLLALLF LCAFLWNYKG QLKIADIADK YVFITGCDTG FGNLAARTFD KKGFRVIAAC LTESGSAALK AKTSERLHTV LLDVTDPENV KKTAQWVKSH VGEKGLWGLI NNAGVLGVLA PTDWLTVDDY REPIEVNLFG LINVTLNMLP LVKKARGRVI NVSSIGGRLA FGGGGYTPSK YAVEGFNDSL RRDMKAFGVH VSCIEPGLFK TELADPIKTT EKKLAIWKHL SPDIKQQYGE GYIEKSLHRL KSNTSSVNLD LSLVVGCMDH ALTSLFPKTR YIAGKDAKTF WIPLSHMPAV LQDFLLLKQK VELANPKAV // ID DHSO_MOUSE Reviewed; 357 AA. AC Q64442; Q569V5; Q9CPS0; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 10-JUL-2007, sequence version 3. DT 19-MAR-2014, entry version 139. DE RecName: Full=Sorbitol dehydrogenase; DE EC=1.1.1.14; DE AltName: Full=L-iditol 2-dehydrogenase; GN Name=Sord; Synonyms=Sdh1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY. RC STRAIN=BALB/c; TISSUE=Liver; RX PubMed=7601136; DOI=10.1111/j.1432-1033.1995.tb20656.x; RA Lee F.K., Lee A.Y.W., Lin C.X.F., Chung S.S.-M., Chung S.K.; RT "Cloning, sequencing, and determination of the sites of expression of RT mouse sorbitol dehydrogenase cDNA."; RL Eur. J. Biochem. 230:1059-1065(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Blastocyst, Lung, and Testis; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Kidney, and Liver; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-169, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=18630941; DOI=10.1021/pr800223m; RA Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.; RT "Specific phosphopeptide enrichment with immobilized titanium ion RT affinity chromatography adsorbent for phosphoproteome analysis."; RL J. Proteome Res. 7:3957-3967(2008). RN [6] RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL RP STAGE. RX PubMed=18799757; DOI=10.1095/biolreprod.108.068882; RA Cao W., Aghajanian H.K., Haig-Ladewig L.A., Gerton G.L.; RT "Sorbitol can fuel mouse sperm motility and protein tyrosine RT phosphorylation via sorbitol dehydrogenase."; RL Biol. Reprod. 80:124-133(2009). CC -!- FUNCTION: Converts sorbitol to fructose. Part of the polyol CC pathway that plays an important role in sperm physiology. May play CC a role in the sperm motility by providing an energetic source for CC sperm. CC -!- CATALYTIC ACTIVITY: L-iditol + NAD(+) = L-sorbose + NADH. CC -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity). CC -!- SUBUNIT: Homotetramer (By similarity). CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane; Peripheral membrane CC protein. Cell projection, cilium, flagellum. Note=Associated with CC mitochondria of the midpiece and near the plasma membrane in the CC principal piece of the flagellum. Also found in the epididymosome, CC secreted by the epididymal epithelium and that transfers proteins CC from the epididymal fluid to the sperm surface. CC -!- TISSUE SPECIFICITY: Testis has the highest level of expression, CC followed by kidney, liver, and lung. Low levels of expression are CC also observed in lens, brain, and skeletal muscle. Expressed in CC sperm flagellum and very low expression in the sperm head. CC -!- DEVELOPMENTAL STAGE: Detected early in spermatogenesis. Detected CC in condensing spermatids (at protein level) and is up-regulated CC during late spermatogenesis. CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase CC family. CC -!- SEQUENCE CAUTION: CC Sequence=AAA79043.1; Type=Erroneous initiation; Note=Translation N-terminally shortened; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U27014; AAA79043.1; ALT_INIT; mRNA. DR EMBL; AK004692; BAB23478.1; -; mRNA. DR EMBL; AK015059; BAB29695.1; -; mRNA. DR EMBL; AK166988; BAE39168.1; -; mRNA. DR EMBL; AK166996; BAE39175.1; -; mRNA. DR EMBL; AL844566; CAM16325.1; -; Genomic_DNA. DR EMBL; AL844573; CAM16325.1; JOINED; Genomic_DNA. DR EMBL; AL844573; CAM19389.1; -; Genomic_DNA. DR EMBL; AL844566; CAM19389.1; JOINED; Genomic_DNA. DR EMBL; BC024124; AAH24124.1; -; mRNA. DR EMBL; BC030875; AAH30875.1; -; mRNA. DR EMBL; BC092291; AAH92291.1; -; mRNA. DR PIR; S65956; S65956. DR RefSeq; NP_666238.1; NM_146126.4. DR UniGene; Mm.371580; -. DR UniGene; Mm.471786; -. DR ProteinModelPortal; Q64442; -. DR SMR; Q64442; 7-357. DR IntAct; Q64442; 5. DR MINT; MINT-1869750; -. DR PhosphoSite; Q64442; -. DR REPRODUCTION-2DPAGE; IPI00753038; -. DR REPRODUCTION-2DPAGE; Q64442; -. DR PaxDb; Q64442; -. DR PRIDE; Q64442; -. DR Ensembl; ENSMUST00000110551; ENSMUSP00000106180; ENSMUSG00000027227. DR GeneID; 20322; -. DR KEGG; mmu:20322; -. DR UCSC; uc008maj.1; mouse. DR CTD; 6652; -. DR MGI; MGI:98266; Sord. DR eggNOG; COG1063; -. DR GeneTree; ENSGT00550000074781; -. DR HOGENOM; HOG000294670; -. DR HOVERGEN; HBG005484; -. DR InParanoid; Q64442; -. DR KO; K00008; -. DR OMA; LKCDKND; -. DR OrthoDB; EOG7DRJ36; -. DR TreeFam; TF313060; -. DR NextBio; 298123; -. DR PRO; PR:Q64442; -. DR ArrayExpress; Q64442; -. DR Bgee; Q64442; -. DR CleanEx; MM_SORD; -. DR Genevestigator; Q64442; -. DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB. DR GO; GO:0031514; C:motile cilium; IDA:UniProtKB. DR GO; GO:0003939; F:L-iditol 2-dehydrogenase activity; IDA:MGI. DR GO; GO:0051287; F:NAD binding; IEA:Ensembl. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0046370; P:fructose biosynthetic process; IEA:Ensembl. DR GO; GO:0051160; P:L-xylitol catabolic process; IEA:Ensembl. DR GO; GO:0006062; P:sorbitol catabolic process; IEA:Ensembl. DR GO; GO:0006060; P:sorbitol metabolic process; IDA:MGI. DR GO; GO:0030317; P:sperm motility; IDA:UniProtKB. DR Gene3D; 3.40.50.720; -; 1. DR Gene3D; 3.90.180.10; -; 1. DR InterPro; IPR013149; ADH_C. DR InterPro; IPR013154; ADH_GroES-like. DR InterPro; IPR002085; ADH_SF_Zn-type. DR InterPro; IPR002328; ADH_Zn_CS. DR InterPro; IPR011032; GroES-like. DR InterPro; IPR016040; NAD(P)-bd_dom. DR PANTHER; PTHR11695; PTHR11695; 1. DR Pfam; PF08240; ADH_N; 1. DR Pfam; PF00107; ADH_zinc_N; 1. DR SUPFAM; SSF50129; SSF50129; 1. DR PROSITE; PS00059; ADH_ZINC; 1. PE 1: Evidence at protein level; KW Acetylation; Cell projection; Cilium; Complete proteome; Flagellum; KW Membrane; Metal-binding; Mitochondrion; NAD; Oxidoreductase; KW Phosphoprotein; Reference proteome; Zinc. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 357 Sorbitol dehydrogenase. FT /FTId=PRO_0000000882. FT METAL 45 45 Zinc; catalytic (By similarity). FT METAL 70 70 Zinc; catalytic (By similarity). FT METAL 71 71 Zinc; catalytic (By similarity). FT BINDING 51 51 Substrate (By similarity). FT BINDING 156 156 Substrate (By similarity). FT BINDING 299 299 Substrate (By similarity). FT BINDING 300 300 Substrate (By similarity). FT MOD_RES 2 2 N-acetylalanine (By similarity). FT MOD_RES 169 169 Phosphoserine. FT CONFLICT 49 49 V -> L (in Ref. 1; AAA79043). FT CONFLICT 259 259 T -> S (in Ref. 1; AAA79043). SQ SEQUENCE 357 AA; 38249 MW; FDAA462EF1EB6C21 CRC64; MAAPAKGENL SLVVHGPGDI RLENYPIPEL GPNDVLLKMH SVGICGSDVH YWEHGRIGDF VVKKPMVLGH EAAGTVTKVG ELVKHLKPGD RVAIEPGVPR EVDEYCKIGR YNLTPTIFFC ATPPDDGNLC RFYKHNADFC YKLPDSVTFE EGALIEPLSV GIYACRRGSV SLGNKVLVCG AGPVGMVTLL VAKAMGAAQV VVTDLSASRL TKAKEVGADF TIQVGKETPQ EIASKVESLL GSKPEVTIEC TGAESSVQTG IYATHSGGTL VIVGMGAEMV NLPLVHAAIR EVDIKGVFRY CNTWPMAISM LASKTLNVKP LVTHRFPLEK AVEAFETAKK GVGLKVMIKC DPNDQNP // ID DHTK1_MOUSE Reviewed; 921 AA. AC A2ATU0; Q0VFY3; Q69ZE3; Q8BWT3; DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot. DT 20-FEB-2007, sequence version 1. DT 19-MAR-2014, entry version 57. DE RecName: Full=Probable 2-oxoglutarate dehydrogenase E1 component DHKTD1, mitochondrial; DE EC=1.2.4.2; DE AltName: Full=Dehydrogenase E1 and transketolase domain-containing protein 1; DE Flags: Precursor; GN Name=Dhtkd1; Synonyms=Kiaa1630; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 330-587. RC TISSUE=Brain; RX PubMed=15368895; DOI=10.1093/dnares/11.3.205; RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H., RA Nagase T., Ohara O., Koga H.; RT "Prediction of the coding sequences of mouse homologues of KIAA gene: RT IV. The complete nucleotide sequences of 500 mouse KIAA-homologous RT cDNAs identified by screening of terminal sequences of cDNA clones RT randomly sampled from size-fractionated libraries."; RL DNA Res. 11:205-218(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 525-921. RC STRAIN=C57BL/6J; TISSUE=Liver; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [5] RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-184; LYS-189; LYS-801 AND RP LYS-819, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Liver; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., RA Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). CC -!- FUNCTION: The 2-oxoglutarate dehydrogenase complex catalyzes the CC overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). It CC contains multiple copies of three enzymatic components: 2- CC oxoglutarate dehydrogenase (E1), dihydrolipoamide CC succinyltransferase (E2) and lipoamide dehydrogenase (E3) (By CC similarity). CC -!- CATALYTIC ACTIVITY: 2-oxoglutarate + [dihydrolipoyllysine-residue CC succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue CC succinyltransferase] S-succinyldihydrolipoyllysine + CO(2). CC -!- COFACTOR: Thiamine pyrophosphate (By similarity). CC -!- SUBCELLULAR LOCATION: Mitochondrion (By similarity). CC -!- SIMILARITY: Belongs to the alpha-ketoglutarate dehydrogenase CC family. CC -!- SEQUENCE CAUTION: CC Sequence=BAD32501.1; Type=Miscellaneous discrepancy; Note=Intron retention; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AL928924; CAM20352.1; -; Genomic_DNA. DR EMBL; BC117994; AAI17995.1; -; mRNA. DR EMBL; AK173223; BAD32501.1; ALT_SEQ; mRNA. DR EMBL; AK050057; BAC34055.1; -; mRNA. DR RefSeq; NP_001074600.1; NM_001081131.2. DR UniGene; Mm.222517; -. DR ProteinModelPortal; A2ATU0; -. DR SMR; A2ATU0; 60-919. DR IntAct; A2ATU0; 2. DR MINT; MINT-1839549; -. DR PhosphoSite; A2ATU0; -. DR PaxDb; A2ATU0; -. DR PRIDE; A2ATU0; -. DR Ensembl; ENSMUST00000026924; ENSMUSP00000026924; ENSMUSG00000025815. DR Ensembl; ENSMUST00000095147; ENSMUSP00000092769; ENSMUSG00000025815. DR Ensembl; ENSMUST00000169865; ENSMUSP00000129194; ENSMUSG00000025815. DR GeneID; 209692; -. DR KEGG; mmu:209692; -. DR UCSC; uc008iga.1; mouse. DR CTD; 55526; -. DR MGI; MGI:2445096; Dhtkd1. DR eggNOG; COG0567; -. DR GeneTree; ENSGT00530000063092; -. DR HOGENOM; HOG000259586; -. DR HOVERGEN; HBG001892; -. DR InParanoid; A2ATU0; -. DR KO; K15791; -. DR OMA; LCSGKHY; -. DR OrthoDB; EOG7CZK4Z; -. DR TreeFam; TF314198; -. DR ChiTaRS; DHTKD1; mouse. DR NextBio; 372765; -. DR PRO; PR:A2ATU0; -. DR Bgee; A2ATU0; -. DR Genevestigator; A2ATU0; -. DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB. DR GO; GO:0004591; F:oxoglutarate dehydrogenase (succinyl-transferring) activity; IEA:UniProtKB-EC. DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro. DR GO; GO:0006091; P:generation of precursor metabolites and energy; ISS:UniProtKB. DR GO; GO:0006096; P:glycolysis; IEA:UniProtKB-KW. DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro. DR InterPro; IPR011603; 2oxoglutarate_DH_E1. DR InterPro; IPR001017; DH_E1. DR InterPro; IPR005475; Transketolase-like_Pyr-bd. DR PANTHER; PTHR23152; PTHR23152; 1. DR Pfam; PF00676; E1_dh; 1. DR Pfam; PF02779; Transket_pyr; 1. DR PIRSF; PIRSF000157; Oxoglu_dh_E1; 1. DR SMART; SM00861; Transket_pyr; 1. DR TIGRFAMs; TIGR00239; 2oxo_dh_E1; 1. PE 1: Evidence at protein level; KW Complete proteome; Glycolysis; Mitochondrion; Oxidoreductase; KW Reference proteome; Thiamine pyrophosphate; Transit peptide. FT TRANSIT 1 ? Mitochondrion (Potential). FT CHAIN ? 921 Probable 2-oxoglutarate dehydrogenase E1 FT component DHKTD1, mitochondrial. FT /FTId=PRO_0000307937. FT MOD_RES 184 184 N6-succinyllysine. FT MOD_RES 189 189 N6-succinyllysine. FT MOD_RES 801 801 N6-succinyllysine. FT MOD_RES 819 819 N6-succinyllysine. FT CONFLICT 24 24 G -> S (in Ref. 2; AAI17995). FT CONFLICT 436 436 H -> R (in Ref. 2; AAI17995). SQ SEQUENCE 921 AA; 102793 MW; E40170D7D26EED65 CRC64; MASAATVAAA GRALRRAVLL LRRGYQTERG VYGYRPRKAK SGEPRGDRAR PSVDHGLARL VTVYCEHGHK AAQINPLFPG QALLDTVPEI QALVRTLQGP FTTTGLLNLG KEAASLEEVL AYLNHIYCGP ISIETAQLQS QEERDWFARR FEELKKETFT TEERKYLSKL LLESQEFDHF LATKFATVKR YGGEGAESMM GFFHELLKLS AYGGITDIII GMPHRGRLNL LTGLLQLPPE LMFRKMRGLS EFPENVATIG DVLSHLTSSV DLDFGAHQPL HVTMLPNPSH LEAVNPVAVG KTRGRQQSRE DGDYSPNGSA QPGDKVICLQ VHGDASFCGQ GIVLETFTLS NLPHFRIGGS IHLIVNNQLG YTTPAERGRS SLYSSDIGKL VGCAIIHVNG DSPEEVVRAT RLAFEYQRQF RKDVIVDLLC YRQWGHNELD EPFFTNPVMY KIIRARKSIP DTYAEHLIAS GLMTQEEVSD IKTSYYTKLN DHLANVAHYS PPATNLQARW QGLVQPEACV TTWDTGVPLE LLRFIGVKSV EVPEELQVHS HLLKMYVQSR MEKVKNGSGL DWATAETLAL GSLLAQGFNV RLSGQDVGRG TFSQRHAMVV CQDTDDAYIP LNHMDPNQKG FLEVSNSPLS EEAVLGFEYG MSIESPTLLP LWEAQFGDFF NGAQIIFDTF ISGGEAKWLL QSGLVILLPH GYDGAGPEHS SCRIERFLQM CDSAEEGVDS DTVNMFVVHP TTPAQYFHLL RRQMIRNFRK PLIVASPKML LRYPAAVSTL EEMAPGTAFK PVIGDSSVDP KNVKTLIFCS GKHFYALLKQ RESLGTKKHD FAIIRLEELC PFPLDALQQE MSKYKHVRDV IWSQEEPQNM GPWSFVSPRF EKQLACRLRL VSRPPLPAPA VGIGTVHQQQ HEDILSKTFT Q // ID DJC10_MOUSE Reviewed; 793 AA. AC Q9DC23; A2ASA2; Q71S84; Q8CH78; Q8CIB0; Q99LV4; DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 2. DT 19-FEB-2014, entry version 102. DE RecName: Full=DnaJ homolog subfamily C member 10; DE EC=1.8.4.-; DE AltName: Full=Endoplasmic reticulum DNA J domain-containing protein 5; DE Short=ER-resident protein ERdj5; DE Short=ERdj5; DE AltName: Full=Endoplasmic reticulum DnaJ-PDI fusion protein 1; DE AltName: Full=J domain-containing protein disulfide isomerase-like protein; DE Short=J domain-containing PDI-like protein; DE Short=JPDI; DE Flags: Precursor; GN Name=Dnajc10; Synonyms=Erdj5, Jpdi; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY. RX PubMed=12411443; DOI=10.1074/jbc.M206995200; RA Cunnea P.M., Miranda-Vizuete A., Bertoli G., Simmen T., RA Damdimopoulos A.E., Hermann S., Leinonen S., Huikko M.P., RA Gustafsson J.-A., Sitia R., Spyrou G.; RT "ERdj5, an endoplasmic reticulum (ER)-resident protein containing DnaJ RT and thioredoxin domains, is expressed in secretory cells or following RT ER stress."; RL J. Biol. Chem. 278:1059-1066(2003). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Simmen T., Mezghrani A., Bertoli G., Sitia R.; RT "ERDJPs, a novel family of ER chaperones."; RL Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Lung; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Czech II, and FVB/N x C57BL/6J; TISSUE=Mammary tumor; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, GLYCOSYLATION, AND RP INTERACTION WITH HSPA5. RX PubMed=12446677; DOI=10.1074/jbc.M208346200; RA Hosoda A., Kimata Y., Tsuru A., Kohno K.; RT "JPDI, a novel endoplasmic reticulum-resident protein containing both RT a BiP-interacting J-domain and thioredoxin-like motifs."; RL J. Biol. Chem. 278:2669-2676(2003). RN [7] RP FUNCTION, INTERACTION WITH EDEM1, AND MUTAGENESIS OF CYS-158; CYS-161; RP CYS-480; CYS-483; CYS-588; CYS-591; CYS-700 AND CYS-703. RX PubMed=18653895; DOI=10.1126/science.1159293; RA Ushioda R., Hoseki J., Araki K., Jansen G., Thomas D.Y., Nagata K.; RT "ERdj5 is required as a disulfide reductase for degradation of RT misfolded proteins in the ER."; RL Science 321:569-572(2008). RN [8] RP DISRUPTION PHENOTYPE. RX PubMed=19788412; DOI=10.1042/BJ20091269; RA Hosoda A., Tokuda M., Akai R., Kohno K., Iwawaki T.; RT "Positive contribution of ERdj5/JPDI to endoplasmic reticulum protein RT quality control in the salivary gland."; RL Biochem. J. 425:117-125(2010). RN [9] RP X-RAY CRYSTALLOGRAPHY (1.84 ANGSTROMS) OF 33-793, FUNCTION, RP INTERACTION WITH EDEM1, AND MUTAGENESIS OF CYS-158; CYS-161; CYS-480; RP CYS-483; CYS-588; CYS-591; CYS-700 AND CYS-703. RX PubMed=21329881; DOI=10.1016/j.molcel.2011.01.021; RA Hagiwara M., Maegawa K., Suzuki M., Ushioda R., Araki K., RA Matsumoto Y., Hoseki J., Nagata K., Inaba K.; RT "Structural basis of an ERAD pathway mediated by the ER-resident RT protein disulfide reductase ERdj5."; RL Mol. Cell 41:432-444(2011). CC -!- FUNCTION: Endoplasmic reticulum disulfide reductase involved both CC in the correct folding of proteins and degradation of misfolded CC proteins. Required for efficient folding of proteins in the CC endoplasmic reticulum by catalyzing the removal of non-native CC disulfide bonds formed during the folding of proteins, such as CC LDLR. Also involved in endoplasmic reticulum-associated CC degradation (ERAD) by reducing incorrect disulfide bonds in CC misfolded glycoproteins recognized by EDEM1. Interaction with CC HSPA5 is required its activity, not for the disulfide reductase CC activity, but to facilitate the release of DNAJC10 from its CC substrate. Promotes apoptotic signaling pathway in response to CC endoplasmic reticulum stress. CC -!- SUBUNIT: Interacts with HSPA5 (via its J domain). Interacts with CC EDEM1. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen. CC -!- TISSUE SPECIFICITY: Ubiquitous. Particularly abundant in secretory CC tissues. Ubiquitous in fetal tissues and tumor tissues. Higher CC expression in fetal tissues than in adult tissues. Expressed in CC testis, pancreas, fetal thymus and fetal kidney. High expression CC in heart, liver, kidney, and testis. Low expression in spleen and CC skeletal muscle. CC -!- DOMAIN: Thioredoxin domains 3 and 4 are the primary reductase CC domains (PubMed:21329881). CC -!- DOMAIN: The thioredoxin-like regions Trxb 1 and 2 lack a redox- CC active CXXC motif (PubMed:21329881). CC -!- DISRUPTION PHENOTYPE: Mice are viable and healthy but show CC enhanced endoplasmic reticulum stress response in the salivary CC gland. CC -!- SIMILARITY: Contains 1 J domain. CC -!- SIMILARITY: Contains 4 thioredoxin domains. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF255459; AAN73273.1; -; mRNA. DR EMBL; AF314002; AAQ14555.1; -; mRNA. DR EMBL; AK004617; BAB23413.1; -; mRNA. DR EMBL; AL928587; CAM19646.1; -; Genomic_DNA. DR EMBL; BC002207; AAH02207.1; -; mRNA. DR EMBL; BC033461; AAH33461.1; -; mRNA. DR RefSeq; NP_077143.2; NM_024181.2. DR UniGene; Mm.21762; -. DR PDB; 3APO; X-ray; 2.40 A; A=33-793. DR PDB; 3APQ; X-ray; 1.84 A; A/B=34-242. DR PDB; 3APS; X-ray; 1.90 A; A/B=668-789. DR PDBsum; 3APO; -. DR PDBsum; 3APQ; -. DR PDBsum; 3APS; -. DR ProteinModelPortal; Q9DC23; -. DR SMR; Q9DC23; 34-782. DR BioGrid; 211769; 1. DR PhosphoSite; Q9DC23; -. DR PaxDb; Q9DC23; -. DR PRIDE; Q9DC23; -. DR Ensembl; ENSMUST00000028392; ENSMUSP00000028392; ENSMUSG00000027006. DR GeneID; 66861; -. DR KEGG; mmu:66861; -. DR UCSC; uc008khj.1; mouse. DR CTD; 54431; -. DR MGI; MGI:1914111; Dnajc10. DR eggNOG; COG0526; -. DR GeneTree; ENSGT00730000110455; -. DR HOGENOM; HOG000231882; -. DR HOVERGEN; HBG057048; -. DR InParanoid; A2ASA2; -. DR KO; K09530; -. DR OMA; YPSLFIF; -. DR OrthoDB; EOG7RZ5QH; -. DR TreeFam; TF105169; -. DR EvolutionaryTrace; Q9DC23; -. DR NextBio; 322847; -. DR PRO; PR:Q9DC23; -. DR ArrayExpress; Q9DC23; -. DR Bgee; Q9DC23; -. DR CleanEx; MM_DNAJC10; -. DR Genevestigator; Q9DC23; -. DR GO; GO:0034663; C:endoplasmic reticulum chaperone complex; ISS:UniProtKB. DR GO; GO:0005788; C:endoplasmic reticulum lumen; ISS:UniProtKB. DR GO; GO:0001671; F:ATPase activator activity; IMP:UniProtKB. DR GO; GO:0051087; F:chaperone binding; IDA:UniProtKB. DR GO; GO:0051787; F:misfolded protein binding; ISS:UniProtKB. DR GO; GO:0016671; F:oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor; IDA:UniProtKB. DR GO; GO:0015035; F:protein disulfide oxidoreductase activity; IDA:UniProtKB. DR GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro. DR GO; GO:0030433; P:ER-associated ubiquitin-dependent protein catabolic process; IDA:UniProtKB. DR GO; GO:0070059; P:intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress; ISS:UniProtKB. DR GO; GO:0001933; P:negative regulation of protein phosphorylation; ISS:UniProtKB. DR GO; GO:0034975; P:protein folding in endoplasmic reticulum; ISS:UniProtKB. DR Gene3D; 1.10.287.110; -; 1. DR Gene3D; 3.40.30.10; -; 5. DR InterPro; IPR001623; DnaJ_domain. DR InterPro; IPR021170; DnaJ_homolog_subfam-C. DR InterPro; IPR012336; Thioredoxin-like_fold. DR InterPro; IPR017937; Thioredoxin_CS. DR InterPro; IPR013766; Thioredoxin_domain. DR Pfam; PF00226; DnaJ; 1. DR Pfam; PF00085; Thioredoxin; 4. DR PIRSF; PIRSF037293; DnaJ_homolog_subfam-C; 1. DR PRINTS; PR00625; JDOMAIN. DR SMART; SM00271; DnaJ; 1. DR SUPFAM; SSF46565; SSF46565; 1. DR SUPFAM; SSF52833; SSF52833; 6. DR PROSITE; PS50076; DNAJ_2; 1. DR PROSITE; PS00014; ER_TARGET; 1. DR PROSITE; PS00194; THIOREDOXIN_1; 2. DR PROSITE; PS51352; THIOREDOXIN_2; 3. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Disulfide bond; KW Endoplasmic reticulum; Glycoprotein; Oxidoreductase; KW Redox-active center; Reference proteome; Repeat; Signal. FT SIGNAL 1 32 Potential. FT CHAIN 33 793 DnaJ homolog subfamily C member 10. FT /FTId=PRO_0000281484. FT DOMAIN 35 100 J. FT DOMAIN 130 232 Thioredoxin 1. FT DOMAIN 454 553 Thioredoxin 2. FT DOMAIN 557 665 Thioredoxin 3. FT DOMAIN 671 776 Thioredoxin 4. FT REGION 235 350 Trxb 1. FT REGION 348 463 Trxb 2. FT MOTIF 790 793 Prevents secretion from ER (Potential). FT CARBOHYD 530 530 N-linked (GlcNAc...) (Potential). FT DISULFID 158 161 Redox-active. FT DISULFID 480 483 Redox-active. FT DISULFID 588 591 Redox-active. FT DISULFID 700 703 Redox-active. FT MUTAGEN 158 158 C->A: Abolishes disulfide reductase FT activity; when associated with A-161; A- FT 480; A-483; A-588; A-591; A-700 and A- FT 703. FT MUTAGEN 161 161 C->A: Abolishes disulfide reductase FT activity; when associated with A-158; A- FT 480; A-483; A-588; A-591; A-700 and A- FT 703. FT MUTAGEN 480 480 C->A: Abolishes disulfide reductase FT activity; when associated with A-158; A- FT 161; A-483; A-588; A-591; A-700 and A- FT 703. FT MUTAGEN 483 483 C->A: Abolishes disulfide reductase FT activity; when associated with A-158; A- FT 161; A-480; A-588; A-591; A-700 and A- FT 703. FT MUTAGEN 588 588 C->A: Abolishes disulfide reductase FT activity; when associated with A-158; A- FT 161; A-480; A-483; A-591; A-700 and A- FT 703. FT MUTAGEN 591 591 C->A: Abolishes disulfide reductase FT activity; when associated with A-158; A- FT 161; A-480; A-483; A-588; A-700 and A- FT 703. FT MUTAGEN 700 700 C->A: Abolishes disulfide reductase FT activity; when associated with A-158; A- FT 161; A-480; A-483; A-588; A-591 and A- FT 703. FT MUTAGEN 703 703 C->A: Abolishes disulfide reductase FT activity; when associated with A-158; A- FT 161; A-480; A-483; A-588; A-591 and A- FT 700. FT CONFLICT 91 91 D -> H (in Ref. 3; BAB23413). FT CONFLICT 310 310 T -> A (in Ref. 2; AAQ14555). FT CONFLICT 324 324 E -> G (in Ref. 4; AAH33461). FT CONFLICT 433 433 I -> T (in Ref. 4; AAH33461). FT CONFLICT 538 538 E -> G (in Ref. 2; AAQ14555). FT CONFLICT 651 652 NG -> RP (in Ref. 2; AAQ14555). FT CONFLICT 654 654 N -> NS (in Ref. 1; AAN73273). FT CONFLICT 680 680 F -> FR (in Ref. 1; AAN73273). FT CONFLICT 767 767 D -> M (in Ref. 2; AAQ14555). FT HELIX 36 40 FT HELIX 48 62 FT HELIX 64 66 FT HELIX 73 87 FT HELIX 90 99 FT TURN 100 103 FT HELIX 115 120 FT STRAND 121 123 FT TURN 124 127 FT STRAND 131 133 FT HELIX 136 145 FT STRAND 149 154 FT HELIX 159 174 FT TURN 175 178 FT STRAND 179 185 FT TURN 186 188 FT HELIX 190 195 FT STRAND 200 207 FT HELIX 222 234 FT STRAND 237 239 FT HELIX 242 255 FT STRAND 258 264 FT HELIX 273 282 FT TURN 283 286 FT STRAND 287 293 FT TURN 294 296 FT HELIX 298 301 FT STRAND 311 314 FT TURN 322 324 FT HELIX 325 327 FT STRAND 328 331 FT HELIX 336 346 FT HELIX 355 362 FT STRAND 365 372 FT HELIX 382 386 FT HELIX 387 391 FT HELIX 392 394 FT STRAND 396 402 FT HELIX 403 405 FT HELIX 407 412 FT STRAND 419 426 FT STRAND 429 433 FT HELIX 440 451 FT STRAND 455 457 FT TURN 460 462 FT STRAND 471 476 FT HELIX 481 496 FT TURN 497 500 FT STRAND 502 507 FT TURN 508 510 FT HELIX 512 517 FT STRAND 522 530 FT STRAND 533 537 FT HELIX 543 554 FT STRAND 557 560 FT HELIX 563 569 FT TURN 570 572 FT STRAND 579 584 FT HELIX 589 605 FT TURN 606 608 FT STRAND 609 615 FT TURN 616 619 FT HELIX 620 625 FT STRAND 630 637 FT STRAND 641 643 FT HELIX 657 665 FT STRAND 672 674 FT HELIX 677 683 FT TURN 684 686 FT STRAND 691 696 FT HELIX 701 717 FT TURN 718 720 FT STRAND 722 727 FT TURN 728 730 FT HELIX 732 737 FT STRAND 742 752 FT HELIX 753 755 FT STRAND 757 763 FT HELIX 768 780 SQ SEQUENCE 793 AA; 90583 MW; 00C88EF3F5497BE1 CRC64; MGVWLNKDDF IRDLKRISLC LLILYVVVVV GTDQNFYSLL GVSKTASSRE IRQAFKKLAL KLHPDKNPNN PNAHGDFLKI NRAYEVLKDE DLRKKYDKYG EKGLEDNQGG QYESWSYYRY DFGIYDDDPE IITLERREFD AAVNSGELWF VNFYSPGCSH CHDLAPTWRE FAKEVDGLLR IGAVNCGDDR MLCRMKGVNS YPSLFIFRSG MAAVKYNGDR SKESLVAFAM QHVRSTVTEL STGNFVNAIE TAFAAGVGWL ITFCSKGEDC LTSQTRLRLS GMLDGLVNVG WVDCDAQDSL CKSLDTTAST TAYFPPGATL NDREKSSVLF LNSLDAKEIY MEIIHNLPDF ELLSANQLED RLAHHRWLVF FHFGKNENAN DPELKKLKTL LKNEHIQVGR FDCSSAPGIC SDLYVFQPCL AVFKGQGTKE YEIHHGKKIL YDILAFAKES VNSHVTTLGP QNFPASDKEP WLVDFFAPWC PPCRALLPEL RKASTLLYGQ LKVGTLDCTI HEGLCNMYNI QAYPTTVVFN QSSIHEYEGH HSAEQILEFI EDLRNPSVVS LTPSTFNELV KQRKHDEVWM VDFYSPWCHP CQVLMPEWKR MARTLTGLIN VGSVDCQQYH SFCTQENVQR YPEIRFYPQK SSKAYQYHSY NGWNRDAYSL RSWGLGFLPQ ASIDLTPQTF NEKVLQGKTH WVVDFYAPWC GPCQNFAPEF ELLARMIKGK VRAGKVDCQA YPQTCQKAGI KAYPSVKLYQ YERAKKSIWE EQINSRDAKT IAALIYGKLE TLQSQVKRNK DEL // ID DLDH_MOUSE Reviewed; 509 AA. AC O08749; Q3TG55; Q3U5W5; Q3UWP7; Q99LD3; DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot. DT 28-NOV-2006, sequence version 2. DT 19-MAR-2014, entry version 124. DE RecName: Full=Dihydrolipoyl dehydrogenase, mitochondrial; DE EC=1.8.1.4; DE AltName: Full=Dihydrolipoamide dehydrogenase; DE Flags: Precursor; GN Name=Dld; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=DBA/2J; RX PubMed=9169128; DOI=10.1006/geno.1997.4670; RA Johnson M., Yang H.S., Johanning G.L., Patel M.S.; RT "Characterization of the mouse dihydrolipoamide dehydrogenase (Dld) RT gene: genomic structure, promoter sequence, and chromosomal RT localization."; RL Genomics 41:320-326(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Bone marrow, and Heart; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Czech II; TISSUE=Mammary tumor; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP PROTEIN SEQUENCE OF 73-89; 216-259; 289-334; 316-334; 347-365; 421-428 RP AND 483-509, AND MASS SPECTROMETRY. RC STRAIN=C57BL/6; TISSUE=Brain, and Hippocampus; RA Lubec G., Klug S., Kang S.U.; RL Submitted (APR-2007) to UniProtKB. RN [5] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-66 AND LYS-410, RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-66; LYS-104; LYS-122; RP LYS-132; LYS-143; LYS-159; LYS-166; LYS-273; LYS-277; LYS-334; RP LYS-410; LYS-430 AND LYS-505, AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic fibroblast, and Liver; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., RA Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). RN [6] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-66; LYS-104; LYS-122; RP LYS-132; LYS-143; LYS-334; LYS-346; LYS-410; LYS-420 AND LYS-505, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23576753; DOI=10.1073/pnas.1302961110; RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., RA Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.; RT "Label-free quantitative proteomics of the lysine acetylome in RT mitochondria identifies substrates of SIRT3 in metabolic pathways."; RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013). CC -!- FUNCTION: Lipoamide dehydrogenase is a component of the glycine CC cleavage system as well as of the alpha-ketoacid dehydrogenase CC complexes. Involved in the hyperactivation of spermatazoa during CC capacitation and in the spermatazoal acrosome reaction. CC -!- CATALYTIC ACTIVITY: Protein N(6)-(dihydrolipoyl)lysine + NAD(+) = CC protein N(6)-(lipoyl)lysine + NADH. CC -!- COFACTOR: Binds 1 FAD per subunit (By similarity). CC -!- SUBUNIT: Homodimer. Eukaryotic pyruvate dehydrogenase complexes CC are organized about a core consisting of the oligomeric CC dihydrolipoamide acetyl-transferase, around which are arranged CC multiple copies of pyruvate dehydrogenase, dihydrolipoamide CC dehydrogenase and protein X bound by non-covalent bonds (By CC similarity). CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix. CC -!- PTM: Acetylation of Lys-127 is observed in liver mitochondria from CC fasted mice but not from fed mice. CC -!- PTM: Tyrosine phosphorylated (By similarity). CC -!- MISCELLANEOUS: The active site is a redox-active disulfide bond. CC -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide CC oxidoreductase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U73445; AAC53170.1; -; mRNA. DR EMBL; AK117104; BAE43405.1; -; mRNA. DR EMBL; AK136193; BAE22867.1; -; mRNA. DR EMBL; AK153399; BAE31961.1; -; mRNA. DR EMBL; AK168875; BAE40693.1; -; mRNA. DR EMBL; BC003368; AAH03368.1; -; mRNA. DR RefSeq; NP_031887.2; NM_007861.5. DR UniGene; Mm.3131; -. DR UniGene; Mm.471230; -. DR ProteinModelPortal; O08749; -. DR SMR; O08749; 38-509. DR BioGrid; 199227; 1. DR IntAct; O08749; 8. DR MINT; MINT-4124146; -. DR ChEMBL; CHEMBL2176826; -. DR PhosphoSite; O08749; -. DR REPRODUCTION-2DPAGE; O08749; -. DR SWISS-2DPAGE; O08749; -. DR PaxDb; O08749; -. DR PRIDE; O08749; -. DR Ensembl; ENSMUST00000110857; ENSMUSP00000106481; ENSMUSG00000020664. DR GeneID; 13382; -. DR KEGG; mmu:13382; -. DR UCSC; uc007nhg.2; mouse. DR CTD; 1738; -. DR MGI; MGI:107450; Dld. DR eggNOG; COG1249; -. DR GeneTree; ENSGT00550000074844; -. DR HOGENOM; HOG000276708; -. DR HOVERGEN; HBG002290; -. DR KO; K00382; -. DR OMA; IDSEYRT; -. DR OrthoDB; EOG77126S; -. DR TreeFam; TF300414; -. DR NextBio; 283728; -. DR PRO; PR:O08749; -. DR Bgee; O08749; -. DR CleanEx; MM_DLD; -. DR Genevestigator; O08749; -. DR GO; GO:0043159; C:acrosomal matrix; IDA:MGI. DR GO; GO:0005929; C:cilium; IDA:MGI. DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR GO; GO:0005634; C:nucleus; IEA:Ensembl. DR GO; GO:0004148; F:dihydrolipoyl dehydrogenase activity; IMP:MGI. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. DR GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro. DR GO; GO:0007369; P:gastrulation; IMP:MGI. DR GO; GO:0006120; P:mitochondrial electron transport, NADH to ubiquinone; IMP:MGI. DR GO; GO:0006508; P:proteolysis; IDA:MGI. DR GO; GO:0042391; P:regulation of membrane potential; IMP:MGI. DR GO; GO:0048240; P:sperm capacitation; IDA:MGI. DR Gene3D; 3.30.390.30; -; 1. DR InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer. DR InterPro; IPR013027; FAD_pyr_nucl-diS_OxRdtase. DR InterPro; IPR006258; Lipoamide_DH. DR InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer. DR InterPro; IPR023753; Pyr_nucl-diS_OxRdtase_FAD/NAD. DR InterPro; IPR012999; Pyr_OxRdtase_I_AS. DR InterPro; IPR001327; Pyr_OxRdtase_NAD-bd_dom. DR Pfam; PF00070; Pyr_redox; 1. DR Pfam; PF07992; Pyr_redox_2; 1. DR Pfam; PF02852; Pyr_redox_dim; 1. DR PRINTS; PR00368; FADPNR. DR SUPFAM; SSF55424; SSF55424; 1. DR TIGRFAMs; TIGR01350; lipoamide_DH; 1. DR PROSITE; PS00076; PYRIDINE_REDOX_1; 1. PE 1: Evidence at protein level; KW Acetylation; Complete proteome; Direct protein sequencing; KW Disulfide bond; FAD; Flavoprotein; Mitochondrion; NAD; Oxidoreductase; KW Phosphoprotein; Redox-active center; Reference proteome; KW Transit peptide. FT TRANSIT 1 35 Mitochondrion (By similarity). FT CHAIN 36 509 Dihydrolipoyl dehydrogenase, FT mitochondrial. FT /FTId=PRO_0000030297. FT NP_BIND 71 80 FAD (By similarity). FT NP_BIND 183 185 FAD (By similarity). FT NP_BIND 220 227 NAD (By similarity). FT NP_BIND 361 364 FAD (By similarity). FT ACT_SITE 487 487 Proton acceptor (By similarity). FT BINDING 89 89 FAD (By similarity). FT BINDING 154 154 FAD; via amide nitrogen and carbonyl FT oxygen (By similarity). FT BINDING 243 243 NAD (By similarity). FT BINDING 278 278 NAD; via amide nitrogen and carbonyl FT oxygen (By similarity). FT BINDING 314 314 NAD; via amide nitrogen (By similarity). FT BINDING 355 355 FAD (By similarity). FT MOD_RES 66 66 N6-acetyllysine; alternate. FT MOD_RES 66 66 N6-succinyllysine; alternate. FT MOD_RES 104 104 N6-acetyllysine; alternate. FT MOD_RES 104 104 N6-succinyllysine; alternate. FT MOD_RES 122 122 N6-acetyllysine; alternate. FT MOD_RES 122 122 N6-succinyllysine; alternate. FT MOD_RES 132 132 N6-acetyllysine; alternate. FT MOD_RES 132 132 N6-succinyllysine; alternate. FT MOD_RES 143 143 N6-acetyllysine; alternate. FT MOD_RES 143 143 N6-succinyllysine; alternate. FT MOD_RES 159 159 N6-succinyllysine. FT MOD_RES 166 166 N6-succinyllysine. FT MOD_RES 273 273 N6-succinyllysine. FT MOD_RES 277 277 N6-succinyllysine. FT MOD_RES 334 334 N6-acetyllysine; alternate. FT MOD_RES 334 334 N6-succinyllysine; alternate. FT MOD_RES 346 346 N6-acetyllysine. FT MOD_RES 410 410 N6-acetyllysine; alternate. FT MOD_RES 410 410 N6-succinyllysine; alternate. FT MOD_RES 417 417 N6-acetyllysine (By similarity). FT MOD_RES 420 420 N6-acetyllysine. FT MOD_RES 430 430 N6-succinyllysine. FT MOD_RES 505 505 N6-acetyllysine; alternate. FT MOD_RES 505 505 N6-succinyllysine; alternate. FT DISULFID 80 85 Redox-active (By similarity). FT CONFLICT 54 54 Y -> C (in Ref. 1; AAC53170). FT CONFLICT 144 144 Q -> T (in Ref. 2; BAE22867). FT CONFLICT 149 149 H -> L (in Ref. 2; BAE31961). FT CONFLICT 283 283 K -> E (in Ref. 2; BAE40693). SQ SEQUENCE 509 AA; 54272 MW; 2C381852BAAD0441 CRC64; MQSWSRVYRS LAKKGHFNRI SHGLQGVSSV PLRTYADQPI EADVTVIGSG PGGYVAAIKS AQLGFKTVCI EKNETLGGTC LNVGCIPSKA LLNNSHYYHM AHGKDFASRG IEIPEVRLNL EKMMEQKHSA VKALTGGIAH LFKQNKVVHV NGFGKITGKN QVTATKADGS TQVIDTKNIL VATGSEVTPF PGITIDEDTI VSSTGALSLK KVPEKLVVIG AGVIGVELGS VWQRLGADVT AVEFLGHVGG IGIDMEISKN FQRILQRQGF KFKLNTKVTG ATKKSDGKID VSVEAASGGK AEVITCDVLL VCIGRRPFTQ NLGLEELGIE LDPKGRIPVN NRFQTKIPNI YAIGDVVAGP MLAHKAEDEG IICVEGMAGG AVHIDYNCVP SVIYTHPEVA WVGKSEEQLK EEGIEFKIGK FPFAANSRAK TNADTDGMVK ILGHKSTDRV LGAHILGPGA GEMVNEAALA LEYGASCEDI ARVCHAHPTL SEAFREANLA AAFGKPINF // ID DOHH_MOUSE Reviewed; 302 AA. AC Q99LN9; Q8BNT3; Q8BTD5; DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot. DT 05-SEP-2006, sequence version 2. DT 19-MAR-2014, entry version 100. DE RecName: Full=Deoxyhypusine hydroxylase; DE Short=DOHH; DE EC=1.14.99.29; DE AltName: Full=Deoxyhypusine dioxygenase; DE AltName: Full=Deoxyhypusine monooxygenase; GN Name=Dohh; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC STRAIN=C57BL/6J; TISSUE=Brain cortex; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC STRAIN=Czech II; TISSUE=Mammary tumor; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: Catalyzes the hydroxylation of the N(6)-(4-aminobutyl)- CC L-lysine intermediate to form hypusine, an essential post- CC translational modification only found in mature eIF-5A factor (By CC similarity). CC -!- CATALYTIC ACTIVITY: [eIF5A]-deoxyhypusine + AH(2) + O(2) = CC [eIF5A]-hypusine + A + H(2)O. CC -!- COFACTOR: Binds 2 Fe(2+) ions per subunit (By similarity). CC -!- PATHWAY: Protein modification; eIF5A hypusination. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q99LN9-1; Sequence=Displayed; CC Name=2; CC IsoId=Q99LN9-2; Sequence=VSP_020315, VSP_020316; CC Note=No experimental confirmation available; CC -!- SIMILARITY: Belongs to the deoxyhypusine hydroxylase family. CC -!- SIMILARITY: Contains 5 HEAT-like PBS-type repeats. CC -!- SEQUENCE CAUTION: CC Sequence=BAC25064.1; Type=Frameshift; Positions=171, 302; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK004052; BAC25064.1; ALT_FRAME; mRNA. DR EMBL; AK080664; BAC37972.1; -; mRNA. DR EMBL; BC002295; AAH02295.1; -; mRNA. DR RefSeq; NP_598725.2; NM_133964.2. DR UniGene; Mm.294975; -. DR ProteinModelPortal; Q99LN9; -. DR SMR; Q99LN9; 2-282. DR IntAct; Q99LN9; 1. DR MINT; MINT-4124284; -. DR PhosphoSite; Q99LN9; -. DR PaxDb; Q99LN9; -. DR PRIDE; Q99LN9; -. DR Ensembl; ENSMUST00000072751; ENSMUSP00000072534; ENSMUSG00000078440. [Q99LN9-1] DR Ensembl; ENSMUST00000144647; ENSMUSP00000116074; ENSMUSG00000078440. [Q99LN9-2] DR GeneID; 102115; -. DR KEGG; mmu:102115; -. DR UCSC; uc007ghu.2; mouse. [Q99LN9-1] DR CTD; 83475; -. DR MGI; MGI:1915964; Dohh. DR eggNOG; COG1413; -. DR GeneTree; ENSGT00500000044957; -. DR HOGENOM; HOG000248665; -. DR HOVERGEN; HBG081460; -. DR InParanoid; Q99LN9; -. DR KO; K06072; -. DR OMA; RESCQVA; -. DR OrthoDB; EOG75TMCH; -. DR TreeFam; TF105626; -. DR UniPathway; UPA00354; -. DR NextBio; 355294; -. DR PRO; PR:Q99LN9; -. DR ArrayExpress; Q99LN9; -. DR Bgee; Q99LN9; -. DR CleanEx; MM_DOHH; -. DR Genevestigator; Q99LN9; -. DR GO; GO:0019135; F:deoxyhypusine monooxygenase activity; ISS:UniProtKB. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008612; P:peptidyl-lysine modification to hypusine; ISS:UniProtKB. DR Gene3D; 1.25.10.10; -; 1. DR HAMAP; MF_03101; Deoxyhypusine_hydroxylase; 1. DR InterPro; IPR011989; ARM-like. DR InterPro; IPR016024; ARM-type_fold. DR InterPro; IPR027517; Deoxyhypusine_hydroxylase. DR InterPro; IPR004155; PBS_lyase_HEAT. DR SMART; SM00567; EZ_HEAT; 6. DR SUPFAM; SSF48371; SSF48371; 1. PE 2: Evidence at transcript level; KW Acetylation; Alternative splicing; Complete proteome; KW Hypusine biosynthesis; Iron; Metal-binding; Monooxygenase; KW Oxidoreductase; Reference proteome; Repeat. FT CHAIN 1 302 Deoxyhypusine hydroxylase. FT /FTId=PRO_0000248576. FT REPEAT 54 80 HEAT-like PBS-type 1. FT REPEAT 87 113 HEAT-like PBS-type 2. FT REPEAT 175 201 HEAT-like PBS-type 3. FT REPEAT 206 232 HEAT-like PBS-type 4. FT REPEAT 239 265 HEAT-like PBS-type 5. FT METAL 56 56 Iron 1 (By similarity). FT METAL 57 57 Iron 1 (By similarity). FT METAL 89 89 Iron 1 (By similarity). FT METAL 90 90 Iron 1 (By similarity). FT METAL 208 208 Iron 2 (By similarity). FT METAL 209 209 Iron 2 (By similarity). FT METAL 241 241 Iron 2 (By similarity). FT METAL 242 242 Iron 2 (By similarity). FT MOD_RES 1 1 N-acetylmethionine (By similarity). FT VAR_SEQ 199 200 LQ -> SC (in isoform 2). FT /FTId=VSP_020315. FT VAR_SEQ 201 302 Missing (in isoform 2). FT /FTId=VSP_020316. FT CONFLICT 68 68 A -> V (in Ref. 2; AAH02295). FT CONFLICT 75 76 AD -> VG (in Ref. 2; AAH02295). FT CONFLICT 298 298 L -> V (in Ref. 1; BAC25064). SQ SEQUENCE 302 AA; 32905 MW; 524712E1EABF90C9 CRC64; MVTEQEIEAI GKTLVDPKQP LQARFRALFT LRGLGGPDAI SWISRGFEDS SALLKHELAY CLGQMRDARA IPVLADVLQD TSQEPMVRHE AGEALGAIGN PEVLGLLKQY STDPVVEVAE TCQLAVGRLE WLQQHPGEAT CAGPYLSVDP APPAAEQDVG RLREALLDEA RPLFERYRAM FALRNVGGKE AALALAEGLQ CGSALFRHEV GYVLGQLQHE AAVPGLAATL ARTTESPMVR HECAEALGAI ARPACLAALR EHIEDPEQVV RESCEVALDM YEYESSQDFQ YADGLERLRP PP // ID DOPO_MOUSE Reviewed; 622 AA. AC Q64237; Q3V1U4; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 18-SEP-2013, sequence version 2. DT 19-FEB-2014, entry version 115. DE RecName: Full=Dopamine beta-hydroxylase; DE EC=1.14.17.1; DE AltName: Full=Dopamine beta-monooxygenase; DE Contains: DE RecName: Full=Soluble dopamine beta-hydroxylase; GN Name=Dbh; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=1280432; DOI=10.1016/0006-291X(92)91598-K; RA Nakano T., Kobayashi K., Saito S., Fujita K., Nagatsu T.; RT "Mouse dopamine beta-hydroxylase: primary structure deduced from the RT cDNA sequence and exon/intron organization of the gene."; RL Biochem. Biophys. Res. Commun. 189:590-599(1992). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Embryo; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: Conversion of dopamine to noradrenaline. CC -!- CATALYTIC ACTIVITY: 3,4-dihydroxyphenethylamine + ascorbate + O(2) CC = noradrenaline + dehydroascorbate + H(2)O. CC -!- COFACTOR: Binds 1 PQQ per subunit (By similarity). CC -!- COFACTOR: Binds 2 copper ions per subunit (By similarity). CC -!- PATHWAY: Catecholamine biosynthesis; (R)-noradrenaline CC biosynthesis; (R)-noradrenaline from dopamine: step 1/1. CC -!- SUBUNIT: Homotetramer composed of two non-covalently bound CC disulfide-linked dimers (By similarity). CC -!- SUBCELLULAR LOCATION: Soluble dopamine beta-hydroxylase: CC Cytoplasmic vesicle, secretory vesicle lumen (By similarity). CC Cytoplasmic vesicle, secretory vesicle, chromaffin granule lumen CC (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle CC membrane; Single-pass type II membrane protein (By similarity). CC Cytoplasmic vesicle, secretory vesicle, chromaffin granule CC membrane; Single-pass type II membrane protein (By similarity). CC -!- SIMILARITY: Belongs to the copper type II ascorbate-dependent CC monooxygenase family. CC -!- SIMILARITY: Contains 1 DOMON domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; S50200; AAB24330.1; -; mRNA. DR EMBL; AK132245; BAE21055.1; -; mRNA. DR EMBL; AL954801; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH466542; EDL08360.1; -; Genomic_DNA. DR EMBL; BC141022; AAI41023.1; -; mRNA. DR EMBL; BC171949; AAI71949.1; -; mRNA. DR PIR; JC1346; JC1346. DR RefSeq; NP_620392.2; NM_138942.3. DR UniGene; Mm.167781; -. DR ProteinModelPortal; Q64237; -. DR STRING; 10090.ENSMUSP00000000910; -. DR PhosphoSite; Q64237; -. DR PRIDE; Q64237; -. DR Ensembl; ENSMUST00000000910; ENSMUSP00000000910; ENSMUSG00000000889. DR GeneID; 13166; -. DR KEGG; mmu:13166; -. DR UCSC; uc008ixe.1; mouse. DR CTD; 1621; -. DR MGI; MGI:94864; Dbh. DR eggNOG; NOG286384; -. DR GeneTree; ENSGT00530000063085; -. DR HOVERGEN; HBG005519; -. DR InParanoid; Q64237; -. DR KO; K00503; -. DR OMA; GAKAFYY; -. DR OrthoDB; EOG78WKR4; -. DR TreeFam; TF320698; -. DR UniPathway; UPA00748; UER00735. DR NextBio; 283246; -. DR PRO; PR:Q64237; -. DR CleanEx; MM_DBH; -. DR Genevestigator; Q64237; -. DR GO; GO:0034466; C:chromaffin granule lumen; IEA:UniProtKB-SubCell. DR GO; GO:0042584; C:chromaffin granule membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0030658; C:transport vesicle membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005507; F:copper ion binding; IEA:InterPro. DR GO; GO:0004500; F:dopamine beta-monooxygenase activity; IEA:UniProtKB-EC. DR GO; GO:0031418; F:L-ascorbic acid binding; IEA:UniProtKB-KW. DR GO; GO:0048149; P:behavioral response to ethanol; IMP:MGI. DR GO; GO:0001974; P:blood vessel remodeling; IMP:MGI. DR GO; GO:0001816; P:cytokine production; IMP:MGI. DR GO; GO:0042420; P:dopamine catabolic process; IMP:MGI. DR GO; GO:0042596; P:fear response; IMP:MGI. DR GO; GO:0042593; P:glucose homeostasis; IMP:MGI. DR GO; GO:0042309; P:homoiothermy; IMP:MGI. DR GO; GO:0002443; P:leukocyte mediated immunity; IMP:MGI. DR GO; GO:0050900; P:leukocyte migration; IMP:MGI. DR GO; GO:0007626; P:locomotory behavior; IMP:MGI. DR GO; GO:0042711; P:maternal behavior; IMP:MGI. DR GO; GO:0007613; P:memory; IMP:MGI. DR GO; GO:0042421; P:norepinephrine biosynthetic process; IMP:MGI. DR GO; GO:0045907; P:positive regulation of vasoconstriction; IMP:MGI. DR GO; GO:0042127; P:regulation of cell proliferation; IMP:MGI. DR GO; GO:2001236; P:regulation of extrinsic apoptotic signaling pathway; IMP:MGI. DR GO; GO:0001975; P:response to amphetamine; IMP:MGI. DR GO; GO:0048265; P:response to pain; IMP:MGI. DR GO; GO:0007268; P:synaptic transmission; IEA:InterPro. DR GO; GO:0008542; P:visual learning; IMP:MGI. DR Gene3D; 2.60.120.230; -; 1. DR Gene3D; 2.60.120.310; -; 1. DR InterPro; IPR014784; Cu2_ascorb_mOase-like_C. DR InterPro; IPR020611; Cu2_ascorb_mOase_CS-1. DR InterPro; IPR014783; Cu2_ascorb_mOase_CS-2. DR InterPro; IPR000323; Cu2_ascorb_mOase_N. DR InterPro; IPR028461; DBH. DR InterPro; IPR000945; DBH-rel. DR InterPro; IPR005018; DOMON_domain. DR InterPro; IPR008977; PHM/PNGase_F_dom. DR PANTHER; PTHR10157; PTHR10157; 1. DR PANTHER; PTHR10157:SF16; PTHR10157:SF16; 1. DR Pfam; PF01082; Cu2_monooxygen; 1. DR Pfam; PF03351; DOMON; 1. DR PRINTS; PR00767; DBMONOXGNASE. DR SMART; SM00664; DoH; 1. DR SUPFAM; SSF49742; SSF49742; 2. DR PROSITE; PS00084; CU2_MONOOXYGENASE_1; 1. DR PROSITE; PS00085; CU2_MONOOXYGENASE_2; 1. DR PROSITE; PS50836; DOMON; 1. PE 2: Evidence at transcript level; KW Catecholamine biosynthesis; Complete proteome; Copper; KW Cytoplasmic vesicle; Disulfide bond; Glycoprotein; Membrane; KW Metal-binding; Monooxygenase; Oxidoreductase; Phosphoprotein; PQQ; KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix; KW Vitamin C. FT CHAIN 1 622 Dopamine beta-hydroxylase. FT /FTId=PRO_0000006357. FT CHAIN 44 622 Soluble dopamine beta-hydroxylase FT (Potential). FT /FTId=PRO_0000308210. FT TOPO_DOM 1 20 Cytoplasmic (Potential). FT TRANSMEM 21 41 Helical; Signal-anchor for type II FT membrane protein; (Potential). FT TOPO_DOM 42 621 Intragranular (Potential). FT DOMAIN 61 177 DOMON. FT ACT_SITE 234 234 Potential. FT ACT_SITE 416 416 Potential. FT METAL 266 266 Copper A (By similarity). FT METAL 267 267 Copper A (By similarity). FT METAL 337 337 Copper A (By similarity). FT METAL 416 416 Copper B (By similarity). FT METAL 418 418 Copper B (By similarity). FT METAL 491 491 Copper B (By similarity). FT MOD_RES 350 350 Phosphoserine; by CaMK (Potential). FT CARBOHYD 68 68 N-linked (GlcNAc...) (Potential). FT CARBOHYD 188 188 N-linked (GlcNAc...) (Potential). FT CARBOHYD 476 476 N-linked (GlcNAc...) (Potential). FT CARBOHYD 570 570 N-linked (GlcNAc...) (Potential). FT DISULFID 158 600 By similarity. FT DISULFID 236 287 By similarity. FT DISULFID 273 299 By similarity. FT DISULFID 394 507 By similarity. FT DISULFID 398 569 By similarity. FT DISULFID 470 492 By similarity. FT DISULFID 532 532 Interchain (By similarity). FT DISULFID 534 534 Interchain (By similarity). FT CONFLICT 109 109 T -> S (in Ref. 1; AAB24330). FT CONFLICT 197 197 Q -> L (in Ref. 1; AAB24330). FT CONFLICT 232 232 T -> Q (in Ref. 1; AAB24330). FT CONFLICT 356 356 H -> P (in Ref. 1; AAB24330). FT CONFLICT 437 437 V -> E (in Ref. 1; AAB24330). FT CONFLICT 449 449 Q -> R (in Ref. 1; AAB24330). FT CONFLICT 554 554 D -> N (in Ref. 1; AAB24330). FT CONFLICT 618 621 EADA -> GGRC (in Ref. 1; AAB24330). SQ SEQUENCE 622 AA; 70314 MW; 7D9FA1B622F3FCA8 CRC64; MQAHLSHQPC WSSLPSPSVR EAASMYGTAV AIFLVILVAA LRGSEPPESP FPYHIPLDPE GILELSWNVS YVQEIIHFQL QVQGLRAGVL FGMSDRGEME NADLIMLWTD GDRAYFADAW SDRKGQIHLD SQQDYQLLQA QRTRDGLSLL FKRPFVTCDP KDYVIEDDTV HLVYGILEEP FQSLEAINTS GLHTGLQRVQ LLKSEVPTPS MPEDVQTMDI RAPDILIPDN ETTYWCYITE LPPRFPRHHI IMYEAIVTEG NEALVHHMEV FQCAAESEDF PQFNGPCDSK MKPDRLNYCR HVLAAWALGA KAFYYPKEAG VPFGGPGSSP FLRLEVHYHN PRKIQGRQDS SGIRLHYTAT LRRYDAGIME LGLVYTPLMA IPPQETAFVL TGYCTDKCTQ MALQDSGIHI FASQLHTHLT GRKVVTVLAR DGQERKVVNR DNHYSPHFQE IRMLKKVVTV YPGDVLITSC TYNTENKTLA TVGGFGILEE MCVNYVHYYP QTELELCKSA VDDGFLQKYF HMVNRFSSEE VCTCPQASVP QQFSSVPWNS FNRDMLKALY DYAPISMHCN KTSAVRFPGE WNLQPLPKIT STLEEPTPRC PIRQTQSPAN PTVPITTEAD AE // ID DPYD_MOUSE Reviewed; 1025 AA. AC Q8CHR6; DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 19-MAR-2014, entry version 97. DE RecName: Full=Dihydropyrimidine dehydrogenase [NADP(+)]; DE Short=DHPDHase; DE Short=DPD; DE EC=1.3.1.2; DE AltName: Full=Dihydrothymine dehydrogenase; DE AltName: Full=Dihydrouracil dehydrogenase; GN Name=Dpyd; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Kidney; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [2] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-905, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=17242355; DOI=10.1073/pnas.0609836104; RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; RT "Large-scale phosphorylation analysis of mouse liver."; RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). CC -!- FUNCTION: Involved in pyrimidine base degradation. Catalyzes the CC reduction of uracil and thymine (By similarity). CC -!- CATALYTIC ACTIVITY: 5,6-dihydrouracil + NADP(+) = uracil + NADPH. CC -!- COFACTOR: Binds 4 4Fe-4S clusters. Contains approximately 16 iron CC atoms per subunit (By similarity). CC -!- COFACTOR: FAD (By similarity). CC -!- COFACTOR: FMN (By similarity). CC -!- ENZYME REGULATION: Inactivated by 5-iodouracil (By similarity). CC -!- PATHWAY: Amino-acid biosynthesis; beta-alanine biosynthesis. CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the dihydropyrimidine dehydrogenase family. CC -!- SIMILARITY: Contains 3 4Fe-4S ferredoxin-type domains. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BC039699; AAH39699.1; -; mRNA. DR RefSeq; NP_740748.1; NM_170778.2. DR UniGene; Mm.27907; -. DR ProteinModelPortal; Q8CHR6; -. DR SMR; Q8CHR6; 2-1019. DR IntAct; Q8CHR6; 2. DR MINT; MINT-4116112; -. DR PhosphoSite; Q8CHR6; -. DR PaxDb; Q8CHR6; -. DR PRIDE; Q8CHR6; -. DR Ensembl; ENSMUST00000039177; ENSMUSP00000039429; ENSMUSG00000033308. DR GeneID; 99586; -. DR KEGG; mmu:99586; -. DR UCSC; uc008rdh.1; mouse. DR CTD; 1806; -. DR MGI; MGI:2139667; Dpyd. DR eggNOG; COG0167; -. DR GeneTree; ENSGT00500000044896; -. DR HOGENOM; HOG000007797; -. DR HOVERGEN; HBG004351; -. DR InParanoid; Q8CHR6; -. DR KO; K00207; -. DR OMA; PWPAVGI; -. DR OrthoDB; EOG7MH0X9; -. DR TreeFam; TF105791; -. DR UniPathway; UPA00131; -. DR NextBio; 354029; -. DR PRO; PR:Q8CHR6; -. DR ArrayExpress; Q8CHR6; -. DR Bgee; Q8CHR6; -. DR Genevestigator; Q8CHR6; -. DR GO; GO:0005829; C:cytosol; IDA:MGI. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0004158; F:dihydroorotate oxidase activity; IEA:InterPro. DR GO; GO:0017113; F:dihydropyrimidine dehydrogenase (NADP+) activity; ISS:UniProtKB. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW. DR GO; GO:0019483; P:beta-alanine biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0006145; P:purine nucleobase catabolic process; IEA:Ensembl. DR GO; GO:0006214; P:thymidine catabolic process; ISS:UniProtKB. DR GO; GO:0006210; P:thymine catabolic process; IEA:Ensembl. DR GO; GO:0006222; P:UMP biosynthetic process; IEA:InterPro. DR GO; GO:0006212; P:uracil catabolic process; ISS:UniProtKB. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR017896; 4Fe4S_Fe-S-bd. DR InterPro; IPR017900; 4Fe4S_Fe_S_CS. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR005720; Dihydroorotate_DH. DR InterPro; IPR012135; Dihydroorotate_DH_1_2. DR InterPro; IPR028261; DPD_II. DR InterPro; IPR009051; Helical_ferredxn. DR Pfam; PF01180; DHO_dh; 1. DR Pfam; PF14691; Fer4_20; 1. DR SUPFAM; SSF46548; SSF46548; 1. DR TIGRFAMs; TIGR01037; pyrD_sub1_fam; 1. DR PROSITE; PS00198; 4FE4S_FER_1; 1. DR PROSITE; PS51379; 4FE4S_FER_2; 3. PE 1: Evidence at protein level; KW 4Fe-4S; Acetylation; Complete proteome; Cytoplasm; FAD; Flavoprotein; KW FMN; Iron; Iron-sulfur; Metal-binding; NADP; Nucleotide-binding; KW Oxidoreductase; Phosphoprotein; Reference proteome; Repeat. FT CHAIN 1 1025 Dihydropyrimidine dehydrogenase FT [NADP(+)]. FT /FTId=PRO_0000327501. FT DOMAIN 69 100 4Fe-4S ferredoxin-type 1. FT DOMAIN 944 976 4Fe-4S ferredoxin-type 2. FT DOMAIN 978 1007 4Fe-4S ferredoxin-type 3. FT NP_BIND 194 198 FAD (By similarity). FT NP_BIND 218 226 FAD (By similarity). FT NP_BIND 340 343 NADP (By similarity). FT NP_BIND 364 365 NADP (By similarity). FT NP_BIND 437 439 NADP (By similarity). FT NP_BIND 480 489 FAD (By similarity). FT NP_BIND 481 487 NADP (By similarity). FT NP_BIND 574 575 FMN (By similarity). FT NP_BIND 793 795 FMN (By similarity). FT NP_BIND 816 817 FMN (By similarity). FT REGION 668 670 Substrate binding (By similarity). FT REGION 736 737 Substrate binding (By similarity). FT ACT_SITE 671 671 Proton acceptor (By similarity). FT METAL 79 79 Iron-sulfur 1 (4Fe-4S) (By similarity). FT METAL 82 82 Iron-sulfur 1 (4Fe-4S) (By similarity). FT METAL 87 87 Iron-sulfur 1 (4Fe-4S) (By similarity). FT METAL 91 91 Iron-sulfur 2 (4Fe-4S) (By similarity). FT METAL 130 130 Iron-sulfur 2 (4Fe-4S) (By similarity). FT METAL 136 136 Iron-sulfur 2 (4Fe-4S) (By similarity). FT METAL 140 140 Iron-sulfur 1 (4Fe-4S) (By similarity). FT METAL 156 156 Iron-sulfur 2 (4Fe-4S) (By similarity). FT METAL 953 953 Iron-sulfur 3 (4Fe-4S) (By similarity). FT METAL 956 956 Iron-sulfur 3 (4Fe-4S) (By similarity). FT METAL 959 959 Iron-sulfur 3 (4Fe-4S) (By similarity). FT METAL 963 963 Iron-sulfur 3 (4Fe-4S) (By similarity). FT METAL 986 986 Iron-sulfur 4 (4Fe-4S) (By similarity). FT METAL 989 989 Iron-sulfur 4 (4Fe-4S) (By similarity). FT METAL 992 992 Iron-sulfur 4 (4Fe-4S) (By similarity). FT METAL 996 996 Iron-sulfur 4 (4Fe-4S) (By similarity). FT BINDING 129 129 FAD; via carbonyl oxygen (By similarity). FT BINDING 235 235 FAD (By similarity). FT BINDING 261 261 FAD; via amide nitrogen and carbonyl FT oxygen (By similarity). FT BINDING 371 371 NADP (By similarity). FT BINDING 550 550 FMN (By similarity). FT BINDING 609 609 Substrate (By similarity). FT BINDING 709 709 FMN (By similarity). FT BINDING 767 767 FMN; via amide nitrogen (By similarity). FT MOD_RES 384 384 N6-acetyllysine (By similarity). FT MOD_RES 905 905 Phosphoserine. SQ SEQUENCE 1025 AA; 111253 MW; AA1D1B3E3B72C504 CRC64; MAGVLSRDAP DIESILALNP RVQAHATLRS TAAKKLDKKH WKRNTDKNCF TCEKLESNFD DIKHTTLGER GALREAVRCL KCADAPCQKS CPTSLDIKSF ITSIANKNYY GAAKLIFSDN PLGLTCGMVC PTSDLCVGGC NLHAAEEGPI NIGGLQQFAT EVFKAMNIPQ IRNPSLPPPE HMPEAYSAKI ALFGAGPASI SCASFLARLG YSNITIFEKQ EYVGGLSTSE IPQFRLPYDV VNFEIELMKD LGVKIICGKS LSTDEMTLSS LKENGYRAAF IGIGLPEPKK DHIFQGLTQV QGFYTSKDFL PLVAKSSKTG MCACHSPLPS IRGAVIVLGA GDTAFDCATS ALRCGALRVF IVFRKGFVNI RAVPEEMELA KEEKCEFLPF LSPRKVIVKD GKIVAMQFVR TEQDETGNWV EDEEQTVRLK ADVVISAFGS VLEDPKVKEA LSPIKFNRWG LPEVNPETMQ TSEPWVFAGG DVVGMANTTV ESVNDGKQAS WYIHKHIQAQ YGTSVPSQPT MPLFYTPVDL VDISVEMAGL RFPNPFGLAS ATPATSTPMI RRAFEAGWGF ALTKTFSLDK DIVTNVSPRI IRGTTSGPLY GPGQSSFLNI ELISEKTAAY WCHSVTELKA DFPDNILIAS IMCSYNKSDW MELSKMAEAS GADALELNLS CPHGMGERGM GLACGQDPEL VRNICRWVRQ AVRVPFFAKL TPNVTDIVSI ARAAKEGGAD GVTATNTVSG LMGLKADGTP WPAVGIGRRT TYGGVSGTAI RPIALRAVTA IARALPGFPI LATGGIDSAE SGLQFLHSGA SVLQVCSAIQ NQDFTVIEDY CTGLKALLYL KSIEELADWD GQSPPIISHQ KGKPVPRVAE LMGQKLPSFG PYLEQRKKII AASKIRQKDQ NTACSPLQRK HFNSQKPIPA IKDVIGKSLQ YLGTFGEMSI MEQVVALIDE EMCINCGKCY MTCNDSGYQA IQFDPETHLP TVSDTCTGCT LCLSVCPIMD CIRMVSRATP YQPKRGLPLA VKPVC // ID DR9C7_MOUSE Reviewed; 313 AA. AC Q8K3P0; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2002, sequence version 1. DT 19-MAR-2014, entry version 90. DE RecName: Full=Short-chain dehydrogenase/reductase family 9C member 7; DE EC=1.1.1.-; DE AltName: Full=Orphan short-chain dehydrogenase/reductase; DE Short=SDR-O; DE AltName: Full=RDH-S; GN Name=Sdr9c7; Synonyms=Rdhs, Sdro; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE RP SPECIFICITY. RC TISSUE=Embryo; RX PubMed=12234675; DOI=10.1016/S0378-1119(02)00757-6; RA Chen W., Song M.-S., Napoli J.L.; RT "SDR-O: an orphan short-chain dehydrogenase/reductase localized at RT mouse chromosome 10/human chromosome 12."; RL Gene 294:141-146(2002). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Skin; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Jaw, and Limb; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: Displays weak conversion of all-trans-retinal to all- CC trans-retinol in the presence of NADH. Has apparently no steroid CC dehydrogenase activity (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (Probable). CC -!- TISSUE SPECIFICITY: Highly expressed in liver. CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases CC (SDR) family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AY044433; AAK95855.1; -; mRNA. DR EMBL; AK037184; BAC29742.1; -; mRNA. DR EMBL; BC064820; AAH64820.1; -; mRNA. DR RefSeq; NP_081577.1; NM_027301.3. DR UniGene; Mm.158320; -. DR ProteinModelPortal; Q8K3P0; -. DR SMR; Q8K3P0; 24-296. DR STRING; 10090.ENSMUSP00000036628; -. DR PhosphoSite; Q8K3P0; -. DR PRIDE; Q8K3P0; -. DR Ensembl; ENSMUST00000047134; ENSMUSP00000036628; ENSMUSG00000040127. DR GeneID; 70061; -. DR KEGG; mmu:70061; -. DR UCSC; uc007hkw.1; mouse. DR CTD; 121214; -. DR MGI; MGI:1917311; Sdr9c7. DR eggNOG; COG1028; -. DR GeneTree; ENSGT00620000087655; -. DR InParanoid; Q8K3P0; -. DR OMA; IRRELHF; -. DR OrthoDB; EOG7FXZZX; -. DR TreeFam; TF325617; -. DR NextBio; 330927; -. DR PRO; PR:Q8K3P0; -. DR Bgee; Q8K3P0; -. DR CleanEx; MM_RDH20; -. DR Genevestigator; Q8K3P0; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005730; C:nucleolus; IEA:Ensembl. DR GO; GO:0004745; F:retinol dehydrogenase activity; IEA:Ensembl. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR002198; DH_sc/Rdtase_SDR. DR InterPro; IPR002347; Glc/ribitol_DH. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR020904; Sc_DH/Rdtase_CS. DR Pfam; PF00106; adh_short; 1. DR PRINTS; PR00081; GDHRDH. DR PRINTS; PR00080; SDRFAMILY. DR PROSITE; PS00061; ADH_SHORT; 1. PE 2: Evidence at transcript level; KW Complete proteome; Cytoplasm; NADP; Oxidoreductase; KW Reference proteome. FT CHAIN 1 313 Short-chain dehydrogenase/reductase FT family 9C member 7. FT /FTId=PRO_0000316886. FT NP_BIND 29 53 NADP (By similarity). FT ACT_SITE 172 172 Proton acceptor (By similarity). FT BINDING 160 160 Substrate (By similarity). SQ SEQUENCE 313 AA; 35149 MW; 8C93F6A4448911E6 CRC64; MAALTDFAFM YRWFKNCNLV KNLSEKYVFI TGCDSGFGNL LAKQLVDRGM KVLAACLTEE GAQKLLQDTS HQLQTFLLDV TKSENVKEAA QWVRDQVGEQ GLWALVNNAG VGLPSGPNEW LTIKDFVKVI NINLVGLIDV TLNMLPMIKK ARGRVVNMSS SGGRVAIFGG GYCVSKFGVE AFSDSIRREL HFFGVKVSII EPGNYKTSIL GQEALESRMK KLWDRLPQET RDSYGEEYFQ TYTKKLVNLM RSAEPRISDV TNSMEHAIVS RSPRIRYNPG LDVKFLYLTL AKLPTPVTDF ILSRYLPRPA DSV // ID DRS7C_MOUSE Reviewed; 311 AA. AC Q8CHS7; B1ATJ2; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 20-MAY-2008, sequence version 3. DT 19-FEB-2014, entry version 83. DE RecName: Full=Dehydrogenase/reductase SDR family member 7C; DE EC=1.1.-.-; DE Flags: Precursor; GN Name=Dhrs7c; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; TISSUE=Mammary gland; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-112. RA Marra M., Hillier L., Allen M., Bowles M., Dietrich N., Dubuque T., RA Geisel S., Kucaba T., Lacy M., Le M., Martin J., Morris M., RA Schellenberg K., Steptoe M., Tan F., Underwood K., Moore B., RA Theising B., Wylie T., Lennon G., Soares B., Wilson R., Waterston R.; RT "The WashU-HHMI Mouse EST Project."; RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Putative oxidoreductase (Potential). CC -!- SUBCELLULAR LOCATION: Secreted (Potential). CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases CC (SDR) family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AL646097; CAI25250.1; -; Genomic_DNA. DR EMBL; AA063835; -; NOT_ANNOTATED_CDS; mRNA. DR RefSeq; NP_001013031.2; NM_001013013.2. DR UniGene; Mm.22167; -. DR ProteinModelPortal; Q8CHS7; -. DR SMR; Q8CHS7; 31-261. DR STRING; 10090.ENSMUSP00000042780; -. DR PhosphoSite; Q8CHS7; -. DR PRIDE; Q8CHS7; -. DR DNASU; 68460; -. DR Ensembl; ENSMUST00000168612; ENSMUSP00000130924; ENSMUSG00000033044. DR GeneID; 68460; -. DR KEGG; mmu:68460; -. DR UCSC; uc011xwp.1; mouse. DR CTD; 201140; -. DR MGI; MGI:1915710; Dhrs7c. DR eggNOG; COG0300; -. DR GeneTree; ENSGT00740000115336; -. DR HOVERGEN; HBG107825; -. DR KO; K11167; -. DR OMA; DISCVQD; -. DR OrthoDB; EOG7W6WM5; -. DR TreeFam; TF313474; -. DR NextBio; 327210; -. DR PRO; PR:Q8CHS7; -. DR Bgee; Q8CHS7; -. DR Genevestigator; Q8CHS7; -. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0014801; C:longitudinal sarcoplasmic reticulum; IDA:MGI. DR GO; GO:0033017; C:sarcoplasmic reticulum membrane; IDA:MGI. DR GO; GO:0004745; F:retinol dehydrogenase activity; IDA:MGI. DR GO; GO:0010880; P:regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum; IDA:MGI. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR002198; DH_sc/Rdtase_SDR. DR InterPro; IPR002347; Glc/ribitol_DH. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR020904; Sc_DH/Rdtase_CS. DR Pfam; PF00106; adh_short; 1. DR PRINTS; PR00081; GDHRDH. DR PRINTS; PR00080; SDRFAMILY. DR PROSITE; PS00061; ADH_SHORT; 1. PE 2: Evidence at transcript level; KW Complete proteome; NAD; NADP; Oxidoreductase; Reference proteome; KW Secreted; Signal. FT SIGNAL 1 18 Potential. FT CHAIN 19 311 Dehydrogenase/reductase SDR family member FT 7C. FT /FTId=PRO_0000333756. FT NP_BIND 41 65 NAD or NADP (By similarity). FT ACT_SITE 191 191 Proton acceptor (By similarity). SQ SEQUENCE 311 AA; 34468 MW; E223E8C363153E5F CRC64; MGLMAVLMLP LLLLGISGLL FIYQEASRLW SKSAVQNKVV VITDAISGLG KECARVFHAG GARLVLCGKN WEGLESLYAT LTSVADPSKT FTPKLVLLDL SDISCVQDVA KEVLDCYGCV DILINNASVK VKGPAHKISL ELDKKIMDAN YFGPITLTKV LLPNMISRRT GQIVLVNNIQ AKFGIPFRTA YAASKHAVMG FFDCLRAEVE EYDVVVSTVS PTFIRSYRAS PEQRNWETSI CKFFCRKLAY GVHPVEVAEE VMRTVRRKKQ EVFMANPVPK AAVFIRTFFP EFFFAVVACG VKEKLNVPEE G // ID DRS7B_MOUSE Reviewed; 323 AA. AC Q99J47; Q3UNS3; Q5NCT5; DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 19-MAR-2014, entry version 104. DE RecName: Full=Dehydrogenase/reductase SDR family member 7B; DE EC=1.1.-.-; GN Name=Dhrs7b; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC STRAIN=C57BL/6J; TISSUE=Cerebellum, Embryonic heart, and Kidney; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC STRAIN=FVB/N-3; TISSUE=Mammary tumor; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: Putative oxidoreductase (Potential). CC -!- SUBCELLULAR LOCATION: Peroxisome membrane; Single-pass type II CC membrane protein (Potential). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q99J47-1; Sequence=Displayed; CC Name=2; CC IsoId=Q99J47-2; Sequence=VSP_029698; CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases CC (SDR) family. CC -!- SEQUENCE CAUTION: CC Sequence=CAI35261.1; Type=Erroneous initiation; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK052209; BAC34887.1; -; mRNA. DR EMBL; AK139084; BAE23884.1; -; mRNA. DR EMBL; AK144057; BAE25674.1; -; mRNA. DR EMBL; AL596215; CAI35261.1; ALT_INIT; Genomic_DNA. DR EMBL; BC003479; AAH03479.1; -; mRNA. DR RefSeq; NP_001165583.1; NM_001172112.1. DR RefSeq; NP_663403.1; NM_145428.2. DR UniGene; Mm.21475; -. DR ProteinModelPortal; Q99J47; -. DR SMR; Q99J47; 50-301. DR IntAct; Q99J47; 1. DR PhosphoSite; Q99J47; -. DR PaxDb; Q99J47; -. DR PRIDE; Q99J47; -. DR Ensembl; ENSMUST00000042281; ENSMUSP00000044924; ENSMUSG00000042569. [Q99J47-1] DR GeneID; 216820; -. DR KEGG; mmu:216820; -. DR UCSC; uc007jgq.2; mouse. [Q99J47-1] DR CTD; 25979; -. DR MGI; MGI:2384931; Dhrs7b. DR eggNOG; COG1028; -. DR GeneTree; ENSGT00740000115336; -. DR HOVERGEN; HBG107825; -. DR InParanoid; Q99J47; -. DR KO; K11166; -. DR OMA; GAPRVEY; -. DR OrthoDB; EOG7W6WM5; -. DR TreeFam; TF313474; -. DR NextBio; 375350; -. DR PRO; PR:Q99J47; -. DR ArrayExpress; Q99J47; -. DR Bgee; Q99J47; -. DR CleanEx; MM_DHRS7B; -. DR Genevestigator; Q99J47; -. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005778; C:peroxisomal membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR002198; DH_sc/Rdtase_SDR. DR InterPro; IPR002347; Glc/ribitol_DH. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR020904; Sc_DH/Rdtase_CS. DR Pfam; PF00106; adh_short; 1. DR PIRSF; PIRSF000126; 11-beta-HSD1; 1. DR PRINTS; PR00081; GDHRDH. DR PRINTS; PR00080; SDRFAMILY. DR PROSITE; PS00061; ADH_SHORT; 1. PE 2: Evidence at transcript level; KW Alternative splicing; Complete proteome; Membrane; NAD; NADP; KW Oxidoreductase; Peroxisome; Reference proteome; Signal-anchor; KW Transmembrane; Transmembrane helix. FT CHAIN 1 323 Dehydrogenase/reductase SDR family member FT 7B. FT /FTId=PRO_0000312106. FT TOPO_DOM 1 17 Cytoplasmic (Potential). FT TRANSMEM 18 38 Helical; Signal-anchor for type II FT membrane protein; (Potential). FT TOPO_DOM 39 323 Peroxisomal (Potential). FT NP_BIND 56 80 NAD or NADP (By similarity). FT ACT_SITE 205 205 Proton acceptor (By similarity). FT BINDING 192 192 Substrate (Potential). FT VAR_SEQ 1 9 Missing (in isoform 2). FT /FTId=VSP_029698. SQ SEQUENCE 323 AA; 34987 MW; 6C75A07F9BC9B398 CRC64; MISPSFRKGM LKERVMDLAS QTTILPLLFG CLGIFSLFRL LQRIRSKAYL RNAVVVVTGA TSGLGRECAK VFHAAGAKLV LCGRNVKALE ELSRELAGSS QGQTHQPFVV TFDLADPGTI AAAAAEILQC FGYVDVLINN AGISYRGTIS DTIVDVDRKV MEINYFGPVA LTKALLPSMV ERKQGHIVAI SSIQGKISIP FRSAYSASKH ATQAFFDCLR AEMEEANIKV TVISPGYIHT NLSVNAVTAD GSRYGALDKN TAQGRSAAEV AQDVFDAVGK KKKDVLLTDF VPSMAVYIRT LAPGLFFRIM ASRARKERKS KSS // ID DUS1L_MOUSE Reviewed; 475 AA. AC Q8C2P3; Q8VCN7; Q9D124; DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 19-MAR-2014, entry version 86. DE RecName: Full=tRNA-dihydrouridine(16/17) synthase [NAD(P)(+)]-like; DE EC=1.3.1.-; DE AltName: Full=tRNA-dihydrouridine synthase 1-like; GN Name=Dus1l; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=NOD; TISSUE=Embryo, and Thymus; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 86-475. RC STRAIN=FVB/N; TISSUE=Mammary gland; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: Catalyzes the synthesis of dihydrouridine, a modified CC base found in the D-loop of most tRNAs (By similarity). CC -!- COFACTOR: FAD (By similarity). CC -!- SIMILARITY: Belongs to the Dus family. Dus1 subfamily. CC -!- SEQUENCE CAUTION: CC Sequence=AAH19480.1; Type=Erroneous initiation; CC Sequence=BAB23138.1; Type=Erroneous initiation; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK004041; BAB23138.1; ALT_INIT; mRNA. DR EMBL; AK088243; BAC40231.1; -; mRNA. DR EMBL; BC019480; AAH19480.1; ALT_INIT; mRNA. DR RefSeq; NP_081100.2; NM_026824.4. DR RefSeq; XP_006534140.1; XM_006534077.1. DR UniGene; Mm.180622; -. DR ProteinModelPortal; Q8C2P3; -. DR SMR; Q8C2P3; 16-310. DR PaxDb; Q8C2P3; -. DR PRIDE; Q8C2P3; -. DR Ensembl; ENSMUST00000167023; ENSMUSP00000132516; ENSMUSG00000025155. DR GeneID; 68730; -. DR KEGG; mmu:68730; -. DR UCSC; uc007mur.1; mouse. DR CTD; 64118; -. DR MGI; MGI:1915980; Dus1l. DR eggNOG; COG0042; -. DR GeneTree; ENSGT00550000075089; -. DR HOVERGEN; HBG061241; -. DR InParanoid; Q8C2P3; -. DR KO; K05542; -. DR OrthoDB; EOG7FR7G9; -. DR NextBio; 327790; -. DR PRO; PR:Q8C2P3; -. DR ArrayExpress; Q8C2P3; -. DR Bgee; Q8C2P3; -. DR CleanEx; MM_DUS1L; -. DR Genevestigator; Q8C2P3; -. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. DR GO; GO:0017150; F:tRNA dihydrouridine synthase activity; IEA:InterPro. DR GO; GO:0002943; P:tRNA dihydrouridine synthesis; IEA:GOC. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR001269; tRNA_hU_synthase. DR InterPro; IPR018517; tRNA_hU_synthase_CS. DR PANTHER; PTHR11082; PTHR11082; 1. DR Pfam; PF01207; Dus; 1. DR PROSITE; PS01136; UPF0034; 1. PE 2: Evidence at transcript level; KW Complete proteome; FAD; Flavoprotein; Oxidoreductase; KW Reference proteome; tRNA processing. FT CHAIN 1 475 tRNA-dihydrouridine(16/17) synthase FT [NAD(P)(+)]-like. FT /FTId=PRO_0000247227. FT CONFLICT 243 244 EG -> DD (in Ref. 1; BAB23138). SQ SEQUENCE 475 AA; 53512 MW; F1CC2254238CD679 CRC64; MPKLQGFEFW SRTLGGARHV VAPMVDQSEL AWRLLSRRHG AQLCYTPMLH AQVFVRDANY RKENLYCDVC PEDRPLIVQF CANDPEVFVQ AALLAQDYCD AIDLNLGCPQ MIAKRGHYGA FLQEEWDLLQ RMILLAHERL SVPVTCKIRV FPEIDKTVRY AQMLEKAGCQ LLTVHGRTKE QKGPMAGTAS WEHIKAVRKA VGIPVFANGN IQCLQDVERC IQDTGVQGVM SAEGNLHNPA LFEGRSPAVW ELAEEYLDIV RQHPCPLSYV RAHLFKLWHH TLQVHQQLRE ELAKVKTLEG VAAVSQALKL RCQEDMSRQQ EGVRPADNLP AFHWICQPYI RPGPREGSKE NSGGRSKRAL EEEEGSMEGL SKNKLKKQLR NPHKTFDPSL KPKYAKCDQC GNPKGNRCVF NLCRGCCKKR AFRETADCPG HGLLFKTKLE KSLAWKGTQP GLQEAQQVRP VTPSGFSEVV GSALA // ID DUS2L_MOUSE Reviewed; 493 AA. AC Q9D7B1; Q6PDX2; DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 19-MAR-2014, entry version 95. DE RecName: Full=tRNA-dihydrouridine(20) synthase [NAD(P)+]-like; DE EC=1.3.1.-; DE AltName: Full=Dihydrouridine synthase 2; DE AltName: Full=tRNA-dihydrouridine synthase 2-like; GN Name=Dus2; Synonyms=Dus2l; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Tongue; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 205-493. RC STRAIN=C57BL/6; TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP STRUCTURE BY NMR OF 350-464. RG RIKEN structural genomics initiative (RSGI); RT "Solution structure of the DSRBD from hypothetical protein BAB26260."; RL Submitted (NOV-2004) to the PDB data bank. CC -!- FUNCTION: Dihydrouridine synthase. Catalyzes the synthesis of CC dihydrouridine, a modified base found in the D-loop of most tRNAs CC (By similarity). Negatively regulates the activation of CC EIF2AK2/PKR (By similarity). CC -!- COFACTOR: FAD (By similarity). CC -!- SUBUNIT: Interacts with EPRS (By similarity). Interacts (via DRBM CC domain) with PRKRA and EIF2AK2/PKR (via DRBM 1 domain) (By CC similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Endoplasmic CC reticulum (By similarity). Note=Mainly at the endoplasmic CC reticulum (By similarity). CC -!- SIMILARITY: Belongs to the Dus family. Dus2 subfamily. CC -!- SIMILARITY: Contains 1 DRBM (double-stranded RNA-binding) domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK009391; BAB26260.1; -; mRNA. DR EMBL; BC058431; AAH58431.1; -; mRNA. DR RefSeq; NP_079794.1; NM_025518.3. DR RefSeq; XP_006531341.1; XM_006531278.1. DR UniGene; Mm.287500; -. DR PDB; 1WHN; NMR; -; A=350-464. DR PDBsum; 1WHN; -. DR ProteinModelPortal; Q9D7B1; -. DR SMR; Q9D7B1; 13-313, 352-464. DR PhosphoSite; Q9D7B1; -. DR PaxDb; Q9D7B1; -. DR PRIDE; Q9D7B1; -. DR Ensembl; ENSMUST00000034375; ENSMUSP00000034375; ENSMUSG00000031901. DR GeneID; 66369; -. DR KEGG; mmu:66369; -. DR UCSC; uc009nfa.1; mouse. DR CTD; 54920; -. DR MGI; MGI:1913619; Dus2. DR eggNOG; COG0042; -. DR GeneTree; ENSGT00550000075019; -. DR HOGENOM; HOG000195580; -. DR HOVERGEN; HBG079551; -. DR InParanoid; Q9D7B1; -. DR KO; K05543; -. DR OMA; EDTSGVI; -. DR TreeFam; TF106151; -. DR EvolutionaryTrace; Q9D7B1; -. DR NextBio; 321469; -. DR PRO; PR:Q9D7B1; -. DR ArrayExpress; Q9D7B1; -. DR Bgee; Q9D7B1; -. DR Genevestigator; Q9D7B1; -. DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR GO; GO:0003725; F:double-stranded RNA binding; ISS:UniProtKB. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. DR GO; GO:0004860; F:protein kinase inhibitor activity; ISS:UniProtKB. DR GO; GO:0017150; F:tRNA dihydrouridine synthase activity; IEA:InterPro. DR GO; GO:0060548; P:negative regulation of cell death; ISS:UniProtKB. DR GO; GO:0002943; P:tRNA dihydrouridine synthesis; IEA:GOC. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.30.160.20; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR014720; dsRNA-bd_dom. DR InterPro; IPR001269; tRNA_hU_synthase. DR InterPro; IPR018517; tRNA_hU_synthase_CS. DR PANTHER; PTHR11082; PTHR11082; 1. DR Pfam; PF00035; dsrm; 1. DR Pfam; PF01207; Dus; 1. DR SMART; SM00358; DSRM; 1. DR PROSITE; PS01136; UPF0034; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Cytoplasm; Endoplasmic reticulum; KW FAD; Flavoprotein; Oxidoreductase; Reference proteome; RNA-binding; KW tRNA processing. FT CHAIN 1 493 tRNA-dihydrouridine(20) synthase FT [NAD(P)+]-like. FT /FTId=PRO_0000162158. FT DOMAIN 369 436 DRBM. FT STRAND 350 355 FT HELIX 361 363 FT HELIX 370 380 FT STRAND 390 392 FT STRAND 394 396 FT STRAND 399 405 FT STRAND 408 414 FT STRAND 416 418 FT HELIX 419 434 FT STRAND 437 439 FT TURN 440 442 SQ SEQUENCE 493 AA; 55325 MW; B66BDCB06B096299 CRC64; MIVNSLSLCY HNKLILAPMV RVGTLPMRLL ALDYGADIVY CEELIDLKML QCKRVVNEVL STVDFVAPDD RVVFRTCERE QSRVVFQMGT SDAERALAVA RLVENDVAGI DVNMGCPKEY STKGGMGAAL LSDPDKIEKI LSTLVKGTHR PVTCKIRILP SLEDTLNLVK RIERTGISAI AVHGRNRDER PQHPVSCEVI RAIAETLSIP VIANGGSHDH IQQHVDIEDF RQATAASSVM VARAAMWNPS IFLKDGLRPL EEVMQKYIRY AVQYDNHYTN TKYCLCQMLR EQLESPQGRL LHAAQSSQEI CEAFGLGAFY EETIRELDAR RADLLAKTPE AVEEPAEDTS GIIKMAIRFD RRAYPPQITP KMCLLEWCRR EKLPQPVYET VQRTIDRMFC SVVTVAEQKY QSTLWDKSKK LAEQTAAIVC LRSQGLPEGR LGEESPSLNK RKREAPDQDP GGPRVQEPAL PGEICKKPFV TLDSSEENLL EGC // ID DUS3L_MOUSE Reviewed; 637 AA. AC Q91XI1; Q3TZQ1; Q7TT12; DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 19-MAR-2014, entry version 90. DE RecName: Full=tRNA-dihydrouridine(47) synthase [NAD(P)(+)]-like; DE EC=1.3.1.-; DE AltName: Full=tRNA-dihydrouridine synthase 3-like; GN Name=Dus3l; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC STRAIN=BALB/c; TISSUE=Heart; RA Leu M., Ehler E., Perriard J.-C.; RT "Cloning of a putative zinc finger protein."; RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC STRAIN=NOD; TISSUE=Spleen; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Eye; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: Catalyzes the synthesis of dihydrouridine, a modified CC base found in the D-loop of most tRNAs (By similarity). CC -!- COFACTOR: FAD (By similarity). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q91XI1-1; Sequence=Displayed; CC Name=2; CC IsoId=Q91XI1-2; Sequence=VSP_019973, VSP_019974; CC Note=No experimental confirmation available; CC -!- SIMILARITY: Belongs to the Dus family. Dus3 subfamily. CC -!- SIMILARITY: Contains 2 C3H1-type zinc fingers. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AY040840; AAK84684.1; -; mRNA. DR EMBL; AK157702; BAE34157.1; -; mRNA. DR EMBL; BC052481; AAH52481.1; -; mRNA. DR RefSeq; NP_659107.2; NM_144858.2. DR UniGene; Mm.293973; -. DR ProteinModelPortal; Q91XI1; -. DR SMR; Q91XI1; 110-171, 293-569. DR PhosphoSite; Q91XI1; -. DR PaxDb; Q91XI1; -. DR PRIDE; Q91XI1; -. DR Ensembl; ENSMUST00000007747; ENSMUSP00000007747; ENSMUSG00000007603. DR GeneID; 224907; -. DR KEGG; mmu:224907; -. DR UCSC; uc008ddd.2; mouse. [Q91XI1-1] DR CTD; 56931; -. DR MGI; MGI:2147092; Dus3l. DR eggNOG; COG0042; -. DR GeneTree; ENSGT00550000075134; -. DR HOGENOM; HOG000240610; -. DR HOVERGEN; HBG062413; -. DR InParanoid; Q91XI1; -. DR KO; K05544; -. DR OrthoDB; EOG76HQ12; -. DR TreeFam; TF105726; -. DR NextBio; 377458; -. DR PRO; PR:Q91XI1; -. DR Bgee; Q91XI1; -. DR CleanEx; MM_DUS3L; -. DR Genevestigator; Q91XI1; -. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0017150; F:tRNA dihydrouridine synthase activity; IEA:InterPro. DR GO; GO:0002943; P:tRNA dihydrouridine synthesis; IEA:GOC. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR001269; tRNA_hU_synthase. DR InterPro; IPR018517; tRNA_hU_synthase_CS. DR InterPro; IPR000571; Znf_CCCH. DR PANTHER; PTHR11082; PTHR11082; 1. DR Pfam; PF01207; Dus; 1. DR PROSITE; PS01136; UPF0034; 1. DR PROSITE; PS50103; ZF_C3H1; 2. PE 2: Evidence at transcript level; KW Alternative splicing; Complete proteome; FAD; Flavoprotein; KW Metal-binding; Oxidoreductase; Phosphoprotein; Reference proteome; KW Repeat; tRNA processing; Zinc; Zinc-finger. FT CHAIN 1 637 tRNA-dihydrouridine(47) synthase FT [NAD(P)(+)]-like. FT /FTId=PRO_0000247343. FT ZN_FING 107 137 C3H1-type 1. FT ZN_FING 145 175 C3H1-type 2. FT MOD_RES 260 260 Phosphothreonine (By similarity). FT VAR_SEQ 392 457 GGGCALMNRSAKFQQIVRGVNGVLDVPLTVKMRTGVQERVS FT LAHRLLPELRDWGVALVTLHGRSRE -> VMAALPWSLGWV FT WPKPGTLPCWPCVSVSPSGHGAH (in isoform 2). FT /FTId=VSP_019973. FT VAR_SEQ 458 637 Missing (in isoform 2). FT /FTId=VSP_019974. FT CONFLICT 413 413 G -> E (in Ref. 2; BAE34157). SQ SEQUENCE 637 AA; 71078 MW; 759FE837CAEBC34A CRC64; MAETAAESGG GGDSGVGACE RGVAPIKAQY RTTKERFHEY LDGDKQEGAC QEVPTGDPAE PGAKRIRLED GQENGKTEVA IESRERQVPK RARGQNKSRP HVKPAHYDKD RLCPSFLQEP ATPCAFGDRC RFLHDVGRYL ETKPADLGPR CVLFETFGRC PFSMTCRFAG AHLGPEGQNL VQEEVVARCA QLPSVRNGLD RALQQQLRKR QVCFERAEQA LNRLTQSPMP TVVPETTVAM ATPKQNSCHA QLDTVGGAGT PQSSPVPTCG PLTDEDVIRL RPCEKKRLDI SGKLYLAPLT TCGNLPFRRI CKRFGADVTC GEMAVCTNLL QGQMSEWALL KRHPCEDIFG VQLEGAFPDT MTKCAELLNR TIDVDFVDIN VGCPIDLVYK KGGGCALMNR SAKFQQIVRG VNGVLDVPLT VKMRTGVQER VSLAHRLLPE LRDWGVALVT LHGRSREQRY TRLADWPYIE QCAKVASPMP LFGNGDILSF EDANCAMQTG VAGIMVARGA LLKPWLFTEI KEQRHWDISS SERLDILRDF THYGLEHWGS DTQGVERTRR FLLEWLSFLC RYVPVGLLER PPQRINERPP YYLGRDYLET LMASQQAADW IRISEMLLGP VPPGFVFLPK HKANAYK // ID DUS4L_MOUSE Reviewed; 324 AA. AC Q32M08; Q9D6P4; DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot. DT 06-DEC-2005, sequence version 1. DT 19-MAR-2014, entry version 64. DE RecName: Full=tRNA-dihydrouridine(20a/20b) synthase [NAD(P)+]-like; DE EC=1.3.1.-; DE AltName: Full=tRNA-dihydrouridine synthase 4-like; GN Name=Dus4l; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Tongue; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: Catalyzes the synthesis of dihydrouridine, a modified CC base found in the D-loop of most tRNAs (By similarity). CC -!- COFACTOR: FAD (By similarity). CC -!- SIMILARITY: Belongs to the Dus family. Dus4 subfamily. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK010138; BAB26724.1; -; mRNA. DR EMBL; BC109351; AAI09352.1; -; mRNA. DR RefSeq; NP_082278.1; NM_028002.2. DR UniGene; Mm.62979; -. DR ProteinModelPortal; Q32M08; -. DR SMR; Q32M08; 26-317. DR STRING; 10090.ENSMUSP00000020977; -. DR PRIDE; Q32M08; -. DR Ensembl; ENSMUST00000020977; ENSMUSP00000020977; ENSMUSG00000020648. DR GeneID; 71916; -. DR KEGG; mmu:71916; -. DR UCSC; uc007nhr.1; mouse. DR CTD; 11062; -. DR MGI; MGI:1919166; Dus4l. DR eggNOG; COG0042; -. DR GeneTree; ENSGT00550000074907; -. DR HOGENOM; HOG000203649; -. DR HOVERGEN; HBG053313; -. DR InParanoid; Q32M08; -. DR KO; K05545; -. DR OrthoDB; EOG751NG3; -. DR TreeFam; TF105618; -. DR NextBio; 334944; -. DR PRO; PR:Q32M08; -. DR Bgee; Q32M08; -. DR CleanEx; MM_DUS4L; -. DR Genevestigator; Q32M08; -. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. DR GO; GO:0017150; F:tRNA dihydrouridine synthase activity; IEA:InterPro. DR GO; GO:0002943; P:tRNA dihydrouridine synthesis; IEA:GOC. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR001269; tRNA_hU_synthase. DR InterPro; IPR018517; tRNA_hU_synthase_CS. DR PANTHER; PTHR11082; PTHR11082; 1. DR Pfam; PF01207; Dus; 1. DR PIRSF; PIRSF006621; Dus; 1. DR PROSITE; PS01136; UPF0034; 1. PE 2: Evidence at transcript level; KW Complete proteome; FAD; Flavoprotein; Oxidoreductase; KW Reference proteome; tRNA processing. FT CHAIN 1 324 tRNA-dihydrouridine(20a/20b) synthase FT [NAD(P)+]-like. FT /FTId=PRO_0000247348. FT CONFLICT 245 245 A -> T (in Ref. 1; BAB26724). SQ SEQUENCE 324 AA; 36620 MW; 0E6FB06B8F1A3B7D CRC64; MRSDSLPTTI CQERKKDPIE MFHSGQLVKV CAPMVRYSKL AFRTLVRKYS CDLCYTPMII AADFVRSIKA RDSEFTTNQG DCPLIVQFAA NDARLLSDAA LLVCPYANGI DINCGCPQRW AMADGYGACL INKPELVHDM VRQVRNRVES PRFSVSIKIR IHDDLARTID LCRKAEATGV SWITVHGRTV EERHQPVHYD AIKMIKENVS IPIVANGDIR SLKEAENVWQ MTGTDGVMVA RGLLANPAMF AGYEETPLKC IWDWVDISLE LGTPFMCFHQ HLMYMMEKIT SRQEKRVFNA LSSTSAVLDY LTDHYGDESL SKSL // ID DYR_MOUSE Reviewed; 187 AA. AC P00375; P70693; Q61485; Q61487; Q61579; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 19-MAR-2014, entry version 134. DE RecName: Full=Dihydrofolate reductase; DE EC=1.5.1.3; GN Name=Dhfr; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=6282858; RA Crouse G.F., Simonsen C.C., McEwan R.N., Schimke R.T.; RT "Structure of amplified normal and variant dihydrofolate reductase RT genes in mouse sarcoma S180 cells."; RL J. Biol. Chem. 257:7887-7897(1982). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=6573667; DOI=10.1073/pnas.80.9.2495; RA Simonsen C.C., Levinson A.D.; RT "Isolation and expression of an altered mouse dihydrofolate reductase RT cDNA."; RL Proc. Natl. Acad. Sci. U.S.A. 80:2495-2499(1983). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=2263462; DOI=10.1093/nar/18.23.7025; RA McIvor R.S., Simonsen C.C.; RT "Isolation and characterization of a variant dihydrofolate reductase RT cDNA from methotrexate-resistant murine L5178Y cells."; RL Nucleic Acids Res. 18:7025-7032(1990). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Mammary gland; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP PROTEIN SEQUENCE OF 2-187. RC TISSUE=Lymphoma; RX PubMed=762074; RA Stone D., Paterson S.J., Raper J.H., Phillips A.W.; RT "The amino acid sequence of dihydrofolate reductase from the mouse RT lymphoma L1210."; RL J. Biol. Chem. 254:480-488(1979). RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-28. RX PubMed=2982814; RA McGrogan M., Simonsen C.C., Smouse D.T., Farnham P.J., Schimke R.T.; RT "Heterogeneity at the 5' termini of mouse dihydrofolate reductase RT mRNAs. Evidence for multiple promoter regions."; RL J. Biol. Chem. 260:2307-2314(1985). RN [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 1-24; 50-127 AND 154-187. RX PubMed=6244105; DOI=10.1016/0092-8674(80)90510-3; RA Nunberg J.H., Kaufman R.J., Chang A.C.Y., Cohen S.N., Schimke R.T.; RT "Structure and genomic organization of the mouse dihydrofolate RT reductase gene."; RL Cell 19:355-364(1980). RN [8] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-24 AND 50-127. RX PubMed=360074; DOI=10.1038/275617a0; RA Chang A.C.Y., Nunberg J.H., Kaufman R.J., Erlich H.A., Schimke R.T., RA Cohen S.N.; RT "Phenotypic expression in E. coli of a DNA sequence coding for mouse RT dihydrofolate reductase."; RL Nature 275:617-624(1978). RN [9] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 163-187. RX PubMed=6121807; RA Setzer D.R., McGrogan M., Schimke R.T.; RT "Nucleotide sequence surrounding multiple polyadenylation sites in the RT mouse dihydrofolate reductase gene."; RL J. Biol. Chem. 257:5143-5147(1982). RN [10] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-33, SUCCINYLATION [LARGE RP SCALE ANALYSIS] AT LYS-33, AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic fibroblast, and Liver; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., RA Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). RN [11] RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) IN COMPLEX WITH NADP AND RP METHOTREXATE, AND CHARACTERIZATION OF METHOTREXATE-RESISTANT VARIANT RP ARG-23. RX PubMed=15681865; DOI=10.1107/S0907444904030422; RA Cody V., Luft J.R., Pangborn W.; RT "Understanding the role of Leu22 variants in methotrexate resistance: RT comparison of wild-type and Leu22Arg variant mouse and human RT dihydrofolate reductase ternary crystal complexes with methotrexate RT and NADPH."; RL Acta Crystallogr. D 61:147-155(2005). RN [12] RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH NADP AND RP SYNTHETIC INHIBITOR. RX PubMed=17019704; DOI=10.1002/prot.21131; RA Cody V., Pace J., Chisum K., Rosowsky A.; RT "New insights into DHFR interactions: analysis of Pneumocystis carinii RT and mouse DHFR complexes with NADPH and two highly potent 5-(omega- RT carboxy(alkyloxy) trimethoprim derivatives reveals conformational RT correlations with activity and novel parallel ring stacking RT interactions."; RL Proteins 65:959-969(2006). RN [13] RP X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) IN COMPLEXES WITH NADP AND RP SYNTHETIC INHIBITOR. RX PubMed=18703847; DOI=10.1107/S0907444908022348; RA Cody V., Pace J., Rosowsky A.; RT "Structural analysis of a holoenzyme complex of mouse dihydrofolate RT reductase with NADPH and a ternary complex with the potent and RT selective inhibitor 2,4-diamino-6-(2'-hydroxydibenz[b,f]azepin-5- RT yl)methylpteridine."; RL Acta Crystallogr. D 64:977-984(2008). RN [14] RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) IN COMPLEXES WITH NADP AND RP SYNTHETIC INHIBITOR, AND CATALYTIC ACTIVITY. RX PubMed=19748785; DOI=10.1016/j.bmc.2009.08.044; RA Gangjee A., Li W., Lin L., Zeng Y., Ihnat M., Warnke L.A., Green D.W., RA Cody V., Pace J., Queener S.F.; RT "Design, synthesis, and X-ray crystal structures of 2,4- RT diaminofuro[2,3-d]pyrimidines as multireceptor tyrosine kinase and RT dihydrofolate reductase inhibitors."; RL Bioorg. Med. Chem. 17:7324-7336(2009). CC -!- FUNCTION: Key enzyme in folate metabolism. Contributes to the de CC novo mitochondrial thymidylate biosynthesis pathway. Catalyzes an CC essential reaction for de novo glycine and purine synthesis, and CC for DNA precursor synthesis. Binds its own mRNA and that of CC DHFRL1. CC -!- CATALYTIC ACTIVITY: 5,6,7,8-tetrahydrofolate + NADP(+) = 7,8- CC dihydrofolate + NADPH. CC -!- PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis; CC 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SIMILARITY: Belongs to the dihydrofolate reductase family. CC -!- SIMILARITY: Contains 1 DHFR (dihydrofolate reductase) domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; V00734; CAA24112.1; -; mRNA. DR EMBL; X56066; CAA39544.1; -; mRNA. DR EMBL; BC005796; AAH05796.1; -; mRNA. DR EMBL; M10071; AAA37637.1; -; Genomic_DNA. DR EMBL; L26316; AAA37523.1; -; mRNA. DR EMBL; J00387; AAA37638.1; -; Genomic_DNA. DR EMBL; J00382; AAA37638.1; JOINED; Genomic_DNA. DR EMBL; J00383; AAA37638.1; JOINED; Genomic_DNA. DR EMBL; J00384; AAA37638.1; JOINED; Genomic_DNA. DR EMBL; J00385; AAA37638.1; JOINED; Genomic_DNA. DR EMBL; J00386; AAA37638.1; JOINED; Genomic_DNA. DR EMBL; V00731; CAB43539.2; -; mRNA. DR EMBL; M10722; AAA37524.1; -; mRNA. DR EMBL; M10811; AAA37525.1; -; mRNA. DR EMBL; V00733; CAA24111.1; -; Genomic_DNA. DR PIR; S13096; RDMSD. DR RefSeq; NP_034179.1; NM_010049.3. DR UniGene; Mm.23695; -. DR PDB; 1U70; X-ray; 2.50 A; A=2-186. DR PDB; 2FZJ; X-ray; 2.00 A; A=2-186. DR PDB; 3D80; X-ray; 1.40 A; A=2-187. DR PDB; 3D84; X-ray; 1.90 A; X=2-187. DR PDB; 3K45; X-ray; 1.60 A; A=2-187. DR PDB; 3K47; X-ray; 2.05 A; A=2-187. DR PDBsum; 1U70; -. DR PDBsum; 2FZJ; -. DR PDBsum; 3D80; -. DR PDBsum; 3D84; -. DR PDBsum; 3K45; -. DR PDBsum; 3K47; -. DR ProteinModelPortal; P00375; -. DR SMR; P00375; 2-187. DR IntAct; P00375; 2. DR MINT; MINT-4093753; -. DR BindingDB; P00375; -. DR ChEMBL; CHEMBL4564; -. DR PhosphoSite; P00375; -. DR PaxDb; P00375; -. DR PRIDE; P00375; -. DR Ensembl; ENSMUST00000022218; ENSMUSP00000022218; ENSMUSG00000021707. DR GeneID; 13361; -. DR KEGG; mmu:13361; -. DR UCSC; uc007rkl.1; mouse. DR CTD; 1719; -. DR MGI; MGI:94890; Dhfr. DR eggNOG; COG0262; -. DR HOGENOM; HOG000040235; -. DR HOVERGEN; HBG000773; -. DR InParanoid; P00375; -. DR KO; K00287; -. DR OMA; SDTFFSE; -. DR OrthoDB; EOG7V1FS3; -. DR TreeFam; TF317636; -. DR Reactome; REACT_188937; Metabolism. DR SABIO-RK; P00375; -. DR UniPathway; UPA00077; UER00158. DR EvolutionaryTrace; P00375; -. DR NextBio; 283696; -. DR PRO; PR:P00375; -. DR ArrayExpress; P00375; -. DR Bgee; P00375; -. DR CleanEx; MM_DHFR; -. DR Genevestigator; P00375; -. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0004146; F:dihydrofolate reductase activity; ISS:UniProtKB. DR GO; GO:0051871; F:dihydrofolic acid binding; IEA:Ensembl. DR GO; GO:0008144; F:drug binding; ISS:UniProtKB. DR GO; GO:0003729; F:mRNA binding; ISS:UniProtKB. DR GO; GO:0050661; F:NADP binding; IEA:Ensembl. DR GO; GO:0046452; P:dihydrofolate metabolic process; IEA:Ensembl. DR GO; GO:0006545; P:glycine biosynthetic process; IEA:InterPro. DR GO; GO:0009165; P:nucleotide biosynthetic process; IEA:InterPro. DR GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW. DR GO; GO:0031427; P:response to methotrexate; IEA:UniProtKB-KW. DR GO; GO:0035094; P:response to nicotine; IEA:Ensembl. DR GO; GO:0046654; P:tetrahydrofolate biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0046653; P:tetrahydrofolate metabolic process; ISS:UniProtKB. DR Gene3D; 3.40.430.10; -; 1. DR InterPro; IPR012259; DHFR. DR InterPro; IPR024072; DHFR-like_dom. DR InterPro; IPR017925; DHFR_CS. DR InterPro; IPR001796; DHFR_dom. DR Pfam; PF00186; DHFR_1; 1. DR PRINTS; PR00070; DHFR. DR SUPFAM; SSF53597; SSF53597; 1. DR PROSITE; PS00075; DHFR_1; 1. DR PROSITE; PS51330; DHFR_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Complete proteome; KW Direct protein sequencing; Methotrexate resistance; NADP; KW One-carbon metabolism; Oxidoreductase; Reference proteome; KW RNA-binding. FT INIT_MET 1 1 Removed. FT CHAIN 2 187 Dihydrofolate reductase. FT /FTId=PRO_0000186364. FT DOMAIN 4 185 DHFR. FT NP_BIND 16 22 NADP. FT NP_BIND 55 57 NADP. FT NP_BIND 77 79 NADP. FT NP_BIND 117 124 NADP. FT REGION 31 36 Substrate binding. FT BINDING 10 10 NADP; via amide nitrogen and carbonyl FT oxygen. FT BINDING 71 71 Substrate. FT MOD_RES 33 33 N6-acetyllysine; alternate. FT MOD_RES 33 33 N6-succinyllysine; alternate. FT VARIANT 23 23 L -> R (in a form with an abnormally low FT affinity for methotrexate). FT VARIANT 32 32 F -> W (in L-5178-Y cell line; FT methotrexate-resistant, requires 2 FT nucleotide substitutions). FT CONFLICT 4 4 P -> A (in Ref. 6; AAA37637). FT CONFLICT 14 14 N -> D (in Ref. 3; CAA39544). FT CONFLICT 123 123 Q -> E (in Ref. 5; AA sequence and 8; FT AAA37525). FT CONFLICT 124 124 E -> Q (in Ref. 5; AA sequence). FT CONFLICT 128 128 Q -> E (in Ref. 5; AA sequence). FT CONFLICT 174 174 K -> D (in Ref. 5; AA sequence). FT STRAND 4 11 FT STRAND 15 19 FT STRAND 24 26 FT HELIX 29 40 FT STRAND 43 46 FT STRAND 50 54 FT HELIX 55 60 FT HELIX 63 65 FT STRAND 71 76 FT STRAND 88 93 FT HELIX 94 101 FT HELIX 104 109 FT STRAND 113 115 FT HELIX 119 126 FT STRAND 128 130 FT STRAND 132 139 FT STRAND 146 148 FT TURN 154 156 FT STRAND 157 159 FT STRAND 171 173 FT STRAND 176 185 SQ SEQUENCE 187 AA; 21606 MW; 47AEF15F879B119C CRC64; MVRPLNCIVA VSQNMGIGKN GDLPWPPLRN EFKYFQRMTT TSSVEGKQNL VIMGRKTWFS IPEKNRPLKD RINIVLSREL KEPPRGAHFL AKSLDDALRL IEQPELASKV DMVWIVGGSS VYQEAMNQPG HLRLFVTRIM QEFESDTFFP EIDLGKYKLL PEYPGVLSEV QEEKGIKYKF EVYEKKD // ID ECHA_MOUSE Reviewed; 763 AA. AC Q8BMS1; Q3TCY3; Q5U5Y5; Q8QZU4; DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 19-MAR-2014, entry version 114. DE RecName: Full=Trifunctional enzyme subunit alpha, mitochondrial; DE AltName: Full=TP-alpha; DE Includes: DE RecName: Full=Long-chain enoyl-CoA hydratase; DE EC=4.2.1.17; DE Includes: DE RecName: Full=Long chain 3-hydroxyacyl-CoA dehydrogenase; DE EC=1.1.1.211; DE Flags: Precursor; GN Name=Hadha; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J, and NOD; TISSUE=Skin; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Eye, Liver, and Olfactory epithelium; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-129, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=16916647; DOI=10.1016/j.molcel.2006.06.026; RA Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T., RA Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.; RT "Substrate and functional diversity of lysine acetylation revealed by RT a proteomics survey."; RL Mol. Cell 23:607-618(2006). RN [4] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-60 AND LYS-406, RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-46; LYS-60; LYS-166; RP LYS-213; LYS-214; LYS-230; LYS-249; LYS-303; LYS-326; LYS-334; RP LYS-350; LYS-406; LYS-411; LYS-415; LYS-436; LYS-440; LYS-460; RP LYS-505; LYS-519; LYS-569; LYS-620; LYS-634; LYS-644; LYS-646; RP LYS-664; LYS-728 AND LYS-759, AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic fibroblast, and Liver; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., RA Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). RN [5] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-46; LYS-60; LYS-129; RP LYS-166; LYS-214; LYS-249; LYS-289; LYS-303; LYS-326; LYS-334; RP LYS-350; LYS-353; LYS-406; LYS-411; LYS-436; LYS-460; LYS-505; RP LYS-519; LYS-540; LYS-569; LYS-644; LYS-664; LYS-728; LYS-735 AND RP LYS-759, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Liver; RX PubMed=23576753; DOI=10.1073/pnas.1302961110; RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., RA Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.; RT "Label-free quantitative proteomics of the lysine acetylome in RT mitochondria identifies substrates of SIRT3 in metabolic pathways."; RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013). CC -!- FUNCTION: Bifunctional subunit. CC -!- CATALYTIC ACTIVITY: (3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl- CC CoA + H(2)O. CC -!- CATALYTIC ACTIVITY: A long-chain (S)-3-hydroxyacyl-CoA + NAD(+) = CC a long-chain 3-oxoacyl-CoA + NADH. CC -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation. CC -!- SUBUNIT: Octamer of 4 alpha (HADHA) and 4 beta (HADHB) subunits CC (By similarity). CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix (By similarity). CC -!- PTM: Acetylation of Lys-569 and Lys-728 is observed in liver CC mitochondria from fasted mice but not from fed mice. CC -!- SIMILARITY: In the N-terminal section; belongs to the enoyl-CoA CC hydratase/isomerase family. CC -!- SIMILARITY: In the central section; belongs to the 3-hydroxyacyl- CC CoA dehydrogenase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK029017; BAC26245.1; -; mRNA. DR EMBL; AK170478; BAE41822.1; -; mRNA. DR EMBL; AK170683; BAE41956.1; -; mRNA. DR EMBL; BC027156; AAH27156.1; -; mRNA. DR EMBL; BC037009; AAH37009.1; -; mRNA. DR EMBL; BC046978; AAH46978.1; -; mRNA. DR EMBL; BC058569; AAH58569.1; -; mRNA. DR RefSeq; NP_849209.1; NM_178878.2. DR UniGene; Mm.200497; -. DR ProteinModelPortal; Q8BMS1; -. DR SMR; Q8BMS1; 44-761. DR BioGrid; 220648; 3. DR IntAct; Q8BMS1; 7. DR MINT; MINT-1860051; -. DR PhosphoSite; Q8BMS1; -. DR REPRODUCTION-2DPAGE; IPI00223092; -. DR PaxDb; Q8BMS1; -. DR PRIDE; Q8BMS1; -. DR Ensembl; ENSMUST00000156859; ENSMUSP00000120976; ENSMUSG00000025745. DR GeneID; 97212; -. DR KEGG; mmu:97212; -. DR UCSC; uc008wvc.1; mouse. DR CTD; 3030; -. DR MGI; MGI:2135593; Hadha. DR eggNOG; COG1250; -. DR GeneTree; ENSGT00720000108673; -. DR HOGENOM; HOG000261346; -. DR HOVERGEN; HBG005557; -. DR InParanoid; Q3TCY3; -. DR KO; K07515; -. DR OMA; MMLNEAA; -. DR OrthoDB; EOG7P2XRF; -. DR TreeFam; TF352288; -. DR UniPathway; UPA00659; -. DR ChiTaRS; HADHA; mouse. DR NextBio; 352627; -. DR PRO; PR:Q8BMS1; -. DR ArrayExpress; Q8BMS1; -. DR Bgee; Q8BMS1; -. DR Genevestigator; Q8BMS1; -. DR GO; GO:0016507; C:mitochondrial fatty acid beta-oxidation multienzyme complex; IEA:Ensembl. DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:MGI. DR GO; GO:0042645; C:mitochondrial nucleoid; IEA:Ensembl. DR GO; GO:0005730; C:nucleolus; IEA:Ensembl. DR GO; GO:0003988; F:acetyl-CoA C-acyltransferase activity; IEA:Ensembl. DR GO; GO:0004300; F:enoyl-CoA hydratase activity; TAS:MGI. DR GO; GO:0000062; F:fatty-acyl-CoA binding; IEA:Ensembl. DR GO; GO:0016509; F:long-chain-3-hydroxyacyl-CoA dehydrogenase activity; IDA:MGI. DR GO; GO:0016508; F:long-chain-enoyl-CoA hydratase activity; IEA:Ensembl. DR GO; GO:0051287; F:NAD binding; IEA:Ensembl. DR GO; GO:0006635; P:fatty acid beta-oxidation; IMP:MGI. DR GO; GO:0042493; P:response to drug; IEA:Ensembl. DR GO; GO:0032868; P:response to insulin; IMP:MGI. DR Gene3D; 1.10.1040.10; -; 2. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR006180; 3-OHacyl-CoA_DH_CS. DR InterPro; IPR006176; 3-OHacyl-CoA_DH_NAD-bd. DR InterPro; IPR006108; 3HC_DH_C. DR InterPro; IPR008927; 6-PGluconate_DH_C-like. DR InterPro; IPR001753; Crotonase_core_superfam. DR InterPro; IPR013328; DH_multihelical. DR InterPro; IPR018376; Enoyl-CoA_hyd/isom_CS. DR InterPro; IPR012803; Fa_ox_alpha_mit. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Pfam; PF00725; 3HCDH; 2. DR Pfam; PF02737; 3HCDH_N; 1. DR Pfam; PF00378; ECH; 1. DR SUPFAM; SSF48179; SSF48179; 2. DR TIGRFAMs; TIGR02441; fa_ox_alpha_mit; 1. DR PROSITE; PS00067; 3HCDH; 1. DR PROSITE; PS00166; ENOYL_COA_HYDRATASE; 1. PE 1: Evidence at protein level; KW Acetylation; Complete proteome; Fatty acid metabolism; KW Lipid metabolism; Lyase; Mitochondrion; Multifunctional enzyme; NAD; KW Oxidoreductase; Reference proteome; Transit peptide. FT TRANSIT 1 36 Mitochondrion (Potential). FT CHAIN 37 763 Trifunctional enzyme subunit alpha, FT mitochondrial. FT /FTId=PRO_0000322639. FT SITE 151 151 Important for catalytic activity (By FT similarity). FT SITE 173 173 Important for catalytic activity (By FT similarity). FT MOD_RES 46 46 N6-acetyllysine; alternate. FT MOD_RES 46 46 N6-succinyllysine; alternate. FT MOD_RES 60 60 N6-acetyllysine; alternate. FT MOD_RES 60 60 N6-succinyllysine; alternate. FT MOD_RES 129 129 N6-acetyllysine. FT MOD_RES 166 166 N6-acetyllysine; alternate. FT MOD_RES 166 166 N6-succinyllysine; alternate. FT MOD_RES 213 213 N6-succinyllysine. FT MOD_RES 214 214 N6-acetyllysine; alternate. FT MOD_RES 214 214 N6-succinyllysine; alternate. FT MOD_RES 230 230 N6-succinyllysine. FT MOD_RES 249 249 N6-acetyllysine; alternate. FT MOD_RES 249 249 N6-succinyllysine; alternate. FT MOD_RES 289 289 N6-acetyllysine. FT MOD_RES 295 295 N6-acetyllysine (By similarity). FT MOD_RES 303 303 N6-acetyllysine; alternate. FT MOD_RES 303 303 N6-succinyllysine; alternate. FT MOD_RES 326 326 N6-acetyllysine; alternate. FT MOD_RES 326 326 N6-succinyllysine; alternate. FT MOD_RES 334 334 N6-acetyllysine; alternate. FT MOD_RES 334 334 N6-succinyllysine; alternate. FT MOD_RES 350 350 N6-acetyllysine; alternate. FT MOD_RES 350 350 N6-succinyllysine; alternate. FT MOD_RES 353 353 N6-acetyllysine. FT MOD_RES 406 406 N6-acetyllysine; alternate. FT MOD_RES 406 406 N6-succinyllysine; alternate. FT MOD_RES 411 411 N6-acetyllysine; alternate. FT MOD_RES 411 411 N6-succinyllysine; alternate. FT MOD_RES 415 415 N6-succinyllysine. FT MOD_RES 436 436 N6-acetyllysine; alternate. FT MOD_RES 436 436 N6-succinyllysine; alternate. FT MOD_RES 440 440 N6-succinyllysine. FT MOD_RES 460 460 N6-acetyllysine; alternate. FT MOD_RES 460 460 N6-succinyllysine; alternate. FT MOD_RES 505 505 N6-acetyllysine; alternate. FT MOD_RES 505 505 N6-succinyllysine; alternate. FT MOD_RES 519 519 N6-acetyllysine; alternate. FT MOD_RES 519 519 N6-succinyllysine; alternate. FT MOD_RES 540 540 N6-acetyllysine. FT MOD_RES 569 569 N6-acetyllysine; alternate. FT MOD_RES 569 569 N6-succinyllysine; alternate. FT MOD_RES 620 620 N6-succinyllysine. FT MOD_RES 634 634 N6-succinyllysine. FT MOD_RES 644 644 N6-acetyllysine; alternate. FT MOD_RES 644 644 N6-succinyllysine; alternate. FT MOD_RES 646 646 N6-succinyllysine. FT MOD_RES 664 664 N6-acetyllysine; alternate. FT MOD_RES 664 664 N6-succinyllysine; alternate. FT MOD_RES 728 728 N6-acetyllysine; alternate. FT MOD_RES 728 728 N6-succinyllysine; alternate. FT MOD_RES 735 735 N6-acetyllysine. FT MOD_RES 759 759 N6-acetyllysine; alternate. FT MOD_RES 759 759 N6-succinyllysine; alternate. FT CONFLICT 196 196 A -> D (in Ref. 1; BAE41822). FT CONFLICT 459 459 L -> S (in Ref. 2; AAH37009). SQ SEQUENCE 763 AA; 82670 MW; 73D203795D5C1141 CRC64; MVASRAIGSL SRFSAFRILR SRGCICRSFT TSSALLTRTH INYGVKGDVA VIRINSPNSK VNTLNKEVQS EFIEVMNEIW ANDQIRSAVL ISSKPGCFVA GADINMLSSC TTPQEATRIS QEGQRMFEKL EKSPKPVVAA ISGSCLGGGL ELAIACQYRI ATKDRKTVLG VPEVLLGILP GAGGTQRLPK MVGVPAAFDM MLTGRNIRAD RAKKMGLVDQ LVEPLGPGIK SPEERTIEYL EEVAVNFAKG LADRKVSAKQ SKGLVEKLTT YAMTVPFVRQ QVYKTVEEKV KKQTKGLYPA PLKIIDAVKA GLEQGSDAGY LAESQKFGEL ALTKESKALM GLYNGQVLCK KNKFGAPQKN VQQLAILGAG LMGAGIAQVS VDKGLKTLLK DTTVTGLGRG QQQVFKGLND KVKKKALTSF ERDSIFSNLI GQLDYKGFEK ADMVIEAVFE DLGVKHKVLK EVESVTPEHC IFASNTSALP INQIAAVSKR PEKVIGMHYF SPVDKMQLLE IITTDKTSKD TTASAVAVGL RQGKVIIVVK DGPGFYTTRC LAPMMSEVMR ILQEGVDPKK LDALTTGFGF PVGAATLADE VGVDVAQHVA EDLGKAFGER FGGGSVELLK QMVSKGFLGR KSGKGFYIYQ EGSKNKSLNS EMDNILANLR LPAKPEVSSD EDVQYRVITR FVNEAVLCLQ EGILATPAEG DIGAVFGLGF PPCLGGPFRF VDLYGAQKVV DRLRKYESAY GTQFTPCQLL LDHANNSSKK FYQ // ID ECHP_MOUSE Reviewed; 718 AA. AC Q9DBM2; Q91W49; DT 24-OCT-2001, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 4. DT 19-MAR-2014, entry version 122. DE RecName: Full=Peroxisomal bifunctional enzyme; DE Short=PBE; DE Short=PBFE; DE Includes: DE RecName: Full=Enoyl-CoA hydratase/3,2-trans-enoyl-CoA isomerase; DE EC=4.2.1.17; DE EC=5.3.3.8; DE Includes: DE RecName: Full=3-hydroxyacyl-CoA dehydrogenase; DE EC=1.1.1.35; GN Name=Ehhadh; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Liver; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Kidney; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-38; LYS-163; LYS-172; RP LYS-181; LYS-189; LYS-217; LYS-240; LYS-252; LYS-274; LYS-278; RP LYS-288; LYS-329; LYS-527; LYS-572; LYS-579; LYS-586; LYS-705 AND RP LYS-717, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Liver; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., RA Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). RN [5] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-172; LYS-189; LYS-217; RP LYS-248; LYS-274; LYS-344; LYS-348; LYS-355; LYS-459; LYS-579; LYS-586 RP AND LYS-705, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Liver; RX PubMed=23576753; DOI=10.1073/pnas.1302961110; RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., RA Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.; RT "Label-free quantitative proteomics of the lysine acetylome in RT mitochondria identifies substrates of SIRT3 in metabolic pathways."; RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013). CC -!- CATALYTIC ACTIVITY: (3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl- CC CoA + H(2)O. CC -!- CATALYTIC ACTIVITY: (3Z)-dodec-3-enoyl-CoA = (2E)-dodec-2-enoyl- CC CoA. CC -!- CATALYTIC ACTIVITY: (S)-3-hydroxyacyl-CoA + NAD(+) = 3-oxoacyl-CoA CC + NADH. CC -!- ENZYME REGULATION: Enzyme activity enhanced by acetylation (By CC similarity). CC -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation. CC -!- SUBUNIT: Monomer (By similarity). CC -!- SUBCELLULAR LOCATION: Peroxisome (By similarity). CC -!- PTM: Acetylated, leading to enhanced enzyme activity. Acetylation CC is enhanced by up to 80% after treatment either with trichostin A CC (TCA) or with nicotinamide (NAM) with highest increase on Lys-344. CC Acetylation and enzyme activity increased by about 1.5% on CC addition of fatty acids (By similarity). CC -!- SIMILARITY: In the N-terminal section; belongs to the enoyl-CoA CC hydratase/isomerase family. CC -!- SIMILARITY: In the C-terminal section; belongs to the 3- CC hydroxyacyl-CoA dehydrogenase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK004867; BAB23628.1; -; mRNA. DR EMBL; BC016899; AAH16899.1; -; mRNA. DR EMBL; CH466521; EDK97607.1; -; Genomic_DNA. DR RefSeq; NP_076226.2; NM_023737.3. DR UniGene; Mm.28100; -. DR ProteinModelPortal; Q9DBM2; -. DR SMR; Q9DBM2; 1-714. DR IntAct; Q9DBM2; 5. DR MINT; MINT-4121269; -. DR PhosphoSite; Q9DBM2; -. DR PaxDb; Q9DBM2; -. DR PRIDE; Q9DBM2; -. DR Ensembl; ENSMUST00000023559; ENSMUSP00000023559; ENSMUSG00000022853. DR GeneID; 74147; -. DR KEGG; mmu:74147; -. DR UCSC; uc007yrm.2; mouse. DR CTD; 1962; -. DR MGI; MGI:1277964; Ehhadh. DR eggNOG; COG1250; -. DR GeneTree; ENSGT00720000108673; -. DR HOGENOM; HOG000261347; -. DR HOVERGEN; HBG104990; -. DR InParanoid; Q91W49; -. DR KO; K07514; -. DR OMA; KGWYQYD; -. DR OrthoDB; EOG725DH0; -. DR TreeFam; TF316708; -. DR UniPathway; UPA00659; -. DR NextBio; 339902; -. DR PRO; PR:Q9DBM2; -. DR ArrayExpress; Q9DBM2; -. DR Bgee; Q9DBM2; -. DR Genevestigator; Q9DBM2; -. DR GO; GO:0005829; C:cytosol; IEA:Ensembl. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR GO; GO:0005634; C:nucleus; IEA:Ensembl. DR GO; GO:0005777; C:peroxisome; TAS:MGI. DR GO; GO:0003857; F:3-hydroxyacyl-CoA dehydrogenase activity; TAS:MGI. DR GO; GO:0050662; F:coenzyme binding; IEA:InterPro. DR GO; GO:0004165; F:dodecenoyl-CoA delta-isomerase activity; IEA:UniProtKB-EC. DR GO; GO:0004300; F:enoyl-CoA hydratase activity; IEA:UniProtKB-EC. DR GO; GO:0006637; P:acyl-CoA metabolic process; TAS:MGI. DR GO; GO:0006635; P:fatty acid beta-oxidation; IMP:MGI. DR GO; GO:0006475; P:internal protein amino acid acetylation; ISS:UniProtKB. DR Gene3D; 1.10.1040.10; -; 2. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR006180; 3-OHacyl-CoA_DH_CS. DR InterPro; IPR006176; 3-OHacyl-CoA_DH_NAD-bd. DR InterPro; IPR006108; 3HC_DH_C. DR InterPro; IPR008927; 6-PGluconate_DH_C-like. DR InterPro; IPR001753; Crotonase_core_superfam. DR InterPro; IPR013328; DH_multihelical. DR InterPro; IPR018376; Enoyl-CoA_hyd/isom_CS. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Pfam; PF00725; 3HCDH; 2. DR Pfam; PF02737; 3HCDH_N; 1. DR Pfam; PF00378; ECH; 1. DR SUPFAM; SSF48179; SSF48179; 2. DR PROSITE; PS00067; 3HCDH; 1. DR PROSITE; PS00166; ENOYL_COA_HYDRATASE; 1. PE 1: Evidence at protein level; KW Acetylation; Complete proteome; Fatty acid metabolism; Isomerase; KW Lipid metabolism; Lyase; Multifunctional enzyme; NAD; Oxidoreductase; KW Peroxisome; Reference proteome. FT CHAIN 1 718 Peroxisomal bifunctional enzyme. FT /FTId=PRO_0000109248. FT REGION 1 280 Enoyl-CoA hydratase / isomerase. FT REGION 281 567 3-hydroxyacyl-CoA dehydrogenase. FT MOTIF 716 718 Microbody targeting signal (By FT similarity). FT BINDING 99 99 Substrate; via amide nitrogen (By FT similarity). FT SITE 102 102 Important for catalytic activity (By FT similarity). FT SITE 122 122 Important for catalytic activity (By FT similarity). FT MOD_RES 38 38 N6-succinyllysine. FT MOD_RES 163 163 N6-acetyllysine; alternate (By FT similarity). FT MOD_RES 163 163 N6-succinyllysine; alternate. FT MOD_RES 172 172 N6-acetyllysine; alternate. FT MOD_RES 172 172 N6-succinyllysine; alternate. FT MOD_RES 181 181 N6-succinyllysine. FT MOD_RES 189 189 N6-acetyllysine; alternate. FT MOD_RES 189 189 N6-succinyllysine; alternate. FT MOD_RES 217 217 N6-acetyllysine; alternate. FT MOD_RES 217 217 N6-succinyllysine; alternate. FT MOD_RES 240 240 N6-succinyllysine. FT MOD_RES 248 248 N6-acetyllysine. FT MOD_RES 252 252 N6-succinyllysine. FT MOD_RES 274 274 N6-acetyllysine; alternate. FT MOD_RES 274 274 N6-succinyllysine; alternate. FT MOD_RES 278 278 N6-succinyllysine. FT MOD_RES 288 288 N6-succinyllysine. FT MOD_RES 329 329 N6-succinyllysine. FT MOD_RES 344 344 N6-acetyllysine. FT MOD_RES 348 348 N6-acetyllysine. FT MOD_RES 355 355 N6-acetyllysine. FT MOD_RES 459 459 N6-acetyllysine. FT MOD_RES 527 527 N6-succinyllysine. FT MOD_RES 572 572 N6-succinyllysine. FT MOD_RES 579 579 N6-acetyllysine; alternate. FT MOD_RES 579 579 N6-succinyllysine; alternate. FT MOD_RES 586 586 N6-acetyllysine; alternate. FT MOD_RES 586 586 N6-succinyllysine; alternate. FT MOD_RES 705 705 N6-acetyllysine; alternate. FT MOD_RES 705 705 N6-succinyllysine; alternate. FT MOD_RES 717 717 N6-succinyllysine. FT CONFLICT 499 499 D -> G (in Ref. 1; BAB23628). SQ SEQUENCE 718 AA; 78301 MW; A405717EC7A3EBD9 CRC64; MAEYLRLPHS LAMIRLCNPP VNAISPTVIT EVRNGLQKAS LDHTVRAIVI CGANDNFCAG ADIHGFKSPT GLTLGSLVDE IQRYQKPVVA AIQGVALGGG LELALGCHYR IANAKARVGF PEVMLGILPG ARGTQLLPRV VGVPVALDLI TSGRHISTDE ALKLGILDVV VKSDPVEEAI KFAQTVIGKP IEPRRILNKP VPSLPNMDSV FAEAIAKVRK QYPGRLAPET CVRSVQASVK HPYEVAIKEE AKLFMYLRGS GQARALQYAF FAEKSANKWS TPSGASWKTA SAQPVSSVGV LGLGTMGRGI AISFARVGIP VVAVESDPKQ LDTAKKIITS TLEKEASKSG QASAKPNLRF SSSTKELSSV DLVIEAVFED MNLKKKVFAE LSALCKPGAF LCTNTSALDV DDIASSTDRP QLVIGTHFFS PAHIMRLLEV IPSRYSSPTT IATVMSLSKR IGKIGVVVGN CYGFVGNRML APYYNQGYFL IEEGSKPEDV DGVLEEFGFR MGPFRVSDLA GLDVGWKVRK GQGLTGPSLP PGTPTRKRGN TRYSPIADML CEAGRFGQKT GKGWYQYDKP LGRIHKPDPW LSEFLSQYRE THHIKQRSIS KEEILERCLY SLINEAFRIL EEGMAASPEH IDVIYLHGYG WPRHVGGPMY YAASVGLPTV LEKLQKYYRQ NPDIPQLEPS DYLRRLVAQG SPPLKEWQSL AGPHSSKL // ID EGLN3_MOUSE Reviewed; 239 AA. AC Q91UZ4; Q3TCG8; Q8C8M6; Q8CCA8; Q8R5C7; DT 16-JUN-2003, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 19-FEB-2014, entry version 106. DE RecName: Full=Egl nine homolog 3; DE EC=1.14.11.29; DE AltName: Full=Hypoxia-inducible factor prolyl hydroxylase 3; DE Short=HIF-PH3; DE Short=HIF-prolyl hydroxylase 3; DE Short=HPH-3; DE AltName: Full=Prolyl hydroxylase domain-containing protein 3; DE Short=PHD3; DE AltName: Full=SM-20; GN Name=Egln3; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE. RC TISSUE=Embryo; RX PubMed=10543731; RA Moschella M.C., Menzies K., Tsao L., Lieb M.A., Kohtz J.D., RA Kohtz D.S., Taubman M.B.; RT "SM-20 is a novel growth factor-responsive gene regulated during RT skeletal muscle development and differentiation."; RL Gene Expr. 8:59-66(1999). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=11574160; DOI=10.1016/S0378-1119(01)00633-3; RA Taylor M.S.; RT "Characterization and comparative analysis of the EGLN gene family."; RL Gene 275:125-132(2001). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J, and NOD; TISSUE=Dendritic cell, Lung, and Retina; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N-3, and NMRI; TISSUE=Mammary gland; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP TISSUE SPECIFICITY. RX PubMed=12234095; RA Lieb M.E., Menzies K., Moschella M.C., Ni R., Taubman M.B.; RT "Mammalian EGLN genes have distinct patterns of mRNA expression and RT regulation."; RL Biochem. Cell Biol. 80:421-426(2002). RN [6] RP DISRUPTION PHENOTYPE. RX PubMed=18332118; DOI=10.1128/MCB.02041-07; RA Bishop T., Gallagher D., Pascual A., Lygate C.A., de Bono J.P., RA Nicholls L.G., Ortega-Saenz P., Oster H., Wijeyekoon B., RA Sutherland A.I., Grosfeld A., Aragones J., Schneider M., van Geyte K., RA Teixeira D., Diez-Juan A., Lopez-Barneo J., Channon K.M., RA Maxwell P.H., Pugh C.W., Davies A.M., Carmeliet P., Ratcliffe P.J.; RT "Abnormal sympathoadrenal development and systemic hypotension in RT PHD3-/-mice."; RL Mol. Cell. Biol. 28:3386-3400(2008). RN [7] RP DISRUPTION PHENOTYPE. RX PubMed=19720742; DOI=10.1128/MCB.00331-09; RA Minamishima Y.A., Moslehi J., Padera R.F., Bronson R.T., Liao R., RA Kaelin W.G. Jr.; RT "A feedback loop involving the Phd3 prolyl hydroxylase tunes the RT mammalian hypoxic response in vivo."; RL Mol. Cell. Biol. 29:5729-5741(2009). RN [8] RP DISRUPTION PHENOTYPE. RX PubMed=19584355; DOI=10.1126/scisignal.2000444; RA Xie L., Xiao K., Whalen E.J., Forrester M.T., Freeman R.S., Fong G., RA Gygi S.P., Lefkowitz R.J., Stamler J.S.; RT "Oxygen-regulated beta(2)-adrenergic receptor hydroxylation by EGLN3 RT and ubiquitylation by pVHL."; RL Sci. Signal. 2:RA33-RA33(2009). RN [9] RP FUNCTION, AND INDUCTION. RX PubMed=21317538; DOI=10.1172/JCI43273; RA Walmsley S.R., Chilvers E.R., Thompson A.A., Vaughan K., RA Marriott H.M., Parker L.C., Shaw G., Parmar S., Schneider M., RA Sabroe I., Dockrell D.H., Milo M., Taylor C.T., Johnson R.S., RA Pugh C.W., Ratcliffe P.J., Maxwell P.H., Carmeliet P., Whyte M.K.; RT "Prolyl hydroxylase 3 (PHD3) is essential for hypoxic regulation of RT neutrophilic inflammation in humans and mice."; RL J. Clin. Invest. 121:1053-1063(2011). CC -!- FUNCTION: Plays a crucial role in DNA damage response (DDR) by CC hydroxylating TELO2, promoting its interaction with ATR which is CC required for activation of the ATR/CHK1/p53 pathway (By CC similarity). Cellular oxygen sensor that catalyzes, under normoxic CC conditions, the post-translational formation of 4-hydroxyproline CC in hypoxia-inducible factor (HIF) alpha proteins. Hydroxylates a CC specific proline found in each of the oxygen-dependent degradation CC (ODD) domains (N-terminal, NODD, and C-terminal, CODD) of HIF1A. CC Also hydroxylates HIF2A. Has a preference for the CODD site for CC both HIF1A and HIF2A. Hydroxylation on the NODD site by EGLN3 CC appears to require prior hydroxylation on the CODD site. CC Hydroxylated HIFs are then targeted for proteasomal degradation CC via the von Hippel-Lindau ubiquitination complex. Under hypoxic CC conditions, the hydroxylation reaction is attenuated allowing HIFs CC to escape degradation resulting in their translocation to the CC nucleus, heterodimerization with HIF1B, and increased expression CC of hypoxy-inducible genes. ELGN3 is the most important isozyme in CC limiting physiological activation of HIFs (particularly HIF2A) in CC hypoxia. Also hydroxylates PKM in hypoxia, limiting glycolysis. CC Under normoxia, hydroxylates and regulates the stability of ADRB2. CC Regulator of cardiomyocyte and neuronal apoptosis. In CC cardiomyocytes, inhibits the anti-apoptotic effect of BCL2 by CC disrupting the BAX-BCL2 complex. In neurons, has a NGF-induced CC proapoptotic effect, probably through regulating CASP3 activity. CC Also essential for hypoxic regulation of neutrophilic CC inflammation. Target proteins are preferencially recognized via a CC LXXLAP motif. CC -!- CATALYTIC ACTIVITY: Hypoxia-inducible factor-L-proline + 2- CC oxoglutarate + O(2) = hypoxia-inducible factor-trans-4-hydroxy-L- CC proline + succinate + CO(2). CC -!- COFACTOR: Binds 1 Fe(2+) ion per subunit (By similarity). CC -!- COFACTOR: Ascorbate (By similarity). CC -!- SUBUNIT: Interacts with ADRB2; the interaction hydroxylates ADRB2 CC facilitating its ubiquitination by the VHL-E3 ligase complex. CC Interacts with PKM; the interaction hydroxylates PKM in hypoxia. CC Interacts with WDR83; the interaction leads to almost complete CC elimination of HIF-mediated reporter activity (By similarity). CC Interacts with BCL2 (via its BH4 domain); the interaction disrupts CC the BAX-BCL4 complex inhibiting the anti-apoptotic activity of CC BCL2. Interacts with LIMD1, WTIP and AJUBA (By similarity). CC -!- SUBCELLULAR LOCATION: Nucleus (By similarity). Cytoplasm (By CC similarity). Note=Colocalizes with WDR83 in the cytoplasm (By CC similarity). CC -!- TISSUE SPECIFICITY: Highly expressed in cardiac and smooth muscle. CC Also high expression in brain, skeletal muscle and kidney. Low CC levels in lung. CC -!- DEVELOPMENTAL STAGE: Detected at E8.5 in proliferating myoblasts CC of the dermomyotome and the developing heart tube. From CC dermomyotomal cells of the rostral somites expression progressed CC in a rostral to caudal pattern, with highest levels seen in the CC muscle primordia and mature muscles. CC -!- INDUCTION: Induced by hypoxia. Up-regulated in proliferating CC myoblasts induced to form differentiated myotubes. CC -!- DOMAIN: The Beta(2)beta(3) 'finger-like' loop domain is important CC for substrate (HIFs' CODD/NODD) selectivity (By similarity). CC -!- DISRUPTION PHENOTYPE: Null mice exhibit reduced apoptosis of in CC sympathetic neurons. However, the sympathoadrenal system appears CC hypofunctional with reduced target tissue innervation, adrenal CC medullary secretory capacity, sympathoadrenal responses, and CC systemic blood pressure. There is an increase in ADRB2 abundance CC and decrease of ADRB1 abundance in heart. CC -!- SIMILARITY: Contains 1 Fe2OG dioxygenase domain. CC -!- SEQUENCE CAUTION: CC Sequence=AAH22961.1; Type=Erroneous initiation; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF421882; AAL17824.1; -; mRNA. DR EMBL; AJ310548; CAC42517.1; -; mRNA. DR EMBL; AK044787; BAC32092.1; -; mRNA. DR EMBL; AK165972; BAE38492.1; -; mRNA. DR EMBL; AK170732; BAE41988.1; -; mRNA. DR EMBL; BC022961; AAH22961.1; ALT_INIT; mRNA. DR EMBL; BC044926; AAH44926.1; -; mRNA. DR EMBL; BC058278; AAH58278.1; -; mRNA. DR EMBL; BC069893; AAH69893.1; -; mRNA. DR RefSeq; NP_082409.2; NM_028133.2. DR UniGene; Mm.133037; -. DR ProteinModelPortal; Q91UZ4; -. DR SMR; Q91UZ4; 13-225. DR BioGrid; 227483; 3. DR STRING; 10090.ENSMUSP00000041874; -. DR PhosphoSite; Q91UZ4; -. DR PRIDE; Q91UZ4; -. DR Ensembl; ENSMUST00000039516; ENSMUSP00000041874; ENSMUSG00000035105. DR GeneID; 112407; -. DR KEGG; mmu:112407; -. DR UCSC; uc007nns.2; mouse. DR CTD; 112399; -. DR MGI; MGI:1932288; Egln3. DR eggNOG; NOG326511; -. DR GeneTree; ENSGT00390000001936; -. DR HOGENOM; HOG000004818; -. DR HOVERGEN; HBG051455; -. DR InParanoid; Q91UZ4; -. DR KO; K09592; -. DR OrthoDB; EOG7TBC2W; -. DR TreeFam; TF314595; -. DR ChiTaRS; EGLN3; mouse. DR NextBio; 367889; -. DR PRO; PR:Q91UZ4; -. DR Bgee; Q91UZ4; -. DR CleanEx; MM_EGLN3; -. DR Genevestigator; Q91UZ4; -. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. DR GO; GO:0005634; C:nucleus; ISS:UniProtKB. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0031418; F:L-ascorbic acid binding; IEA:UniProtKB-KW. DR GO; GO:0031545; F:peptidyl-proline 4-dioxygenase activity; IEA:Ensembl. DR GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; ISS:UniProtKB. DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IEA:UniProtKB-KW. DR GO; GO:0018401; P:peptidyl-proline hydroxylation to 4-hydroxy-L-proline; IEA:Ensembl. DR GO; GO:0018126; P:protein hydroxylation; ISS:UniProtKB. DR GO; GO:0042127; P:regulation of cell proliferation; IMP:UniProtKB. DR GO; GO:0043523; P:regulation of neuron apoptotic process; IMP:UniProtKB. DR GO; GO:0001666; P:response to hypoxia; IEA:Ensembl. DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase. DR InterPro; IPR006620; Pro_4_hyd_alph. DR Pfam; PF13640; 2OG-FeII_Oxy_3; 1. DR SMART; SM00702; P4Hc; 1. DR PROSITE; PS51471; FE2OG_OXY; 1. PE 2: Evidence at transcript level; KW Apoptosis; Complete proteome; Cytoplasm; Dioxygenase; DNA damage; KW Iron; Metal-binding; Nucleus; Oxidoreductase; Reference proteome; KW Vitamin C. FT CHAIN 1 239 Egl nine homolog 3. FT /FTId=PRO_0000206667. FT DOMAIN 116 214 Fe2OG dioxygenase. FT REGION 62 73 Beta(2)beta(3) 'finger-like' loop (By FT similarity). FT REGION 88 104 Required for interaction with ADRB2 (By FT similarity). FT METAL 135 135 Iron (By similarity). FT METAL 137 137 Iron (By similarity). FT METAL 196 196 Iron (By similarity). FT BINDING 205 205 2-oxoglutarate (By similarity). FT CONFLICT 65 65 R -> C (in Ref. 3; BAC32092/BAE38492/ FT BAE41988). SQ SEQUENCE 239 AA; 27302 MW; F4102753C6498DE5 CRC64; MPLGHIMRLD LEKIALEYIV PCLHEVGFCY LDNFLGEVVG DCVLERVKQL HYNGALRDGQ LAGPRAGVSK RHLRGDQITW IGGNEEGCEA INFLLSLIDR LVLYCGSRLG KYYVKERSKA MVACYPGNGT GYVRHVDNPN GDGRCITCIY YLNKNWDAKL HGGVLRIFPE GKSFVADVEP IFDRLLFFWS DRRNPHEVQP SYATRYAMTV WYFDAEERAE AKKKFRNLTR KTESALAKD // ID EGLN2_MOUSE Reviewed; 419 AA. AC Q91YE2; Q8C6I4; Q8CIL9; Q8VHJ1; Q99MI0; DT 16-JUN-2003, integrated into UniProtKB/Swiss-Prot. DT 16-JUN-2003, sequence version 2. DT 19-FEB-2014, entry version 97. DE RecName: Full=Egl nine homolog 2; DE EC=1.14.11.29; DE AltName: Full=Falkor; DE AltName: Full=Hypoxia-inducible factor prolyl hydroxylase 1; DE Short=HIF-PH1; DE Short=HIF-prolyl hydroxylase 1; DE Short=HPH-1; DE AltName: Full=Prolyl hydroxylase domain-containing protein 1; DE Short=PHD1; GN Name=Egln2; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=11574160; DOI=10.1016/S0378-1119(01)00633-3; RA Taylor M.S.; RT "Characterization and comparative analysis of the EGLN gene family."; RL Gene 275:125-132(2001). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY. RC STRAIN=C57BL/6 X DBA/2; RX PubMed=12234095; RA Lieb M.E., Menzies K., Moschella M.C., Ni R., Taubman M.B.; RT "Mammalian EGLN genes have distinct patterns of mRNA expression and RT regulation."; RL Biochem. Cell Biol. 80:421-426(2002). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION. RC STRAIN=BALB/c; RX PubMed=12360397; DOI=10.1038/sj.onc.1205867; RA Erez N., Milyavsky M., Goldfinger N., Peles E., Gudkov A.V., RA Rotter V.; RT "Falkor, a novel cell growth regulator isolated by a functional RT genetic screen."; RL Oncogene 21:6713-6721(2002). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Kidney; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Liver; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP DISRUPTION PHENOTYPE, AND FUNCTION. RX PubMed=18176562; DOI=10.1038/ng.2007.62; RA Aragones J., Schneider M., Van Geyte K., Fraisl P., Dresselaers T., RA Mazzone M., Dirkx R., Zacchigna S., Lemieux H., Jeoung N.H., RA Lambrechts D., Bishop T., Lafuste P., Diez-Juan A., Harten S.K., RA Van Noten P., De Bock K., Willam C., Tjwa M., Grosfeld A., Navet R., RA Moons L., Vandendriessche T., Deroose C., Wijeyekoon B., Nuyts J., RA Jordan B., Silasi-Mansat R., Lupu F., Dewerchin M., Pugh C., RA Salmon P., Mortelmans L., Gallez B., Gorus F., Buyse J., Sluse F., RA Harris R.A., Gnaiger E., Hespel P., Van Hecke P., Schuit F., RA Van Veldhoven P., Ratcliffe P., Baes M., Maxwell P., Carmeliet P.; RT "Deficiency or inhibition of oxygen sensor Phd1 induces hypoxia RT tolerance by reprogramming basal metabolism."; RL Nat. Genet. 40:170-180(2008). RN [7] RP FUNCTION. RX PubMed=19587290; DOI=10.1523/JNEUROSCI.1779-09.2009; RA Siddiq A., Aminova L.R., Troy C.M., Suh K., Messer Z., Semenza G.L., RA Ratan R.R.; RT "Selective inhibition of hypoxia-inducible factor (HIF) prolyl- RT hydroxylase 1 mediates neuroprotection against normoxic oxidative RT death via HIF- and CREB-independent pathways."; RL J. Neurosci. 29:8828-8838(2009). RN [8] RP DISRUPTION PHENOTYPE, AND FUNCTION. RX PubMed=21083501; DOI=10.1089/ars.2010.3769; RA Adluri R.S., Thirunavukkarasu M., Dunna N.R., Zhan L., Oriowo B., RA Takeda K., Sanchez J.A., Otani H., Maulik G., Fong G.H., Maulik N.; RT "Disruption of hypoxia-inducible transcription factor-prolyl RT hydroxylase domain-1 (PHD-1-/-) attenuates ex vivo myocardial RT ischemia/reperfusion injury through hypoxia-inducible factor-1alpha RT transcription factor and its target genes in mice."; RL Antioxid. Redox Signal. 15:1789-1797(2011). CC -!- FUNCTION: Cellular oxygen sensor that catalyzes, under normoxic CC conditions, the post-translational formation of 4-hydroxyproline CC in hypoxia-inducible factor (HIF) alpha proteins. Hydroxylates a CC specific proline found in each of the oxygen-dependent degradation CC (ODD) domains (N-terminal, NODD, and C-terminal, CODD) of HIF1A. CC Also hydroxylates HIF2A. Has a preference for the CODD site for CC both HIF1A and HIF2A. Hydroxylated HIFs are then targeted for CC proteasomal degradation via the von Hippel-Lindau ubiquitination CC complex. Under hypoxic conditions, the hydroxylation reaction is CC attenuated allowing HIFs to escape degradation resulting in their CC translocation to the nucleus, heterodimerization with HIF1B, and CC increased expression of hypoxy-inducible genes. EGLN2 is involved CC in regulating hypoxia tolerance and apoptosis in cardiac and CC skeletal muscle. Also regulates susceptibility to normoxic CC oxidative neuronal death. Links oxygen sensing to cell cycle and CC primary cilia formation by hydroxylating the critical centrosome CC component CEP192 which promotes its ubiquitination and subsequent CC proteasomal degradation. Hydroxylates IKBKB, mediating NF-kappaB CC activation in hypoxic conditions. Target proteins are CC preferencially recognized via a LXXLAP motif. CC -!- CATALYTIC ACTIVITY: Hypoxia-inducible factor-L-proline + 2- CC oxoglutarate + O(2) = hypoxia-inducible factor-trans-4-hydroxy-L- CC proline + succinate + CO(2). CC -!- COFACTOR: Binds 1 Fe(2+) ion per subunit. CC -!- COFACTOR: Ascorbate. CC -!- SUBUNIT: Interacts with E3 ligase SIAH2 (By similarity). Interacts CC with LIMD1, WTIP and AJUBA (By similarity). CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- TISSUE SPECIFICITY: Highly expressed in testis, expression was CC also detected in the heart brain, liver kidney and lung. CC Expression was lowest in spleen and skeletal muscle. CC Constitutively expressed during differentiation of C2C12 skeletal CC myocytes. CC -!- DOMAIN: The Beta(2)beta(3) 'finger-like' loop domain is important CC for substrate (HIFs' CODD/NODD) selectivity (By similarity). CC -!- DISRUPTION PHENOTYPE: Null mice exhibit a lowering of oxygen CC consumption in skeletal muscle. Glucose oxidation is reduced to CC around 35%. Hypoxia tolerance is induced in myofibers. CC -!- SIMILARITY: Contains 1 Fe2OG dioxygenase domain. CC -!- SEQUENCE CAUTION: CC Sequence=CAC42516.1; Type=Frameshift; Positions=118, 125; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJ310547; CAC42516.1; ALT_FRAME; mRNA. DR EMBL; AF453879; AAL65166.1; -; mRNA. DR EMBL; AF340231; AAK37525.1; -; mRNA. DR EMBL; AK075582; BAC35835.1; -; mRNA. DR EMBL; BC023299; AAH23299.2; -; mRNA. DR RefSeq; NP_444438.2; NM_053208.4. DR UniGene; Mm.29978; -. DR ProteinModelPortal; Q91YE2; -. DR SMR; Q91YE2; 188-399. DR BioGrid; 227482; 1. DR PhosphoSite; Q91YE2; -. DR PRIDE; Q91YE2; -. DR Ensembl; ENSMUST00000080058; ENSMUSP00000078966; ENSMUSG00000058709. DR Ensembl; ENSMUST00000108382; ENSMUSP00000104019; ENSMUSG00000058709. DR GeneID; 112406; -. DR KEGG; mmu:112406; -. DR UCSC; uc009fva.2; mouse. DR CTD; 112398; -. DR MGI; MGI:1932287; Egln2. DR eggNOG; NOG326511; -. DR GeneTree; ENSGT00390000001936; -. DR HOGENOM; HOG000013099; -. DR HOVERGEN; HBG051456; -. DR InParanoid; Q91YE2; -. DR KO; K09592; -. DR OMA; GGELWPL; -. DR OrthoDB; EOG7TBC2W; -. DR TreeFam; TF314595; -. DR ChiTaRS; EGLN2; mouse. DR NextBio; 367885; -. DR PRO; PR:Q91YE2; -. DR ArrayExpress; Q91YE2; -. DR Bgee; Q91YE2; -. DR CleanEx; MM_EGLN2; -. DR Genevestigator; Q91YE2; -. DR GO; GO:0005829; C:cytosol; IEA:Ensembl. DR GO; GO:0005634; C:nucleus; ISS:UniProtKB. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0031418; F:L-ascorbic acid binding; IEA:UniProtKB-KW. DR GO; GO:0016706; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors; ISS:UniProtKB. DR GO; GO:0019826; F:oxygen sensor activity; ISS:UniProtKB. DR GO; GO:0031545; F:peptidyl-proline 4-dioxygenase activity; IEA:Ensembl. DR GO; GO:0045454; P:cell redox homeostasis; ISS:UniProtKB. DR GO; GO:0018401; P:peptidyl-proline hydroxylation to 4-hydroxy-L-proline; IEA:Ensembl. DR GO; GO:0045732; P:positive regulation of protein catabolic process; ISS:UniProtKB. DR GO; GO:0043523; P:regulation of neuron apoptotic process; ISS:UniProtKB. DR GO; GO:0001666; P:response to hypoxia; ISS:UniProtKB. DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase. DR InterPro; IPR006620; Pro_4_hyd_alph. DR Pfam; PF13640; 2OG-FeII_Oxy_3; 1. DR SMART; SM00702; P4Hc; 1. DR PROSITE; PS51471; FE2OG_OXY; 1. PE 2: Evidence at transcript level; KW Complete proteome; Dioxygenase; Iron; Metal-binding; Nucleus; KW Oxidoreductase; Reference proteome; Vitamin C. FT CHAIN 1 419 Egl nine homolog 2. FT /FTId=PRO_0000206665. FT DOMAIN 290 388 Fe2OG dioxygenase. FT REGION 89 134 Bipartite nuclear localization signal (By FT similarity). FT REGION 237 247 Beta(2)beta(3) 'finger-like' loop (By FT similarity). FT COMPBIAS 64 72 Poly-Thr. FT COMPBIAS 157 164 Poly-Ser. FT METAL 309 309 Iron (By similarity). FT METAL 311 311 Iron (By similarity). FT METAL 370 370 Iron (By similarity). FT BINDING 379 379 2-oxoglutarate (By similarity). FT CONFLICT 8 8 Q -> H (in Ref. 4; BAC35835). FT CONFLICT 10 10 L -> C (in Ref. 4; BAC35835). FT CONFLICT 92 92 Q -> K (in Ref. 3; AAK37525). SQ SEQUENCE 419 AA; 45109 MW; 13BAA52A0709CE98 CRC64; MDSPCQPQAL NQALPQLPGS VSESLESSRA RMGVESYLPC PLLPAYHRPG ASGEASAGNG TPRTTATATT TTASPLREGF GGQDGGELWP LQSEGAAALV TKECQRLAAQ GARPEAPKRK WAKDGGDAPS PSKRPWARQE NQEAKGESGM GCDSGASNSS SSSSNTTSSS GEASARLREE VQPSAPERLA LDYIVPCMRY YGICVKDNFL GAVLGGRVLA EVEALKWGGR LRDGQLVSQR AIPPRSIRGD QIAWVEGHEP GCRSIGALMA HVDAVIRHCA GRLGNYVING RTKAMVACYP GNGLGYVRHV DNPHGDGRCI TCIYYLNQNW DVKVHGGLLQ IFPEGRPVVA NIEPLFDRLL IFWSDRRNPH EVKPAYATRY AITVWYFDAK ERAAARDKYQ LASGQKGVQV PVSQPTTPT // ID EGLN1_MOUSE Reviewed; 400 AA. AC Q91YE3; Q8VHJ2; Q922P3; DT 16-JUN-2003, integrated into UniProtKB/Swiss-Prot. DT 16-JUN-2003, sequence version 2. DT 19-FEB-2014, entry version 104. DE RecName: Full=Egl nine homolog 1; DE EC=1.14.11.29; DE AltName: Full=Hypoxia-inducible factor prolyl hydroxylase 2; DE Short=HIF-PH2; DE Short=HIF-prolyl hydroxylase 2; DE Short=HPH-2; DE AltName: Full=Prolyl hydroxylase domain-containing protein 2; DE Short=PHD2; DE AltName: Full=SM-20; GN Name=Egln1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] OF 34-400. RX PubMed=11574160; DOI=10.1016/S0378-1119(01)00633-3; RA Taylor M.S.; RT "Characterization and comparative analysis of the EGLN gene family."; RL Gene 275:125-132(2001). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] OF 205-400, AND TISSUE SPECIFICITY. RX PubMed=12234095; RA Lieb M.E., Menzies K., Moschella M.C., Ni R., Taubman M.B.; RT "Mammalian EGLN genes have distinct patterns of mRNA expression and RT regulation."; RL Biochem. Cell Biol. 80:421-426(2002). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 268-400. RC TISSUE=Mammary gland; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP INDUCTION. RX PubMed=10543731; RA Moschella M.C., Menzies K., Tsao L., Lieb M.A., Kohtz J.D., RA Kohtz D.S., Taubman M.B.; RT "SM-20 is a novel growth factor-responsive gene regulated during RT skeletal muscle development and differentiation."; RL Gene Expr. 8:59-66(1999). RN [6] RP DISRUPTION PHENOTYPE, AND FUNCTION. RX PubMed=18096761; DOI=10.1182/blood-2007-10-117812; RA Minamishima Y.A., Moslehi J., Bardeesy N., Cullen D., Bronson R.T., RA Kaelin W.G. Jr.; RT "Somatic inactivation of the PHD2 prolyl hydroxylase causes RT polycythemia and congestive heart failure."; RL Blood 111:3236-3244(2008). RN [7] RP DISRUPTION PHENOTYPE, AND FUNCTION. RX PubMed=18500250; DOI=10.1038/mt.2008.90; RA Wu S., Nishiyama N., Kano M.R., Morishita Y., Miyazono K., Itaka K., RA Chung U.I., Kataoka K.; RT "Enhancement of angiogenesis through stabilization of hypoxia- RT inducible factor-1 by silencing prolyl hydroxylase domain-2 gene."; RL Mol. Ther. 16:1227-1234(2008). RN [8] RP DISRUPTION PHENOTYPE, AND FUNCTION. RX PubMed=21435465; DOI=10.1016/j.ajpath.2010.12.016; RA Duan L.J., Takeda K., Fong G.H.; RT "Prolyl hydroxylase domain protein 2 (PHD2) mediates oxygen-induced RT retinopathy in neonatal mice."; RL Am. J. Pathol. 178:1881-1890(2011). CC -!- FUNCTION: Cellular oxygen sensor that catalyzes, under normoxic CC conditions, the post-translational formation of 4-hydroxyproline CC in hypoxia-inducible factor (HIF) alpha proteins. Hydroxylates a CC specific proline found in each of the oxygen-dependent degradation CC (ODD) domains (N-terminal, NODD, and C-terminal, CODD) of HIF1A. CC Also hydroxylates HIF2A. Has a preference for the CODD site for CC both HIF1A and HIF1B. Hydroxylated HIFs are then targeted for CC proteasomal degradation via the von Hippel-Lindau ubiquitination CC complex. Under hypoxic conditions, the hydroxylation reaction is CC attenuated allowing HIFs to escape degradation resulting in their CC translocation to the nucleus, heterodimerization with HIF1B, and CC increased expression of hypoxy-inducible genes. EGLN1 is the most CC important isozyme under normoxia and, through regulating the CC stability of HIF1, involved in various hypoxia-influenced CC processes such as angiogenesis in retinal and cardiac CC functionality. Target proteins are preferencially recognized via a CC LXXLAP motif. CC -!- CATALYTIC ACTIVITY: Hypoxia-inducible factor-L-proline + 2- CC oxoglutarate + O(2) = hypoxia-inducible factor-trans-4-hydroxy-L- CC proline + succinate + CO(2). CC -!- COFACTOR: Binds 1 Fe(2+) ion per subunit (By similarity). CC -!- COFACTOR: Ascorbate (By similarity). CC -!- ENZYME REGULATION: Seems to be inhibited by ING4 (By similarity). CC -!- SUBUNIT: Monomer. Interacts with ING4; the interaction inhibits CC the hydroxylation of HIFs (By similarity). Interacts with LIMD1. CC Found in a complex composed of LIMD1, VHL, EGLN1/PHD2, TCEB2 AND CC CUL2 (By similarity). Interacts with EPAS1 (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By CC similarity). Note=Mainly cytoplasmic. Shuttles between the nucleus CC and cytoplasm. Nuclear export requires functional XPO1 (By CC similarity). CC -!- TISSUE SPECIFICITY: Expressed in heart, brain liver, skeletal CC muscle and kidney. Low levels were detected in the lung. CC Constitutively expressed during differentiation of C2C12 skeletal CC myocytes. CC -!- INDUCTION: Induced by growth factors in cultured vascular smooth CC muscle. Up-regulated in proliferating myoblasts induced to form CC differentiated myotubes. CC -!- DOMAIN: The beta(2)beta(3) 'finger-like' loop domain is important CC for substrate (HIFs' CODD/NODD) selectivity (By similarity). CC -!- PTM: S-nitrosylation inhibits the enzyme activity up to 60% under CC aerobic conditions. Chelation of Fe(2+) has no effect on the S- CC nitrosylation. It is uncertain whether nitrosylation occurs on CC Cys-300 or Cys-303 (By similarity). CC -!- DISRUPTION PHENOTYPE: Null mice are smaller than wild type and are CC erythematous with some animals having evidence of retroperitoneal CC hemorrhage. The resulting polycythemia can cause thrombosis and CC cardiac failure and animals die off after 10 weeks. Erythropoietin CC levels are increased in kidneys but not in livers. In neonatal CC null mice exposed to 75% oxygen, there are high levels of HIF1A CC nuclear abundance in retinal tissues accompanied by well-preserved CC retinal microvessels compared to wild type where oxygen-treated CC retinas exhibit reverse effects with increased risks of CC retinopathy. CC -!- SIMILARITY: Contains 1 Fe2OG dioxygenase domain. CC -!- SIMILARITY: Contains 1 MYND-type zinc finger. CC -!- SEQUENCE CAUTION: CC Sequence=AAH06903.1; Type=Erroneous initiation; Note=Translation N-terminally extended; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AL672234; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AJ310546; CAC42515.1; -; mRNA. DR EMBL; AF453878; AAL65165.1; -; mRNA. DR EMBL; BC006903; AAH06903.1; ALT_INIT; mRNA. DR RefSeq; NP_444437.2; NM_053207.2. DR UniGene; Mm.140619; -. DR ProteinModelPortal; Q91YE3; -. DR SMR; Q91YE3; 10-58, 165-380. DR BioGrid; 227481; 1. DR STRING; 10090.ENSMUSP00000034469; -. DR PhosphoSite; Q91YE3; -. DR PaxDb; Q91YE3; -. DR PRIDE; Q91YE3; -. DR DNASU; 112405; -. DR Ensembl; ENSMUST00000034469; ENSMUSP00000034469; ENSMUSG00000031987. DR GeneID; 112405; -. DR KEGG; mmu:112405; -. DR UCSC; uc012gna.1; mouse. DR CTD; 54583; -. DR MGI; MGI:1932286; Egln1. DR eggNOG; COG3751; -. DR GeneTree; ENSGT00390000001936; -. DR HOGENOM; HOG000004818; -. DR HOVERGEN; HBG051455; -. DR InParanoid; Q91YE3; -. DR KO; K09592; -. DR OMA; LGRSPLC; -. DR OrthoDB; EOG7TBC2W; -. DR TreeFam; TF314595; -. DR ChiTaRS; EGLN1; mouse. DR NextBio; 367881; -. DR PRO; PR:Q91YE3; -. DR Bgee; Q91YE3; -. DR CleanEx; MM_EGLN1; -. DR Genevestigator; Q91YE3; -. DR GO; GO:0005829; C:cytosol; IEA:Ensembl. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0031418; F:L-ascorbic acid binding; IEA:UniProtKB-KW. DR GO; GO:0031545; F:peptidyl-proline 4-dioxygenase activity; IEA:Ensembl. DR GO; GO:0055008; P:cardiac muscle tissue morphogenesis; IMP:MGI. DR GO; GO:0060347; P:heart trabecula formation; IMP:MGI. DR GO; GO:0060711; P:labyrinthine layer development; IMP:MGI. DR GO; GO:0030821; P:negative regulation of cAMP catabolic process; IEA:Ensembl. DR GO; GO:0051344; P:negative regulation of cyclic-nucleotide phosphodiesterase activity; IEA:Ensembl. DR GO; GO:0043433; P:negative regulation of sequence-specific DNA binding transcription factor activity; IEA:Ensembl. DR GO; GO:0032364; P:oxygen homeostasis; IEA:Ensembl. DR GO; GO:0018401; P:peptidyl-proline hydroxylation to 4-hydroxy-L-proline; IEA:Ensembl. DR GO; GO:0045765; P:regulation of angiogenesis; IMP:UniProtKB. DR GO; GO:0001666; P:response to hypoxia; IEA:Ensembl. DR GO; GO:0071731; P:response to nitric oxide; ISS:UniProtKB. DR GO; GO:0060412; P:ventricular septum morphogenesis; IMP:MGI. DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase. DR InterPro; IPR006620; Pro_4_hyd_alph. DR InterPro; IPR002893; Znf_MYND. DR Pfam; PF13640; 2OG-FeII_Oxy_3; 1. DR Pfam; PF01753; zf-MYND; 1. DR SMART; SM00702; P4Hc; 1. DR PROSITE; PS51471; FE2OG_OXY; 1. DR PROSITE; PS01360; ZF_MYND_1; 1. DR PROSITE; PS50865; ZF_MYND_2; 1. PE 2: Evidence at transcript level; KW Acetylation; Complete proteome; Cytoplasm; Dioxygenase; Iron; KW Metal-binding; Nucleus; Oxidoreductase; Reference proteome; KW S-nitrosylation; Vitamin C; Zinc; Zinc-finger. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 400 Egl nine homolog 1. FT /FTId=PRO_0000206662. FT DOMAIN 271 369 Fe2OG dioxygenase. FT ZN_FING 21 58 MYND-type. FT REGION 6 20 Required for nuclear export. FT REGION 218 228 Beta(2)beta(3) 'finger-like' loop (By FT similarity). FT METAL 290 290 Iron (By similarity). FT METAL 292 292 Iron (By similarity). FT METAL 351 351 Iron (By similarity). FT BINDING 360 360 2-oxoglutarate (By similarity). FT MOD_RES 2 2 N-acetylalanine (By similarity). FT MOD_RES 178 178 S-nitrosocysteine (By similarity). FT MOD_RES 185 185 S-nitrosocysteine (By similarity). FT MOD_RES 279 279 S-nitrosocysteine (By similarity). FT MOD_RES 300 300 S-nitrosocysteine (By similarity). FT MOD_RES 303 303 S-nitrosocysteine (By similarity). FT CONFLICT 205 209 ALHDT -> RIRHE (in Ref. 3; AAL65165). SQ SEQUENCE 400 AA; 43111 MW; A7EBC2BF6E22CDB9 CRC64; MASDSGGPGV LSASERDRQY CELCGKMENL LRCGRCRSSF YCCKEHQRQD WKKHKLVCQG GEAPRAQPAP AQPRVAPPPG GAPGAARAGG AARRGDSAAA SRVPGPEDAA QARSGPGPAE PGSEDPPLSR SPGPERASLC PAGGGPGEAL SPGGGLRPNG QTKPLPALKL ALEYIVPCMN KHGICVVDDF LGRETGQQIG DEVRALHDTG KFTDGQLVSQ KSDSSKDIRG DQITWIEGKE PGCETIGLLM SSMDDLIRHC SGKLGNYRIN GRTKAMVACY PGNGTGYVRH VDNPNGDGRC VTCIYYLNKD WDAKVSGGIL RIFPEGKAQF ADIEPKFDRL LFFWSDRRNP HEVQPAYATR YAITVWYFDA DERARAKVKY LTGEKGVRVE LKPNSVSKDV // ID ENOX1_MOUSE Reviewed; 643 AA. AC Q8BHR2; Q80WS5; DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 19-MAR-2014, entry version 87. DE RecName: Full=Ecto-NOX disulfide-thiol exchanger 1; DE AltName: Full=Constitutive Ecto-NOX; DE Short=cNOX; DE Includes: DE RecName: Full=Hydroquinone [NADH] oxidase; DE EC=1.-.-.-; DE Includes: DE RecName: Full=Protein disulfide-thiol oxidoreductase; DE EC=1.-.-.-; GN Name=Enox1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC STRAIN=C57BL/6J; TISSUE=Eye; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC STRAIN=C57BL/6; TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: Probably acts as a terminal oxidase of plasma electron CC transport from cytosolic NAD(P)H via hydroquinones to acceptors at CC the cell surface. Hydroquinone oxidase activity alternates with a CC protein disulfide-thiol interchange/oxidoreductase activity which CC may control physical membrane displacements associated with CC vesicle budding or cell enlargement. The activities oscillate with CC a period length of 24 minutes and play a role in control of the CC ultradian cellular biological clock (By similarity). CC -!- COFACTOR: Copper (By similarity). CC -!- ENZYME REGULATION: Not inhibited by the antitumor sulfonylurea CC LY181984, the vabilloid capsaicin, and retinoids (By similarity). CC -!- SUBCELLULAR LOCATION: Cell membrane (By similarity). Secreted, CC extracellular space (By similarity). Note=Extracellular and plasma CC membrane-associated (By similarity). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q8BHR2-1; Sequence=Displayed; CC Name=2; CC IsoId=Q8BHR2-2; Sequence=VSP_027122; CC -!- SIMILARITY: Belongs to the ENOX family. CC -!- SIMILARITY: Contains 1 RRM (RNA recognition motif) domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK051821; BAC34782.1; -; mRNA. DR EMBL; BC052062; AAH52062.1; -; mRNA. DR RefSeq; NP_001240688.1; NM_001253759.1. DR RefSeq; NP_766401.1; NM_172813.3. DR RefSeq; XP_006519062.1; XM_006518999.1. DR RefSeq; XP_006519063.1; XM_006519000.1. DR RefSeq; XP_006519064.1; XM_006519001.1. DR RefSeq; XP_006519065.1; XM_006519002.1. DR RefSeq; XP_006519066.1; XM_006519003.1. DR UniGene; Mm.441158; -. DR UniGene; Mm.490096; -. DR ProteinModelPortal; Q8BHR2; -. DR SMR; Q8BHR2; 142-200. DR PhosphoSite; Q8BHR2; -. DR PRIDE; Q8BHR2; -. DR Ensembl; ENSMUST00000022589; ENSMUSP00000022589; ENSMUSG00000022012. [Q8BHR2-1] DR GeneID; 239188; -. DR KEGG; mmu:239188; -. DR UCSC; uc007urv.2; mouse. [Q8BHR2-1] DR UCSC; uc007urz.2; mouse. [Q8BHR2-2] DR CTD; 55068; -. DR MGI; MGI:2444896; Enox1. DR eggNOG; NOG69825; -. DR GeneTree; ENSGT00390000006788; -. DR HOGENOM; HOG000049275; -. DR HOVERGEN; HBG051083; -. DR OMA; DANEINV; -. DR OrthoDB; EOG7DVD9H; -. DR TreeFam; TF323802; -. DR NextBio; 384035; -. DR PRO; PR:Q8BHR2; -. DR Bgee; Q8BHR2; -. DR CleanEx; MM_ENOX1; -. DR Genevestigator; Q8BHR2; -. DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro. DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro. DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW. DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW. DR Gene3D; 3.30.70.330; -; 1. DR InterPro; IPR012677; Nucleotide-bd_a/b_plait. DR InterPro; IPR000504; RRM_dom. DR Pfam; PF00076; RRM_1; 1. DR SMART; SM00360; RRM; 1. DR PROSITE; PS50102; RRM; 1. PE 2: Evidence at transcript level; KW Alternative splicing; Biological rhythms; Cell membrane; Coiled coil; KW Complete proteome; Copper; Electron transport; Membrane; NAD; KW Oxidoreductase; Reference proteome; Secreted; Transport. FT CHAIN 1 643 Ecto-NOX disulfide-thiol exchanger 1. FT /FTId=PRO_0000295901. FT VAR_SEQ 420 420 S -> SEADIEDCAGDPADRGLHSA (in isoform 2). FT /FTId=VSP_027122. SQ SEQUENCE 643 AA; 73281 MW; 42D58E3EC6B2FF53 CRC64; MVDAAGFESV AQCPRELHQM MAAAADGLGS IALDTTQLNM SVTDPTAWAT AMNNLGMVPV GLPGQQLVSD SICVPGFDPG LNMMTGITPI NPMIPGLGLV PPPPPTEVAV VKEIIHCKSC TLFPQNPNLP PPSTRERPPG CKTVFVGGLP ENATEEIIQE VFEQCGDITA IRKSKKNFCH IRFAEEFMVD KAIYLSGYRM RLGSSTDKKD SGRLHVDFAQ ARDDFYEWEC KQRMRAREER HRRKLEEDRL RPPSPPAIMH YSEHEAALLA DKLKDDSKFS EAITVLLSWI ERGEVNRRSA NQFYSMVQSA NSHVRRLMNE KATHEQEMEE AKENFKNALT GILTQFEQIV AVFNASTRQK AWDHFSKAQR KNIDIWRKHS EELRNAQSEQ LMGIRREEEM EMSDDENCDS PTKKMRVDES ALAAQAYALK EENDSLRWQL DAYRNEVELL KQEKEQLFRT EENLTKDQQL QFLQQTMQGM QQQLLAIQEE LNNKKSELEQ AKEEQSHTQA LLKVLQEQLK GTKDLVETNG HSHEDANEIN VLTVALVNQD RENNTEKRSQ GLKSEKEALL IGIISTFLHV HPFGANIEYL WSYMQQLDSK ISANEIEMLL MRLPRMFKQE FTGVGATLEK RWKLCAFEGI KTT // ID ENOX2_MOUSE Reviewed; 598 AA. AC Q8R0Z2; B1B073; Q8BY59; Q8R372; DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2002, sequence version 1. DT 19-MAR-2014, entry version 94. DE RecName: Full=Ecto-NOX disulfide-thiol exchanger 2; DE AltName: Full=APK1 antigen; DE AltName: Full=Cytosolic ovarian carcinoma antigen 1; DE AltName: Full=Tumor-associated hydroquinone oxidase; DE Short=tNOX; DE Includes: DE RecName: Full=Hydroquinone [NADH] oxidase; DE EC=1.-.-.-; DE Includes: DE RecName: Full=Protein disulfide-thiol oxidoreductase; DE EC=1.-.-.-; GN Name=Enox2; Synonyms=Cova1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC STRAIN=C57BL/6J; TISSUE=Diencephalon, and Thymus; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE RP SEQUENCE [LARGE SCALE MRNA] OF 328-598 (ISOFORM 3). RC STRAIN=FVB/N; TISSUE=Kidney, and Mammary gland; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: May be involved in cell growth. Probably acts as a CC terminal oxidase of plasma electron transport from cytosolic CC NAD(P)H via hydroquinones to acceptors at the cell surface. CC Hydroquinone oxidase activity alternates with a protein disulfide- CC thiol interchange/oxidoreductase activity which may control CC physical membrane displacements associated with vesicle budding or CC cell enlargement. The activities oscillate with a period length of CC 22 minutes and play a role in control of the ultradian cellular CC biological clock (By similarity). CC -!- COFACTOR: Copper (By similarity). CC -!- ENZYME REGULATION: Inhibited by the antitumor sulfonylurea CC LY181984, the vabilloid capsaicin, and retinoids (By similarity). CC -!- SUBCELLULAR LOCATION: Cell membrane (By similarity). Secreted, CC extracellular space (By similarity). Note=Extracellular and plasma CC membrane-associated (By similarity). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q8R0Z2-1; Sequence=Displayed; CC Name=2; CC IsoId=Q8R0Z2-2; Sequence=VSP_051830; CC Note=No experimental confirmation available; CC Name=3; CC IsoId=Q8R0Z2-3; Sequence=VSP_051831; CC Note=No experimental confirmation available; CC -!- PTM: Glycosylated (By similarity). CC -!- SIMILARITY: Belongs to the ENOX family. CC -!- SIMILARITY: Contains 1 RRM (RNA recognition motif) domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK034058; BAC28565.1; -; mRNA. DR EMBL; AK041822; BAC31077.1; -; mRNA. DR EMBL; BX294194; CAM21582.1; -; Genomic_DNA. DR EMBL; BC025915; AAH25915.1; -; mRNA. DR EMBL; BC026450; AAH26450.1; -; mRNA. DR RefSeq; NP_001258376.1; NM_001271447.1. DR RefSeq; NP_001258377.1; NM_001271448.1. DR RefSeq; NP_001258378.1; NM_001271449.1. DR RefSeq; NP_001258379.1; NM_001271450.1. DR RefSeq; NP_666063.1; NM_145951.5. DR UniGene; Mm.327730; -. DR ProteinModelPortal; Q8R0Z2; -. DR SMR; Q8R0Z2; 53-157. DR PhosphoSite; Q8R0Z2; -. DR PaxDb; Q8R0Z2; -. DR PRIDE; Q8R0Z2; -. DR Ensembl; ENSMUST00000033437; ENSMUSP00000033437; ENSMUSG00000031109. [Q8R0Z2-1] DR Ensembl; ENSMUST00000114911; ENSMUSP00000110561; ENSMUSG00000031109. [Q8R0Z2-2] DR Ensembl; ENSMUST00000114912; ENSMUSP00000110562; ENSMUSG00000031109. [Q8R0Z2-3] DR Ensembl; ENSMUST00000114914; ENSMUSP00000110564; ENSMUSG00000031109. [Q8R0Z2-1] DR Ensembl; ENSMUST00000114918; ENSMUSP00000110568; ENSMUSG00000031109. [Q8R0Z2-1] DR Ensembl; ENSMUST00000167659; ENSMUSP00000128885; ENSMUSG00000031109. [Q8R0Z2-1] DR GeneID; 209224; -. DR KEGG; mmu:209224; -. DR UCSC; uc009tcv.1; mouse. [Q8R0Z2-1] DR UCSC; uc012hgt.1; mouse. [Q8R0Z2-2] DR CTD; 10495; -. DR MGI; MGI:2384799; Enox2. DR eggNOG; NOG69825; -. DR GeneTree; ENSGT00390000006788; -. DR HOGENOM; HOG000049275; -. DR HOVERGEN; HBG051083; -. DR InParanoid; Q8R0Z2; -. DR OMA; NIHNDEL; -. DR OrthoDB; EOG7DVD9H; -. DR TreeFam; TF323802; -. DR ChiTaRS; ENOX2; mouse. DR NextBio; 372590; -. DR PRO; PR:Q8R0Z2; -. DR Bgee; Q8R0Z2; -. DR CleanEx; MM_ENOX2; -. DR Genevestigator; Q8R0Z2; -. DR GO; GO:0009897; C:external side of plasma membrane; ISS:UniProtKB. DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell. DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro. DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro. DR GO; GO:0015035; F:protein disulfide oxidoreductase activity; ISS:UniProtKB. DR GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW. DR GO; GO:0007624; P:ultradian rhythm; ISS:UniProtKB. DR Gene3D; 3.30.70.330; -; 1. DR InterPro; IPR012677; Nucleotide-bd_a/b_plait. DR InterPro; IPR000504; RRM_dom. DR Pfam; PF00076; RRM_1; 1. DR SMART; SM00360; RRM; 1. DR PROSITE; PS50102; RRM; 1. PE 2: Evidence at transcript level; KW Alternative splicing; Biological rhythms; Cell membrane; Coiled coil; KW Complete proteome; Copper; Electron transport; Glycoprotein; KW Growth regulation; Membrane; NAD; Oxidoreductase; Reference proteome; KW Secreted; Transport. FT CHAIN 1 598 Ecto-NOX disulfide-thiol exchanger 2. FT /FTId=PRO_0000079276. FT DOMAIN 99 178 RRM. FT COILED 264 299 Potential. FT COILED 352 476 Potential. FT COMPBIAS 29 96 Pro-rich. FT VAR_SEQ 463 473 Missing (in isoform 2). FT /FTId=VSP_051830. FT VAR_SEQ 540 555 Missing (in isoform 3). FT /FTId=VSP_051831. SQ SEQUENCE 598 AA; 68285 MW; C115D1130E4D6094 CRC64; MTLPVSDPAA WATAMNNLGM APLGIAGQPI LPDFDPALGM MTGIPPITPM MPGLGIVPPP IPPDMPVAKE IIHCKSCTLF PPNPNLPPPA TRERPPGCKT VFVGGLPENG TEQIIVEVFE QCGEIIAIRK SKKNFCHIRF AEEYMVDKAL YLSGYRIRLG SSTDKKDTGR LHVDFAQARD DLYEWECKQR MLAREERHRR RMEEERMRPP SPPPVVHYSD HECSIVAEKL KDDSKFSEAV QTLLTWIERG EVNRRSANHF YSMIQSANSH VRRLVNEKAT HEKEMEEAKE KFKQALSGIL IQFEQIVAVY HSASKQKAWD HFTKAQRKNI SVWCKQAEEI RNIHNDELMG IRREEEMEMS DDEIEETTET KETEESALVS QAEALKEEND SLRWQLDAYR NEVELLKQEQ GKAHREDDPN KEQQLKLLQQ ALQGMQQHLL KVQEEYKKKE AELDRIKDDN LQVEQLLENF HEKQENCGSR LCASSQEGEQ PLEKTAVSNP VKSEREALLV GIISTFLHVH PFGASIEYIC SYLNRLDNKA SYQIPSKLTT SPLLPISTSD VESLMSRLQH TFRQEMTGVG ASLEKRWKFC GFEGLKLT // ID ERG1_MOUSE Reviewed; 572 AA. AC P52019; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 19-MAR-2014, entry version 122. DE RecName: Full=Squalene monooxygenase; DE EC=1.14.13.132; DE AltName: Full=Squalene epoxidase; DE Short=SE; GN Name=Sqle; Synonyms=Erg1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=C57BL/6 X CBA; TISSUE=Liver; RX PubMed=7873613; DOI=10.1016/0167-4781(94)00245-X; RA Kosuga K., Hata S., Osumi T., Sakakibara J., Ono T.; RT "Nucleotide sequence of a cDNA for mouse squalene epoxidase."; RL Biochim. Biophys. Acta 1260:345-348(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6, and NMRI; TISSUE=Brain, and Mammary gland; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: Catalyzes the first oxygenation step in sterol CC biosynthesis and is suggested to be one of the rate-limiting CC enzymes in this pathway. CC -!- CATALYTIC ACTIVITY: Squalene + NADPH + O(2) = (3S)-2,3-epoxy-2,3- CC dihydrosqualene + NADP(+) + H(2)O. CC -!- COFACTOR: FAD. CC -!- PATHWAY: Terpene metabolism; lanosterol biosynthesis; lanosterol CC from farnesyl diphosphate: step 2/3. CC -!- SUBUNIT: May form a complex with squalene synthase. CC -!- SUBCELLULAR LOCATION: Microsome membrane; Multi-pass membrane CC protein. Endoplasmic reticulum membrane; Multi-pass membrane CC protein. CC -!- SIMILARITY: Belongs to the squalene monooxygenase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; D42048; BAA07649.1; -; mRNA. DR EMBL; BC042781; AAH42781.1; -; mRNA. DR EMBL; BC056361; AAH56361.1; -; mRNA. DR PIR; S52113; S52113. DR RefSeq; NP_033296.1; NM_009270.3. DR UniGene; Mm.296169; -. DR ProteinModelPortal; P52019; -. DR SMR; P52019; 115-480. DR PhosphoSite; P52019; -. DR PaxDb; P52019; -. DR PRIDE; P52019; -. DR Ensembl; ENSMUST00000022977; ENSMUSP00000022977; ENSMUSG00000022351. DR GeneID; 20775; -. DR KEGG; mmu:20775; -. DR UCSC; uc007vxq.1; mouse. DR CTD; 6713; -. DR MGI; MGI:109296; Sqle. DR eggNOG; COG0654; -. DR HOGENOM; HOG000174713; -. DR HOVERGEN; HBG005603; -. DR InParanoid; P52019; -. DR KO; K00511; -. DR OMA; VMGVQYK; -. DR OrthoDB; EOG7J446G; -. DR TreeFam; TF331056; -. DR UniPathway; UPA00767; UER00752. DR ChiTaRS; SQLE; mouse. DR NextBio; 299491; -. DR PRO; PR:P52019; -. DR ArrayExpress; P52019; -. DR Bgee; P52019; -. DR CleanEx; MM_SQLE; -. DR Genevestigator; P52019; -. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. DR GO; GO:0004506; F:squalene monooxygenase activity; IEA:UniProtKB-EC. DR GO; GO:0006725; P:cellular aromatic compound metabolic process; IEA:Ensembl. DR GO; GO:0008203; P:cholesterol metabolic process; IEA:Ensembl. DR GO; GO:0010033; P:response to organic substance; IEA:Ensembl. DR InterPro; IPR003042; Rng_hydrolase-like. DR InterPro; IPR013698; Squalene_epoxidase. DR Pfam; PF08491; SE; 1. DR PRINTS; PR00420; RNGMNOXGNASE. PE 2: Evidence at transcript level; KW Complete proteome; Endoplasmic reticulum; FAD; Flavoprotein; Membrane; KW Microsome; NADP; Oxidoreductase; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 572 Squalene monooxygenase. FT /FTId=PRO_0000209839. FT TRANSMEM 20 40 Helical; (Potential). FT TRANSMEM 60 80 Helical; (Potential). FT TRANSMEM 118 138 Helical; (Potential). FT TRANSMEM 544 564 Helical; (Potential). FT NP_BIND 124 151 FAD (Potential). SQ SEQUENCE 572 AA; 63770 MW; 5C30D80A204664D4 CRC64; MWTFLGIATF TYFYKKCGDV TLANKELLLC VLVFLSLGLV LSYRCRHRHG GLLGRHQSGA QFAAFSDILS ALPLIGFFWA KSPESEKKEQ LESKKCRKEI GLSETTLTGA ATSVSTSFVT DPEVIIVGSG VLGSALAAVL SRDGRKVTVI ERDLKEPDRI VGELLQPGGY RVLQELGLGD TVEGLNAHHI HGYIVHDYES RSEVQIPYPL SETNQVQSGI AFHHGRFIMS LRKAAMAEPN VKFIEGVVLQ LLEEDDAVIG VQYKDKETGD TKELHAPLTV VADGLFSKFR KSLISSKVSV SSHFVGFLMK DAPQFKPNFA ELVLVNPSPV LIYQISSSET RVLVDIRGEL PRNLREYMAE QIYPQLPEHL KESFLEASQN GRLRTMPASF LPPSSVNKRG VLILGDAYNL RHPLTGGGMT VALKDIKLWR QLLKDIPDLY DDAAIFQAKK SFFWSRKRTH SFVVNVLAQA LYELFSATDD SLHQLRKACF LYFKLGGECV TGPVGLLSIL SPHPLVLIRH FFSVAIYATY FCFKSEPWAT KPRALFSSGA VLYKACSILF PLIYSEMKYL VH // ID ERG24_MOUSE Reviewed; 418 AA. AC Q71KT5; B5LBK0; DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 2. DT 19-MAR-2014, entry version 71. DE RecName: Full=Delta(14)-sterol reductase; DE Short=Delta-14-SR; DE EC=1.3.1.70; DE AltName: Full=C-14 sterol reductase; DE Short=C14SR; DE AltName: Full=Sterol C14-reductase; DE AltName: Full=Transmembrane 7 superfamily member 2; GN Name=Tm7sf2; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Roberti R., Bennati A.M.; RT "cDNA cloning and expression of the gene encoding the mouse C-14 RT sterol reductase."; RL Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, RP DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY. RC STRAIN=129/SvJ; RA Bennati A.M., Schiavoni G., Franken S., Piobbico D., Della Fazia M.A., RA Caruso D., De Fabiani E., Benedetti L., Cusella De Angelis M.G., RA Gieselmann V., Servillo G., Beccari T., Roberti R.; RT "Disruption of the gene encoding 3beta-hydroxysterol Delta14-reductase RT (Tm7sf2) in mice does not impair cholesterol biosynthesis."; RL FEBS J. 275:5034-5047(2008). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=NOD; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Involved in the conversion of lanosterol to cholesterol. CC -!- CATALYTIC ACTIVITY: 4,4-dimethyl-5-alpha-cholesta-8,24-dien-3- CC beta-ol + NADP(+) = 4,4-dimethyl-5-alpha-cholesta-8,14,24-trien-3- CC beta-ol + NADPH. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass CC membrane protein (By similarity). Microsome membrane; Multi-pass CC membrane protein. CC -!- TISSUE SPECIFICITY: Strongly expressed in liver, weaker in ovary, CC testis, kidney and brain. CC -!- DISRUPTION PHENOTYPE: mice develop normally, appear healthy and CC are fertile. CC -!- SIMILARITY: Belongs to the ERG4/ERG24 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF480070; AAQ05836.1; -; mRNA. DR EMBL; EU672836; ACF94776.1; -; Genomic_DNA. DR EMBL; AK155475; BAE33285.1; -; mRNA. DR EMBL; CH466612; EDL33202.1; -; Genomic_DNA. DR RefSeq; NP_082730.2; NM_028454.2. DR UniGene; Mm.489613; -. DR MINT; MINT-1857062; -. DR PhosphoSite; Q71KT5; -. DR PaxDb; Q71KT5; -. DR PRIDE; Q71KT5; -. DR Ensembl; ENSMUST00000025713; ENSMUSP00000025713; ENSMUSG00000024799. DR GeneID; 73166; -. DR KEGG; mmu:73166; -. DR UCSC; uc008ggw.1; mouse. DR CTD; 7108; -. DR MGI; MGI:1920416; Tm7sf2. DR eggNOG; NOG72042; -. DR GeneTree; ENSGT00390000000417; -. DR HOGENOM; HOG000193296; -. DR HOVERGEN; HBG007825; -. DR InParanoid; B5LBK0; -. DR KO; K00222; -. DR OMA; GDALWYE; -. DR TreeFam; TF101179; -. DR NextBio; 337585; -. DR PRO; PR:Q71KT5; -. DR ArrayExpress; Q71KT5; -. DR Bgee; Q71KT5; -. DR Genevestigator; Q71KT5; -. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0043235; C:receptor complex; ISO:MGI. DR GO; GO:0050613; F:delta14-sterol reductase activity; IEA:UniProtKB-EC. DR GO; GO:0006695; P:cholesterol biosynthetic process; IEA:UniProtKB-KW. DR InterPro; IPR001171; Ergosterol_biosynth_ERG4_ERG24. DR InterPro; IPR018083; Sterol_reductase_CS. DR Pfam; PF01222; ERG4_ERG24; 1. DR PROSITE; PS01017; STEROL_REDUCT_1; 1. DR PROSITE; PS01018; STEROL_REDUCT_2; 1. PE 2: Evidence at transcript level; KW Cholesterol biosynthesis; Cholesterol metabolism; Complete proteome; KW Endoplasmic reticulum; Lipid biosynthesis; Lipid metabolism; Membrane; KW Microsome; NADP; Oxidoreductase; Reference proteome; KW Steroid biosynthesis; Steroid metabolism; Sterol biosynthesis; KW Sterol metabolism; Transmembrane; Transmembrane helix. FT CHAIN 1 418 Delta(14)-sterol reductase. FT /FTId=PRO_0000331121. FT TRANSMEM 13 35 Helical; (Potential). FT TRANSMEM 62 81 Helical; (Potential). FT TRANSMEM 102 124 Helical; (Potential). FT TRANSMEM 129 148 Helical; (Potential). FT TRANSMEM 255 277 Helical; (Potential). FT TRANSMEM 287 304 Helical; (Potential). FT TRANSMEM 355 377 Helical; (Potential). FT CONFLICT 298 298 V -> A (in Ref. 1; AAQ05836 and 3; FT BAE33285). SQ SEQUENCE 418 AA; 46521 MW; 0DCCA4E4B9423A31 CRC64; MTSREASQAP LEFGGPLGVA ALLILLPATM FHLLLAARSG PARLLALPAY LPGLEELWSP WALLLLFIWL GLQVALYLLP ARKVAEGLEL KDKSRLRYPI NGFQALVLTA LLMGLGVSVG LPLGALPGML LPLAFATTLT SFIFSLLLYA KALVAPASAL APGGNSGNSM YDFFLGRELN PRLGSFDFKY FCELRPGLIG WVFINLALLM QEAELRGSPS LAMWLVNGFQ LLYVGDALWY EESVLTTMDI IHDGFGFMLV FGDLAWVPFT YSLQAQFLLY HPQPLGLPMA LLICLLKVIG YYIFRGANSQ KNTFRKNPSD PSVAGLETIP TATGRQLLVS GWWGMVRHPN YLGDLIMALA WSLPCGLSHL LPYFYVLYFT ALLVHREARD EQQCLQKYGR AWQEYCKRVP YRIIPYVY // ID ERO1B_MOUSE Reviewed; 467 AA. AC Q8R2E9; Q14DN0; DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2002, sequence version 1. DT 19-MAR-2014, entry version 88. DE RecName: Full=ERO1-like protein beta; DE Short=ERO1-L-beta; DE EC=1.8.4.-; DE AltName: Full=Endoplasmic reticulum oxidoreductin-1-like protein B; DE AltName: Full=Oxidoreductin-1-L-beta; DE Flags: Precursor; GN Name=Ero1lb; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=FVB/N; TISSUE=Intestine, and Liver; RA Li B., Abplanalp W.A., Kim P.S.; RT "Cloning of the two forms of Ero1, alpha and beta and their regulation RT in cultured thyrocytes."; RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Thymus; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6; TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP TISSUE SPECIFICITY, AND DIMERIZATION. RX PubMed=16012172; DOI=10.1074/jbc.M505023200; RA Dias-Gunasekara S., Gubbens J., van Lith M., Dunne C., Williams J.A., RA Kataky R., Scoones D., Lapthorn A., Bulleid N.J., Benham A.M.; RT "Tissue-specific expression and dimerization of the endoplasmic RT reticulum oxidoreductase Ero1beta."; RL J. Biol. Chem. 280:33066-33075(2005). RN [5] RP FUNCTION, TISSUE SPECIFICITY, AND MUTAGENESIS OF CYS-396. RX PubMed=20308425; DOI=10.1083/jcb.200911086; RA Zito E., Chin K.T., Blais J., Harding H.P., Ron D.; RT "ERO1-beta, a pancreas-specific disulfide oxidase, promotes insulin RT biogenesis and glucose homeostasis."; RL J. Cell Biol. 188:821-832(2010). CC -!- FUNCTION: Oxidoreductase involved in disulfide bond formation in CC the endoplasmic reticulum. Efficiently reoxidizes P4HB/PDI, the CC enzyme catalyzing protein disulfide formation, in order to allow CC P4HB to sustain additional rounds of disulfide formation. Other CC protein disulfide isomerase family members can also be reoxidized, CC but at lower rates compared to P4HB, including PDIA2, PDIA3, CC PDIA4, PDIA6 and NXNDC12. Following P4HB reoxidation, passes its CC electrons to molecular oxygen via FAD, leading to the production CC of reactive oxygen species (ROS) in the cell (By similarity). CC Involved in oxidative proinsulin folding in pancreatic cells, CC hence required for glucose homeostasis in vivo. CC -!- COFACTOR: FAD (By similarity). CC -!- ENZYME REGULATION: Glutathione may be required to regulate its CC activity in the endoplasmic reticulum (By similarity). CC -!- SUBUNIT: Homodimer; disulfide-linked (By similarity). Heterodimer CC with ERO1L; disulfide-linked (By similarity). Also detected as CC monomer. Homodimers may be somewhat less active than monomers. The CC abundance of monomers and homodimers may be tissue-specific. CC Interacts with P4HB (By similarity). Interacts with ERP44 (By CC similarity). CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral CC membrane protein; Lumenal side (By similarity). Note=The CC association with ERP44 may be essential for its retention in the CC endoplasmic reticulum (By similarity). CC -!- TISSUE SPECIFICITY: Predominantly expressed in stomach and CC pancreas (mostly in the islets of Langerhans) (at protein level). CC -!- PTM: N-glycosylated (By similarity). CC -!- PTM: The Cys-90/Cys-95 and Cys-393/Cys-396 disulfide bonds CC constitute the redox-active center. The Cys-90/Cys-95 disulfide CC bond may accept electron from P4HB and funnel them to the active CC site disulfide Cys-393/Cys-396 (By similarity). CC -!- SIMILARITY: Belongs to the EROs family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF489856; AAL96670.1; -; mRNA. DR EMBL; AK041951; BAC31108.1; -; mRNA. DR EMBL; BC058721; AAH58721.1; -; mRNA. DR EMBL; BC112426; AAI12427.1; -; mRNA. DR EMBL; BC145888; AAI45889.1; -; mRNA. DR EMBL; BC145890; AAI45891.1; -; mRNA. DR RefSeq; NP_080460.2; NM_026184.2. DR UniGene; Mm.358706; -. DR ProteinModelPortal; Q8R2E9; -. DR SMR; Q8R2E9; 34-464. DR IntAct; Q8R2E9; 1. DR MINT; MINT-4094706; -. DR PhosphoSite; Q8R2E9; -. DR PaxDb; Q8R2E9; -. DR PRIDE; Q8R2E9; -. DR Ensembl; ENSMUST00000071973; ENSMUSP00000071864; ENSMUSG00000057069. DR GeneID; 67475; -. DR KEGG; mmu:67475; -. DR UCSC; uc007plr.1; mouse. DR CTD; 56605; -. DR MGI; MGI:1914725; Ero1lb. DR eggNOG; COG5061; -. DR GeneTree; ENSGT00390000007753; -. DR HOGENOM; HOG000012778; -. DR HOVERGEN; HBG051507; -. DR InParanoid; Q14DN0; -. DR KO; K10976; -. DR OMA; SNKYSKV; -. DR OrthoDB; EOG7PP579; -. DR TreeFam; TF314471; -. DR ChiTaRS; ERO1LB; mouse. DR NextBio; 324694; -. DR PRO; PR:Q8R2E9; -. DR Bgee; Q8R2E9; -. DR CleanEx; MM_ERO1LB; -. DR Genevestigator; Q8R2E9; -. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016671; F:oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor; IEA:InterPro. DR GO; GO:0003756; F:protein disulfide isomerase activity; IEA:InterPro. DR GO; GO:0019471; P:4-hydroxyproline metabolic process; IGI:MGI. DR GO; GO:0045454; P:cell redox homeostasis; IGI:MGI. DR GO; GO:0030198; P:extracellular matrix organization; IGI:MGI. DR GO; GO:0022417; P:protein maturation by protein folding; IGI:MGI. DR InterPro; IPR007266; Ero1. DR PANTHER; PTHR12613:SF0; PTHR12613:SF0; 1. DR Pfam; PF04137; ERO1; 1. DR PIRSF; PIRSF017205; ERO1; 1. PE 1: Evidence at protein level; KW Complete proteome; Disulfide bond; Electron transport; KW Endoplasmic reticulum; FAD; Flavoprotein; Glycoprotein; Membrane; KW Oxidoreductase; Redox-active center; Reference proteome; Signal; KW Transport. FT SIGNAL 1 33 Potential. FT CHAIN 34 467 ERO1-like protein beta. FT /FTId=PRO_0000008419. FT BINDING 186 186 FAD (By similarity). FT BINDING 188 188 FAD (By similarity). FT BINDING 199 199 FAD (By similarity). FT BINDING 251 251 FAD (By similarity). FT BINDING 254 254 FAD (By similarity). FT BINDING 286 286 FAD (By similarity). FT CARBOHYD 122 122 N-linked (GlcNAc...) (Potential). FT CARBOHYD 140 140 N-linked (GlcNAc...) (Potential). FT CARBOHYD 145 145 N-linked (GlcNAc...) (Potential). FT CARBOHYD 383 383 N-linked (GlcNAc...) (Potential). FT DISULFID 81 390 By similarity. FT DISULFID 90 95 Redox-active (By similarity). FT DISULFID 393 396 Redox-active (By similarity). FT MUTAGEN 396 396 C->A: Complete loss of disulfide oxidase FT activity in vitro. SQ SEQUENCE 467 AA; 53518 MW; 442E7D6CB42A2446 CRC64; MSPGFRRAVT GQGAAAAVQL LVTLSFLSSL VKTQVTGVLD DCLCDIDSID KFNTYKIFPK IKKLQERDYF RYYKVNLKRP CPFWAEDGHC SIKDCHVEPC PESKIPVGIK AGRSNKYSQA ANSTKELDDC EQANKLGAIN STLSNESKEA FIDWARYDDS QDHFCELDDE RSPAAQYVDL LLNPERYTGY KGSSAWRVWN SIYEENCFKP RSVYRPLNPL APSRGEDDGE SFYTWLEGLC LEKRVFYKLI SGLHASINLH LCANYLLEET WGKPSWGPNI KEFRRRFDPV ETKGEGPRRL KNLYFLYLIE LRALSKVAPY FERSIVDLYT GNVEDDADTK TLLLSIFQDT KSFPMHFDEK SMFAGDKKGA KSLKEEFRLH FKNISRIMDC VGCDKCRLWG KLQTQGLGTA LKILFSEKEI QNLPENSPSK GFQLTRQEIV ALLNAFGRLS TSIRELQNFK ALLQHRR // ID ERO1A_MOUSE Reviewed; 464 AA. AC Q8R180; Q9CV47; Q9QY03; DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot. DT 24-MAR-2009, sequence version 2. DT 19-MAR-2014, entry version 104. DE RecName: Full=ERO1-like protein alpha; DE Short=ERO1-L; DE Short=ERO1-L-alpha; DE EC=1.8.4.-; DE AltName: Full=Endoplasmic reticulum oxidoreductin-1-like protein; DE AltName: Full=Oxidoreductin-1-L-alpha; DE Flags: Precursor; GN Name=Ero1l; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=10671517; DOI=10.1074/jbc.275.7.4827; RA Cabibbo A., Pagani M., Fabbri M., Rocchi M., Farmery M.R., RA Bulleid N.J., Sitia R.; RT "ERO1-L, a human protein that favors disulfide bond formation in the RT endoplasmic reticulum."; RL J. Biol. Chem. 275:4827-4833(2000). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Mammary tumor; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 232-464. RC STRAIN=C57BL/6J; TISSUE=Tongue; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [4] RP INDUCTION. RX PubMed=12752442; DOI=10.1046/j.1432-1033.2003.03590.x; RA Gess B., Hofbauer K.H., Wenger R.H., Lohaus C., Meyer H.E., Kurtz A.; RT "The cellular oxygen tension regulates expression of the endoplasmic RT oxidoreductase ERO1-Lalpha."; RL Eur. J. Biochem. 270:2228-2235(2003). RN [5] RP FUNCTION, AND INDUCTION. RX PubMed=19752026; DOI=10.1083/jcb.200904060; RA Li G., Mongillo M., Chin K.T., Harding H., Ron D., Marks A.R., RA Tabas I.; RT "Role of ERO1-alpha-mediated stimulation of inositol 1,4,5- RT triphosphate receptor activity in endoplasmic reticulum stress-induced RT apoptosis."; RL J. Cell Biol. 186:783-792(2009). RN [6] RP FUNCTION, AND TISSUE SPECIFICITY. RX PubMed=20308425; DOI=10.1083/jcb.200911086; RA Zito E., Chin K.T., Blais J., Harding H.P., Ron D.; RT "ERO1-beta, a pancreas-specific disulfide oxidase, promotes insulin RT biogenesis and glucose homeostasis."; RL J. Cell Biol. 188:821-832(2010). CC -!- FUNCTION: Oxidoreductase involved in disulfide bond formation in CC the endoplasmic reticulum. Efficiently reoxidizes P4HB/PDI, the CC enzyme catalyzing protein disulfide formation, in order to allow CC P4HB to sustain additional rounds of disulfide formation. CC Following P4HB reoxidation, passes its electrons to molecular CC oxygen via FAD, leading to the production of reactive oxygen CC species (ROS) in the cell. Required for the proper folding of CC immunoglobulins (By similarity). Plays an important role in ER CC stress-induced, CHOP-dependent apoptosis by activating the CC inositol 1,4,5-trisphosphate receptor IP3R1. CC -!- COFACTOR: FAD (By similarity). CC -!- ENZYME REGULATION: Enzyme activity is tightly regulated to prevent CC the accumulation of reactive oxygen species in the endoplasmic CC reticulum. Reversibly down-regulated by the formation of disulfide CC bonds between the active site Cys-94 and Cys-130, and between Cys- CC 99 and Cys-104. Glutathione may be required to regulate its CC activity in the endoplasmic reticulum (By similarity). CC -!- SUBUNIT: Predominantly monomer. May function both as a monomer and CC a homodimer. Interacts with PDILT (By similarity). CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral CC membrane protein; Lumenal side (By similarity). Note=The CC association with ERP44 is essential for its retention in the CC endoplasmic reticulum (By similarity). CC -!- TISSUE SPECIFICITY: Widely expressed (at protein level). CC -!- INDUCTION: Stimulated by hypoxia; suggesting that it is regulated CC via the HIF-pathway. By ER stress in a DDIT3/CHOP-dependent CC manner. CC -!- PTM: N-glycosylated (By similarity). CC -!- PTM: The Cys-94/Cys-99 and Cys-390/Cys-393 disulfide bonds CC constitute the redox-active center. The Cys-94/Cys-99 disulfide CC bond may accept electron from P4HB and funnel them to the active CC site disulfide Cys-390/Cys-393. The regulatory Cys-99/Cys-104 CC disulfide bond stabilizes the other regulatory bond Cys-94/Cys-130 CC (By similarity). CC -!- SIMILARITY: Belongs to the EROs family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF144695; AAF20364.1; -; mRNA. DR EMBL; BC025102; AAH25102.1; -; mRNA. DR EMBL; AK009667; BAB26428.1; -; mRNA. DR RefSeq; NP_056589.1; NM_015774.3. DR UniGene; Mm.387108; -. DR ProteinModelPortal; Q8R180; -. DR SMR; Q8R180; 34-461. DR IntAct; Q8R180; 1. DR MINT; MINT-4094692; -. DR PhosphoSite; Q8R180; -. DR PaxDb; Q8R180; -. DR PRIDE; Q8R180; -. DR Ensembl; ENSMUST00000022378; ENSMUSP00000022378; ENSMUSG00000021831. DR GeneID; 50527; -. DR KEGG; mmu:50527; -. DR UCSC; uc007tgm.2; mouse. DR CTD; 30001; -. DR MGI; MGI:1354385; Ero1l. DR eggNOG; COG5061; -. DR GeneTree; ENSGT00390000007753; -. DR HOGENOM; HOG000012778; -. DR HOVERGEN; HBG051507; -. DR InParanoid; Q8R180; -. DR KO; K10950; -. DR OMA; QVENCEE; -. DR OrthoDB; EOG7PP579; -. DR TreeFam; TF314471; -. DR ChiTaRS; ERO1L; mouse. DR NextBio; 307530; -. DR PRO; PR:Q8R180; -. DR ArrayExpress; Q8R180; -. DR Bgee; Q8R180; -. DR CleanEx; MM_ERO1L; -. DR Genevestigator; Q8R180; -. DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; ISO:MGI. DR GO; GO:0016491; F:oxidoreductase activity; IDA:MGI. DR GO; GO:0016671; F:oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor; IEA:InterPro. DR GO; GO:0003756; F:protein disulfide isomerase activity; IEA:InterPro. DR GO; GO:0019471; P:4-hydroxyproline metabolic process; IGI:MGI. DR GO; GO:0050873; P:brown fat cell differentiation; IDA:MGI. DR GO; GO:0045454; P:cell redox homeostasis; IGI:MGI. DR GO; GO:0051085; P:chaperone mediated protein folding requiring cofactor; IEA:Ensembl. DR GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; IDA:MGI. DR GO; GO:0030198; P:extracellular matrix organization; IGI:MGI. DR GO; GO:0070059; P:intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress; IMP:UniProtKB. DR GO; GO:0022417; P:protein maturation by protein folding; IGI:MGI. DR GO; GO:0051209; P:release of sequestered calcium ion into cytosol; IMP:UniProtKB. DR InterPro; IPR007266; Ero1. DR PANTHER; PTHR12613:SF0; PTHR12613:SF0; 1. DR Pfam; PF04137; ERO1; 1. DR PIRSF; PIRSF017205; ERO1; 1. PE 1: Evidence at protein level; KW Apoptosis; Complete proteome; Disulfide bond; Electron transport; KW Endoplasmic reticulum; FAD; Flavoprotein; Glycoprotein; Membrane; KW Oxidoreductase; Phosphoprotein; Redox-active center; KW Reference proteome; Signal; Transport. FT SIGNAL 1 23 Potential. FT CHAIN 24 464 ERO1-like protein alpha. FT /FTId=PRO_0000008416. FT BINDING 186 186 FAD (By similarity). FT BINDING 188 188 FAD (By similarity). FT BINDING 199 199 FAD (By similarity). FT BINDING 248 248 FAD (By similarity). FT BINDING 251 251 FAD (By similarity). FT BINDING 283 283 FAD (By similarity). FT BINDING 296 296 FAD (By similarity). FT MOD_RES 142 142 Phosphoserine (By similarity). FT CARBOHYD 276 276 N-linked (GlcNAc...) (Potential). FT CARBOHYD 380 380 N-linked (GlcNAc...) (Potential). FT DISULFID 35 48 By similarity. FT DISULFID 37 46 By similarity. FT DISULFID 85 387 By similarity. FT DISULFID 94 130 Alternate; alternate. FT DISULFID 94 99 Redox-active; alternate (By similarity). FT DISULFID 99 104 Alternate (By similarity). FT DISULFID 207 237 By similarity. FT DISULFID 390 393 Redox-active (By similarity). FT CONFLICT 130 130 C -> G (in Ref. 2; AAH25102). SQ SEQUENCE 464 AA; 54084 MW; FED19B00E1FBD2A1 CRC64; MGRAWGLLVG LLGVVWLLRL GHGEERRPET AAQRCFCQVS GYLDDCTCDV ETIDKFNNYR LFPRLQKLLE SDYFRYYKVN LKKPCPFWND INQCGRRDCA VKPCHSDEVP DGIKSASYKY SEEANRIEEC EQAERLGAVD ESLSEETQKA VLQWTKHDDS SDSFCEIDDI QSPDAEYVDL LLNPERYTGY KGPDAWRIWS VIYEENCFKP QTIQRPLASG RGKSKENTFY NWLEGLCVEK RAFYRLISGL HASINVHLSA RYLLQDTWLE KKWGHNVTEF QQRFDGILTE GEGPRRLRNL YFLYLIELRA LSKVLPFFER PDFQLFTGNK VQDAENKALL LEILHEIKSF PLHFDENSFF AGDKNEAHKL KEDFRLHFRN ISRIMDCVGC FKCRLWGKLQ TQGLGTALKI LFSEKLIANM PESGPSYEFQ LTRQEIVSLF NAFGRISTSV RELENFRHLL QNVH // ID ETHE1_MOUSE Reviewed; 254 AA. AC Q9DCM0; Q9ESL5; DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 2. DT 19-MAR-2014, entry version 87. DE RecName: Full=Persulfide dioxygenase ETHE1, mitochondrial; DE EC=1.13.11.18; DE AltName: Full=Ethylmalonic encephalopathy protein 1 homolog; DE AltName: Full=Hepatoma subtracted clone one protein; DE AltName: Full=Sulfur dioxygenase ETHE1; DE Flags: Precursor; GN Name=Ethe1; Synonyms=Hsco; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Liver; RA Fujita J., Higashitsuji H., Higashitsuji H.; RT "Expression of HSCO in hepatomas."; RL Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Kidney; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Colon, Kidney, and Mammary tumor; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP DISRUPTION PHENOTYPE, AND FUNCTION. RX PubMed=19136963; DOI=10.1038/nm.1907; RA Tiranti V., Viscomi C., Hildebrandt T., Di Meo I., Mineri R., RA Tiveron C., Levitt M.D., Prelle A., Fagiolari G., Rimoldi M., RA Zeviani M.; RT "Loss of ETHE1, a mitochondrial dioxygenase, causes fatal sulfide RT toxicity in ethylmalonic encephalopathy."; RL Nat. Med. 15:200-205(2009). RN [5] RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-32 AND LYS-172, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., RA Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). RN [6] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-32; LYS-66 AND LYS-172, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23576753; DOI=10.1073/pnas.1302961110; RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., RA Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.; RT "Label-free quantitative proteomics of the lysine acetylome in RT mitochondria identifies substrates of SIRT3 in metabolic pathways."; RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013). CC -!- FUNCTION: First described as a protein that can shuttle between CC the nucleus and the cytoplasm and suppress p53-induced apoptosis CC by sequestering the transcription factor RELA/NFKB3 in the CC cytoplasm and preventing its accumulation in the nucleus (By CC similarity). Sulfur dioxygenase that plays an essential role in CC hydrogen sulfide catabolism in the mitochondrial matrix. Hydrogen CC sulfide (H(2)S) is first oxidized by SQRDL, giving rise to CC cysteine persulfide residues. ETHE1 consumes molecular oxygen to CC catalyze the oxidation of the persulfide, once it has been CC transferred to a thiophilic acceptor, such as glutathione (R-SSH). CC Plays an important role in metabolic homeostasis in mitochondria CC by metabolizing hydrogen sulfide and preventing the accumulation CC of supraphysiological H(2)S levels that have toxic effects, due to CC the inhibition of cytochrome c oxidase. CC -!- CATALYTIC ACTIVITY: Sulfur + O(2) + H(2)O = sulfite + 2 H(+). CC -!- COFACTOR: Binds 1 Fe(2+) ion per subunit (By similarity). CC -!- SUBUNIT: Monomer. Interacts with TST. May interact with RELA (By CC similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By CC similarity). Mitochondrion matrix (By similarity). CC -!- DISRUPTION PHENOTYPE: Mice are born at slightly less than the CC expected Mendelian rate. Pups display growth arrest at about 15 CC days after birth and die five to six weeks after birth. Mice CC exhibit elevated levels of hydrogen sulfide (H(2)S) in liver, CC muscle and brain, together with increased urinary levels of CC ethylmalonic acid and thiosulfate. Their mitochondria show CC decreased cytochrome c oxidase activity, probably due to the toxic CC effects of supraphysiological levels of hydrogen sulfide. CC -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily. CC Glyoxalase II family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AB049623; BAB16409.1; -; mRNA. DR EMBL; AK002666; BAB22271.2; -; mRNA. DR EMBL; BC010592; AAH10592.1; -; mRNA. DR EMBL; BC083162; AAH83162.1; -; mRNA. DR EMBL; BC094044; AAH94044.1; -; mRNA. DR RefSeq; NP_075643.1; NM_023154.3. DR RefSeq; XP_006540342.1; XM_006540279.1. DR UniGene; Mm.29553; -. DR ProteinModelPortal; Q9DCM0; -. DR SMR; Q9DCM0; 23-245. DR IntAct; Q9DCM0; 2. DR MINT; MINT-1850653; -. DR STRING; 10090.ENSMUSP00000076433; -. DR PhosphoSite; Q9DCM0; -. DR REPRODUCTION-2DPAGE; Q9DCM0; -. DR PaxDb; Q9DCM0; -. DR PRIDE; Q9DCM0; -. DR Ensembl; ENSMUST00000077191; ENSMUSP00000076433; ENSMUSG00000064254. DR GeneID; 66071; -. DR KEGG; mmu:66071; -. DR UCSC; uc009fqb.2; mouse. DR CTD; 23474; -. DR MGI; MGI:1913321; Ethe1. DR eggNOG; COG0491; -. DR GeneTree; ENSGT00530000063033; -. DR HOGENOM; HOG000058040; -. DR HOVERGEN; HBG053310; -. DR InParanoid; Q9DCM0; -. DR KO; K17725; -. DR OMA; QIDIAVP; -. DR OrthoDB; EOG7MH107; -. DR TreeFam; TF312952; -. DR ChiTaRS; ETHE1; mouse. DR NextBio; 320540; -. DR PRO; PR:Q9DCM0; -. DR Bgee; Q9DCM0; -. DR CleanEx; MM_ETHE1; -. DR Genevestigator; Q9DCM0; -. DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0016787; F:hydrolase activity; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; ISS:UniProtKB. DR GO; GO:0050313; F:sulfur dioxygenase activity; ISS:UniProtKB. DR GO; GO:0006749; P:glutathione metabolic process; ISS:UniProtKB. DR GO; GO:0070813; P:hydrogen sulfide metabolic process; ISS:UniProtKB. DR Gene3D; 3.60.15.10; -; 1. DR InterPro; IPR001279; Beta-lactamas-like. DR Pfam; PF00753; Lactamase_B; 1. DR SMART; SM00849; Lactamase_B; 1. PE 1: Evidence at protein level; KW Acetylation; Complete proteome; Cytoplasm; Dioxygenase; Metal-binding; KW Mitochondrion; Nucleus; Oxidoreductase; Reference proteome; KW Transit peptide. FT TRANSIT 1 7 Mitochondrion (By similarity). FT CHAIN 8 254 Persulfide dioxygenase ETHE1, FT mitochondrial. FT /FTId=PRO_0000012290. FT METAL 79 79 Iron; catalytic (By similarity). FT METAL 135 135 Iron; catalytic (By similarity). FT METAL 154 154 Iron; catalytic (By similarity). FT MOD_RES 32 32 N6-acetyllysine; alternate. FT MOD_RES 32 32 N6-succinyllysine; alternate. FT MOD_RES 66 66 N6-acetyllysine. FT MOD_RES 172 172 N6-acetyllysine; alternate. FT MOD_RES 172 172 N6-succinyllysine; alternate. SQ SEQUENCE 254 AA; 27739 MW; 3F28C0ED465A3062 CRC64; MASAVVRVAG RRLSQQSASG APVLLRQMFE PKSCTYTYLL GDRESREAVL IDPVLETAHR DAQLIKELGL KLLYAVNTHC HADHITGTGV LRSLLPGCQS VISRLSGAQA DLHIGEGDSI RFGRFALETR ASPGHTPGCV TFVLNDQSMA FTGDALLIRG CGRTDFQQGC AKTLYHSVHE KIFTLPGNCL IYPAHDYHGL TVSTVEEERT LNPRLTLSCE EFIKVMDNLN LPKPQQIDIA VPANMRCGVQ TPPS // ID ETFD_MOUSE Reviewed; 616 AA. AC Q921G7; Q3U7K2; Q8BK82; Q9DCT9; DT 13-SEP-2004, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 19-MAR-2014, entry version 106. DE RecName: Full=Electron transfer flavoprotein-ubiquinone oxidoreductase, mitochondrial; DE Short=ETF-QO; DE Short=ETF-ubiquinone oxidoreductase; DE EC=1.5.5.1; DE AltName: Full=Electron-transferring-flavoprotein dehydrogenase; DE Short=ETF dehydrogenase; DE Flags: Precursor; GN Name=Etfdh; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J, and NOD; TISSUE=Bone marrow, Kidney, and Thymus; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Mammary tumor; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP PROTEIN SEQUENCE OF 212-222, AND MASS SPECTROMETRY. RC STRAIN=C57BL/6; TISSUE=Brain; RA Lubec G., Kang S.U.; RL Submitted (APR-2007) to UniProtKB. RN [4] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-95, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=16916647; DOI=10.1016/j.molcel.2006.06.026; RA Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T., RA Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.; RT "Substrate and functional diversity of lysine acetylation revealed by RT a proteomics survey."; RL Mol. Cell 23:607-618(2006). RN [5] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-550, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=17242355; DOI=10.1073/pnas.0609836104; RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; RT "Large-scale phosphorylation analysis of mouse liver."; RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). RN [6] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-131; LYS-222; LYS-356 AND RP LYS-415, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Liver; RX PubMed=23576753; DOI=10.1073/pnas.1302961110; RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., RA Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.; RT "Label-free quantitative proteomics of the lysine acetylome in RT mitochondria identifies substrates of SIRT3 in metabolic pathways."; RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013). CC -!- FUNCTION: Accepts electrons from ETF and reduces ubiquinone (By CC similarity). CC -!- CATALYTIC ACTIVITY: Reduced electron-transferring flavoprotein + CC ubiquinone = electron-transferring flavoprotein + ubiquinol. CC -!- COFACTOR: Binds 1 4Fe-4S cluster (By similarity). CC -!- COFACTOR: FAD (By similarity). CC -!- SUBUNIT: Monomer (By similarity). CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane (By CC similarity). CC -!- PTM: Acetylation of Lys-95 and Lys-222 is observed in liver CC mitochondria from fasted mice but not from fed mice. CC -!- SIMILARITY: Belongs to the ETF-QO/FixC family. CC -!- SIMILARITY: Contains 1 4Fe-4S ferredoxin-type domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK002483; BAB22135.1; -; mRNA. DR EMBL; AK075673; BAC35888.1; -; mRNA. DR EMBL; AK141684; BAE24798.1; -; mRNA. DR EMBL; AK152624; BAE31367.1; -; mRNA. DR EMBL; AK169686; BAE41304.1; -; mRNA. DR EMBL; BC012522; AAH12522.1; -; mRNA. DR RefSeq; NP_080070.2; NM_025794.2. DR UniGene; Mm.28336; -. DR ProteinModelPortal; Q921G7; -. DR SMR; Q921G7; 38-616. DR IntAct; Q921G7; 3. DR MINT; MINT-1844957; -. DR PhosphoSite; Q921G7; -. DR PaxDb; Q921G7; -. DR PRIDE; Q921G7; -. DR Ensembl; ENSMUST00000029386; ENSMUSP00000029386; ENSMUSG00000027809. DR GeneID; 66841; -. DR KEGG; mmu:66841; -. DR UCSC; uc008pnq.2; mouse. DR CTD; 2110; -. DR MGI; MGI:106100; Etfdh. DR eggNOG; COG0644; -. DR GeneTree; ENSGT00390000010773; -. DR HOGENOM; HOG000259450; -. DR HOVERGEN; HBG005615; -. DR InParanoid; Q921G7; -. DR KO; K00311; -. DR OMA; EKDIRVC; -. DR OrthoDB; EOG7WX07W; -. DR TreeFam; TF105687; -. DR NextBio; 322795; -. DR PRO; PR:Q921G7; -. DR ArrayExpress; Q921G7; -. DR Bgee; Q921G7; -. DR CleanEx; MM_ETFDH; -. DR Genevestigator; Q921G7; -. DR GO; GO:0031305; C:integral component of mitochondrial inner membrane; IEA:Ensembl. DR GO; GO:0017133; C:mitochondrial electron transfer flavoprotein complex; TAS:MGI. DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:MGI. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0009055; F:electron carrier activity; ISS:UniProtKB. DR GO; GO:0004174; F:electron-transferring-flavoprotein dehydrogenase activity; ISS:UniProtKB. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0043783; F:oxidoreductase activity, oxidizing metal ions with flavin as acceptor; ISS:UniProtKB. DR GO; GO:0048039; F:ubiquinone binding; IEA:Ensembl. DR GO; GO:0022900; P:electron transport chain; IEA:Ensembl. DR GO; GO:0033539; P:fatty acid beta-oxidation using acyl-CoA dehydrogenase; IEA:Ensembl. DR GO; GO:0006979; P:response to oxidative stress; IDA:UniProtKB. DR InterPro; IPR017896; 4Fe4S_Fe-S-bd. DR InterPro; IPR007859; ETFD_OxRdtase. DR InterPro; IPR000103; Pyridine_nuc-diS_OxRdtase_2. DR Pfam; PF05187; ETF_QO; 1. DR PRINTS; PR00469; PNDRDTASEII. DR PROSITE; PS51379; 4FE4S_FER_2; 1. PE 1: Evidence at protein level; KW 4Fe-4S; Acetylation; Complete proteome; Direct protein sequencing; KW Electron transport; FAD; Flavoprotein; Iron; Iron-sulfur; Membrane; KW Metal-binding; Mitochondrion; Mitochondrion inner membrane; KW Oxidoreductase; Phosphoprotein; Reference proteome; Transit peptide; KW Transport; Ubiquinone. FT TRANSIT 1 32 Mitochondrion (Potential). FT CHAIN 33 616 Electron transfer flavoprotein-ubiquinone FT oxidoreductase, mitochondrial. FT /FTId=PRO_0000008662. FT INTRAMEM 108 129 By similarity. FT INTRAMEM 427 446 By similarity. FT DOMAIN 576 605 4Fe-4S ferredoxin-type. FT NP_BIND 70 84 FAD (Potential). FT METAL 560 560 Iron-sulfur (4Fe-4S) (Potential). FT METAL 585 585 Iron-sulfur (4Fe-4S) (Potential). FT METAL 588 588 Iron-sulfur (4Fe-4S) (Potential). FT METAL 591 591 Iron-sulfur (4Fe-4S) (Potential). FT BINDING 304 304 Ubiquinone; via carbonyl oxygen (By FT similarity). FT BINDING 305 305 Ubiquinone; via amide nitrogen (By FT similarity). FT MOD_RES 95 95 N6-acetyllysine. FT MOD_RES 131 131 N6-acetyllysine. FT MOD_RES 222 222 N6-acetyllysine. FT MOD_RES 356 356 N6-acetyllysine. FT MOD_RES 415 415 N6-acetyllysine. FT MOD_RES 550 550 Phosphoserine. FT CONFLICT 342 342 W -> C (in Ref. 1; BAB22135). FT CONFLICT 355 355 G -> W (in Ref. 1; BAC35888). SQ SEQUENCE 616 AA; 68091 MW; 1E5C6F85725E3CEE CRC64; MLVRLTKLSC PAYHWFHALK IKKCLPLCAP RCSSTSAVPQ ITTHYTVHPR EKDKRWEGVN MERFAEEADV VIVGAGPAGL SAAIRLKQLA AEQGKDIRVC LVEKAAQIGA HTLSGACLDP AAFKELFPDW KEKGAPLNTP VTEDRFAILT EKHRIPVPIL PGLPMNNHGN YIVRLGHLVS WMGEQAEALG VEVYPGYAAA EVLYHEDGSV KGIATNDVGI QKDGAPKTTF ERGLELHAKV TVFAEGCHGH LAKQLYKKFD LRASCDAQTY GIGLKELWII DEKKWKPGRV DHTVGWPLDR HTYGGSFLYH LNEGEPLVAV GFVVGLDYQN PYLSPFREFQ RWKHHPSIQP TLEGGKRIAY GARALNEGGL QSIPKLTFPG GLLIGCSPGF MNVPKIKGTH TAMKSGSLAA ESIFKQLTSE NLQSKTTGLH VTEYEDNLKQ SWVWKELHAV RNIRPSCHGI LGVYGGMIYT GIFYWILRGM EPWTLKHKGS DSDQLKPAKD CTPIEYPKPD GQISFDLLSS VALSGTNHEH DQPAHLTLKD DSIPVNRNLS IYDGPEQRFC PAGVYEFVPL EQGDGFRLQI NAQNCVHCKT CDIKDPSQNI NWVVPEGGGG PAYNGM // ID FA2H_MOUSE Reviewed; 372 AA. AC Q5MPP0; Q2M2M0; Q5RL53; Q8BTH1; Q8R0M0; Q8R0V1; DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-2005, sequence version 1. DT 19-MAR-2014, entry version 86. DE RecName: Full=Fatty acid 2-hydroxylase; DE EC=1.-.-.-; DE AltName: Full=Fatty acid alpha-hydroxylase; GN Name=Fa2h; Synonyms=Faah; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS ILE-103; LEU-348 AND RP PRO-354, FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND RP TISSUE SPECIFICITY. RC STRAIN=FVB/N; RX PubMed=15658937; DOI=10.1042/BJ20041451; RA Eckhardt M., Yaghootfam A., Fewou S.N., Zoeller I., Gieselmann V.; RT "A mammalian fatty acid hydroxylase responsible for the formation of RT alpha-hydroxylated galactosylceramide in myelin."; RL Biochem. J. 388:245-254(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS RP ILE-103; LEU-348 AND PRO-354. RC STRAIN=C57BL/6J; TISSUE=Diencephalon, and Testis; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3). RC STRAIN=FVB/N; TISSUE=Colon; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP FUNCTION, DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY. RX PubMed=16998236; DOI=10.1194/jlr.M600362-JLR200; RA Alderson N.L., Maldonado E.N., Kern M.J., Bhat N.R., Hama H.; RT "FA2H-dependent fatty acid 2-hydroxylation in postnatal mouse brain."; RL J. Lipid Res. 47:2772-2780(2006). CC -!- FUNCTION: Required for alpha-hydroxylation of free fatty acids and CC the formation of alpha-hydroxylated sphingolipids. CC -!- COFACTOR: Iron (By similarity). CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass CC membrane protein. Microsome membrane; Multi-pass membrane protein. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q5MPP0-1; Sequence=Displayed; CC Name=2; CC IsoId=Q5MPP0-2; Sequence=VSP_029838; CC Name=3; CC IsoId=Q5MPP0-3; Sequence=VSP_029837; CC -!- TISSUE SPECIFICITY: Detected in brain and skin (at protein level). CC Detected in brain white matter, cerebellum forebrain, stomach, CC kidney, skin and testis. Detected in oligodendrocytes. CC -!- DEVELOPMENTAL STAGE: Levels increase rapidly in brains from CC newborns, in parallel with myelination in the central nervous CC system. Present at very low levels in newborns. Levels are highest CC at 2 to 3 weeks, and then decrease slightly to reach an constant, CC intermediate level after 4 months. Constitutively expressed at an CC intermediate level throughout adult life. CC -!- DOMAIN: The histidine box domains may contain the active site CC and/or be involved in metal ion binding. CC -!- SIMILARITY: Belongs to the sterol desaturase family. SCS7 CC subfamily. CC -!- SIMILARITY: Contains 1 cytochrome b5 heme-binding domain. CC -!- SEQUENCE CAUTION: CC Sequence=AAH46985.1; Type=Frameshift; Positions=34; CC Sequence=AAI11913.1; Type=Erroneous initiation; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AY660882; AAV70494.1; -; mRNA. DR EMBL; AK090338; BAC41174.1; -; mRNA. DR EMBL; AK161502; BAE36428.1; -; mRNA. DR EMBL; BC026400; AAH26400.1; -; mRNA. DR EMBL; BC026629; AAH26629.1; -; mRNA. DR EMBL; BC046985; AAH46985.1; ALT_FRAME; mRNA. DR EMBL; BC111912; AAI11913.1; ALT_INIT; mRNA. DR EMBL; BC128080; AAI28081.1; -; mRNA. DR EMBL; BC128081; AAI28082.1; -; mRNA. DR RefSeq; NP_835187.2; NM_178086.3. DR UniGene; Mm.41083; -. DR ProteinModelPortal; Q5MPP0; -. DR SMR; Q5MPP0; 7-114. DR PRIDE; Q5MPP0; -. DR Ensembl; ENSMUST00000038475; ENSMUSP00000043597; ENSMUSG00000033579. [Q5MPP0-1] DR GeneID; 338521; -. DR KEGG; mmu:338521; -. DR UCSC; uc009nmf.2; mouse. [Q5MPP0-1] DR CTD; 79152; -. DR MGI; MGI:2443327; Fa2h. DR eggNOG; COG3000; -. DR GeneTree; ENSGT00390000002142; -. DR HOGENOM; HOG000023981; -. DR HOVERGEN; HBG054265; -. DR OMA; MKAHHVK; -. DR OrthoDB; EOG71P2BJ; -. DR TreeFam; TF314955; -. DR NextBio; 400217; -. DR PRO; PR:Q5MPP0; -. DR Bgee; Q5MPP0; -. DR CleanEx; MM_FA2H; -. DR CleanEx; MM_FAAH; -. DR Genevestigator; Q5MPP0; -. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0080132; F:fatty acid alpha-hydroxylase activity; IDA:MGI. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0032286; P:central nervous system myelin maintenance; IMP:MGI. DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0006631; P:fatty acid metabolic process; IDA:MGI. DR GO; GO:0030258; P:lipid modification; IDA:MGI. DR GO; GO:0032287; P:peripheral nervous system myelin maintenance; IMP:MGI. DR GO; GO:0042127; P:regulation of cell proliferation; IMP:MGI. DR GO; GO:0042634; P:regulation of hair cycle; IMP:MGI. DR GO; GO:0001949; P:sebaceous gland cell differentiation; IMP:MGI. DR GO; GO:0006665; P:sphingolipid metabolic process; IEA:InterPro. DR Gene3D; 3.10.120.10; -; 1. DR InterPro; IPR001199; Cyt_B5-like_heme/steroid-bd. DR InterPro; IPR018506; Cyt_B5_heme-BS. DR InterPro; IPR006694; Fatty_acid_hydroxylase. DR InterPro; IPR014430; Ino-phos-ceramide-B_Hydrxlase. DR Pfam; PF00173; Cyt-b5; 1. DR Pfam; PF04116; FA_hydroxylase; 1. DR PIRSF; PIRSF005149; IPC-B_HD; 1. DR PRINTS; PR00363; CYTOCHROMEB5. DR SUPFAM; SSF55856; SSF55856; 1. DR PROSITE; PS00191; CYTOCHROME_B5_1; 1. DR PROSITE; PS50255; CYTOCHROME_B5_2; 1. PE 1: Evidence at protein level; KW Alternative splicing; Complete proteome; Electron transport; KW Endoplasmic reticulum; Fatty acid biosynthesis; Fatty acid metabolism; KW Heme; Iron; Lipid biosynthesis; Lipid metabolism; Membrane; KW Metal-binding; Microsome; Oxidoreductase; Polymorphism; KW Reference proteome; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 372 Fatty acid 2-hydroxylase. FT /FTId=PRO_0000312351. FT TRANSMEM 168 188 Helical; (Potential). FT TRANSMEM 213 233 Helical; (Potential). FT TRANSMEM 268 288 Helical; (Potential). FT TRANSMEM 290 310 Helical; (Potential). FT DOMAIN 8 86 Cytochrome b5 heme-binding. FT METAL 43 43 Iron (heme axial ligand) (By similarity). FT METAL 69 69 Iron (heme axial ligand) (By similarity). FT VAR_SEQ 1 208 Missing (in isoform 3). FT /FTId=VSP_029837. FT VAR_SEQ 267 325 Missing (in isoform 2). FT /FTId=VSP_029838. FT VARIANT 103 103 T -> I (in strain: C57BL/6J). FT VARIANT 348 348 F -> L (in strain: C57BL/6J). FT VARIANT 354 354 L -> P (in strain: C57BL/6J). SQ SEQUENCE 372 AA; 42981 MW; 8E3311FE6491F088 CRC64; MAPAPPPAAS FTPAEVQRRL AAGACWVRRG ASLYDLTSFV RHHPGGEQLL LARAGQDISA DLDGPPHRHS DNARRWLEQY YVGELRADPQ DPTENGAVAS AETQKTDPAL EPQFKVVDWD KDLVDWQKPL LWQVGHLGEK YDEWVHQPVA RPIRLFHSDL IEAFSKTVWY SVPIIWVPLV LYLSWSYYRT LTQDNIRLFA SLTREYSMMM PESVFIGLFV LGMLFWTFVE YVIHRFLFHM KPPSNSHYLI MLHFVMHGQH HKAPFDGSRL VFPPVPASLV IAFFYVFLRL ILPETVGGII FAGGLLGYVL YDMTHYYLHF GSPHKGSYLY NMKAHHVKHH FEYQKSGFGI STKLWDYFFH TLIPEEAHPK MQ // ID FACR1_MOUSE Reviewed; 515 AA. AC Q922J9; Q8BZS2; Q9CXE8; Q9D0Q1; Q9DAU2; DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 19-MAR-2014, entry version 94. DE RecName: Full=Fatty acyl-CoA reductase 1; DE EC=1.2.1.n2; DE AltName: Full=Male sterility domain-containing protein 2; GN Name=Far1; Synonyms=Mlstd2; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3 AND 4). RC STRAIN=C57BL/6J; TISSUE=Cecum, Embryo, Liver, Placenta, and Testis; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC STRAIN=Czech II; TISSUE=Mammary tumor; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, AND RP TISSUE SPECIFICITY. RX PubMed=15220348; DOI=10.1074/jbc.M406225200; RA Cheng J.B., Russell D.W.; RT "Mammalian wax biosynthesis: I. Identification of two fatty acyl- RT coenzyme A reductases with different substrate specificities and RT tissue distributions."; RL J. Biol. Chem. 279:37789-37797(2004). RN [4] RP FUNCTION. RX PubMed=15220349; DOI=10.1074/jbc.M406226200; RA Cheng J.B., Russell D.W.; RT "Mammalian wax biosynthesis. II. Expression cloning of wax synthase RT cDNAs encoding a member of the acyltransferase enzyme family."; RL J. Biol. Chem. 279:37798-37807(2004). CC -!- FUNCTION: Catalyzes the reduction of saturated fatty acyl-CoA with CC chain length C16 or C18 to fatty alcohols. CC -!- CATALYTIC ACTIVITY: Hexadecanal + CoA + NADP(+) = hexadecanoyl-CoA CC + NADPH. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC pH dependence: CC Optimum pH is 7.4; CC -!- SUBCELLULAR LOCATION: Peroxisome membrane; Single-pass membrane CC protein (Potential). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; CC IsoId=Q922J9-1; Sequence=Displayed; CC Name=2; CC IsoId=Q922J9-2; Sequence=VSP_021678, VSP_021679; CC Name=3; CC IsoId=Q922J9-3; Sequence=VSP_021680; CC Note=No experimental confirmation available; CC Name=4; CC IsoId=Q922J9-4; Sequence=VSP_021681; CC Note=No experimental confirmation available; CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed in all tissues CC examined. Highest expression seen in preputial gland. Expressed in CC the brain where large quantities of ether lipids are synthesized. CC -!- SIMILARITY: Belongs to the fatty acyl-CoA reductase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK005531; BAB24102.1; -; mRNA. DR EMBL; AK011187; BAB27453.1; -; mRNA. DR EMBL; AK014486; BAB29388.1; -; mRNA. DR EMBL; AK033674; BAC28423.1; -; mRNA. DR EMBL; AK030067; BAC26766.1; -; mRNA. DR EMBL; BC007178; AAH07178.1; -; mRNA. DR RefSeq; NP_001272760.1; NM_001285831.1. DR RefSeq; NP_081655.2; NM_027379.3. DR RefSeq; XP_006508190.1; XM_006508127.1. DR RefSeq; XP_006508191.1; XM_006508128.1. DR RefSeq; XP_006508192.1; XM_006508129.1. DR RefSeq; XP_006508193.1; XM_006508130.1. DR RefSeq; XP_006508194.1; XM_006508131.1. DR UniGene; Mm.206919; -. DR UniGene; Mm.477631; -. DR ProteinModelPortal; Q922J9; -. DR SMR; Q922J9; 9-154. DR BioGrid; 212175; 2. DR MINT; MINT-1853515; -. DR PhosphoSite; Q922J9; -. DR PaxDb; Q922J9; -. DR PRIDE; Q922J9; -. DR Ensembl; ENSMUST00000033018; ENSMUSP00000033018; ENSMUSG00000030759. [Q922J9-1] DR Ensembl; ENSMUST00000067929; ENSMUSP00000064334; ENSMUSG00000030759. [Q922J9-3] DR Ensembl; ENSMUST00000164745; ENSMUSP00000128695; ENSMUSG00000030759. [Q922J9-1] DR GeneID; 67420; -. DR KEGG; mmu:67420; -. DR UCSC; uc009jhn.1; mouse. [Q922J9-2] DR UCSC; uc009jho.1; mouse. [Q922J9-1] DR UCSC; uc009jhq.1; mouse. [Q922J9-3] DR CTD; 84188; -. DR MGI; MGI:1914670; Far1. DR eggNOG; COG3320; -. DR GeneTree; ENSGT00390000006367; -. DR HOGENOM; HOG000261667; -. DR HOVERGEN; HBG076152; -. DR InParanoid; Q922J9; -. DR KO; K13356; -. DR OMA; GRTIEIN; -. DR OrthoDB; EOG7FFMRM; -. DR TreeFam; TF313011; -. DR BRENDA; 1.2.1.50; 3474. DR NextBio; 324518; -. DR PRO; PR:Q922J9; -. DR ArrayExpress; Q922J9; -. DR Bgee; Q922J9; -. DR Genevestigator; Q922J9; -. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005778; C:peroxisomal membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005777; C:peroxisome; IDA:MGI. DR GO; GO:0080019; F:fatty-acyl-CoA reductase (alcohol-forming) activity; IEA:InterPro. DR GO; GO:0050062; F:long-chain-fatty-acyl-CoA reductase activity; IDA:MGI. DR GO; GO:0008611; P:ether lipid biosynthetic process; IEA:Ensembl. DR GO; GO:0046474; P:glycerophospholipid biosynthetic process; IEA:Ensembl. DR GO; GO:0035336; P:long-chain fatty-acyl-CoA metabolic process; IEA:Ensembl. DR GO; GO:0010025; P:wax biosynthetic process; IDA:UniProtKB. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR026055; FAR. DR InterPro; IPR013120; Male_sterile_NAD-bd. DR InterPro; IPR016040; NAD(P)-bd_dom. DR PANTHER; PTHR11011; PTHR11011; 1. DR Pfam; PF07993; NAD_binding_4; 1. DR Pfam; PF03015; Sterile; 1. PE 1: Evidence at protein level; KW Alternative splicing; Complete proteome; Lipid biosynthesis; KW Lipid metabolism; Membrane; NADP; Oxidoreductase; Peroxisome; KW Reference proteome; Transmembrane; Transmembrane helix. FT CHAIN 1 515 Fatty acyl-CoA reductase 1. FT /FTId=PRO_0000261395. FT TRANSMEM 466 483 Helical; (Potential). FT VAR_SEQ 242 260 GWIDNFNGPSGLFIAAGKG -> VSSSKLLSSWDSEFQVRT FT V (in isoform 2). FT /FTId=VSP_021678. FT VAR_SEQ 261 515 Missing (in isoform 2). FT /FTId=VSP_021679. FT VAR_SEQ 319 376 EYHVISTFKRNPLEQAFRRPNVNLTSNHLLYHYWIAVSHKA FT PAFLYDIYLRMTGRSPR -> GDYLNHSFKMNPLNQVFRHP FT YVKFCSNNLMLHYWKGVKHTVPALLLDLALRLTGQKPW FT (in isoform 3). FT /FTId=VSP_021680. FT VAR_SEQ 515 515 Y -> RRPRI (in isoform 4). FT /FTId=VSP_021681. FT CONFLICT 35 35 P -> R (in Ref. 1; BAB24102). FT CONFLICT 364 364 Y -> H (in Ref. 1; BAB24102). SQ SEQUENCE 515 AA; 59435 MW; 6A9E9EF9A2F835A4 CRC64; MVSIPEYYEG KNILLTGATG FLGKVLLEKL LRSCPRVNSV YVLVRQKAGQ TPQERVEEIL SSKLFDRLRD ENPDFREKII AINSELTQPK LALSEEDKEI IIDSTNVIFH CAATVRFNEN LRDAVQLNVI ATRQLILLAQ QMKNLEVFMH VSTAYAYCNR KHIDEVVYPP PVDPKKLIDS LEWMDDGLVN DITPKLIGDR PNTYIYTKAL AEYVVQQEGA KLNVAIVRPS IVGASWKEPF PGWIDNFNGP SGLFIAAGKG ILRTMRASNN ALADLVPVDV VVNTSLAAAW YSGVNRPRNI MVYNCTTGST NPFHWGEVEY HVISTFKRNP LEQAFRRPNV NLTSNHLLYH YWIAVSHKAP AFLYDIYLRM TGRSPRMMKT ITRLHKAMVF LEYFTSNSWV WNTDNVNMLM NQLNPEDKKT FNIDVRQLHW AEYIENYCMG TKKYVLNEEM SGLPAARKHL NKLRNIRYGF NTILVILIWR IFIARSQMAR NIWYFVVSLC YKFLSYFRAS STMRY // ID FACR2_MOUSE Reviewed; 515 AA. AC Q7TNT2; B2KFC6; Q3TTT7; Q8BH72; Q8CAK7; DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2003, sequence version 1. DT 19-MAR-2014, entry version 80. DE RecName: Full=Fatty acyl-CoA reductase 2; DE EC=1.2.1.n2; DE AltName: Full=Male sterility domain-containing protein 1; GN Name=Far2; Synonyms=Mlstd1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC STRAIN=C57BL/6J; RC TISSUE=Brain cortex, Cerebellum, Head, and Hypothalamus; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC STRAIN=C57BL/6; TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RX PubMed=15220348; DOI=10.1074/jbc.M406225200; RA Cheng J.B., Russell D.W.; RT "Mammalian wax biosynthesis: I. Identification of two fatty acyl- RT coenzyme A reductases with different substrate specificities and RT tissue distributions."; RL J. Biol. Chem. 279:37789-37797(2004). CC -!- FUNCTION: Catalyzes the reduction of fatty acyl-CoA to fatty CC alcohols. The preferred substrates are C16, C18, C18:1 and C18:2 CC but low activity can be observed with C10-C14 substrates. CC -!- CATALYTIC ACTIVITY: Hexadecanal + CoA + NADP(+) = hexadecanoyl-CoA CC + NADPH. CC -!- SUBCELLULAR LOCATION: Peroxisome membrane; Multi-pass membrane CC protein (Potential). Endoplasmic reticulum membrane; Multi-pass CC membrane protein (Potential). Note=Peroxisome in cells expressing CC low levels of the protein. Peroxisome and endoplasmic reticulum in CC cells expressing high levels of the protein (Potential). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q7TNT2-1; Sequence=Displayed; CC Name=2; CC IsoId=Q7TNT2-2; Sequence=VSP_021682; CC Note=No experimental confirmation available; CC -!- TISSUE SPECIFICITY: Highly expressed in the meibomian glands of CC the eyelid and the sebaceous glands of the skin. Expressed in the CC brain where large quantities of ether lipids are synthesized. CC -!- SIMILARITY: Belongs to the fatty acyl-CoA reductase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK038584; BAC30056.1; -; mRNA. DR EMBL; AK043388; BAC31532.1; -; mRNA. DR EMBL; AK043589; BAC31590.1; -; mRNA. DR EMBL; AK161201; BAE36237.1; -; mRNA. DR EMBL; CU207318; CAQ51877.1; -; Genomic_DNA. DR EMBL; BC055759; AAH55759.1; -; mRNA. DR RefSeq; NP_848912.1; NM_178797.3. DR RefSeq; XP_006507132.1; XM_006507069.1. DR RefSeq; XP_006507133.1; XM_006507070.1. DR RefSeq; XP_006536153.1; XM_006536090.1. DR RefSeq; XP_006536154.1; XM_006536091.1. DR UniGene; Mm.475174; -. DR ProteinModelPortal; Q7TNT2; -. DR PhosphoSite; Q7TNT2; -. DR PRIDE; Q7TNT2; -. DR Ensembl; ENSMUST00000032443; ENSMUSP00000032443; ENSMUSG00000030303. [Q7TNT2-1] DR Ensembl; ENSMUST00000111607; ENSMUSP00000107234; ENSMUSG00000030303. [Q7TNT2-2] DR GeneID; 330450; -. DR KEGG; mmu:330450; -. DR UCSC; uc009etb.1; mouse. [Q7TNT2-1] DR UCSC; uc009etc.1; mouse. [Q7TNT2-2] DR CTD; 55711; -. DR MGI; MGI:2687035; Far2. DR eggNOG; NOG325153; -. DR GeneTree; ENSGT00390000006367; -. DR HOGENOM; HOG000261667; -. DR HOVERGEN; HBG076152; -. DR InParanoid; Q7TNT2; -. DR KO; K13356; -. DR OMA; LRNIHYL; -. DR OrthoDB; EOG7FFMRM; -. DR TreeFam; TF313011; -. DR BRENDA; 1.2.1.50; 3474. DR NextBio; 399377; -. DR PRO; PR:Q7TNT2; -. DR Bgee; Q7TNT2; -. DR Genevestigator; Q7TNT2; -. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005778; C:peroxisomal membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005777; C:peroxisome; IDA:MGI. DR GO; GO:0080019; F:fatty-acyl-CoA reductase (alcohol-forming) activity; IEA:InterPro. DR GO; GO:0050062; F:long-chain-fatty-acyl-CoA reductase activity; IDA:MGI. DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW. DR GO; GO:0035336; P:long-chain fatty-acyl-CoA metabolic process; IEA:Ensembl. DR GO; GO:0010025; P:wax biosynthetic process; TAS:MGI. DR Gene3D; 3.40.50.720; -; 2. DR InterPro; IPR026055; FAR. DR InterPro; IPR013120; Male_sterile_NAD-bd. DR InterPro; IPR016040; NAD(P)-bd_dom. DR PANTHER; PTHR11011; PTHR11011; 1. DR Pfam; PF07993; NAD_binding_4; 1. DR Pfam; PF03015; Sterile; 1. PE 2: Evidence at transcript level; KW Alternative splicing; Complete proteome; Endoplasmic reticulum; KW Lipid biosynthesis; Lipid metabolism; Membrane; NADP; Oxidoreductase; KW Peroxisome; Reference proteome; Transmembrane; Transmembrane helix. FT CHAIN 1 515 Fatty acyl-CoA reductase 2. FT /FTId=PRO_0000261402. FT TRANSMEM 465 484 Helical; (Potential). FT TRANSMEM 491 510 Helical; (Potential). FT VAR_SEQ 497 515 VSFCYKFISYFRASSTLKV -> CPLFKL (in isoform FT 2). FT /FTId=VSP_021682. FT CONFLICT 84 84 A -> T (in Ref. 1; BAC30056). FT CONFLICT 194 194 P -> H (in Ref. 1; BAE36237). FT CONFLICT 321 321 Q -> E (in Ref. 1; BAE36237). SQ SEQUENCE 515 AA; 59167 MW; 86CBE93ECC4116C2 CRC64; MSMIAAFYSN KSILITGATG FLGKVLMEKL FRTSPHLKVI YILVRPKSGQ TLQERVFQIL NSKLFEKVKE VCPNVHEKIR PISADLNQRD FAISKEDVQE LLSCTNIIFH CAATVRFDAH LREAVQLNVT ATQQLLLMAS QMPKLEAFIH ISTAFSNCNL SHIDEVIYPC PVEPRKIIDS MEWLDDSIIE EITPKLIGDR PNTYTYTKAL GEIVVQQESG NLNVAIVRPS IVGATWQEPF PGWVDNLNGP SGLIIATGKG FLRSIKATPM AVADVIPVDT VVNLTIAVGW YTAVHRPKST LIYHSTSGNL NPCNWYKMGL QVLATIEKIP FESAFRRPNA DFTTSNFTTH YWNTVSHRVP AIIYDFYLRL TGRKPRMLKL MNRLLKTISM LEYFINHSWE WSTNNTEMLL SELSPEDQRV FNFDVRQLNW LEYIENYVLG VKKYLLKEDL AGIPKAKQHL RRLRNIHYLF NTALFLIIWR LLIARSQMAR NVWFFIVSFC YKFISYFRAS STLKV // ID FADS6_MOUSE Reviewed; 342 AA. AC Q80UG1; Q80YA0; Q810B5; DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2003, sequence version 1. DT 19-MAR-2014, entry version 79. DE RecName: Full=Fatty acid desaturase 6; DE EC=1.14.19.-; GN Name=Fads6; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1). RX PubMed=12588793; DOI=10.1093/hmg/ddg042; RA Kikkawa Y., Shitara H., Wakana S., Kohara Y., Takada T., Okamoto M., RA Taya C., Kamiya K., Yoshikawa Y., Tokano H., Kitamura K., Shimizu K., RA Wakabayashi Y., Shiroishi T., Kominami R., Yonekawa H.; RT "Mutations in a new scaffold protein Sans cause deafness in Jackson RT shaker mice."; RL Hum. Mol. Genet. 12:453-461(2003). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE RP SEQUENCE [LARGE SCALE MRNA] OF 25-342 (ISOFORM 2). RC TISSUE=Brain, and Eye; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- PATHWAY: Lipid metabolism; fatty acid metabolism. CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein CC (Potential). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q80UG1-1; Sequence=Displayed; CC Name=2; CC IsoId=Q80UG1-2; Sequence=VSP_034321; CC Note=No experimental confirmation available; CC -!- SIMILARITY: Belongs to the fatty acid desaturase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AB087501; BAC57425.1; -; Genomic_DNA. DR EMBL; AB087503; BAC67683.1; -; mRNA. DR EMBL; AL603828; CAM13802.1; -; Genomic_DNA. DR EMBL; BC044804; AAH44804.1; -; mRNA. DR EMBL; BC132041; AAI32042.1; -; mRNA. DR EMBL; BC132067; AAI32068.1; -; mRNA. DR RefSeq; NP_828874.3; NM_178035.4. DR UniGene; Mm.21995; -. DR PhosphoSite; Q80UG1; -. DR PaxDb; Q80UG1; -. DR PRIDE; Q80UG1; -. DR Ensembl; ENSMUST00000056153; ENSMUSP00000058783; ENSMUSG00000044788. [Q80UG1-1] DR GeneID; 328035; -. DR KEGG; mmu:328035; -. DR UCSC; uc007mgz.2; mouse. [Q80UG1-1] DR CTD; 283985; -. DR MGI; MGI:3039592; Fads6. DR eggNOG; NOG74273; -. DR GeneTree; ENSGT00390000009739; -. DR HOGENOM; HOG000008225; -. DR HOVERGEN; HBG096401; -. DR InParanoid; Q80UG1; -. DR KO; K12419; -. DR OMA; HGVDCAI; -. DR OrthoDB; EOG747PJC; -. DR TreeFam; TF333083; -. DR UniPathway; UPA00199; -. DR NextBio; 398082; -. DR PRO; PR:Q80UG1; -. DR Bgee; Q80UG1; -. DR Genevestigator; Q80UG1; -. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW. DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW. DR InterPro; IPR005804; Fatty_acid_desaturase-1. DR Pfam; PF00487; FA_desaturase; 1. PE 2: Evidence at transcript level; KW Alternative splicing; Complete proteome; Fatty acid biosynthesis; KW Fatty acid metabolism; Lipid biosynthesis; Lipid metabolism; Membrane; KW Oxidoreductase; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 342 Fatty acid desaturase 6. FT /FTId=PRO_0000341547. FT TRANSMEM 39 59 Helical; (Potential). FT TRANSMEM 63 83 Helical; (Potential). FT TRANSMEM 100 120 Helical; (Potential). FT TRANSMEM 151 171 Helical; (Potential). FT TRANSMEM 185 205 Helical; (Potential). FT MOTIF 87 91 Histidine box-1. FT MOTIF 124 128 Histidine box-2. FT MOTIF 277 281 Histidine box-3. FT VAR_SEQ 262 342 QLVLDWAFGHSLISCHVEHHLFPWLSDHMCLKVKPLVSKFL FT HEKQLPYNEDSYLARFQLFLSRYEEFMVHVPPITELVGVQ FT -> GAPPLPLAL (in isoform 2). FT /FTId=VSP_034321. FT CONFLICT 29 29 V -> A (in Ref. 1; BAC67683). SQ SEQUENCE 342 AA; 38831 MW; 3C25389B97DC8513 CRC64; METVRSAPPG DGAAEALLKE LERQVQDVVR ASSWWERHGV DCAILALSLL ALPAGFLCLR AHNILAFATG ITILGVCHYT LTVKGSHLAT HSALTESKRW SKILMIFFLE VCTAFSAEFA KFNHVNLHHV YTNVVGLGDS STWKVPLLNR YVYMFLGPLL VPIITPLVAL EHLRKEEPRT ALRTLGFICL GLYSQYWLFM NVSGFKNPSS ALACMLLTRS LLAHPYLHVN IFQHIGLPMF SPDKKPRRIH MMTLGVLNLP RQLVLDWAFG HSLISCHVEH HLFPWLSDHM CLKVKPLVSK FLHEKQLPYN EDSYLARFQL FLSRYEEFMV HVPPITELVG VQ // ID FADS3_MOUSE Reviewed; 449 AA. AC Q9JJE7; Q7TND7; Q8C4Y5; Q8CDZ4; DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot. DT 02-OCT-2007, sequence version 2. DT 19-FEB-2014, entry version 79. DE RecName: Full=Fatty acid desaturase 3; DE EC=1.14.19.-; GN Name=Fads3; ORFNames=MNCb-0629; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6; TISSUE=Brain; RA Osada N., Kusuda J., Tanuma R., Ito A., Hirata M., Sugano S., RA Hashimoto K.; RT "Isolation of full-length cDNA clones from mouse brain cDNA library RT made by oligo-capping method."; RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Cerebellum, and Head; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 46-449. RC STRAIN=FVB/N; TISSUE=Colon; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass CC membrane protein (By similarity). CC -!- DOMAIN: The histidine box domains may contain the active site CC and/or be involved in metal ion binding. CC -!- SIMILARITY: Belongs to the fatty acid desaturase family. CC -!- SIMILARITY: Contains 1 cytochrome b5 heme-binding domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AB041560; BAA95044.1; -; mRNA. DR EMBL; AK080414; BAC37908.1; -; mRNA. DR EMBL; AK029318; BAC26393.1; -; mRNA. DR EMBL; BC055950; AAH55950.1; -; mRNA. DR RefSeq; NP_068690.3; NM_021890.3. DR UniGene; Mm.253875; -. DR ProteinModelPortal; Q9JJE7; -. DR SMR; Q9JJE7; 27-104. DR IntAct; Q9JJE7; 1. DR MINT; MINT-4114355; -. DR PhosphoSite; Q9JJE7; -. DR PaxDb; Q9JJE7; -. DR PRIDE; Q9JJE7; -. DR Ensembl; ENSMUST00000115995; ENSMUSP00000111659; ENSMUSG00000024664. DR GeneID; 60527; -. DR KEGG; mmu:60527; -. DR UCSC; uc008goz.1; mouse. DR CTD; 3995; -. DR MGI; MGI:1928740; Fads3. DR eggNOG; NOG70688; -. DR GeneTree; ENSGT00510000046574; -. DR HOVERGEN; HBG002839; -. DR InParanoid; Q9JJE7; -. DR KO; K10225; -. DR OMA; DGAQNAQ; -. DR OrthoDB; EOG7G1V6P; -. DR TreeFam; TF313604; -. DR NextBio; 314953; -. DR PRO; PR:Q9JJE7; -. DR ArrayExpress; Q9JJE7; -. DR Bgee; Q9JJE7; -. DR CleanEx; MM_FADS3; -. DR Genevestigator; Q9JJE7; -. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0016717; F:oxidoreductase activity, acting on paired donors, with oxidation of a pair of donors resulting in the reduction of molecular oxygen to two molecules of water; IEA:InterPro. DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW. DR Gene3D; 3.10.120.10; -; 1. DR InterPro; IPR001199; Cyt_B5-like_heme/steroid-bd. DR InterPro; IPR012171; Fatty_acid/sphinglp_desaturase. DR InterPro; IPR005804; Fatty_acid_desaturase-1. DR Pfam; PF00173; Cyt-b5; 1. DR Pfam; PF00487; FA_desaturase; 1. DR PIRSF; PIRSF015921; FA_sphinglp_des; 1. DR SUPFAM; SSF55856; SSF55856; 1. DR PROSITE; PS50255; CYTOCHROME_B5_2; 1. PE 2: Evidence at transcript level; KW Complete proteome; Electron transport; Endoplasmic reticulum; KW Fatty acid biosynthesis; Fatty acid metabolism; Lipid biosynthesis; KW Lipid metabolism; Membrane; Oxidoreductase; Reference proteome; KW Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 449 Fatty acid desaturase 3. FT /FTId=PRO_0000307109. FT TOPO_DOM 1 134 Cytoplasmic (Potential). FT TRANSMEM 135 155 Helical; (Potential). FT TOPO_DOM 156 163 Lumenal (Potential). FT TRANSMEM 164 184 Helical; (Potential). FT TOPO_DOM 185 268 Cytoplasmic (Potential). FT TRANSMEM 269 289 Helical; (Potential). FT TOPO_DOM 290 310 Lumenal (Potential). FT TRANSMEM 311 331 Helical; (Potential). FT TOPO_DOM 332 449 Cytoplasmic (Potential). FT DOMAIN 24 101 Cytochrome b5 heme-binding. FT MOTIF 186 190 Histidine box-1. FT MOTIF 223 227 Histidine box-2. FT MOTIF 387 391 Histidine box-3. FT CONFLICT 136 136 T -> S (in Ref. 2; BAC37908). FT CONFLICT 205 205 Q -> R (in Ref. 1; BAA95044). FT CONFLICT 367 367 A -> P (in Ref. 2; BAC26393). SQ SEQUENCE 449 AA; 51469 MW; 0E0B74EC8C9E5199 CRC64; MGGVGEPGGG PGPREGPAPL GAPLPIFRWE QIRQHDLPGD KWLVIERRVY DISRWAQRHP GGSRLIGHHG AEDATDAFHA FHQDLHFVRK FLKPLLIGEL APEEPSQDGA QNAQLIEDFR ALRQAAEDMK LFEADTTFFA LLLGHILAME LLAWLIIYLL GPGWVSSILA ALILAISQAQ CWCLQHDLGH ASIFTKSRWN HVAQQFVMGQ LKGFSAHWWN FRHFQHHAKP NIFHKDPDVT VAPVFLLGES SVEYGKKKRR YLPYNHQHLY FFLIGPPLLT LVNFEVENLA YMLVCMQWTD LLWAASFYSR FFLSYSPFYG ATGTLLLFVA VRVLESHWFV WITQMNHIPK EIGHEKHRDW ASSQLAATCN VEPSLFIDWF SGHLNFQIEH HLFPTMPRHN YRRVAPLVKA FCAKHGLHYE VKPFLTALVD IIGSLKKSGD IWLDAYLHQ // ID FADS1_MOUSE Reviewed; 447 AA. AC Q920L1; Q3U494; Q8BZX7; Q8R0G8; Q8VC07; DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 19-MAR-2014, entry version 101. DE RecName: Full=Fatty acid desaturase 1; DE EC=1.14.19.-; DE AltName: Full=Delta(5) fatty acid desaturase; DE Short=D5D; DE Short=Delta(5) desaturase; DE Short=Delta-5 desaturase; GN Name=Fads1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INDUCTION. RC STRAIN=C57BL/6J; TISSUE=Liver; RX PubMed=11792729; RA Matsuzaka T., Shimano H., Yahagi N., Amemiya-Kudo M., Yoshikawa T., RA Hasty A.H., Tamura Y., Osuga J., Okazaki H., Iizuka Y., Takahashi A., RA Sone H., Gotoda T., Ishibashi S., Yamada N.; RT "Dual regulation of mouse Delta(5)- and Delta(6)-desaturase gene RT expression by SREBP-1 and PPARalpha."; RL J. Lipid Res. 43:107-114(2002). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J, and NOD; TISSUE=Spinal ganglion, and Testis; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6, and FVB/N; TISSUE=Brain, Kidney, and Liver; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: Component of a lipid metabolic pathway that catalyzes CC biosynthesis of highly unsaturated fatty acids (HUFA) from CC precursor essential polyunsaturated fatty acids (PUFA) linoleic CC acid (LA) (18:2n-6) and alpha-linolenic acid (ALA) (18:3n-3). CC Catalyzes the desaturation of dihomo-gamma-linoleic acid (DHGLA) CC (20:3n-6) and eicosatetraenoic acid (20:4n-3) to generate CC arachidonic acid (AA) (20:4n-6) and eicosapentaenoic acid CC (EPA)(20:5n-3) respectively (By similarity). CC -!- PATHWAY: Lipid metabolism; polyunsaturated fatty acid CC biosynthesis. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass CC membrane protein (By similarity). Mitochondrion (By similarity). CC -!- TISSUE SPECIFICITY: Highly expressed in the adrenal gland, liver, CC brain, and testis, tissues where lipogenesis and steroidogenesis CC are active. CC -!- INDUCTION: Expression in liver is down-regulated by dietary PUFA. CC -!- DOMAIN: The histidine box domains may contain the active site CC and/or be involved in metal ion binding. CC -!- SIMILARITY: Belongs to the fatty acid desaturase family. CC -!- SIMILARITY: Contains 1 cytochrome b5 heme-binding domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AB072976; BAB69894.1; -; mRNA. DR EMBL; AK033308; BAC28228.1; -; mRNA. DR EMBL; AK083959; BAC39079.1; -; mRNA. DR EMBL; AK154367; BAE32539.1; -; mRNA. DR EMBL; BC022139; AAH22139.1; -; mRNA. DR EMBL; BC026831; AAH26831.1; -; mRNA. DR EMBL; BC026848; AAH26848.1; -; mRNA. DR EMBL; BC063053; AAH63053.1; -; mRNA. DR RefSeq; NP_666206.1; NM_146094.2. DR UniGene; Mm.30158; -. DR ProteinModelPortal; Q920L1; -. DR SMR; Q920L1; 21-74. DR IntAct; Q920L1; 2. DR MINT; MINT-1867264; -. DR BindingDB; Q920L1; -. DR ChEMBL; CHEMBL5725; -. DR PhosphoSite; Q920L1; -. DR PaxDb; Q920L1; -. DR PRIDE; Q920L1; -. DR Ensembl; ENSMUST00000010807; ENSMUSP00000010807; ENSMUSG00000010663. DR GeneID; 76267; -. DR KEGG; mmu:76267; -. DR UCSC; uc008gpd.2; mouse. DR CTD; 3992; -. DR MGI; MGI:1923517; Fads1. DR eggNOG; COG5274; -. DR GeneTree; ENSGT00510000046574; -. DR HOGENOM; HOG000012997; -. DR HOVERGEN; HBG002839; -. DR InParanoid; Q920L1; -. DR KO; K10224; -. DR OMA; DLAWMIT; -. DR OrthoDB; EOG7G1V6P; -. DR TreeFam; TF313604; -. DR UniPathway; UPA00658; -. DR ChiTaRS; FADS1; mouse. DR NextBio; 344887; -. DR PRO; PR:Q920L1; -. DR Bgee; Q920L1; -. DR CleanEx; MM_FADS1; -. DR Genevestigator; Q920L1; -. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell. DR GO; GO:0005634; C:nucleus; IEA:Ensembl. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0016717; F:oxidoreductase activity, acting on paired donors, with oxidation of a pair of donors resulting in the reduction of molecular oxygen to two molecules of water; IEA:Ensembl. DR GO; GO:0007568; P:aging; IEA:Ensembl. DR GO; GO:0019369; P:arachidonic acid metabolic process; IEA:Ensembl. DR GO; GO:0009267; P:cellular response to starvation; IEA:Ensembl. DR GO; GO:0032868; P:response to insulin; IEA:Ensembl. DR GO; GO:0014070; P:response to organic cyclic compound; IEA:Ensembl. DR GO; GO:0009744; P:response to sucrose; IEA:Ensembl. DR GO; GO:0033189; P:response to vitamin A; IEA:Ensembl. DR GO; GO:0006636; P:unsaturated fatty acid biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.10.120.10; -; 1. DR InterPro; IPR001199; Cyt_B5-like_heme/steroid-bd. DR InterPro; IPR012171; Fatty_acid/sphinglp_desaturase. DR InterPro; IPR005804; Fatty_acid_desaturase-1. DR Pfam; PF00173; Cyt-b5; 1. DR Pfam; PF00487; FA_desaturase; 1. DR PIRSF; PIRSF015921; FA_sphinglp_des; 1. DR PRINTS; PR00363; CYTOCHROMEB5. DR SUPFAM; SSF55856; SSF55856; 1. DR PROSITE; PS50255; CYTOCHROME_B5_2; 1. PE 2: Evidence at transcript level; KW Acetylation; Complete proteome; Electron transport; KW Endoplasmic reticulum; Fatty acid biosynthesis; Fatty acid metabolism; KW Lipid biosynthesis; Lipid metabolism; Membrane; Mitochondrion; KW Oxidoreductase; Reference proteome; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1 447 Fatty acid desaturase 1. FT /FTId=PRO_0000307097. FT TOPO_DOM 1 124 Cytoplasmic (Potential). FT TRANSMEM 125 145 Helical; (Potential). FT TOPO_DOM 146 160 Lumenal (Potential). FT TRANSMEM 161 180 Helical; (Potential). FT TOPO_DOM 181 268 Cytoplasmic (Potential). FT TRANSMEM 269 289 Helical; (Potential). FT TOPO_DOM 290 308 Lumenal (Potential). FT TRANSMEM 309 329 Helical; (Potential). FT TOPO_DOM 330 447 Cytoplasmic (Potential). FT DOMAIN 19 97 Cytochrome b5 heme-binding. FT MOTIF 182 186 Histidine box-1. FT MOTIF 219 223 Histidine box-2. FT MOTIF 385 389 Histidine box-3. FT MOD_RES 1 1 N-acetylmethionine (By similarity). FT CONFLICT 32 32 G -> W (in Ref. 2; BAE32539). FT CONFLICT 297 297 V -> L (in Ref. 3; AAH26848). FT CONFLICT 369 369 V -> I (in Ref. 3; AAH26848/AAH22139/ FT AAH26831). SQ SEQUENCE 447 AA; 52323 MW; 1C69B61DF919A009 CRC64; MAPDPVPTPG PASAQLRQTR YFTWEEVAQR SGREKERWLV IDRKVYNISD FSRRHPGGSR VISHYAGQDA TDPFVAFHIN KGLVRKYMNS LLIGELAPEQ PSFEPTKNKA LTDEFRELRA TVERMGLMKA NHLFFLVYLL HILLLDVAAW LTLWIFGTSL VPFILCAVLL STVQAQAGWL QHDFGHLSVF GTSTWNHLLH HFVIGHLKGA PASWWNHMHF QHHAKPNCFR KDPDINMHPL FFALGKVLPV ELGREKKKHM PYNHQHKYFF LIGPPALLPL YFQWYIFYFV VQRKKWVDLA WMLSFYARIF FTYMPLLGLK GFLGLFFIVR FLESNWFVWV TQMNHIPMHI DHDRNVDWVS TQLQATCNVH QSAFNNWFSG HLNFQIEHHL FPTMPRHNYH KVAPLVQSLC AKYGIKYESK PLLTAFADIV YSLKESGQLW LDAYLHQ // ID FADS2_MOUSE Reviewed; 444 AA. AC Q9Z0R9; DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1999, sequence version 1. DT 19-FEB-2014, entry version 104. DE RecName: Full=Fatty acid desaturase 2; DE EC=1.14.19.-; DE AltName: Full=Delta(6) fatty acid desaturase; DE Short=D6D; DE Short=Delta(6) desaturase; DE Short=Delta-6 desaturase; GN Name=Fads2; Synonyms=Fadsd2; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INDUCTION. RX PubMed=9867867; DOI=10.1074/jbc.274.1.471; RA Cho H.P., Nakamura M.T., Clarke S.D.; RT "Cloning, expression, and nutritional regulation of the mammalian RT Delta-6 desaturase."; RL J. Biol. Chem. 274:471-477(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Embryo; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Liver; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP TISSUE SPECIFICITY, AND INDUCTION. RC STRAIN=C57BL/6J; TISSUE=Liver; RX PubMed=11792729; RA Matsuzaka T., Shimano H., Yahagi N., Amemiya-Kudo M., Yoshikawa T., RA Hasty A.H., Tamura Y., Osuga J., Okazaki H., Iizuka Y., Takahashi A., RA Sone H., Gotoda T., Ishibashi S., Yamada N.; RT "Dual regulation of mouse Delta(5)- and Delta(6)-desaturase gene RT expression by SREBP-1 and PPARalpha."; RL J. Lipid Res. 43:107-114(2002). CC -!- FUNCTION: Component of a lipid metabolic pathway that catalyzes CC biosynthesis of highly unsaturated fatty acids (HUFA) from CC precursor essential polyunsaturated fatty acids (PUFA) linoleic CC acid (LA) (18:2n-6) and alpha-linolenic acid (ALA) (18:3n-3). CC Catalyzes the first and rate limiting step in this pathway which CC is the desaturation of LA (18:2n-6) and ALA (18:3n-3) into gamma- CC linoleic acid (GLA) (18:3n-6) and stearidonic acid (18:4n-3) CC respectively and other desaturation steps. Highly unsaturated CC fatty acids (HUFA) play pivotal roles in many biological functions CC (By similarity). CC -!- PATHWAY: Lipid metabolism; polyunsaturated fatty acid CC biosynthesis. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass CC membrane protein (Potential). CC -!- TISSUE SPECIFICITY: Highly expressed in the adrenal gland, liver, CC brain, and testis, tissues where lipogenesis and steroidogenesis CC are active. Also detected in lung, heart, and skeletal muscle. CC -!- DEVELOPMENTAL STAGE: Found in 13-day-old embryo heart. CC -!- INDUCTION: Induced by dietary PUFA-deficient diet. Induced by a CC fat-free diet and by a diet containing triolein (18:1n-9) as the CC only fat source. Down-regulated in liver by dietary PUFA. CC -!- DOMAIN: The histidine box domains may contain the active site CC and/or be involved in metal ion binding. CC -!- SIMILARITY: Belongs to the fatty acid desaturase family. CC -!- SIMILARITY: Contains 1 cytochrome b5 heme-binding domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF126798; AAD20017.1; -; mRNA. DR EMBL; AK143524; BAE25416.1; -; mRNA. DR EMBL; BC057189; AAH57189.1; -; mRNA. DR RefSeq; NP_062673.1; NM_019699.1. DR UniGene; Mm.38901; -. DR ProteinModelPortal; Q9Z0R9; -. DR SMR; Q9Z0R9; 21-98. DR IntAct; Q9Z0R9; 1. DR MINT; MINT-4131280; -. DR STRING; 10090.ENSMUSP00000025567; -. DR BindingDB; Q9Z0R9; -. DR ChEMBL; CHEMBL5087; -. DR PhosphoSite; Q9Z0R9; -. DR PaxDb; Q9Z0R9; -. DR PRIDE; Q9Z0R9; -. DR Ensembl; ENSMUST00000025567; ENSMUSP00000025567; ENSMUSG00000024665. DR GeneID; 56473; -. DR KEGG; mmu:56473; -. DR UCSC; uc008gpb.1; mouse. DR CTD; 9415; -. DR MGI; MGI:1930079; Fads2. DR eggNOG; NOG70688; -. DR GeneTree; ENSGT00510000046574; -. DR HOGENOM; HOG000012997; -. DR HOVERGEN; HBG002839; -. DR InParanoid; Q9Z0R9; -. DR KO; K10226; -. DR OMA; QPLEYGK; -. DR OrthoDB; EOG7G1V6P; -. DR TreeFam; TF313604; -. DR UniPathway; UPA00658; -. DR ChiTaRS; FADS2; mouse. DR NextBio; 312742; -. DR PRO; PR:Q9Z0R9; -. DR ArrayExpress; Q9Z0R9; -. DR Bgee; Q9Z0R9; -. DR CleanEx; MM_FADS2; -. DR Genevestigator; Q9Z0R9; -. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0016020; C:membrane; TAS:MGI. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0004768; F:stearoyl-CoA 9-desaturase activity; IDA:MGI. DR GO; GO:0006636; P:unsaturated fatty acid biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.10.120.10; -; 1. DR InterPro; IPR001199; Cyt_B5-like_heme/steroid-bd. DR InterPro; IPR012171; Fatty_acid/sphinglp_desaturase. DR InterPro; IPR005804; Fatty_acid_desaturase-1. DR Pfam; PF00173; Cyt-b5; 1. DR Pfam; PF00487; FA_desaturase; 1. DR PIRSF; PIRSF015921; FA_sphinglp_des; 1. DR SUPFAM; SSF55856; SSF55856; 1. DR PROSITE; PS50255; CYTOCHROME_B5_2; 1. PE 2: Evidence at transcript level; KW Complete proteome; Electron transport; Endoplasmic reticulum; KW Fatty acid biosynthesis; Fatty acid metabolism; Lipid biosynthesis; KW Lipid metabolism; Membrane; Oxidoreductase; Reference proteome; KW Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 444 Fatty acid desaturase 2. FT /FTId=PRO_0000307103. FT TOPO_DOM 1 130 Cytoplasmic (Potential). FT TRANSMEM 131 151 Helical; (Potential). FT TOPO_DOM 152 152 Lumenal (Potential). FT TRANSMEM 153 173 Helical; (Potential). FT TOPO_DOM 174 264 Cytoplasmic (Potential). FT TRANSMEM 265 285 Helical; (Potential). FT TOPO_DOM 286 305 Lumenal (Potential). FT TRANSMEM 306 326 Helical; (Potential). FT TOPO_DOM 327 444 Cytoplasmic (Potential). FT DOMAIN 18 95 Cytochrome b5 heme-binding. FT MOTIF 180 184 Histidine box-1. FT MOTIF 217 221 Histidine box-2. FT MOTIF 382 386 Histidine box-3. SQ SEQUENCE 444 AA; 52387 MW; 7615D17024D3B771 CRC64; MGKGGNQGEG STERQAPMPT FRWEEIQKHN LRTDRWLVID RKVYNVTKWS QRHPGGHRVI GHYSGEDATD AFRAFHLDLD FVGKFLKPLL IGELAPEEPS LDRGKSSQIT EDFRALKKTA EDMNLFKTNH LFFFLLLSHI IVMESLAWFI LSYFGTGWIP TLVTAFVLAT SQAQAGWLQH DYGHLSVYKK SIWNHVVHKF VIGHLKGASA NWWNHRHFQH HAKPNIFHKD PDIKSLHVFV LGEWQPLEYG KKKLKYLPYN HQHEYFFLIG PPLLIPMYFQ YQIIMTMISR RDWVDLAWAI SYYMRFFYTY IPFYGILGAL VFLNFIRFLE SHWFVWVTQM NHLVMEIDLD HYRDWFSSQL AATCNVEQSF FNDWFSGHLN FQIEHHLFPT MPRHNLHKIA PLVKSLCAKH GIEYQEKPLL RALIDIVSSL KKSGELWLDA YLHK // ID FAS_MOUSE Reviewed; 2504 AA. AC P19096; B1ATU8; Q6PB72; Q8C4Z0; Q9EQR0; DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 2. DT 19-MAR-2014, entry version 141. DE RecName: Full=Fatty acid synthase; DE EC=2.3.1.85; DE Includes: DE RecName: Full=[Acyl-carrier-protein] S-acetyltransferase; DE EC=2.3.1.38; DE Includes: DE RecName: Full=[Acyl-carrier-protein] S-malonyltransferase; DE EC=2.3.1.39; DE Includes: DE RecName: Full=3-oxoacyl-[acyl-carrier-protein] synthase; DE EC=2.3.1.41; DE Includes: DE RecName: Full=3-oxoacyl-[acyl-carrier-protein] reductase; DE EC=1.1.1.100; DE Includes: DE RecName: Full=3-hydroxyacyl-[acyl-carrier-protein] dehydratase; DE EC=4.2.1.59; DE Includes: DE RecName: Full=Enoyl-[acyl-carrier-protein] reductase; DE EC=1.3.1.39; DE Includes: DE RecName: Full=Oleoyl-[acyl-carrier-protein] hydrolase; DE EC=3.1.2.14; GN Name=Fasn; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=C57BL/6J; RX PubMed=11029661; DOI=10.1046/j.1365-2443.2000.00369.x; RA Ueno K.; RT "Involvement of fatty acid synthase in axonal development in mouse RT embryos."; RL Genes Cells 5:859-869(2000). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Brain, and Liver; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP PROTEIN SEQUENCE OF 1-12; 225-235; 299-310; 385-409; 469-478; RP 1252-1270; 1333-1344; 1388-1398; 1501-1508; 1705-1717; 1733-1745; RP 2124-2132; 2376-2384 AND 2476-2498, ACETYLATION AT MET-1, AND MASS RP SPECTROMETRY. RC STRAIN=C57BL/6; TISSUE=Liver; RA Bienvenut W.V.; RL Submitted (JUL-2005) to UniProtKB. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1527-2504. RC STRAIN=C57BL/6J; TISSUE=Thymus; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1666-2504. RC STRAIN=CD-1; TISSUE=Liver; RX PubMed=2920037; DOI=10.1016/0006-291X(89)92776-9; RA Paulauskis J.D., Sul H.S.; RT "Structure of mouse fatty acid synthase mRNA. Identification of the RT two NADPH binding sites."; RL Biochem. Biophys. Res. Commun. 158:690-695(1989). RN [7] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-59; LYS-790; LYS-993; RP LYS-1071; LYS-1276; LYS-1840 AND LYS-2384, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic fibroblast; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., RA Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). CC -!- FUNCTION: Fatty acid synthetase catalyzes the formation of long- CC chain fatty acids from acetyl-CoA, malonyl-CoA and NADPH. This CC multifunctional protein has 7 catalytic activities and an acyl CC carrier protein. CC -!- CATALYTIC ACTIVITY: Acetyl-CoA + n malonyl-CoA + 2n NADPH = a CC long-chain fatty acid + (n+1) CoA + n CO(2) + 2n NADP(+). CC -!- CATALYTIC ACTIVITY: Acetyl-CoA + [acyl-carrier-protein] = CoA + CC acetyl-[acyl-carrier-protein]. CC -!- CATALYTIC ACTIVITY: Malonyl-CoA + [acyl-carrier-protein] = CoA + CC malonyl-[acyl-carrier-protein]. CC -!- CATALYTIC ACTIVITY: Acyl-[acyl-carrier-protein] + malonyl-[acyl- CC carrier-protein] = 3-oxoacyl-[acyl-carrier-protein] + CO(2) + CC [acyl-carrier-protein]. CC -!- CATALYTIC ACTIVITY: (3R)-3-hydroxyacyl-[acyl-carrier-protein] + CC NADP(+) = 3-oxoacyl-[acyl-carrier-protein] + NADPH. CC -!- CATALYTIC ACTIVITY: A (3R)-3-hydroxyacyl-[acyl-carrier protein] = CC a trans-2-enoyl-[acyl-carrier protein] + H(2)O. CC -!- CATALYTIC ACTIVITY: An acyl-[acyl-carrier protein] + NADP(+) = a CC trans-2,3-dehydroacyl-[acyl-carrier protein] + NADPH. CC -!- CATALYTIC ACTIVITY: Oleoyl-[acyl-carrier-protein] + H(2)O = [acyl- CC carrier-protein] + oleate. CC -!- SUBUNIT: Homodimer which is arranged in a head to tail fashion. CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Melanosome (By CC similarity). CC -!- SIMILARITY: Contains 1 acyl carrier domain. CC -!- SEQUENCE CAUTION: CC Sequence=CAA31525.1; Type=Frameshift; Positions=1842, 1855, 1863, 1964, 1967; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF127033; AAG02285.1; -; mRNA. DR EMBL; AL663090; CAM27545.1; -; Genomic_DNA. DR EMBL; BC046513; AAH46513.1; -; mRNA. DR EMBL; BC059850; AAH59850.1; -; mRNA. DR EMBL; AK080374; BAC37895.1; -; mRNA. DR EMBL; X13135; CAA31525.1; ALT_FRAME; mRNA. DR PIR; A32262; A32262. DR RefSeq; NP_032014.3; NM_007988.3. DR UniGene; Mm.236443; -. DR ProteinModelPortal; P19096; -. DR SMR; P19096; 2-853, 1215-2107, 2113-2201, 2211-2484. DR BioGrid; 199596; 3. DR IntAct; P19096; 8. DR MINT; MINT-2514287; -. DR BindingDB; P19096; -. DR ChEMBL; CHEMBL1795189; -. DR PhosphoSite; P19096; -. DR PaxDb; P19096; -. DR PRIDE; P19096; -. DR Ensembl; ENSMUST00000055655; ENSMUSP00000052872; ENSMUSG00000025153. DR GeneID; 14104; -. DR KEGG; mmu:14104; -. DR UCSC; uc007mut.1; mouse. DR CTD; 2194; -. DR MGI; MGI:95485; Fasn. DR eggNOG; COG3319; -. DR GeneTree; ENSGT00530000063309; -. DR HOGENOM; HOG000019642; -. DR HOVERGEN; HBG005640; -. DR InParanoid; B1ATU8; -. DR KO; K00665; -. DR OMA; MVVANEN; -. DR OrthoDB; EOG71K623; -. DR TreeFam; TF300549; -. DR NextBio; 285138; -. DR PRO; PR:P19096; -. DR Bgee; P19096; -. DR CleanEx; MM_FASN; -. DR Genevestigator; P19096; -. DR GO; GO:0042587; C:glycogen granule; IDA:MGI. DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl. DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl. DR GO; GO:0047451; F:3-hydroxyoctanoyl-[acyl-carrier-protein] dehydratase activity; IEA:UniProtKB-EC. DR GO; GO:0004317; F:3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase activity; IEA:InterPro. DR GO; GO:0004316; F:3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity; IEA:UniProtKB-EC. DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:UniProtKB-EC. DR GO; GO:0004313; F:[acyl-carrier-protein] S-acetyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0004314; F:[acyl-carrier-protein] S-malonyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0008144; F:drug binding; IEA:Ensembl. DR GO; GO:0047117; F:enoyl-[acyl-carrier-protein] reductase (NADPH, A-specific) activity; IEA:UniProtKB-EC. DR GO; GO:0004319; F:enoyl-[acyl-carrier-protein] reductase (NADPH, B-specific) activity; IEA:InterPro. DR GO; GO:0016295; F:myristoyl-[acyl-carrier-protein] hydrolase activity; IEA:UniProtKB-EC. DR GO; GO:0070402; F:NADPH binding; IEA:Ensembl. DR GO; GO:0004320; F:oleoyl-[acyl-carrier-protein] hydrolase activity; IEA:UniProtKB-EC. DR GO; GO:0016296; F:palmitoyl-[acyl-carrier-protein] hydrolase activity; IEA:UniProtKB-EC. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0006084; P:acetyl-CoA metabolic process; IEA:Ensembl. DR GO; GO:0071353; P:cellular response to interleukin-4; IDA:MGI. DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW. DR Gene3D; 1.10.1200.10; -; 1. DR Gene3D; 1.10.1470.20; -; 1. DR Gene3D; 3.40.366.10; -; 2. DR Gene3D; 3.40.47.10; -; 2. DR Gene3D; 3.40.50.720; -; 2. DR InterPro; IPR001227; Ac_transferase_dom. DR InterPro; IPR009081; Acyl_carrier_prot-like. DR InterPro; IPR014043; Acyl_transferase. DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase. DR InterPro; IPR013149; ADH_C. DR InterPro; IPR023102; Fatty_acid_synthase_dom_2. DR InterPro; IPR011032; GroES-like. DR InterPro; IPR018201; Ketoacyl_synth_AS. DR InterPro; IPR014031; Ketoacyl_synth_C. DR InterPro; IPR014030; Ketoacyl_synth_N. DR InterPro; IPR016036; Malonyl_transacylase_ACP-bd. DR InterPro; IPR013217; Methyltransf_12. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR020842; PKS/FAS_KR. DR InterPro; IPR020843; PKS_ER. DR InterPro; IPR013968; PKS_KR. DR InterPro; IPR006162; PPantetheine_attach_site. DR InterPro; IPR001031; Thioesterase. DR InterPro; IPR016039; Thiolase-like. DR InterPro; IPR016038; Thiolase-like_subgr. DR Pfam; PF00698; Acyl_transf_1; 1. DR Pfam; PF00107; ADH_zinc_N; 1. DR Pfam; PF00109; ketoacyl-synt; 1. DR Pfam; PF02801; Ketoacyl-synt_C; 1. DR Pfam; PF08659; KR; 1. DR Pfam; PF08242; Methyltransf_12; 1. DR Pfam; PF00550; PP-binding; 1. DR Pfam; PF00975; Thioesterase; 1. DR SMART; SM00829; PKS_ER; 1. DR SMART; SM00822; PKS_KR; 1. DR SUPFAM; SSF47336; SSF47336; 1. DR SUPFAM; SSF50129; SSF50129; 1. DR SUPFAM; SSF52151; SSF52151; 2. DR SUPFAM; SSF53901; SSF53901; 2. DR SUPFAM; SSF55048; SSF55048; 1. DR PROSITE; PS50075; ACP_DOMAIN; 1. DR PROSITE; PS00606; B_KETOACYL_SYNTHASE; 1. DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1. PE 1: Evidence at protein level; KW Acetylation; Complete proteome; Cytoplasm; Direct protein sequencing; KW Fatty acid biosynthesis; Fatty acid metabolism; Hydrolase; KW Lipid biosynthesis; Lipid metabolism; Lyase; Multifunctional enzyme; KW NAD; NADP; Oxidoreductase; Phosphopantetheine; Phosphoprotein; KW Pyridoxal phosphate; Reference proteome; Transferase. FT CHAIN 1 2504 Fatty acid synthase. FT /FTId=PRO_0000180277. FT DOMAIN 2117 2173 Acyl carrier. FT NP_BIND 1664 1681 NADP (ER) (By similarity). FT NP_BIND 1879 1894 NADP (KR) (By similarity). FT REGION 1 414 Beta-ketoacyl synthase. FT REGION 429 817 Acyl and malonyl transferases. FT REGION 1628 1856 Enoyl reductase. FT REGION 1857 2111 Beta-ketoacyl reductase. FT REGION 2201 2504 Thioesterase. FT ACT_SITE 161 161 For beta-ketoacyl synthase activity (By FT similarity). FT ACT_SITE 581 581 For malonyltransferase activity (By FT similarity). FT ACT_SITE 878 878 For beta-hydroxyacyl dehydratase activity FT (By similarity). FT ACT_SITE 2301 2301 For thioesterase activity (By FT similarity). FT ACT_SITE 2474 2474 For thioesterase activity (By FT similarity). FT MOD_RES 1 1 N-acetylmethionine. FT MOD_RES 59 59 N6-acetyllysine. FT MOD_RES 70 70 N6-acetyllysine (By similarity). FT MOD_RES 207 207 Phosphoserine (By similarity). FT MOD_RES 298 298 N6-acetyllysine (By similarity). FT MOD_RES 528 528 N6-acetyllysine (By similarity). FT MOD_RES 673 673 N6-acetyllysine (By similarity). FT MOD_RES 790 790 N6-acetyllysine. FT MOD_RES 993 993 N6-acetyllysine. FT MOD_RES 1071 1071 N6-acetyllysine. FT MOD_RES 1276 1276 N6-acetyllysine. FT MOD_RES 1697 1697 N6-(pyridoxal phosphate)lysine; alternate FT (By similarity). FT MOD_RES 1697 1697 N6-acetyllysine; alternate (By FT similarity). FT MOD_RES 1764 1764 N6-acetyllysine (By similarity). FT MOD_RES 1840 1840 N6-acetyllysine. FT MOD_RES 1988 1988 N6-acetyllysine (By similarity). FT MOD_RES 2150 2150 O-(pantetheine 4'-phosphoryl)serine (By FT similarity). FT MOD_RES 2229 2229 Phosphoserine (By similarity). FT MOD_RES 2384 2384 N6-acetyllysine. FT CONFLICT 1992 1992 T -> N (in Ref. 6; CAA31525). FT CONFLICT 2028 2028 G -> C (in Ref. 6; CAA31525). FT CONFLICT 2045 2045 G -> V (in Ref. 6; CAA31525). FT CONFLICT 2117 2117 T -> N (in Ref. 6; CAA31525). FT CONFLICT 2175 2175 Q -> R (in Ref. 6; CAA31525). FT CONFLICT 2295 2295 Y -> H (in Ref. 6; CAA31525). SQ SEQUENCE 2504 AA; 272428 MW; 2B48068B9D370C6F CRC64; MEEVVIAGMS GKLPESENLQ EFWANLIGGV DMVTDDDRRW KAGLYGLPKR SGKLKDLSKF DASFFGVHPK QAHTMDPQLR LLLEVSYEAI VDGGINPASL RGTNTGVWVG VSGSEASEAL SRDPETLLGY SMVGCQRAMM ANRLSFFFDF KGPSIALDTA CSSSLLALQN AYQAIRSGEC PAALVGGINL LLKPNTSVQF MKLGMLSPDG TCRSFDDSGS GYCRSEAVVA VLLTKKSLAR RVYATILNAG TNTDGSKEQG VTFPSGEVQE QLICSLYQPA GLAPESLEYI EAHGTGTKVG DPQELNGITR SLCAFRQAPL LIGSTKSNMG HPEPASGLAA LTKVLLSLEH GVWAPNLHFH NPNPEIPALL DGRLQVVDRP LPVRGGNVGI NSFGFGGSNV HVILQPNTRQ APAPTAHAAL PHLLHASGRT LEAVQDLLEQ GRQHSQDLAF VSMLNDIAAT PTAAMPFRGY TVLGVEGRVQ EVQQVSTNKR PLWFICSGMG TQWRGMGLSL MRLDSFRESI LRSDEAVKPL GVKVSDLLLS TDERTFDDIV HAFVSLTAIQ IALIDLLTSV GLKPDGIIGH SLGEVACGYA DGCLSQREAV LAAYWRGQCI KDAHLPPGSM AAVGLSWEEC KQRCPAGVVP ACHNSEDTVT ISGPQAAVNE FVEQLKQEGV FAKEVRTGGL AFHSYFMEGI APTLLQALKK VIREPRPRSA RWLSTSIPEA QWQSSLARTS SAEYNVNNLV SPVLFQEALW HIPEHAVVLE IAPHALLQAV LKRGVKSSCT IIPLMKRDHK DNLEFFLTNL GKVHLTGINV NPNALFPPVE FPAPRGTPLI SPHIKWDHSQ TWDVPVAEDF PNGSSSSSAT VYSIDASPES PDHYLVDHCI DGRVIFPGTG YLCLVWKTLA RSLGLSLEET PVVFENVSFH QATILPKTGT VALEVRLLEA SHAFEVSDTG NLIVSGKVYL WEDPNSKLFD HPEVPTPPES ASVSRLTQGE VYKELRLRGY DYGPQFQGIC EATLEGEQGK LLWKDNWVTF MDTMLQVSIL GSSQQSLQLP TRVTAIYIDP ATHRQKVYRL KEDTQVADVT TSRCLGITVS GGIHISRLQT TATSRRQQEQ LVPTLEKFVF TPHMEAECLS ESTALQKELQ LCKGLARALQ TKATQQGLKA AMLGQEDPPQ HGLPRLLAAA CQLQLNGNLQ LELGEALAQE RLLLPEDPLI SGLLNSQALK ACVDTALENL STLKMKVAEV LAGEGHLYSR IPALLNTQPM LQLEYTATDR HPQALKDVQT KLQQHDVAQG QWNPSDPAPS SLGALDLLVC NCALATLGDP ALALDNMVAA LKEGGFLLVH TVLKGHALGE TLACLPSEVQ PAPSLLSQEE WESLFSRKAL HLVGLKRSFY GTALFLCRRA IPQEKPIFLS VEDTSFQWVD SLKSTLATSS SQPVWLTAMD CPTSGVVGLV NCLRKEPGGH RIRCILLSNL SNTSHAPKLD PGSPELQQVL KHDLVMNVYR DGAWGAFRHF QLEQDKPKEQ TAHAFVNVLT RGDLASIRWV SSPLKHTQPS SSGAQLCTVY YASLNFRDIM LATGKLSPDA IPGKWASRDC MLGMEFSGRD RCGRRVMGLV PAEGLATSVL LSSDFLWDVP SSWTLEEAAS VPVVYTTAYY SLVVRGRIQR GETVLIHSGS GGVGQAAISI ALSLGCRVFT TVGSAEKRAY LQARFPQLDD TSFANSRDTS FEQHVLLHTG GKGVDLVLNS LAEEKLQASV RCLAQHGRFL EIGKFDLSNN HPLGMAIFLK NVTFHGILLD ALFEEANDSW REVAALLKAG IRDGVVKPLK CTVFPKAQVE DAFRYMAQGK HIGKVLVQVR EEEPEAVLPG AQPTLISAIS KTFCPAHKSY IITGGLGGFG LELARWLVLR GAQRLVLTSR SGIRTGYQAK HIREWRRQGI QVLVSTSNVS SLEGARALIA EATKLGPVGG VFNLAMVLRD AMLENQTPEL FQDVNKPKYN GTLNLDRATR EACPELDYFV AFSSVSCGRG NAGQTNYGFA NSTMERICEQ RRHDGLPGLA VQWGAIGDVG IVLEAMGTND TVIGGTLPQR ISSCMEVLDL FLNQPHAVLS SFVLAEKKAV AHGDGDTQRD LVKAVAHILG IRDLAGINLD STLADLGLDS LMGVEVRQIL EREHDLVLPM REVRQLTLRK LQEMSSKTDS ATDTTAPKSR SDTSLKQNQL NLSTLLVNPE GPTLTQLNSV QSSERPLFLV HPIEGSTTVF HSLAAKLSVP TYGLQCTQAA PLDSIPNLAA YYIDCIKQVQ PEGPYRIAGY SFGACVAFEM CSQLQAQQGP APTHNNLFLF DGSHTYVLAY TQSYRAKMTP GCEAEAEAEA LCFFIKQFLD VEHSKVLEAL LPLKSLEDRV AASVDLITKS HHSLDRRELS FAAVSFYHKL RAADQYKPKA KYHGNVTLLR AKTGGTYGED LGADYNLSQV CDGKVSVHII EGDHRTLLEG SGLESIINII HSSLAEPRVS VREG // ID FCL_MOUSE Reviewed; 321 AA. AC P23591; DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot. DT 27-MAY-2002, sequence version 3. DT 19-MAR-2014, entry version 119. DE RecName: Full=GDP-L-fucose synthase; DE EC=1.1.1.271; DE AltName: Full=GDP-4-keto-6-deoxy-D-mannose-3,5-epimerase-4-reductase; DE AltName: Full=Protein FX; DE AltName: Full=Red cell NADP(H)-binding protein; DE AltName: Full=Transplantation antigen P35B; DE AltName: Full=Tum-P35B antigen; GN Name=Tsta3; Synonyms=P35b, Tstap35b; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND VARIANT ASN-139. RC STRAIN=DBA/2; TISSUE=Mast cell; RX PubMed=2108859; RA Szikora J.-P., van Pel A., Brichard V., Andre M., van Baren N., RA Henry P., de Plaen E., Boon T.; RT "Structure of the gene of tum- transplantation antigen P35B: presence RT of a point mutation in the antigenic allele."; RL EMBO J. 9:1041-1050(1990). RN [2] RP SEQUENCE REVISION. RA de Plaen E.; RL Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Testis; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). CC -!- FUNCTION: Catalyzes the two-step NADP-dependent conversion of GDP- CC 4-dehydro-6-deoxy-D-mannose to GDP-fucose, involving an epimerase CC and a reductase reaction (By similarity). CC -!- CATALYTIC ACTIVITY: GDP-beta-L-fucose + NADP(+) = GDP-4-dehydro-6- CC deoxy-alpha-D-mannose + NADPH. CC -!- PATHWAY: Nucleotide-sugar biosynthesis; GDP-L-fucose biosynthesis CC via de novo pathway; GDP-L-fucose from GDP-alpha-D-mannose: step CC 2/2. CC -!- SUBUNIT: Homodimer (By similarity). CC -!- MISCELLANEOUS: Mutagen treatment of P815 tumor cells produces tum- CC variants that elicit a cytolytic T-lymphocyte response (CTL). The CC antigenic allele differs from the normal allele by a single CC mutation in position 139. CC -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase CC family. Fucose synthase subfamily. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X53620; CAB94217.1; ALT_SEQ; Genomic_DNA. DR EMBL; X53621; CAB94217.1; JOINED; Genomic_DNA. DR EMBL; X53622; CAB94217.1; JOINED; Genomic_DNA. DR EMBL; X53623; CAB94217.1; JOINED; Genomic_DNA. DR EMBL; X53624; CAB94217.1; JOINED; Genomic_DNA. DR EMBL; X53625; CAB94217.1; JOINED; Genomic_DNA. DR EMBL; X53626; CAB94217.1; JOINED; Genomic_DNA. DR EMBL; X53627; CAB94217.1; JOINED; Genomic_DNA. DR EMBL; X53628; CAB94217.1; JOINED; Genomic_DNA. DR EMBL; M30127; AAA39673.2; -; mRNA. DR EMBL; M30128; AAA39674.1; ALT_FRAME; Genomic_DNA. DR EMBL; AK029632; BAC26539.1; -; mRNA. DR PIR; S12516; S12516. DR RefSeq; NP_112478.1; NM_031201.1. DR RefSeq; XP_006520814.1; XM_006520751.1. DR UniGene; Mm.22596; -. DR ProteinModelPortal; P23591; -. DR SMR; P23591; 7-321. DR IntAct; P23591; 2. DR MINT; MINT-1856547; -. DR STRING; 10090.ENSMUSP00000023231; -. DR PhosphoSite; P23591; -. DR PaxDb; P23591; -. DR PRIDE; P23591; -. DR Ensembl; ENSMUST00000023231; ENSMUSP00000023231; ENSMUSG00000022570. DR GeneID; 22122; -. DR KEGG; mmu:22122; -. DR UCSC; uc007whs.1; mouse. DR CTD; 7264; -. DR MGI; MGI:98857; Tsta3. DR eggNOG; COG0451; -. DR HOGENOM; HOG000168011; -. DR HOVERGEN; HBG000059; -. DR InParanoid; P23591; -. DR KO; K02377; -. DR OMA; IHCAGRV; -. DR OrthoDB; EOG7C5M8M; -. DR TreeFam; TF314936; -. DR UniPathway; UPA00128; UER00191. DR NextBio; 301985; -. DR PRO; PR:P23591; -. DR ArrayExpress; P23591; -. DR Bgee; P23591; -. DR CleanEx; MM_TSTA3; -. DR Genevestigator; P23591; -. DR GO; GO:0050662; F:coenzyme binding; IEA:InterPro. DR GO; GO:0050577; F:GDP-L-fucose synthase activity; IEA:UniProtKB-EC. DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW. DR GO; GO:0042351; P:'de novo' GDP-L-fucose biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0019835; P:cytolysis; IMP:MGI. DR GO; GO:0019673; P:GDP-mannose metabolic process; IEA:Ensembl. DR Gene3D; 3.40.50.720; -; 1. DR HAMAP; MF_00956; GDP_fucose_synth; 1. DR InterPro; IPR001509; Epimerase_deHydtase. DR InterPro; IPR028614; GDP_fucose_synth. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Pfam; PF01370; Epimerase; 1. PE 2: Evidence at transcript level; KW Complete proteome; Isomerase; Multifunctional enzyme; NADP; KW Oxidoreductase; Reference proteome; Tumor antigen. FT CHAIN 1 321 GDP-L-fucose synthase. FT /FTId=PRO_0000174351. FT NP_BIND 14 20 NADP (By similarity). FT NP_BIND 170 173 NADP (By similarity). FT ACT_SITE 143 143 Proton donor/acceptor (By similarity). FT BINDING 147 147 NADP (By similarity). FT BINDING 186 186 NADP (By similarity). FT BINDING 194 194 Substrate (By similarity). FT BINDING 208 208 Substrate (By similarity). FT BINDING 215 215 Substrate (By similarity). FT BINDING 277 277 Substrate (By similarity). FT SITE 114 114 Important for catalytic activity (By FT similarity). FT SITE 116 116 Important for catalytic activity (By FT similarity). FT SITE 147 147 Lowers pKa of active site Tyr (By FT similarity). FT VARIANT 139 139 S -> N (in allele TUM-). SQ SEQUENCE 321 AA; 35878 MW; 358D86D68F173531 CRC64; MGEPHGSMRI LVTGGSGLVG RAIQKVVADG AGLPGEEWVF VSSKDADLTD AAQTQALFQK VQPTHVIHLA AMVGGLFRNI KYNLDFWRKN VHINDNVLHS AFEVGARKVV SCLSTCIFPD KTTYPIDETM IHNGPPHSSN FGYSYAKRMI DVQNRAYFQQ HGCTFTAVIP TNVFGPYDNF NIEDGHVLPG LIHKVHLAKS SDSALTVWGT GKPRRQFIYS LDLARLFIWV LREYSEVEPI ILSVGEEDEV SIKEAAEAVV EAMDFNGEVT FDSTKSDGQY KKTASNGKLR SYLPDFRFTP FKQAVKETCT WFTDNYEQAR K // ID FMO1_MOUSE Reviewed; 532 AA. AC P50285; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 19-MAR-2014, entry version 115. DE RecName: Full=Dimethylaniline monooxygenase [N-oxide-forming] 1; DE EC=1.14.13.8; DE AltName: Full=Dimethylaniline oxidase 1; DE AltName: Full=Hepatic flavin-containing monooxygenase 1; DE Short=FMO 1; GN Name=Fmo1; Synonyms=Fmo-1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Itoh K., Nakamura K., Kimura T., Itoh S., Kamataki T.; RL Submitted (MAY-1993) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=CD-1; TISSUE=Liver; RX PubMed=9580872; RX DOI=10.1002/(SICI)1099-0461(1998)12:4<205::AID-JBT2>3.0.CO;2-P; RA Cherrington N.J., Falls J.G., Rose R.L., Clements K.M., Philpot R.M., RA Levi P.E., Hodgson E.; RT "Molecular cloning, sequence, and expression of mouse flavin- RT containing monooxygenases 1 and 5 (FMO1 and FMO5)."; RL J. Biochem. Mol. Toxicol. 12:205-212(1998). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Liver; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP PROTEIN SEQUENCE OF 297-307, AND MASS SPECTROMETRY. RC STRAIN=OF1; TISSUE=Hippocampus; RA Lubec G., Sunyer B., Chen W.-Q.; RL Submitted (JAN-2009) to UniProtKB. CC -!- FUNCTION: This protein is involved in the oxidative metabolism of CC a variety of xenobiotics such as drugs and pesticides. Form I CC catalyzes the N-oxygenation of secondary and tertiary amines. CC -!- CATALYTIC ACTIVITY: N,N-dimethylaniline + NADPH + O(2) = N,N- CC dimethylaniline N-oxide + NADP(+) + H(2)O. CC -!- COFACTOR: FAD. CC -!- SUBCELLULAR LOCATION: Microsome membrane. Endoplasmic reticulum CC membrane. CC -!- TISSUE SPECIFICITY: Liver. CC -!- SIMILARITY: Belongs to the FMO family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; D16215; BAA03745.1; -; mRNA. DR EMBL; U87456; AAB47569.1; -; mRNA. DR EMBL; BC011229; AAH11229.1; -; mRNA. DR PIR; B61243; B61243. DR RefSeq; NP_034361.1; NM_010231.2. DR RefSeq; XP_006496725.1; XM_006496662.1. DR RefSeq; XP_006496726.1; XM_006496663.1. DR UniGene; Mm.976; -. DR ProteinModelPortal; P50285; -. DR SMR; P50285; 2-487. DR IntAct; P50285; 3. DR MINT; MINT-1838390; -. DR PhosphoSite; P50285; -. DR PaxDb; P50285; -. DR PRIDE; P50285; -. DR Ensembl; ENSMUST00000046049; ENSMUSP00000037259; ENSMUSG00000040181. DR GeneID; 14261; -. DR KEGG; mmu:14261; -. DR UCSC; uc007dgx.1; mouse. DR CTD; 2326; -. DR MGI; MGI:1310002; Fmo1. DR eggNOG; COG2072; -. DR GeneTree; ENSGT00740000115433; -. DR HOGENOM; HOG000076537; -. DR HOVERGEN; HBG002037; -. DR InParanoid; P50285; -. DR KO; K00485; -. DR OMA; TRFQNML; -. DR OrthoDB; EOG7GXPB6; -. DR TreeFam; TF105285; -. DR NextBio; 285603; -. DR PRO; PR:P50285; -. DR ArrayExpress; P50285; -. DR Bgee; P50285; -. DR CleanEx; MM_FMO1; -. DR Genevestigator; P50285; -. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. DR GO; GO:0004497; F:monooxygenase activity; IMP:MGI. DR GO; GO:0004499; F:N,N-dimethylaniline monooxygenase activity; IEA:UniProtKB-EC. DR GO; GO:0050661; F:NADP binding; IEA:InterPro. DR GO; GO:0017144; P:drug metabolic process; IMP:MGI. DR GO; GO:0070995; P:NADPH oxidation; IEA:Ensembl. DR GO; GO:0006082; P:organic acid metabolic process; IEA:Ensembl. DR GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl. DR GO; GO:0006970; P:response to osmotic stress; IEA:Ensembl. DR GO; GO:0009404; P:toxin metabolic process; IEA:Ensembl. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR012143; DiMe-aniline_mOase. DR InterPro; IPR000960; Flavin_mOase. DR InterPro; IPR020946; Flavin_mOase-like. DR InterPro; IPR002253; Flavin_mOase_1. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Pfam; PF00743; FMO-like; 1. DR PIRSF; PIRSF000332; FMO; 1. DR PRINTS; PR00370; FMOXYGENASE. DR PRINTS; PR01121; FMOXYGENASE1. PE 1: Evidence at protein level; KW Complete proteome; Direct protein sequencing; Endoplasmic reticulum; KW FAD; Flavoprotein; Membrane; Microsome; Monooxygenase; NADP; KW Oxidoreductase; Reference proteome; Transmembrane. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 532 Dimethylaniline monooxygenase [N-oxide- FT forming] 1. FT /FTId=PRO_0000147640. FT NP_BIND 9 14 FAD (Potential). FT NP_BIND 191 196 NADP (Potential). FT SITE 208 208 Important for substrate binding (By FT similarity). SQ SEQUENCE 532 AA; 59915 MW; C3CEDC7FC82DAC59 CRC64; MVKRVAIVGA GVSGLASIKC CLEEGLEPTC FERSSDLGGL WRFTEHVEEG RASLYKSVVS NSSREMSCYP DFPFPEDYPN FVPNSLFLEY LKLYSTQFNL QRCIYFNTKV CSITKRPDFA VSGQWEVVTV TNGKQNSAIF DAVMVCTGFL TNPHLPLDSF PGILTFKGEY FHSRQYKHPD IFKDKRVLVV GMGNSGTDIA VEASHLAKKV FLSTTGGAWV ISRVFDSGYP WDMIFMTRFQ NMLRNLLPTP IVSWLISKKM NSWFNHVNYG VAPEDRTQLR EPVLNDELPG RIITGKVFIK PSIKEVKENS VVFNNTPKEE PIDIIVFATG YTFAFPFLDE SVVKVEDGQA SLYKYIFPAH LPKPTLAVIG LIKPLGSMVP TGETQARWVV QVLKGATTLP PPSVMMEEVN ERKKNKHSGF GLCYCKALQT DYITYIDDLL TSINAKPDLR AMLLTDPRLA LSIFFGPCTP YHFRLTGPGK WEGARKAILT QWDRTVKVTK TRTIQESPSS FETLLKLFSF LALLIAVFLI FL // ID FMO3_MOUSE Reviewed; 534 AA. AC P97501; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1997, sequence version 1. DT 19-MAR-2014, entry version 112. DE RecName: Full=Dimethylaniline monooxygenase [N-oxide-forming] 3; DE EC=1.14.13.8; DE AltName: Full=Dimethylaniline oxidase 3; DE AltName: Full=Hepatic flavin-containing monooxygenase 3; DE Short=FMO 3; DE AltName: Full=Trimethylamine monooxygenase; DE EC=1.14.13.148; GN Name=Fmo3; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=CD-1; TISSUE=Liver; RX PubMed=9344459; DOI=10.1006/abbi.1997.0322; RA Falls J.G., Cherrington N.J., Clements K.M., Philpot R.M., Levi P.E., RA Rose R.L., Hodgson E.; RT "Molecular cloning, sequencing, and expression in Escherichia coli of RT mouse flavin-containing monooxygenase 3 (FMO3): comparison with the RT human isoform."; RL Arch. Biochem. Biophys. 347:9-18(1997). RN [2] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-401, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic fibroblast; RX PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200; RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.; RT "Large scale localization of protein phosphorylation by use of RT electron capture dissociation mass spectrometry."; RL Mol. Cell. Proteomics 8:904-912(2009). RN [3] RP FUNCTION, AND INDUCTION. RX PubMed=23177478; DOI=10.1016/j.cub.2012.10.047; RA Li Q., Korzan W.J., Ferrero D.M., Chang R.B., Roy D.S., Buchi M., RA Lemon J.K., Kaur A.W., Stowers L., Fendt M., Liberles S.D.; RT "Synchronous evolution of an odor biosynthesis pathway and behavioral RT response."; RL Curr. Biol. 23:11-20(2013). CC -!- FUNCTION: Involved in the oxidative metabolism of a variety of CC xenobiotics such as drugs and pesticides. It N-oxygenates primary CC aliphatic alkylamines as well as secondary and tertiary amines. CC Acts on TMA to produce TMA-N-oxide. CC -!- CATALYTIC ACTIVITY: N,N-dimethylaniline + NADPH + O(2) = N,N- CC dimethylaniline N-oxide + NADP(+) + H(2)O. CC -!- CATALYTIC ACTIVITY: N,N,N-trimethylamine + NADPH + O(2) = N,N,N- CC trimethylamine N-oxide + NADP(+) + H(2)O. CC -!- COFACTOR: FAD (By similarity). CC -!- SUBCELLULAR LOCATION: Microsome membrane. Endoplasmic reticulum CC membrane (By similarity). CC -!- TISSUE SPECIFICITY: Liver. CC -!- INDUCTION: Expression is specifically repressed in male mice after CC puberty, preventing trimethylamine degradation. Trimethylamine is CC present at high concentration in the urine of male mice after CC puberty and acts as an attractant. CC -!- MISCELLANEOUS: Trimethylamine is a bacterial metabolite found in CC some animal odors, and is a repulsive odor associated with bad CC breath and spoiled food for most organisms, except for M.musculus, CC where it acts as an attractant (PubMed:23177478). CC -!- SIMILARITY: Belongs to the FMO family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U87147; AAB47541.1; -; mRNA. DR RefSeq; NP_032056.1; NM_008030.1. DR UniGene; Mm.2900; -. DR ProteinModelPortal; P97501; -. DR SMR; P97501; 1-489. DR IntAct; P97501; 3. DR MINT; MINT-4095189; -. DR STRING; 10090.ENSMUSP00000028010; -. DR PhosphoSite; P97501; -. DR PaxDb; P97501; -. DR PRIDE; P97501; -. DR DNASU; 14262; -. DR Ensembl; ENSMUST00000028010; ENSMUSP00000028010; ENSMUSG00000026691. DR GeneID; 14262; -. DR KEGG; mmu:14262; -. DR UCSC; uc007dhe.1; mouse. DR CTD; 2328; -. DR MGI; MGI:1100496; Fmo3. DR eggNOG; COG2072; -. DR HOGENOM; HOG000076537; -. DR HOVERGEN; HBG002037; -. DR InParanoid; P97501; -. DR KO; K00485; -. DR OMA; FMHNSKL; -. DR OrthoDB; EOG7GXPB6; -. DR TreeFam; TF105285; -. DR NextBio; 285607; -. DR PRO; PR:P97501; -. DR ArrayExpress; P97501; -. DR Bgee; P97501; -. DR CleanEx; MM_FMO3; -. DR Genevestigator; P97501; -. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0016597; F:amino acid binding; IEA:Ensembl. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. DR GO; GO:0004499; F:N,N-dimethylaniline monooxygenase activity; IEA:UniProtKB-EC. DR GO; GO:0050661; F:NADP binding; IEA:Ensembl. DR GO; GO:0034899; F:trimethylamine monooxygenase activity; IEA:UniProtKB-EC. DR GO; GO:0017144; P:drug metabolic process; IEA:Ensembl. DR Gene3D; 3.40.50.720; -; 2. DR InterPro; IPR012143; DiMe-aniline_mOase. DR InterPro; IPR000960; Flavin_mOase. DR InterPro; IPR020946; Flavin_mOase-like. DR InterPro; IPR002255; Flavin_mOase_3. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Pfam; PF00743; FMO-like; 1. DR PIRSF; PIRSF000332; FMO; 1. DR PRINTS; PR00370; FMOXYGENASE. DR PRINTS; PR01123; FMOXYGENASE3. PE 1: Evidence at protein level; KW Complete proteome; Endoplasmic reticulum; FAD; Flavoprotein; Membrane; KW Microsome; Monooxygenase; NADP; Oxidoreductase; Phosphoprotein; KW Reference proteome; Transmembrane. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 534 Dimethylaniline monooxygenase [N-oxide- FT forming] 3. FT /FTId=PRO_0000147656. FT NP_BIND 9 14 FAD (Potential). FT NP_BIND 191 196 NADP (Potential). FT MOD_RES 401 401 Phosphoserine. SQ SEQUENCE 534 AA; 60516 MW; F72F7993C01AF9C9 CRC64; MKKKVAIIGA GVSGLAAIRS CLEEGLEPTC FERSDDVGGL WKFSDHIEEG RASIYQSVFT NSSKEMMCFP DFPYPDDFPN FMHHSKLQEY ITSFAKEKNL LKYIQFETPV TSINKCPNFS TTGKWEVTTE KHGKKETAVF DATMICSGHH IFPHVPKDSF PGLNRFKGKC FHSRDYKEPG IWKGKRVLVI GLGNSGCDIA AELSHVAQKV TISSRSGSWV MSRVWDDGYP WDMVVLTRFQ TFLKNNLPTA ISDWWYTRQM NARFKHENYG LVPLNRTLRK EPVFNDELPA RILCGMVTIK PNVKEFTETS AVFEDGTMFE AIDCVIFATG YGYAYPFLDD SIIKSRNNEV TLYKGVFPPQ LEKPTMAVIG LVQSLGATIP ITDLQARWAA QVIKGTCTLP SVNDMMDDID EKMGEKFKWY GNSTTIQTDY IVYMDELASF IGAKPNLLWL FLKDPRLAVE VFFGPCSPYQ FRLVGPGKWS GARNAILTQW DRSLKPMKTR VVSKVQKSCS HFYSRLLRLL AVPVLLIALF LVLI // ID FMO4_MOUSE Reviewed; 560 AA. AC Q8VHG0; DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 19-MAR-2014, entry version 85. DE RecName: Full=Dimethylaniline monooxygenase [N-oxide-forming] 4; DE EC=1.14.13.8; DE AltName: Full=Dimethylaniline oxidase 4; DE AltName: Full=Hepatic flavin-containing monooxygenase 4; DE Short=FMO 4; GN Name=Fmo4; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=129/Sv; TISSUE=Kidney; RA Hernandez D., Janmohamed A., Chandan P., Phillips I.R., Shephard E.A.; RT "The mouse flavin-containing monooxygenase gene cluster."; RL Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: This protein is involved in the oxidative metabolism of CC a variety of xenobiotics such as drugs and pesticides (By CC similarity). CC -!- CATALYTIC ACTIVITY: N,N-dimethylaniline + NADPH + O(2) = N,N- CC dimethylaniline N-oxide + NADP(+) + H(2)O. CC -!- COFACTOR: FAD (By similarity). CC -!- SUBCELLULAR LOCATION: Microsome membrane (By similarity). CC Endoplasmic reticulum membrane (By similarity). CC -!- SIMILARITY: Belongs to the FMO family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF461145; AAL66366.1; -; mRNA. DR RefSeq; NP_659127.1; NM_144878.1. DR RefSeq; XP_006496839.1; XM_006496776.1. DR RefSeq; XP_006496840.1; XM_006496777.1. DR UniGene; Mm.155164; -. DR ProteinModelPortal; Q8VHG0; -. DR SMR; Q8VHG0; 2-444. DR PhosphoSite; Q8VHG0; -. DR PaxDb; Q8VHG0; -. DR PRIDE; Q8VHG0; -. DR Ensembl; ENSMUST00000028014; ENSMUSP00000028014; ENSMUSG00000026692. DR Ensembl; ENSMUST00000111525; ENSMUSP00000107150; ENSMUSG00000026692. DR GeneID; 226564; -. DR KEGG; mmu:226564; -. DR UCSC; uc007dgv.1; mouse. DR CTD; 2329; -. DR MGI; MGI:2429497; Fmo4. DR eggNOG; COG2072; -. DR GeneTree; ENSGT00740000115132; -. DR HOGENOM; HOG000076537; -. DR HOVERGEN; HBG002037; -. DR InParanoid; Q8VHG0; -. DR KO; K00485; -. DR OMA; INWTHER; -. DR OrthoDB; EOG7GXPB6; -. DR TreeFam; TF105285; -. DR NextBio; 378238; -. DR PRO; PR:Q8VHG0; -. DR ArrayExpress; Q8VHG0; -. DR Bgee; Q8VHG0; -. DR CleanEx; MM_FMO4; -. DR Genevestigator; Q8VHG0; -. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. DR GO; GO:0004499; F:N,N-dimethylaniline monooxygenase activity; IEA:UniProtKB-EC. DR GO; GO:0050661; F:NADP binding; IEA:InterPro. DR GO; GO:0042737; P:drug catabolic process; IMP:MGI. DR InterPro; IPR012143; DiMe-aniline_mOase. DR InterPro; IPR000960; Flavin_mOase. DR InterPro; IPR020946; Flavin_mOase-like. DR InterPro; IPR002256; Flavin_mOase_4. DR Pfam; PF00743; FMO-like; 1. DR PIRSF; PIRSF000332; FMO; 1. DR PRINTS; PR00370; FMOXYGENASE. DR PRINTS; PR01124; FMOXYGENASE4. PE 2: Evidence at transcript level; KW Complete proteome; Endoplasmic reticulum; FAD; Flavoprotein; Membrane; KW Microsome; Monooxygenase; NADP; Oxidoreductase; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 560 Dimethylaniline monooxygenase [N-oxide- FT forming] 4. FT /FTId=PRO_0000147661. FT TRANSMEM 516 530 Helical; (Potential). FT NP_BIND 9 14 FAD (Potential). FT NP_BIND 191 196 NADP (Potential). SQ SEQUENCE 560 AA; 63792 MW; 75C3AEE53693B7AD CRC64; MAKKVAVIGA GVSGLSSIKC CLDENLEPTC FERTSDFGGL WKFADTSEDG MTRVYRSLVT NVCKEMSCYS DFPFREDYPN FMSHEKFWDY LREFAEHFGL LRYIRFKTTV LSVTKRPDFS ETGQWDVVTE TEGKRDRAVF DAVMVCTGQF LSPHLPLESF PGIHKFKGQI LHSQEYRIPD AFRGKRILVV GLGNTGGDIA VELSEIAAQV FLSTRTGTWV LSRSSPGGYP FNMIQTRWLN FLVRVLPSRF INWTHERKMN KILNHENYGL SIAKGKKPKF IVNDELPTCI LCGKVTMKTS VKDFTESSVI FEDGTTEANI DVVIFTTGYE FSFPFFEEPL KSLCTKKIIL YKRVFPPNLE RATLAIIGLI SLNGSILVGT EFQARWATRV FKGLCSIPPS QKLMAEATKT EQLIKRGVIK DTSQDKLDFI TYMDELTQCI GAKPSIPLLF IKDPRLAWEV FFGPCTPYQY RLVGPGRWDG ARNAILTQWD RTLKPLKTRI VPKSPEPTSL SHYLIAWGAP VLLVSLLLIY KSSHFLELVQ GKLPRRFPPY RLLWYMPQNS // ID FMO2_MOUSE Reviewed; 535 AA. AC Q8K2I3; Q9QZF7; DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 19-MAR-2014, entry version 97. DE RecName: Full=Dimethylaniline monooxygenase [N-oxide-forming] 2; DE EC=1.14.13.8; DE AltName: Full=Dimethylaniline oxidase 2; DE AltName: Full=Pulmonary flavin-containing monooxygenase 2; DE Short=FMO 2; GN Name=Fmo2; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION. RC STRAIN=C57BL/6; TISSUE=Kidney; RX PubMed=11835629; DOI=10.1002/jbt.10009; RA Karoly E.D., Rose R.L.; RT "Sequencing, expression, and characterization of cDNA expressed RT flavin-containing monooxygenase 2 from mouse."; RL J. Biochem. Mol. Toxicol. 15:300-308(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Czech II; TISSUE=Mammary tumor; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: This protein is involved in the oxidative metabolism of CC a variety of xenobiotics such as drugs and pesticides. Shows CC catalytic activity towards methimazole, thiourea, trimethylamine, CC and the insecticide phorate. CC -!- CATALYTIC ACTIVITY: N,N-dimethylaniline + NADPH + O(2) = N,N- CC dimethylaniline N-oxide + NADP(+) + H(2)O. CC -!- COFACTOR: FAD (By similarity). CC -!- COFACTOR: Magnesium (By similarity). CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC pH dependence: CC Optimum pH is 10.5; CC -!- SUBCELLULAR LOCATION: Microsome membrane (By similarity). CC Endoplasmic reticulum membrane (By similarity). CC -!- SIMILARITY: Belongs to the FMO family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF184981; AAD56413.1; -; mRNA. DR EMBL; BC031415; AAH31415.1; -; mRNA. DR RefSeq; NP_061369.2; NM_018881.3. DR RefSeq; XP_006497012.1; XM_006496949.1. DR UniGene; Mm.10929; -. DR ProteinModelPortal; Q8K2I3; -. DR SMR; Q8K2I3; 2-486. DR IntAct; Q8K2I3; 1. DR MINT; MINT-4117353; -. DR STRING; 10090.ENSMUSP00000107135; -. DR PhosphoSite; Q8K2I3; -. DR PaxDb; Q8K2I3; -. DR PRIDE; Q8K2I3; -. DR Ensembl; ENSMUST00000045902; ENSMUSP00000044405; ENSMUSG00000040170. DR Ensembl; ENSMUST00000111510; ENSMUSP00000107135; ENSMUSG00000040170. DR GeneID; 55990; -. DR KEGG; mmu:55990; -. DR UCSC; uc007dgz.1; mouse. DR CTD; 2327; -. DR MGI; MGI:1916776; Fmo2. DR eggNOG; COG2072; -. DR GeneTree; ENSGT00740000115433; -. DR HOGENOM; HOG000076537; -. DR HOVERGEN; HBG002037; -. DR InParanoid; Q8K2I3; -. DR KO; K00485; -. DR OMA; DIGATRR; -. DR OrthoDB; EOG7GXPB6; -. DR TreeFam; TF105285; -. DR ChiTaRS; FMO2; mouse. DR NextBio; 311714; -. DR PRO; PR:Q8K2I3; -. DR ArrayExpress; Q8K2I3; -. DR Bgee; Q8K2I3; -. DR CleanEx; MM_FMO2; -. DR Genevestigator; Q8K2I3; -. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0016020; C:membrane; ISS:UniProtKB. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. DR GO; GO:0004497; F:monooxygenase activity; IDA:MGI. DR GO; GO:0004499; F:N,N-dimethylaniline monooxygenase activity; IEA:UniProtKB-EC. DR GO; GO:0050661; F:NADP binding; IEA:InterPro. DR GO; GO:0017144; P:drug metabolic process; IEA:Ensembl. DR GO; GO:0070995; P:NADPH oxidation; ISS:UniProtKB. DR GO; GO:0006082; P:organic acid metabolic process; IEA:Ensembl. DR GO; GO:0072592; P:oxygen metabolic process; IDA:MGI. DR GO; GO:0009404; P:toxin metabolic process; IEA:Ensembl. DR GO; GO:0006805; P:xenobiotic metabolic process; IEA:Ensembl. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR012143; DiMe-aniline_mOase. DR InterPro; IPR000960; Flavin_mOase. DR InterPro; IPR020946; Flavin_mOase-like. DR InterPro; IPR002254; Flavin_mOase_2. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Pfam; PF00743; FMO-like; 1. DR PIRSF; PIRSF000332; FMO; 1. DR PRINTS; PR00370; FMOXYGENASE. DR PRINTS; PR01122; FMOXYGENASE2. PE 1: Evidence at protein level; KW Acetylation; Complete proteome; Endoplasmic reticulum; FAD; KW Flavoprotein; Isopeptide bond; Magnesium; Membrane; Microsome; KW Monooxygenase; NADP; Oxidoreductase; Reference proteome; KW Transmembrane; Ubl conjugation. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 535 Dimethylaniline monooxygenase [N-oxide- FT forming] 2. FT /FTId=PRO_0000147648. FT NP_BIND 9 14 FAD (Potential). FT NP_BIND 191 196 NADP (Potential). FT MOD_RES 2 2 N-acetylalanine (By similarity). FT CROSSLNK 492 492 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO-1) (By FT similarity). FT CONFLICT 169 169 Q -> R (in Ref. 1; AAD56413). SQ SEQUENCE 535 AA; 60974 MW; 705FAD9D8EADB1B1 CRC64; MAKKVVVIGA GVSGLISLKC CVDEGLEPTC FERTEDIGGL WRFKENVEDG RASIYRSVIT NTSKEMSCFS DFPMPEDFPN FLHNSKLLEY FRIFAKKFDL LKYIQFQTTV ISVKKRPDFA SSGQWEVYTQ SNGKEQRTVF DAVMVCSGHH IQPHLPLKSF PGIERFRGQY FHSREYKHPV GFEGKRILVV GIGNSAADIA SELSKTAAQV FVSTRHGSWV MSRISEDGYP WDMVFHTRFS SMLRNVLPRT VVKWMMEQQM NRWFNHENYG LVPQNKYLMK EPVLNDDLPS RLLYGAIKVK TRVKELTETA VVFEDGTVEE DVDIIVFATG YTFSFSFLED SLVKVEDNRV SLYKAMFPPH LEKPTLACIG LIQPLGSIFP TVELQARWAT RVFKGLCSLP SETTMMADIV ERNEKRVNLF GKSQSQILQT NYVDYLDELA LEIGAKPDFV SLFFKDPKLA VKLYFGPCNS YQYRLVGPGQ WEGARNAILT QKQRILKPLK TRTLQSSDSA PVSFLLKILG LLAVVLAFFF QLQGF // ID FMO5_MOUSE Reviewed; 533 AA. AC P97872; Q8R1W6; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 4. DT 19-MAR-2014, entry version 106. DE RecName: Full=Dimethylaniline monooxygenase [N-oxide-forming] 5; DE EC=1.14.13.8; DE AltName: Full=Dimethylaniline oxidase 5; DE AltName: Full=Hepatic flavin-containing monooxygenase 5; DE Short=FMO 5; GN Name=Fmo5; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=CD-1; TISSUE=Liver; RX PubMed=9580872; RX DOI=10.1002/(SICI)1099-0461(1998)12:4<205::AID-JBT2>3.0.CO;2-P; RA Cherrington N.J., Falls J.G., Rose R.L., Clements K.M., Philpot R.M., RA Levi P.E., Hodgson E.; RT "Molecular cloning, sequence, and expression of mouse flavin- RT containing monooxygenases 1 and 5 (FMO1 and FMO5)."; RL J. Biochem. Mol. Toxicol. 12:205-212(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Pituitary; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Liver; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: In contrast with other forms of FMO it does not seem to CC be a drug-metabolizing enzyme (By similarity). CC -!- CATALYTIC ACTIVITY: N,N-dimethylaniline + NADPH + O(2) = N,N- CC dimethylaniline N-oxide + NADP(+) + H(2)O. CC -!- COFACTOR: FAD. CC -!- SUBCELLULAR LOCATION: Microsome membrane. Endoplasmic reticulum CC membrane (By similarity). CC -!- SIMILARITY: Belongs to the FMO family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U90535; AAB50013.1; -; mRNA. DR EMBL; AK133675; BAE21778.1; -; mRNA. DR EMBL; CH466620; EDL38939.1; -; Genomic_DNA. DR EMBL; BC022991; AAH22991.1; -; mRNA. DR RefSeq; NP_001155235.1; NM_001161763.1. DR RefSeq; NP_001155237.1; NM_001161765.1. DR RefSeq; NP_034362.2; NM_010232.4. DR RefSeq; XP_006501058.1; XM_006500995.1. DR UniGene; Mm.385180; -. DR ProteinModelPortal; P97872; -. DR SMR; P97872; 1-490. DR IntAct; P97872; 8. DR MINT; MINT-1858630; -. DR PhosphoSite; P97872; -. DR PaxDb; P97872; -. DR PRIDE; P97872; -. DR Ensembl; ENSMUST00000029729; ENSMUSP00000029729; ENSMUSG00000028088. DR Ensembl; ENSMUST00000107049; ENSMUSP00000102664; ENSMUSG00000028088. DR Ensembl; ENSMUST00000107050; ENSMUSP00000102665; ENSMUSG00000028088. DR GeneID; 14263; -. DR KEGG; mmu:14263; -. DR UCSC; uc008qoy.2; mouse. DR CTD; 2330; -. DR MGI; MGI:1310004; Fmo5. DR eggNOG; COG2072; -. DR GeneTree; ENSGT00740000115132; -. DR HOGENOM; HOG000076537; -. DR HOVERGEN; HBG002037; -. DR InParanoid; Q8R1W6; -. DR KO; K00485; -. DR OMA; NREMCRY; -. DR OrthoDB; EOG7GXPB6; -. DR TreeFam; TF105285; -. DR NextBio; 285611; -. DR PRO; PR:P97872; -. DR ArrayExpress; P97872; -. DR Bgee; P97872; -. DR CleanEx; MM_FMO5; -. DR Genevestigator; P97872; -. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. DR GO; GO:0004499; F:N,N-dimethylaniline monooxygenase activity; IEA:UniProtKB-EC. DR GO; GO:0050661; F:NADP binding; IEA:InterPro. DR Gene3D; 3.40.50.720; -; 2. DR InterPro; IPR012143; DiMe-aniline_mOase. DR InterPro; IPR000960; Flavin_mOase. DR InterPro; IPR020946; Flavin_mOase-like. DR InterPro; IPR002257; Flavin_mOase_5. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Pfam; PF00743; FMO-like; 1. DR PIRSF; PIRSF000332; FMO; 1. DR PRINTS; PR00370; FMOXYGENASE. DR PRINTS; PR01125; FMOXYGENASE5. PE 2: Evidence at transcript level; KW Complete proteome; Endoplasmic reticulum; FAD; Flavoprotein; Membrane; KW Methylation; Microsome; Monooxygenase; NADP; Oxidoreductase; KW Reference proteome; Transmembrane. FT CHAIN 1 533 Dimethylaniline monooxygenase [N-oxide- FT forming] 5. FT /FTId=PRO_0000147666. FT NP_BIND 10 15 FAD (Potential). FT NP_BIND 192 197 NADP (By similarity). FT MOD_RES 5 5 Omega-N-methylated arginine (By FT similarity). FT CONFLICT 313 313 V -> I (in Ref. 1; AAB50013). FT CONFLICT 450 450 L -> Q (in Ref. 1; AAB50013). SQ SEQUENCE 533 AA; 60001 MW; 4B9B246C4D7EBE34 CRC64; MAKKRIAVIG AGASGLTCIK CCLEEGLEPV CFERSGDIGG LWRFQEAPEE GRASIYQSVV INTSKEMMCF SDYPIPDHYP NYMHNSQVLE YFRMYAKEFD LLKYIQFKTT VCSVKKQPDF STSGQWQVVT ECEGKQQVDV FDGVLVCTGH HTDAHLPLES FPGIEKFKGK YFHSRDYKNP VEFTGKRVIV IGIGNSGGDL AVEISHTAKQ VFLSTRRGAW ILNRVGKHGY PIDLLLSSRI MYYLSRICGP SLKNNYMEKQ MNQRFDHEMF GLKPKHRALS QHPTVNDDLP NRIIAGLVKV KGNVKEFTET AAVFEDGSRE DGIDVVIFAT GYSFAFPFLE DSVKVVKNKV SLYKKVFPPN LEKPTLAIIG LIQPLGAIMP ISELQGRWAT QVFKGLKKLP SQSEMMAEIN KAREEMAKRY VDSQRHTIQG DYIDTMEEIA DLVGVRPNIL PLVFTDPRLA LRLLLGPCTP VQYRLQGPGK WAGARKTILT TEDRVRKPLM TRVVERDSSG GSLVTVRVLM LAVAFFAVIL AYF // ID FRDA_MOUSE Reviewed; 207 AA. AC O35943; DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1998, sequence version 1. DT 19-FEB-2014, entry version 105. DE RecName: Full=Frataxin, mitochondrial; DE Short=Fxn; DE EC=1.16.3.1; DE Contains: DE RecName: Full=Frataxin intermediate form; DE Contains: DE RecName: Full=Frataxin mature form; DE Flags: Precursor; GN Name=Fxn; Synonyms=Frda; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, RP AND DEVELOPMENTAL STAGE. RC TISSUE=Embryo; RX PubMed=9241270; DOI=10.1038/ng0897-345; RA Koutnikova H., Campuzano V., Foury F., Dolle P., Cazzalini O., RA Koenig M.; RT "Studies of human, mouse and yeast homologues indicate a mitochondrial RT function for frataxin."; RL Nat. Genet. 16:345-351(1997). RN [2] RP SUBUNIT. RX PubMed=11823441; DOI=10.1093/hmg/11.3.217; RA Cavadini P., O'Neill H.A., Benada O., Isaya G.; RT "Assembly and iron-binding properties of human frataxin, the protein RT deficient in Friedreich ataxia."; RL Hum. Mol. Genet. 11:217-227(2002). RN [3] RP SUBCELLULAR LOCATION. RX PubMed=17597094; DOI=10.1093/hmg/ddm163; RA Martelli A., Wattenhofer-Donze M., Schmucker S., Bouvet S., RA Reutenauer L., Puccio H.; RT "Frataxin is essential for extramitochondrial Fe-S cluster proteins in RT mammalian tissues."; RL Hum. Mol. Genet. 16:2651-2658(2007). RN [4] RP PROTEOLYTIC PROCESSING. RX PubMed=18725397; DOI=10.1093/hmg/ddn244; RA Schmucker S., Argentini M., Carelle-Calmels N., Martelli A., RA Puccio H.; RT "The in vivo mitochondrial two-step maturation of human frataxin."; RL Hum. Mol. Genet. 17:3521-3531(2008). RN [5] RP DISRUPTION PHENOTYPE. RX PubMed=19629184; DOI=10.1371/journal.pone.0006379; RA Calmels N., Schmucker S., Wattenhofer-Donze M., Martelli A., RA Vaucamps N., Reutenauer L., Messaddeq N., Bouton C., Koenig M., RA Puccio H.; RT "The first cellular models based on frataxin missense mutations that RT reproduce spontaneously the defects associated with Friedreich RT ataxia."; RL PLoS ONE 4:E6379-E6379(2009). RN [6] RP FUNCTION. RX PubMed=19805308; DOI=10.1073/pnas.0906784106; RA Huang M.L., Becker E.M., Whitnall M., Rahmanto Y.S., Ponka P., RA Richardson D.R.; RT "Elucidation of the mechanism of mitochondrial iron loading in RT Friedreich's ataxia by analysis of a mouse mutant."; RL Proc. Natl. Acad. Sci. U.S.A. 106:16381-16386(2009). CC -!- FUNCTION: Promotes the biosynthesis of heme and assembly and CC repair of iron-sulfur clusters by delivering Fe(2+) to proteins CC involved in these pathways. May play a role in the protection CC against iron-catalyzed oxidative stress through its ability to CC catalyze the oxidation of Fe(2+) to Fe(3+); the oligomeric form CC but not the monomeric form has in vitro ferroxidase activity. May CC be able to store large amounts of iron in the form of a CC ferrihydrite mineral by oligomerization. Modulates the RNA-binding CC activity of ACO1 (By similarity). CC -!- CATALYTIC ACTIVITY: 4 Fe(2+) + 4 H(+) + O(2) = 4 Fe(3+) + 2 H(2)O. CC -!- SUBUNIT: Monomer (probable predominant form). Oligomer. Interacts CC with LYRM4 AND HSPA9. Interacts with ACO1. Interacts with ISCU. CC Interacts with FECH; one iron-bound FXN monomer seems to interact CC with a FECH homodimer. Interacts with SDHA and SDHB. Interacts CC with ACO2; the interaction is dependent on citrate (By CC similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Mitochondrion. CC Note=PubMed:17597094 describes localization exclusively in CC mitochondria. CC -!- TISSUE SPECIFICITY: Heart, liver, skeletal muscle, kidney, spleen CC and thymus. Weakly expressed in the brain and lung. CC -!- DEVELOPMENTAL STAGE: Expression in the ventricular zone which CC corresponds to dividing neuronal precursors begins at day 12.5, CC increases during embryonic development and persists at postnatal CC day 7 (P7) in the ependymal layer, which is the remenant of the CC ventricular zone. Weak expression seen in the spinal cord and CC medulla oblongata, starting at embryonic day 14.5 (E14.5) and CC expression also observed in dorsal root ganglia, starting at CC E14.5. At P14, expression in the dorsal root ganglia is restricted CC to the cortical region where the sensory neuron cell bodies are CC located. In non-neural tissues strong expression seen in the CC developing liver from E10.5. Expression detected in the heart and CC in the cortex of the developing kidney at E12.5 and later. Very CC high expression observed in the brown adipose tissue. Expression CC seen in small islands around the neck and back at E14.5, then in CC large masses at E16.5 and E18.5 and at P14 is absent in brown CC adipose tissue. Expression also seen in the thymus and developing CC gut at E14.5 and until postnatal life. At P14, expression in CC thymus is restricted to the proliferating cells in the cortical CC zone and is also prominent in the spleen. Found in the lung at CC E14.5. CC -!- PTM: Processed in two steps by mitochondrial processing peptidase CC (MPP). MPP first cleaves the precursor to intermediate form and CC subsequently converts the intermediate to yield frataxin mature CC form (By similarity). CC -!- DISRUPTION PHENOTYPE: Loss of cell division and lethal in CC fibroblasts. CC -!- SIMILARITY: Belongs to the frataxin family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U95736; AAB67778.1; -; mRNA. DR RefSeq; NP_032070.1; NM_008044.2. DR UniGene; Mm.7319; -. DR ProteinModelPortal; O35943; -. DR SMR; O35943; 86-205. DR IntAct; O35943; 2. DR MINT; MINT-1847605; -. DR PhosphoSite; O35943; -. DR PaxDb; O35943; -. DR PRIDE; O35943; -. DR Ensembl; ENSMUST00000081333; ENSMUSP00000080081; ENSMUSG00000059363. DR GeneID; 14297; -. DR KEGG; mmu:14297; -. DR UCSC; uc008hao.1; mouse. DR CTD; 2395; -. DR MGI; MGI:1096879; Fxn. DR eggNOG; COG1965; -. DR HOGENOM; HOG000190729; -. DR HOVERGEN; HBG005745; -. DR InParanoid; O35943; -. DR OMA; KQSVCLM; -. DR OrthoDB; EOG7HHWVD; -. DR TreeFam; TF318958; -. DR NextBio; 285709; -. DR PRO; PR:O35943; -. DR ArrayExpress; O35943; -. DR Bgee; O35943; -. DR CleanEx; MM_FXN; -. DR Genevestigator; O35943; -. DR GO; GO:0005829; C:cytosol; IEA:Ensembl. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:Ensembl. DR GO; GO:0008199; F:ferric iron binding; IEA:InterPro. DR GO; GO:0008198; F:ferrous iron binding; IEA:Ensembl. DR GO; GO:0004322; F:ferroxidase activity; IEA:UniProtKB-EC. DR GO; GO:0034986; F:iron chaperone activity; IEA:Ensembl. DR GO; GO:0007628; P:adult walking behavior; IMP:MGI. DR GO; GO:0009060; P:aerobic respiration; IMP:MGI. DR GO; GO:0006879; P:cellular iron ion homeostasis; IMP:MGI. DR GO; GO:0070301; P:cellular response to hydrogen peroxide; IEA:Ensembl. DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:MGI. DR GO; GO:0006783; P:heme biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW. DR GO; GO:0018283; P:iron incorporation into metallo-sulfur cluster; IEA:Ensembl. DR GO; GO:0016226; P:iron-sulfur cluster assembly; IMP:MGI. DR GO; GO:0007005; P:mitochondrion organization; IMP:MGI. DR GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl. DR GO; GO:0040015; P:negative regulation of multicellular organism growth; IMP:MGI. DR GO; GO:0046621; P:negative regulation of organ growth; IMP:MGI. DR GO; GO:0090201; P:negative regulation of release of cytochrome c from mitochondria; IEA:Ensembl. DR GO; GO:0006119; P:oxidative phosphorylation; IMP:MGI. DR GO; GO:0030307; P:positive regulation of cell growth; IEA:Ensembl. DR GO; GO:0008284; P:positive regulation of cell proliferation; IEA:Ensembl. DR GO; GO:0051349; P:positive regulation of lyase activity; IEA:Ensembl. DR GO; GO:0048554; P:positive regulation of metalloenzyme activity; IEA:Ensembl. DR GO; GO:0051353; P:positive regulation of oxidoreductase activity; IEA:Ensembl. DR GO; GO:0051347; P:positive regulation of transferase activity; IEA:Ensembl. DR GO; GO:0019230; P:proprioception; IMP:MGI. DR GO; GO:0016540; P:protein autoprocessing; IEA:Ensembl. DR GO; GO:0010722; P:regulation of ferrochelatase activity; IEA:Ensembl. DR GO; GO:0010039; P:response to iron ion; IEA:Ensembl. DR Gene3D; 3.30.920.10; -; 1. DR InterPro; IPR017789; Frataxin. DR InterPro; IPR002908; Frataxin/CyaY. DR InterPro; IPR020895; Frataxin_CS. DR PANTHER; PTHR16821; PTHR16821; 1. DR Pfam; PF01491; Frataxin_Cyay; 1. DR PRINTS; PR00904; FRATAXIN. DR SUPFAM; SSF55387; SSF55387; 1. DR TIGRFAMs; TIGR03421; FeS_CyaY; 1. DR TIGRFAMs; TIGR03422; mito_frataxin; 1. DR PROSITE; PS01344; FRATAXIN_1; 1. DR PROSITE; PS50810; FRATAXIN_2; 1. PE 1: Evidence at protein level; KW Complete proteome; Cytoplasm; Heme biosynthesis; Ion transport; Iron; KW Iron storage; Iron transport; Metal-binding; Mitochondrion; KW Oxidoreductase; Reference proteome; Transit peptide; Transport. FT TRANSIT 1 40 Mitochondrion (By similarity). FT CHAIN 41 207 Frataxin intermediate form. FT /FTId=PRO_0000010132. FT CHAIN 78 207 Frataxin mature form (By similarity). FT /FTId=PRO_0000399390. SQ SEQUENCE 207 AA; 22924 MW; C46FD21B44FB26A2 CRC64; MWAFGGRAAV GLLPRTASRA SAWVGNPRWR EPIVTCGRRG LHVTVNAGAT RHAHLNLHYL QILNIKKQSV CVVHLRNLGT LDNPSSLDET AYERLAEETL DSLAEFFEDL ADKPYTLEDY DVSFGDGVLT IKLGGDLGTY VINKQTPNKQ IWLSSPSSGP KRYDWTGKNW VYSHDGVSLH ELLARELTKA LNTKLDLSSL AYSGKGT // ID FRIH_MOUSE Reviewed; 182 AA. AC P09528; Q3UI44; DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 19-MAR-2014, entry version 136. DE RecName: Full=Ferritin heavy chain; DE Short=Ferritin H subunit; DE EC=1.16.3.1; DE Contains: DE RecName: Full=Ferritin heavy chain, N-terminally processed; GN Name=Fth1; Synonyms=Fth; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=BALB/c; RX PubMed=2798146; DOI=10.1093/nar/17.19.8005; RA Yachaou A., Renaudie F., Grandchamp B., Beaumont C.; RT "Nucleotide sequence of the mouse ferritin H chain gene."; RL Nucleic Acids Res. 17:8005-8005(1989). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=ICR; TISSUE=Macrophage; RX PubMed=3194211; DOI=10.1093/nar/16.21.10373; RA Miyazaki Y., Setoguchi M., Higuchi Y., Yoshida S., Akizuki S., RA Yamamoto S.; RT "Nucleotide sequence of cDNA encoding the heavy subunit of mouse RT macrophage ferritin."; RL Nucleic Acids Res. 16:10373-10373(1988). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=3410854; RA Torti S.V., Kwak E.L., Miller S.C., Miller L.L., Ringold G.M., RA Myambo K.B., Young A.P., Torti F.M.; RT "The molecular cloning and characterization of murine ferritin heavy RT chain, a tumor necrosis factor-inducible gene."; RL J. Biol. Chem. 263:12638-12644(1988). RN [4] RP NUCLEOTIDE SEQUENCE. RX PubMed=2258056; DOI=10.1016/0378-1119(90)90396-9; RA Kwak E.L., Torti S.V., Torti F.M.; RT "Murine ferritin heavy chain: isolation and characterization of a RT functional gene."; RL Gene 94:255-261(1990). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=2708374; RA Beaumont C., Dugast I., Renaudie F., Souroujon M., Grandchamp B.; RT "Transcriptional regulation of ferritin H and L subunits in adult RT erythroid and liver cells from the mouse. Unambiguous identification RT of mouse ferritin subunits and in vitro formation of the ferritin RT shells."; RL J. Biol. Chem. 264:7498-7504(1989). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Amnion, Heart, and Kidney; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Mammary tumor; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [8] RP PROTEIN SEQUENCE OF 11-23 AND 55-64, AND MASS SPECTROMETRY. RC TISSUE=Hippocampus; RA Lubec G., Klug S.; RL Submitted (MAR-2007) to UniProtKB. RN [9] RP DISRUPTION PHENOTYPE, AND DEVELOPMENTAL STAGE. RX PubMed=10652280; DOI=10.1074/jbc.275.5.3021; RA Ferreira C., Bucchini D., Martin M.E., Levi S., Arosio P., RA Grandchamp B., Beaumont C.; RT "Early embryonic lethality of H ferritin gene deletion in mice."; RL J. Biol. Chem. 275:3021-3024(2000). RN [10] RP DISRUPTION PHENOTYPE. RX PubMed=11468145; DOI=10.1182/blood.V98.3.525; RA Ferreira C., Santambrogio P., Martin M.E., Andrieu V., Feldmann G., RA Henin D., Beaumont C.; RT "H ferritin knockout mice: a model of hyperferritinemia in the absence RT of iron overload."; RL Blood 98:525-532(2001). RN [11] RP FUNCTION. RX PubMed=19154717; DOI=10.1016/j.devcel.2008.12.002; RA Li J.Y., Paragas N., Ned R.M., Qiu A., Viltard M., Leete T., RA Drexler I.R., Chen X., Sanna-Cherchi S., Mohammed F., Williams D., RA Lin C.S., Schmidt-Ott K.M., Andrews N.C., Barasch J.; RT "Scara5 is a ferritin receptor mediating non-transferrin iron RT delivery."; RL Dev. Cell 16:35-46(2009). CC -!- FUNCTION: Stores iron in a soluble, non-toxic, readily available CC form. Important for iron homeostasis. Has ferroxidase activity. CC Iron is taken up in the ferrous form and deposited as ferric CC hydroxides after oxidation. Also plays a role in delivery of iron CC to cells. Mediates iron uptake in capsule cells of the developing CC kidney. CC -!- CATALYTIC ACTIVITY: 4 Fe(2+) + 4 H(+) + O(2) = 4 Fe(3+) + 2 H(2)O. CC -!- SUBUNIT: Oligomer of 24 subunits. There are two types of subunits: CC L (light) chain and H (heavy) chain. The major chain can be light CC or heavy, depending on the species and tissue type. The functional CC molecule forms a roughly spherical shell with a diameter of 12 nm CC and contains a central cavity into which the insoluble mineral CC iron core is deposited. CC -!- DEVELOPMENTAL STAGE: At 9.5 dpc, detected at low levels in the CC developing heart and central nervous system. At later stages of CC development, widely expressed, predominantly in the heart and CC brown fat tissue. CC -!- DISRUPTION PHENOTYPE: Homozygous mutant embryos die in utero CC between 3.5 and 9.5 dpc (PubMed:10652280). Heterozygous animals CC are healthy and fertile and do not present any apparent CC abnormalities. They show slightly elevated tissue light chain CC ferritin content and 7- to 10-fold more light chain ferritin in CC the serum than normal mice, but their serum iron remains CC unchanged. CC -!- SIMILARITY: Belongs to the ferritin family. CC -!- SIMILARITY: Contains 1 ferritin-like diiron domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X52561; CAA36795.1; -; Genomic_DNA. DR EMBL; X12812; CAA31300.1; -; mRNA. DR EMBL; J03941; AAA37611.1; -; mRNA. DR EMBL; M60170; AAA37613.1; -; Genomic_DNA. DR EMBL; M24509; AAA37612.1; -; mRNA. DR EMBL; AK027998; BAC25694.1; -; mRNA. DR EMBL; AK139622; BAE24084.1; -; mRNA. DR EMBL; AK147082; BAE27662.1; -; mRNA. DR EMBL; AK150262; BAE29419.1; -; mRNA. DR EMBL; AK150508; BAE29621.1; -; mRNA. DR EMBL; AK150628; BAE29718.1; -; mRNA. DR EMBL; AK150679; BAE29759.1; -; mRNA. DR EMBL; AK150693; BAE29772.1; -; mRNA. DR EMBL; AK151192; BAE30189.1; -; mRNA. DR EMBL; AK151241; BAE30233.1; -; mRNA. DR EMBL; AK151399; BAE30367.1; -; mRNA. DR EMBL; AK151609; BAE30548.1; -; mRNA. DR EMBL; AK151675; BAE30600.1; -; mRNA. DR EMBL; AK152071; BAE30924.1; -; mRNA. DR EMBL; AK152542; BAE31297.1; -; mRNA. DR EMBL; AK152702; BAE31431.1; -; mRNA. DR EMBL; AK153017; BAE31651.1; -; mRNA. DR EMBL; AK153195; BAE31795.1; -; mRNA. DR EMBL; AK153199; BAE31799.1; -; mRNA. DR EMBL; AK159243; BAE34925.1; -; mRNA. DR EMBL; AK168601; BAE40468.1; -; mRNA. DR EMBL; AK169004; BAE40803.1; -; mRNA. DR EMBL; BC012314; AAH12314.1; -; mRNA. DR PIR; S06070; S06070. DR RefSeq; NP_034369.1; NM_010239.2. DR UniGene; Mm.1776; -. DR ProteinModelPortal; P09528; -. DR SMR; P09528; 7-177. DR IntAct; P09528; 4. DR MINT; MINT-1856685; -. DR STRING; 10090.ENSMUSP00000025563; -. DR PhosphoSite; P09528; -. DR REPRODUCTION-2DPAGE; P09528; -. DR PaxDb; P09528; -. DR PRIDE; P09528; -. DR Ensembl; ENSMUST00000025563; ENSMUSP00000025563; ENSMUSG00000024661. DR GeneID; 14319; -. DR KEGG; mmu:14319; -. DR UCSC; uc008got.1; mouse. DR CTD; 2495; -. DR MGI; MGI:95588; Fth1. DR eggNOG; COG1528; -. DR GeneTree; ENSGT00700000104283; -. DR HOGENOM; HOG000223383; -. DR HOVERGEN; HBG000410; -. DR InParanoid; P09528; -. DR KO; K00522; -. DR OMA; ASENNDP; -. DR OrthoDB; EOG7DRJ49; -. DR TreeFam; TF313885; -. DR Reactome; REACT_196573; Binding and Uptake of Ligands by Scavenger Receptors. DR ChiTaRS; FTH1; mouse. DR NextBio; 285759; -. DR PRO; PR:P09528; -. DR Bgee; P09528; -. DR CleanEx; MM_FTH1; -. DR Genevestigator; P09528; -. DR GO; GO:0071682; C:endocytic vesicle lumen; TAS:Reactome. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR GO; GO:0008199; F:ferric iron binding; IEA:InterPro. DR GO; GO:0004322; F:ferroxidase activity; IEA:UniProtKB-EC. DR GO; GO:0006955; P:immune response; ISS:UniProtKB. DR GO; GO:0006880; P:intracellular sequestering of iron ion; IEA:Ensembl. DR GO; GO:0006826; P:iron ion transport; IEA:InterPro. DR GO; GO:0008285; P:negative regulation of cell proliferation; ISS:UniProtKB. DR GO; GO:0048147; P:negative regulation of fibroblast proliferation; IEA:Ensembl. DR Gene3D; 1.20.1260.10; -; 1. DR InterPro; IPR001519; Ferritin. DR InterPro; IPR009040; Ferritin-like_diiron. DR InterPro; IPR009078; Ferritin-like_SF. DR InterPro; IPR012347; Ferritin-rel. DR InterPro; IPR014034; Ferritin_CS. DR InterPro; IPR008331; Ferritin_DPS_dom. DR PANTHER; PTHR11431; PTHR11431; 1. DR Pfam; PF00210; Ferritin; 1. DR SUPFAM; SSF47240; SSF47240; 1. DR PROSITE; PS00540; FERRITIN_1; 1. DR PROSITE; PS00204; FERRITIN_2; 1. DR PROSITE; PS50905; FERRITIN_LIKE; 1. PE 1: Evidence at protein level; KW Acetylation; Complete proteome; Direct protein sequencing; Iron; KW Iron storage; Metal-binding; Oxidoreductase; Reference proteome. FT CHAIN 1 182 Ferritin heavy chain. FT /FTId=PRO_0000201049. FT INIT_MET 1 1 Removed; alternate (By similarity). FT CHAIN 2 182 Ferritin heavy chain, N-terminally FT processed. FT /FTId=PRO_0000424473. FT DOMAIN 11 160 Ferritin-like diiron. FT METAL 28 28 Iron 1 (By similarity). FT METAL 63 63 Iron 1 (By similarity). FT METAL 63 63 Iron 2 (By similarity). FT METAL 66 66 Iron 1 (By similarity). FT METAL 108 108 Iron 2 (By similarity). FT METAL 142 142 Iron 2 (By similarity). FT MOD_RES 1 1 N-acetylmethionine (By similarity). FT MOD_RES 2 2 N-acetylthreonine; in Ferritin heavy FT chain, N-terminally processed (By FT similarity). FT CONFLICT 17 17 A -> S (in Ref. 5; AAA37612). FT CONFLICT 137 137 Y -> H (in Ref. 5; AAA37612). FT CONFLICT 140 140 S -> N (in Ref. 5; AAA37612). FT CONFLICT 164 164 A -> S (in Ref. 5; AAA37612). SQ SEQUENCE 182 AA; 21067 MW; 129A8887A2BC650B CRC64; MTTASPSQVR QNYHQDAEAA INRQINLELY ASYVYLSMSC YFDRDDVALK NFAKYFLHQS HEEREHAEKL MKLQNQRGGR IFLQDIKKPD RDDWESGLNA MECALHLEKS VNQSLLELHK LATDKNDPHL CDFIETYYLS EQVKSIKELG DHVTNLRKMG APEAGMAEYL FDKHTLGHGD ES // ID FRRS1_MOUSE Reviewed; 592 AA. AC Q8K385; P97301; Q3TJV0; Q3UMF5; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2002, sequence version 1. DT 19-MAR-2014, entry version 70. DE RecName: Full=Ferric-chelate reductase 1; DE EC=1.-.-.-; DE AltName: Full=Stromal cell-derived receptor 2; DE Short=SDR-2; GN Name=FRRS1; Synonyms=Sdfr2, Sdr2; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY. RX PubMed=8938438; DOI=10.1006/geno.1996.0560; RA Shirozu M., Tada H., Tashiro K., Nakamura T., Lopez N.D., Nazarea M., RA Hamada T., Sato T., Nakano T., Honjo T.; RT "Characterization of novel secreted and membrane proteins isolated by RT the signal sequence trap method."; RL Genomics 37:273-280(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Mammary gland, and Vagina; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Mammary tumor; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP FUNCTION, ENZYME ACTIVITY, TISSUE SPECIFICITY, AND INDUCTION. RX PubMed=14499595; DOI=10.1016/S1570-9639(03)00242-5; RA Vargas J.D., Herpers B., McKie A.T., Gledhill S., McDonnell J., RA van den Heuvel M., Davies K.E., Ponting C.P.; RT "Stromal cell-derived receptor 2 and cytochrome b561 are functional RT ferric reductases."; RL Biochim. Biophys. Acta 1651:116-123(2003). RN [5] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-321 AND ASN-353. RX PubMed=19349973; DOI=10.1038/nbt.1532; RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., RA Schiess R., Aebersold R., Watts J.D.; RT "Mass-spectrometric identification and relative quantification of N- RT linked cell surface glycoproteins."; RL Nat. Biotechnol. 27:378-386(2009). CC -!- FUNCTION: Ferric-chelate reductases reduce Fe(3+) to Fe(2+) before CC its transport from the endosome to the cytoplasm. CC -!- COFACTOR: Binds 2 heme groups non-covalently (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein CC (Potential). CC -!- TISSUE SPECIFICITY: Expressed in spleen, liver and kidney with low CC expression in brain. Localizes in adult brain to the choroid CC plexus of the fourth, third, and lateral ventricles and to CC ependymal cells that line the ventricles. CC -!- INDUCTION: Down-regulated in kidney and liver of mice lacking CC hypotransferrinemic (hpx), which have iron overload of the liver CC and pancreas. CC -!- SIMILARITY: Belongs to the FRRS1 family. CC -!- SIMILARITY: Contains 1 cytochrome b561 domain. CC -!- SIMILARITY: Contains 1 DOMON domain. CC -!- SIMILARITY: Contains 1 reelin domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; D50464; BAA09055.1; -; mRNA. DR EMBL; AK144933; BAE26143.1; -; mRNA. DR EMBL; AK162693; BAE37025.1; -; mRNA. DR EMBL; AK167289; BAE39395.1; -; mRNA. DR EMBL; BC027770; AAH27770.1; -; mRNA. DR RefSeq; NP_001106950.1; NM_001113478.1. DR RefSeq; NP_033172.2; NM_009146.3. DR UniGene; Mm.66293; -. DR ProteinModelPortal; Q8K385; -. DR SMR; Q8K385; 32-157. DR BioGrid; 203144; 1. DR PhosphoSite; Q8K385; -. DR PaxDb; Q8K385; -. DR PRIDE; Q8K385; -. DR Ensembl; ENSMUST00000040260; ENSMUSP00000039487; ENSMUSG00000033386. DR GeneID; 20321; -. DR KEGG; mmu:20321; -. DR UCSC; uc008rcv.2; mouse. DR CTD; 391059; -. DR MGI; MGI:108076; Frrs1. DR eggNOG; NOG281275; -. DR GeneTree; ENSGT00540000071525; -. DR HOGENOM; HOG000112648; -. DR HOVERGEN; HBG107929; -. DR InParanoid; Q8K385; -. DR OrthoDB; EOG7K3TKQ; -. DR TreeFam; TF316169; -. DR NextBio; 298119; -. DR PRO; PR:Q8K385; -. DR Bgee; Q8K385; -. DR CleanEx; MM_FRRS1; -. DR Genevestigator; Q8K385; -. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0000293; F:ferric-chelate reductase activity; IDA:UniProtKB. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR InterPro; IPR006593; Cyt_b561/ferric_Rdtase_TM. DR InterPro; IPR005018; DOMON_domain. DR InterPro; IPR002861; Reeler_dom. DR Pfam; PF03351; DOMON; 1. DR Pfam; PF02014; Reeler; 1. DR SMART; SM00665; B561; 1. DR SMART; SM00664; DoH; 1. DR PROSITE; PS50939; CYTOCHROME_B561; 1. DR PROSITE; PS50836; DOMON; 1. DR PROSITE; PS51019; REELIN; 1. PE 1: Evidence at protein level; KW Complete proteome; Electron transport; Glycoprotein; Heme; Iron; KW Membrane; Metal-binding; Oxidoreductase; Reference proteome; KW Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 592 Ferric-chelate reductase 1. FT /FTId=PRO_0000314844. FT TRANSMEM 2 22 Helical; Name=1; (Potential). FT TRANSMEM 372 392 Helical; Name=2; (Potential). FT TRANSMEM 415 435 Helical; Name=3; (Potential). FT TRANSMEM 446 466 Helical; Name=4; (Potential). FT TRANSMEM 477 499 Helical; Name=5; (Potential). FT TRANSMEM 515 535 Helical; Name=6; (Potential). FT TRANSMEM 569 589 Helical; Name=7; (Potential). FT DOMAIN 13 179 Reelin. FT DOMAIN 216 331 DOMON. FT DOMAIN 335 534 Cytochrome b561. FT METAL 373 373 Iron (heme axial ligand) (Potential). FT METAL 414 414 Iron (heme axial ligand) (Potential). FT METAL 446 446 Iron (heme axial ligand) (Potential). FT METAL 482 482 Iron (heme axial ligand) (Potential). FT CARBOHYD 85 85 N-linked (GlcNAc...) (Potential). FT CARBOHYD 308 308 N-linked (GlcNAc...) (Potential). FT CARBOHYD 321 321 N-linked (GlcNAc...). FT CARBOHYD 353 353 N-linked (GlcNAc...). FT CONFLICT 9 9 S -> R (in Ref. 1; BAA09055). FT CONFLICT 61 61 G -> E (in Ref. 1; BAA09055). FT CONFLICT 65 65 E -> K (in Ref. 2; BAE26143/BAE39395/ FT BAE37025). FT CONFLICT 272 272 P -> S (in Ref. 2; BAE39395/BAE37025). FT CONFLICT 299 299 G -> S (in Ref. 2; BAE39395/BAE37025). FT CONFLICT 419 419 V -> I (in Ref. 1; BAA09055). FT CONFLICT 428 428 A -> G (in Ref. 1; BAA09055). SQ SEQUENCE 592 AA; 66047 MW; EAC9146163E85ED3 CRC64; MAAPQITLSV LVIALLTCSV TAYPNGKVPM SCGGMIPQHN HSPQSEPIHQ ITVSQTTFKP GDQIEVTLSG PPFRGFLLEA RDAENLSGPP IGSFTLIDSE ESQLLTCTDV QGLAVSHTRS SKKTEIKVYW DAPSPAPDHI RFLATVVQKF KIYWVKIPSP VISQPNAPPF TTPKATTQPL TTPPSVSHLT KPFSAFECGN KKFCVRSPLN CDPEKEPACV FLSFTRDNQS VMVEMSGPSD GYVSFAFSHD QWMGDDDAYL CIREDQTVDI QPSYLTGRSY PVMDSRGTLE DMAWRLADGV IQCSFRRNIT LPEAKNRFVL NESYYIFFAE GPSHDGRIFR HSQQPLITYE KYNVTDTPKS VGGSRSSPLL KAHGALMFVA WMTTVSIGVL VARFFRSVWS KAFFLREAAW FQVHRMLMVA TSLLTCVAFV LPFVYRGGWS WRAGYHPYLG CTVMTLAVLQ PLLATFRPPL HDPRRQVFNW THWSVGTAAR IIAVAAMFLG MDLPGLNLPS PQKTYAMMGF VVWHIGTEVI LEIHAYRLSR KVEILDNDRI QILQSLTVAE AEGHVFKKVV LAVYICGNVI FLSIFLSAIN HI // ID FTMT_MOUSE Reviewed; 237 AA. AC Q9D5H4; Q14BZ8; Q3V0N6; Q9D5F4; DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot. DT 26-APR-2005, sequence version 2. DT 19-FEB-2014, entry version 94. DE RecName: Full=Ferritin, mitochondrial; DE EC=1.16.3.1; DE Flags: Precursor; GN Name=Ftmt; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Testis; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: Stores iron in a soluble, non-toxic, readily available CC form. Important for iron homeostasis. Has ferroxidase activity. CC Iron is taken up in the ferrous form and deposited as ferric CC hydroxides after oxidation (By similarity). CC -!- CATALYTIC ACTIVITY: 4 Fe(2+) + 4 H(+) + O(2) = 4 Fe(3+) + 2 H(2)O. CC -!- SUBUNIT: Homooligomer of 24 subunits. The functional molecule is CC roughly spherical and contains a central cavity into which the CC polymeric mineral iron core is deposited (By similarity). CC -!- SUBCELLULAR LOCATION: Mitochondrion (By similarity). CC -!- SIMILARITY: Belongs to the ferritin family. CC -!- SIMILARITY: Contains 1 ferritin-like diiron domain. CC -!- SEQUENCE CAUTION: CC Sequence=BAB29806.1; Type=Erroneous initiation; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK015346; BAB29806.1; ALT_INIT; mRNA. DR EMBL; AK015400; BAB29831.1; -; mRNA. DR EMBL; AK133009; BAE21468.1; -; mRNA. DR EMBL; BC115514; AAI15515.1; -; mRNA. DR EMBL; BC115515; AAI15516.1; -; mRNA. DR RefSeq; NP_080562.2; NM_026286.3. DR UniGene; Mm.179144; -. DR ProteinModelPortal; Q9D5H4; -. DR SMR; Q9D5H4; 62-231. DR PaxDb; Q9D5H4; -. DR PRIDE; Q9D5H4; -. DR Ensembl; ENSMUST00000025388; ENSMUSP00000025388; ENSMUSG00000024510. DR GeneID; 67634; -. DR KEGG; mmu:67634; -. DR UCSC; uc008exc.2; mouse. DR CTD; 94033; -. DR MGI; MGI:1914884; Ftmt. DR eggNOG; COG1528; -. DR GeneTree; ENSGT00700000104283; -. DR HOGENOM; HOG000223383; -. DR HOVERGEN; HBG000410; -. DR InParanoid; Q14BZ8; -. DR KO; K00522; -. DR OMA; FANFYIQ; -. DR OrthoDB; EOG7DRJ49; -. DR TreeFam; TF313885; -. DR NextBio; 325089; -. DR PRO; PR:Q9D5H4; -. DR Bgee; Q9D5H4; -. DR CleanEx; MM_FTMT; -. DR Genevestigator; Q9D5H4; -. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR GO; GO:0008199; F:ferric iron binding; IEA:InterPro. DR GO; GO:0004322; F:ferroxidase activity; TAS:MGI. DR GO; GO:0005506; F:iron ion binding; TAS:MGI. DR GO; GO:0006879; P:cellular iron ion homeostasis; TAS:MGI. DR GO; GO:0006826; P:iron ion transport; IEA:InterPro. DR GO; GO:0008284; P:positive regulation of cell proliferation; IEA:Ensembl. DR GO; GO:0051349; P:positive regulation of lyase activity; IEA:Ensembl. DR GO; GO:0051353; P:positive regulation of oxidoreductase activity; IEA:Ensembl. DR GO; GO:0051347; P:positive regulation of transferase activity; IEA:Ensembl. DR Gene3D; 1.20.1260.10; -; 1. DR InterPro; IPR001519; Ferritin. DR InterPro; IPR009040; Ferritin-like_diiron. DR InterPro; IPR009078; Ferritin-like_SF. DR InterPro; IPR012347; Ferritin-rel. DR InterPro; IPR014034; Ferritin_CS. DR InterPro; IPR008331; Ferritin_DPS_dom. DR PANTHER; PTHR11431; PTHR11431; 1. DR Pfam; PF00210; Ferritin; 1. DR SUPFAM; SSF47240; SSF47240; 1. DR PROSITE; PS00540; FERRITIN_1; 1. DR PROSITE; PS00204; FERRITIN_2; 1. DR PROSITE; PS50905; FERRITIN_LIKE; 1. PE 2: Evidence at transcript level; KW Complete proteome; Iron; Iron storage; Metal-binding; Mitochondrion; KW Oxidoreductase; Reference proteome; Transit peptide. FT TRANSIT 1 49 Mitochondrion (Potential). FT CHAIN 50 237 Ferritin, mitochondrial. FT /FTId=PRO_0000008851. FT DOMAIN 66 215 Ferritin-like diiron. FT METAL 83 83 Iron 1 (By similarity). FT METAL 118 118 Iron 1 (By similarity). FT METAL 118 118 Iron 2 (By similarity). FT METAL 121 121 Iron 1 (By similarity). FT METAL 163 163 Iron 2 (By similarity). FT METAL 197 197 Iron 2 (By similarity). FT CONFLICT 163 163 E -> G (in Ref. 1; BAB29831). FT CONFLICT 164 164 K -> R (in Ref. 1; BAB29806). FT CONFLICT 167 167 N -> T (in Ref. 1; BAB29806). SQ SEQUENCE 237 AA; 27158 MW; 6EC3D9B1539B3B5E CRC64; MLSCFWFFSK HISSALMSLP RVLHRFTAPQ CLASRYPLGP LLASPRRLLA SVASSQDSTR PSRVRQNFHP DSEAAINRQI NLELYASYVY LSMAYYFSRD DVALYNFSKY FLRQSLEERE HAEKLMKLQN QRGGRICLQD IKKPDKDDWE CGLRAMECAL LLEKNVNQSL LDLHTLASEK GDPHLCDFLE THYLHEQVKS IKELGDHVHN LVTMGAPAAG LAEYLFDKHT LGSESKH // ID FTO_MOUSE Reviewed; 502 AA. AC Q8BGW1; Q3TTZ5; Q6ZPI7; Q8BR68; Q8CB66; Q8R250; Q9QZ13; DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 19-MAR-2014, entry version 83. DE RecName: Full=Alpha-ketoglutarate-dependent dioxygenase FTO; DE EC=1.14.11.-; DE AltName: Full=Fat mass and obesity-associated protein; DE AltName: Full=Protein fatso; GN Name=Fto; Synonyms=Kiaa1752; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=10501967; DOI=10.1007/s003359901144; RA Peters T., Ausmeier K., Ruether U.; RT "Cloning of Fatso (Fto), a novel gene deleted by the Fused toes (Ft) RT mouse mutation."; RL Mamm. Genome 10:983-986(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Brain; RX PubMed=14621295; DOI=10.1093/dnares/10.4.167; RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., RA Saga Y., Nagase T., Ohara O., Koga H.; RT "Prediction of the coding sequences of mouse homologues of KIAA gene: RT III. The complete nucleotide sequences of 500 mouse KIAA-homologous RT cDNAs identified by screening of terminal sequences of cDNA clones RT randomly sampled from size-fractionated libraries."; RL DNA Res. 10:167-180(2003). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4). RC STRAIN=C57BL/6J, and NOD; RC TISSUE=Aorta, Bone, Corpora quadrigemina, Skin, Thymus, and Vein; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC STRAIN=C57BL/6, and FVB/N; TISSUE=Brain, and Kidney; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP FUNCTION, COFACTOR, ENZYME REGULATION, SUBCELLULAR LOCATION, RP MUTAGENESIS OF HIS-304 AND ARG-313, INDUCTION, AND TISSUE SPECIFICITY. RX PubMed=17991826; DOI=10.1126/science.1151710; RA Gerken T., Girard C.A., Tung Y.C., Webby C.J., Saudek V., RA Hewitson K.S., Yeo G.S., McDonough M.A., Cunliffe S., McNeill L.A., RA Galvanovskis J., Rorsman P., Robins P., Prieur X., Coll A.P., Ma M., RA Jovanovic Z., Farooqi I.S., Sedgwick B., Barroso I., Lindahl T., RA Ponting C.P., Ashcroft F.M., O'Rahilly S., Schofield C.J.; RT "The obesity-associated FTO gene encodes a 2-oxoglutarate-dependent RT nucleic acid demethylase."; RL Science 318:1469-1472(2007). RN [6] RP FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=18775698; DOI=10.1016/j.febslet.2008.08.019; RA Jia G., Yang C.G., Yang S., Jian X., Yi C., Zhou Z., He C.; RT "Oxidative demethylation of 3-methylthymine and 3-methyluracil in RT single-stranded DNA and RNA by mouse and human FTO."; RL FEBS Lett. 582:3313-3319(2008). RN [7] RP DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, FUNCTION, AND TISSUE RP SPECIFICITY. RX PubMed=19234441; DOI=10.1038/nature07848; RA Fischer J., Koch L., Emmerling C., Vierkotten J., Peters T., RA Bruning J.C., Ruther U.; RT "Inactivation of the Fto gene protects from obesity."; RL Nature 458:894-898(2009). RN [8] RP FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, CIRCULAR DICHROISM, AND RP MUTAGENESIS OF ILE-367. RX PubMed=19680540; DOI=10.1371/journal.pgen.1000599; RA Church C., Lee S., Bagg E.A., McTaggart J.S., Deacon R., Gerken T., RA Lee A., Moir L., Mecinovic J., Quwailid M.M., Schofield C.J., RA Ashcroft F.M., Cox R.D.; RT "A mouse model for the metabolic effects of the human fat mass and RT obesity associated FTO gene."; RL PLoS Genet. 5:E1000599-E1000599(2009). CC -!- FUNCTION: Dioxygenase that repairs alkylated DNA and RNA by CC oxidative demethylation. Has highest activity towards single- CC stranded RNA containing 3-methyluracil, followed by single- CC stranded DNA containing 3-methylthymine. Has low demethylase CC activity towards single-stranded DNA containing 1-methyladenine or CC 3-methylcytosine. Specifically demethylates N(6)-methyladenosine CC (m6A) RNA, the most prevalent internal modification of messenger CC RNA (mRNA) in higher eukaryotes. Has no activity towards 1- CC methylguanine. Has no detectable activity towards double-stranded CC DNA. Requires molecular oxygen, alpha-ketoglutarate and iron. CC Contributes to the regulation of the global metabolic rate, energy CC expenditure and energy homeostasis. Contributes to the regulation CC of body size and body fat accumulation. CC -!- COFACTOR: Binds 1 Fe(2+) ion per subunit. CC -!- ENZYME REGULATION: Activated by ascorbate. Inhibited by N- CC oxalylglycine, fumarate and succinate. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC pH dependence: CC Optimum pH is 5.5-6; CC -!- SUBUNIT: Monomer. May also exist as homodimer. CC -!- SUBCELLULAR LOCATION: Nucleus. Nucleus speckle (By similarity). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; CC IsoId=Q8BGW1-1; Sequence=Displayed; CC Name=2; CC IsoId=Q8BGW1-2; Sequence=VSP_025011; CC Note=No experimental confirmation available; CC Name=3; CC IsoId=Q8BGW1-3; Sequence=VSP_025009, VSP_025010; CC Note=No experimental confirmation available; CC Name=4; CC IsoId=Q8BGW1-4; Sequence=VSP_025007, VSP_025008; CC Note=No experimental confirmation available; CC -!- TISSUE SPECIFICITY: Ubiquitous. Detected in brain, brain cortex, CC hypothalamus, cerebellum, liver, pancreas, heart, kidney, white CC adipose tissue and skeletal muscle. Most abundant in the brain, CC particularly in hypothalamic nuclei governing energy balance. CC -!- INDUCTION: Down-regulated in fasting animals. CC -!- DOMAIN: The 3D-structure of the Fe2OG dioxygenase domain is CC similar to that of the Fe2OG dioxygenase domain found in the CC bacterial DNA repair dioxygenase alkB and its mammalian orthologs, CC but sequence similarity is very low. As a consequence, the domain CC is not detected by protein signature databases (By similarity). CC -!- DISRUPTION PHENOTYPE: Elevated perinatal mortality. Mice have CC normal body weight at birth, but show growth retardation from day CC 2 onwards, resulting in a weight reduction of 30-40% after 6 CC weeks, both in males and females. In addition, animals display CC reduced nose to anus length. Fat mass is reduced by 60% in males CC and by 23% in females. Lean body mass is reduced by 26% in males CC and 19% in females. White adipose tissue decreases more and more CC over time, while brown adipose tissue is not affected. Serum CC leptin levels are decreased, while serum levels of adiponectin are CC increased. Mice exhibit significant hyperphagia after correction CC for body weight. They show increased oxygen consumption, carbon CC dioxide production and heat generation, indicating increased CC energy expenditure, in spite of reduced spontaneous locomotor CC activity. Plasma adrenaline concentrations are significantly CC increased. Overall glucose metabolism appears normal. CC -!- SIMILARITY: Belongs to the fto family. CC -!- SEQUENCE CAUTION: CC Sequence=BAC98247.1; Type=Erroneous initiation; Note=Translation N-terminally shortened; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJ237917; CAB59324.1; -; mRNA. DR EMBL; AK129437; BAC98247.1; ALT_INIT; mRNA. DR EMBL; AK036677; BAC29533.1; -; mRNA. DR EMBL; AK040866; BAC30724.1; -; mRNA. DR EMBL; AK045465; BAC32382.1; -; mRNA. DR EMBL; AK049502; BAC33780.1; -; mRNA. DR EMBL; AK088881; BAC40629.1; -; mRNA. DR EMBL; AK161060; BAE36177.1; -; mRNA. DR EMBL; BC022222; AAH22222.1; -; mRNA. DR EMBL; BC057008; AAH57008.1; -; mRNA. DR RefSeq; NP_036066.2; NM_011936.2. DR UniGene; Mm.4375; -. DR ProteinModelPortal; Q8BGW1; -. DR SMR; Q8BGW1; 30-500. DR PhosphoSite; Q8BGW1; -. DR PaxDb; Q8BGW1; -. DR PRIDE; Q8BGW1; -. DR Ensembl; ENSMUST00000069718; ENSMUSP00000068380; ENSMUSG00000055932. [Q8BGW1-1] DR GeneID; 26383; -. DR KEGG; mmu:26383; -. DR UCSC; uc009msq.2; mouse. [Q8BGW1-4] DR UCSC; uc009msr.2; mouse. [Q8BGW1-3] DR UCSC; uc009mss.2; mouse. [Q8BGW1-2] DR UCSC; uc009mst.2; mouse. [Q8BGW1-1] DR CTD; 79068; -. DR MGI; MGI:1347093; Fto. DR eggNOG; NOG45792; -. DR GeneTree; ENSGT00390000017730; -. DR HOVERGEN; HBG101847; -. DR InParanoid; Q8BGW1; -. DR OMA; AVYNYSC; -. DR OrthoDB; EOG7CK36T; -. DR TreeFam; TF333296; -. DR ChiTaRS; FTO; mouse. DR NextBio; 304305; -. DR PRO; PR:Q8BGW1; -. DR ArrayExpress; Q8BGW1; -. DR Bgee; Q8BGW1; -. DR CleanEx; MM_FTO; -. DR Genevestigator; Q8BGW1; -. DR GO; GO:0016607; C:nuclear speck; ISS:UniProtKB. DR GO; GO:0043734; F:DNA-N1-methyladenine dioxygenase activity; IDA:UniProtKB. DR GO; GO:0008198; F:ferrous iron binding; ISS:UniProtKB. DR GO; GO:0035516; F:oxidative DNA demethylase activity; IDA:BHF-UCL. DR GO; GO:0035515; F:oxidative RNA demethylase activity; IDA:BHF-UCL. DR GO; GO:0060612; P:adipose tissue development; IMP:UniProtKB. DR GO; GO:0006307; P:DNA dealkylation involved in DNA repair; ISS:UniProtKB. DR GO; GO:0035552; P:oxidative single-stranded DNA demethylation; IDA:BHF-UCL. DR GO; GO:0035553; P:oxidative single-stranded RNA demethylation; IDA:BHF-UCL. DR GO; GO:0010883; P:regulation of lipid storage; IMP:UniProtKB. DR GO; GO:0040014; P:regulation of multicellular organism growth; IMP:UniProtKB. DR GO; GO:0044065; P:regulation of respiratory system process; IMP:UniProtKB. DR GO; GO:0070350; P:regulation of white fat cell proliferation; IMP:UniProtKB. DR GO; GO:0042245; P:RNA repair; IDA:BHF-UCL. DR GO; GO:0001659; P:temperature homeostasis; IMP:UniProtKB. DR InterPro; IPR024366; FTO_C. DR InterPro; IPR024367; FTO_cat_dom. DR Pfam; PF12934; FTO_CTD; 1. DR Pfam; PF12933; FTO_NTD; 1. PE 1: Evidence at protein level; KW Acetylation; Alternative splicing; Complete proteome; Dioxygenase; KW DNA damage; DNA repair; Iron; Metal-binding; Nucleus; Obesity; KW Oxidoreductase; Reference proteome; RNA repair. FT CHAIN 1 502 Alpha-ketoglutarate-dependent dioxygenase FT FTO. FT /FTId=PRO_0000286164. FT REGION 42 324 Fe2OG dioxygenase domain (By similarity). FT REGION 210 221 Loop L1; predicted to block binding of FT double-stranded DNA or RNA (By FT similarity). FT REGION 228 231 Substrate binding (By similarity). FT REGION 313 315 Alpha-ketoglutarate binding (By FT similarity). FT METAL 228 228 Iron; catalytic (By similarity). FT METAL 230 230 Iron; catalytic (By similarity). FT METAL 304 304 Iron; catalytic (By similarity). FT BINDING 96 96 Substrate (By similarity). FT BINDING 108 108 Substrate (By similarity). FT BINDING 202 202 Alpha-ketoglutarate (By similarity). FT BINDING 292 292 Alpha-ketoglutarate (By similarity). FT BINDING 317 317 Alpha-ketoglutarate (By similarity). FT BINDING 319 319 Alpha-ketoglutarate (By similarity). FT MOD_RES 213 213 N6-acetyllysine (By similarity). FT VAR_SEQ 296 316 DDLNATHQHCVLAGSQPRFSS -> GNVGSLRVGHLWGFEI FT HFWIL (in isoform 4). FT /FTId=VSP_025007. FT VAR_SEQ 317 502 Missing (in isoform 4). FT /FTId=VSP_025008. FT VAR_SEQ 411 413 TNA -> VSA (in isoform 3). FT /FTId=VSP_025009. FT VAR_SEQ 414 502 Missing (in isoform 3). FT /FTId=VSP_025010. FT VAR_SEQ 453 502 CQSRVVRTLPVQQKPDCRPYWEKDDPSMPLPFDLTDVVSEL FT RGQLLEARS -> FVLLRGGVWCPCPSSARPAQRTKVEDIL FT S (in isoform 2). FT /FTId=VSP_025011. FT MUTAGEN 304 304 H->A: Reduced enzyme activity. FT MUTAGEN 313 313 R->A: Loss of enzyme activity. FT MUTAGEN 367 367 I->A: Reduces enzyme activity by about FT 60%. FT MUTAGEN 367 367 I->F: Alters protein structure and causes FT an increase in whole body metabolism, FT leading to a lean phenotype in adult FT males, but not in females. FT CONFLICT 181 181 G -> R (in Ref. 3; BAC32382). FT CONFLICT 384 384 N -> S (in Ref. 1; CAB59324, 2; BAC98247, FT 3; BAC40629 and 4; AAH22222). FT CONFLICT 410 410 M -> V (in Ref. 2; BAC98247, 3; BAC40629 FT and 4; AAH22222). FT CONFLICT 463 463 V -> A (in Ref. 3; BAC40629 and 4; FT AAH22222). SQ SEQUENCE 502 AA; 58007 MW; 69223B824028D872 CRC64; MKRVQTAEER EREAKKLRLL EELEDTWLPY LTPKDDEFYQ QWQLKYPKLV FREAGSIPEE LHKEVPEAFL TLHKHGCLFR DVVRIQGKDV LTPVSRILIG DPGCTYKYLN TRLFTVPWPV KGCTVKYTEA EIAAACQTFL KLNDYLQVET IQALEELAVR EKANEDAVPL CMAEFPRAGV GPSCDDEVDL KSRAAYNVTL LNFMDPQKMP YLKEEPYFGM GKMAVSWHHD ENLVDRSAVA VYSYSCEGSE DESEDESSFE GRDPDTWHVG FKISWDIETP GLTIPLHQGD CYFMLDDLNA THQHCVLAGS QPRFSSTHRV AECSTGTLDY ILERCQLALQ NVLNDSDDGD VSLKSFDPAV LKQGEEIHNE VEFEWLRQFW FQGNRYKLCT DWWCEPMTHL EGLWKKMESM TNAVLREVKR EGLPVEQRSE ILSAILVPLT VRQNLRKEWH ARCQSRVVRT LPVQQKPDCR PYWEKDDPSM PLPFDLTDVV SELRGQLLEA RS // ID FXRD1_MOUSE Reviewed; 487 AA. AC Q3TQB2; Q8R1D0; DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2005, sequence version 1. DT 19-MAR-2014, entry version 64. DE RecName: Full=FAD-dependent oxidoreductase domain-containing protein 1; DE EC=1.-.-.-; GN Name=Foxred1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC STRAIN=C57BL/6J; TISSUE=Cerebellum, and Lung; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Eye; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- COFACTOR: FAD (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein CC (Potential). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q3TQB2-1; Sequence=Displayed; CC Name=2; CC IsoId=Q3TQB2-2; Sequence=VSP_022630; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK144759; BAE26052.1; -; mRNA. DR EMBL; AK163722; BAE37472.1; -; mRNA. DR EMBL; BC024806; AAH24806.1; -; mRNA. DR RefSeq; NP_758495.1; NM_172291.1. DR RefSeq; XP_006510285.1; XM_006510222.1. DR UniGene; Mm.138512; -. DR ProteinModelPortal; Q3TQB2; -. DR SMR; Q3TQB2; 57-485. DR PhosphoSite; Q3TQB2; -. DR PaxDb; Q3TQB2; -. DR PRIDE; Q3TQB2; -. DR Ensembl; ENSMUST00000043805; ENSMUSP00000038924; ENSMUSG00000039048. [Q3TQB2-2] DR Ensembl; ENSMUST00000127996; ENSMUSP00000118037; ENSMUSG00000039048. [Q3TQB2-1] DR GeneID; 235169; -. DR KEGG; mmu:235169; -. DR UCSC; uc009ost.1; mouse. [Q3TQB2-2] DR UCSC; uc009osu.1; mouse. [Q3TQB2-1] DR CTD; 55572; -. DR MGI; MGI:2446262; Foxred1. DR eggNOG; COG0665; -. DR GeneTree; ENSGT00390000006114; -. DR HOGENOM; HOG000042035; -. DR HOVERGEN; HBG081543; -. DR InParanoid; Q3TQB2; -. DR OMA; QRQEGAK; -. DR TreeFam; TF314003; -. DR ChiTaRS; FOXRED1; mouse. DR NextBio; 382532; -. DR PRO; PR:Q3TQB2; -. DR ArrayExpress; Q3TQB2; -. DR Bgee; Q3TQB2; -. DR CleanEx; MM_FOXRED1; -. DR Genevestigator; Q3TQB2; -. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW. DR InterPro; IPR006076; FAD-dep_OxRdtase. DR Pfam; PF01266; DAO; 1. PE 2: Evidence at transcript level; KW Alternative splicing; Complete proteome; FAD; Flavoprotein; Membrane; KW Oxidoreductase; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 487 FAD-dependent oxidoreductase domain- FT containing protein 1. FT /FTId=PRO_0000274144. FT TRANSMEM 62 82 Helical; (Potential). FT COMPBIAS 368 371 Poly-Glu. FT VAR_SEQ 403 403 E -> EHLLHLQ (in isoform 2). FT /FTId=VSP_022630. SQ SEQUENCE 487 AA; 54178 MW; C3694EF4015CA11F CRC64; MFRRALRLGL GPGLPYRGLR TRKGGFTLDW DAKVSDFKKK VDSILPGKKY EVLYDTSHLP PEQADVVIIG GGILGLSVAF WLKKLESRRG AIRVLVVEQD HTYSRASSTG PSVGGIWQQF SVPENVQLSL FSINFLRNIN EYLAVVDAPP VELQFNPSGC LLLASEKDAA TLENNVKMQR QEGAKVCLMS PEQLQTKFPW INVEGVALAS YGLEDEGWFD AWSLLQGLRR KVQSMGVFFC QGEVTRFITS STPMKTPTGE HVVLRRINNV HVKMDKSLEY QPVECAVVIN AAGAWSGKIA ELAGVGKGLP GTLQGTKLPV EPRKRYVHLW HCPQGPGLET PLVADISGVY FRREGLGSNY LGGCSPTEEE EPDPTNLNVD HDFFQNKVWP HLVQRVPSFK TLEVQSAWAG YYDYNTFDQN GVVGPHPLVV NMYFATGFSG RGLQHAPGIG RAVAEIMLEG HFKTIDMSPF LFTRFYLGEK LQEYNIL // ID G3PT_MOUSE Reviewed; 440 AA. AC Q64467; Q60650; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 19-FEB-2014, entry version 125. DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase, testis-specific; DE EC=1.2.1.12; DE AltName: Full=Spermatogenic cell-specific glyceraldehyde 3-phosphate dehydrogenase 2; DE Short=GAPDH-2; DE AltName: Full=Spermatogenic glyceraldehyde-3-phosphate dehydrogenase; GN Name=Gapdhs; Synonyms=Gapd-s, Gapds; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=CD-1; TISSUE=Testis; RX PubMed=1375514; RA Welch J.E., Schatte E.C., O'Brien D.A., Eddy E.M.; RT "Expression of a glyceraldehyde 3-phosphate dehydrogenase gene RT specific to mouse spermatogenic cells."; RL Biol. Reprod. 46:869-878(1992). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ICR X Swiss Webster; TISSUE=Testis; RX PubMed=7736666; DOI=10.1002/dvg.1020160210; RA Welch J.E., Brown P.R., O'Brien D.A., Eddy E.M.; RT "Genomic organization of a mouse glyceraldehyde 3-phosphate RT dehydrogenase gene (Gapd-s) expressed in post-meiotic spermatogenic RT cells."; RL Dev. Genet. 16:179-189(1995). RN [3] RP FUNCTION, AND DISRUPTION PHENOTYPE. RX PubMed=15546993; DOI=10.1073/pnas.0407708101; RA Miki K., Qu W., Goulding E.H., Willis W.D., Bunch D.O., Strader L.F., RA Perreault S.D., Eddy E.M., O'Brien D.A.; RT "Glyceraldehyde 3-phosphate dehydrogenase-S, a sperm-specific RT glycolytic enzyme, is required for sperm motility and male RT fertility."; RL Proc. Natl. Acad. Sci. U.S.A. 101:16501-16506(2004). CC -!- FUNCTION: May play an important role in regulating the switch CC between different pathways for energy production during CC spermiogenesis and in the spermatozoon. Required for sperm CC motility and male fertility. CC -!- CATALYTIC ACTIVITY: D-glyceraldehyde 3-phosphate + phosphate + CC NAD(+) = 3-phospho-D-glyceroyl phosphate + NADH. CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D- CC glyceraldehyde 3-phosphate: step 1/5. CC -!- SUBUNIT: Homotetramer (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- TISSUE SPECIFICITY: Testis specific. CC -!- DEVELOPMENTAL STAGE: First expressed at day 20 in post-meiotic CC germ cells. Levels increase until day 24 and then remain constant CC during maturity. CC -!- DOMAIN: The testis-specific N-terminal extension mediates tight CC association with the cytoskeletal fibrous sheath of the CC spermatozoa flagellum, possibly via interchain disulfide-bonding CC of Cys-33 with sheath components (By similarity). CC -!- DISRUPTION PHENOTYPE: Mice display greatly reduced ATP levels in CC sperm, severely impaired sperm motility and are infertile. CC -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate CC dehydrogenase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M60978; AAA53033.1; -; mRNA. DR EMBL; U09964; AAA80276.1; -; Genomic_DNA. DR PIR; I49681; I49681. DR RefSeq; NP_032111.1; NM_008085.1. DR UniGene; Mm.436562; -. DR ProteinModelPortal; Q64467; -. DR SMR; Q64467; 108-440. DR IntAct; Q64467; 2. DR MINT; MINT-4095460; -. DR PhosphoSite; Q64467; -. DR PaxDb; Q64467; -. DR PRIDE; Q64467; -. DR DNASU; 14447; -. DR Ensembl; ENSMUST00000074758; ENSMUSP00000074317; ENSMUSG00000061099. DR GeneID; 14447; -. DR KEGG; mmu:14447; -. DR CTD; 26330; -. DR MGI; MGI:95653; Gapdhs. DR eggNOG; COG0057; -. DR GeneTree; ENSGT00720000108591; -. DR HOGENOM; HOG000071678; -. DR HOVERGEN; HBG000227; -. DR InParanoid; Q64467; -. DR KO; K10705; -. DR OrthoDB; EOG7Q5HDF; -. DR TreeFam; TF300533; -. DR UniPathway; UPA00109; UER00184. DR ChiTaRS; GAPDHS; mouse. DR NextBio; 286061; -. DR PRO; PR:Q64467; -. DR Bgee; Q64467; -. DR Genevestigator; Q64467; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0035686; C:sperm fibrous sheath; IDA:MGI. DR GO; GO:0097228; C:sperm principal piece; IDA:MGI. DR GO; GO:0004365; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity; TAS:UniProtKB. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR GO; GO:0050661; F:NADP binding; IEA:InterPro. DR GO; GO:0006096; P:glycolysis; IMP:MGI. DR GO; GO:0045821; P:positive regulation of glycolysis; TAS:UniProtKB. DR GO; GO:0030317; P:sperm motility; IDA:UniProtKB. DR GO; GO:0007286; P:spermatid development; IEA:Ensembl. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR020831; GlycerAld/Erythrose_P_DH. DR InterPro; IPR020830; GlycerAld_3-P_DH_AS. DR InterPro; IPR020829; GlycerAld_3-P_DH_cat. DR InterPro; IPR020828; GlycerAld_3-P_DH_NAD(P)-bd. DR InterPro; IPR006424; Glyceraldehyde-3-P_DH_1. DR InterPro; IPR016040; NAD(P)-bd_dom. DR PANTHER; PTHR10836; PTHR10836; 1. DR Pfam; PF02800; Gp_dh_C; 1. DR Pfam; PF00044; Gp_dh_N; 1. DR PRINTS; PR00078; G3PDHDRGNASE. DR SMART; SM00846; Gp_dh_N; 1. DR TIGRFAMs; TIGR01534; GAPDH-I; 1. DR PROSITE; PS00071; GAPDH; 1. PE 2: Evidence at transcript level; KW Complete proteome; Cytoplasm; Glycolysis; NAD; Oxidoreductase; KW Reference proteome. FT CHAIN 1 440 Glyceraldehyde-3-phosphate dehydrogenase, FT testis-specific. FT /FTId=PRO_0000145504. FT NP_BIND 117 118 NAD (By similarity). FT REGION 1 105 Testis-specific N-terminal extension (By FT similarity). FT REGION 255 257 Glyceraldehyde 3-phosphate binding (By FT similarity). FT REGION 315 316 Glyceraldehyde 3-phosphate binding (By FT similarity). FT COMPBIAS 21 41 Cys/Pro-rich. FT COMPBIAS 54 73 Poly-Pro. FT COMPBIAS 84 100 Poly-Pro. FT ACT_SITE 256 256 Nucleophile (By similarity). FT BINDING 138 138 NAD (By similarity). FT BINDING 183 183 NAD; via carbonyl oxygen (By similarity). FT BINDING 205 205 NAD (By similarity). FT BINDING 225 225 NAD (By similarity). FT BINDING 286 286 Glyceraldehyde 3-phosphate (By FT similarity). FT BINDING 338 338 Glyceraldehyde 3-phosphate (By FT similarity). FT BINDING 420 420 NAD (By similarity). FT SITE 283 283 Activates thiol group during catalysis FT (By similarity). FT CONFLICT 33 34 Missing (in Ref. 2; AAA80276). FT CONFLICT 43 43 L -> V (in Ref. 2; AAA80276). SQ SEQUENCE 440 AA; 47657 MW; 05FF0A093D1ABD9C CRC64; MSRRDVVLTN VTVVQLRRDR CPCPCPCPCP CPCPVIRPPP PKLEDPPPTV EEQPPPPPPP PPPPPPPPPP PPPQIEPDKF EEAPPPPPPP PPPPPPPPPP LQKPARELTV GINGFGRIGR LVLRVCMEKG IRVVAVNDPF IDPEYMVYMF KYDSTHGRYK GNVEHKNGQL VVDNLEINTY QCKDPKEIPW SSIGNPYVVE CTGVYLSIEA ASAHISSGAR RVVVTAPSPD APMFVMGVNE KDYNPGSMTI VSNASCTTNC LAPLAKVIHE NFGIVEGLMT TVHSYTATQK TVDGPSKKDW RGGRGAHQNI IPSSTGAAKA VGKVIPELKG KLTGMAFRVP TPNVSVVDLT CRLAKPASYS AITEAVKAAA KGPLAGILAY TEDQVVSTDF NGNPHSSIFD AKAGIALNDN FVKLVAWYDN EYGYSNRVVD LLRYMFSREK // ID G3P_MOUSE Reviewed; 333 AA. AC P16858; A6H6A8; Q0QEU0; Q3THM2; Q3TUI2; Q3UMT2; Q4V783; Q569X2; AC Q569X5; Q5U410; DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 19-MAR-2014, entry version 147. DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase; DE Short=GAPDH; DE EC=1.2.1.12; DE AltName: Full=Peptidyl-cysteine S-nitrosylase GAPDH; DE EC=2.6.99.-; GN Name=Gapdh; Synonyms=Gapd; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=2145197; DOI=10.1016/0378-1119(90)90087-8; RA Sabath D.E., Broome H.E., Prystowsky M.B.; RT "Glyceraldehyde-3-phosphate dehydrogenase mRNA is a major interleukin RT 2-induced transcript in a cloned T-helper lymphocyte."; RL Gene 91:185-191(1990). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=BALB/c, C57BL/6J, and DBA/2; RC TISSUE=Cerebellum, Eye, Head, Kidney, and Lung; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=129, C57BL/6, C57BL/6J, Czech II, FVB/N, and FVB/N-3; RC TISSUE=Brain, Colon, Embryo, Eye, Mammary gland, and Mammary tumor; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP PROTEIN SEQUENCE OF 4-11; 27-50; 65-78; 85-105; 116-137; 144-189; RP 199-213; 218-246 AND 262-333, AND MASS SPECTROMETRY. RC STRAIN=C57BL/6, and OF1; TISSUE=Brain, and Hippocampus; RA Lubec G., Kang S.U., Klug S., Yang J.W., Zigmond M., Sunyer B., RA Chen W.-Q.; RL Submitted (JAN-2009) to UniProtKB. RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] OF 24-249. RX PubMed=16751257; DOI=10.1093/molbev/msl027; RA Kullberg M., Nilsson M.A., Arnason U., Harley E.H., Janke A.; RT "Housekeeping genes for phylogenetic analysis of eutherian RT relationships."; RL Mol. Biol. Evol. 23:1493-1503(2006). RN [7] RP CATALYTIC ACTIVITY, SULFHYDRATION AT CYS-150, AND MUTAGENESIS OF RP CYS-150. RX PubMed=19903941; DOI=10.1126/scisignal.2000464; RA Mustafa A.K., Gadalla M.M., Sen N., Kim S., Mu W., Gazi S.K., RA Barrow R.K., Yang G., Wang R., Snyder S.H.; RT "H2S signals through protein S-sulfhydration."; RL Sci. Signal. 2:RA72-RA72(2009). RN [8] RP FUNCTION, SUBUNIT, AND RECONSTITUTION OF THE GAIT COMPLEX. RX PubMed=23071094; DOI=10.1128/MCB.01168-12; RA Arif A., Chatterjee P., Moodt R.A., Fox P.L.; RT "Heterotrimeric GAIT complex drives transcript-selective translation RT inhibition in murine macrophages."; RL Mol. Cell. Biol. 32:5046-5055(2012). CC -!- FUNCTION: Has both glyceraldehyde-3-phosphate dehydrogenase and CC nitrosylase activities, thereby playing a role in glycolysis and CC nuclear functions, respectively. Glyceraldehyde-3-phosphate CC dehydrogenase is a key enzyme in glycolysis that catalyzes the CC first step of the pathway by converting D-glyceraldehyde 3- CC phosphate (G3P) into 3-phospho-D-glyceroyl phosphate. Modulates CC the organization and assembly of the cytoskeleton. Facilitates the CC CHP1-dependent microtubule and membrane associations through its CC ability to stimulate the binding of CHP1 to microtubules. Also CC participates in nuclear events including transcription, RNA CC transport, DNA replication and apoptosis. Nuclear functions are CC probably due to the nitrosylase activity that mediates cysteine S- CC nitrosylation of nuclear target proteins such as SIRT1, HDAC2 and CC PRKDC. Component of the GAIT (gamma interferon-activated inhibitor CC of translation) complex which mediates interferon-gamma-induced CC transcript-selective translation inhibition in inflammation CC processes. Upon interferon-gamma treatment assembles into the GAIT CC complex which binds to stem loop-containing GAIT elements in the CC 3'-UTR of diverse inflammatory mRNAs (such as ceruplasmin) and CC suppresses their translation. CC -!- CATALYTIC ACTIVITY: D-glyceraldehyde 3-phosphate + phosphate + CC NAD(+) = 3-phospho-D-glyceroyl phosphate + NADH. CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D- CC glyceraldehyde 3-phosphate: step 1/5. CC -!- SUBUNIT: Homotetramer. Interacts with EIF1AD, USP25, PRKCI and CC WARS. Interacts with TPPP; the interaction is direct. Interacts CC (when S-nitrosylated) with SIAH1; leading to nuclear CC translocation. Interacts with RILPL1/GOSPEL, leading to prevent CC the interaction between GAPDH and SIAH1 and prevent nuclear CC translocation. Interacts with CHP1; the interaction increases the CC binding of CHP1 with microtubules. Associates with microtubules CC (By similarity). Component of the GAIT complex. CC -!- INTERACTION: CC Q08460:Kcnma1; NbExp=3; IntAct=EBI-444871, EBI-1633915; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol (By similarity). Nucleus CC (By similarity). Cytoplasm, cytoskeleton (By similarity). CC Note=Translocates to the nucleus following S-nitrosylation and CC interaction with SIAH1, which contains a nuclear localization CC signal (By similarity). CC -!- PTM: ISGylated (By similarity). CC -!- PTM: S-nitrosylation of Cys-150 leads to interaction with SIAH1, CC followed by translocation to the nucleus (By similarity). CC -!- PTM: Sulfhydration at Cys-150 increases catalytic activity. CC -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate CC dehydrogenase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M32599; AAA37659.1; -; mRNA. DR EMBL; AK002273; BAB21979.1; -; mRNA. DR EMBL; AK081405; BAC38211.1; -; mRNA. DR EMBL; AK140794; BAE24481.1; -; mRNA. DR EMBL; AK144690; BAE26016.1; -; mRNA. DR EMBL; AK146435; BAE27169.1; -; mRNA. DR EMBL; AK147738; BAE28105.1; -; mRNA. DR EMBL; AK147891; BAE28208.1; -; mRNA. DR EMBL; AK160399; BAE35768.1; -; mRNA. DR EMBL; AK160753; BAE35989.1; -; mRNA. DR EMBL; AK164415; BAE37778.1; -; mRNA. DR EMBL; AK168217; BAE40174.1; -; mRNA. DR EMBL; AL662926; CAI25599.1; -; Genomic_DNA. DR EMBL; BC082592; AAH82592.1; -; mRNA. DR EMBL; BC083065; AAH83065.1; -; mRNA. DR EMBL; BC083079; AAH83079.1; -; mRNA. DR EMBL; BC083080; AAH83080.1; -; mRNA. DR EMBL; BC083149; AAH83149.1; -; mRNA. DR EMBL; BC085274; AAH85274.1; -; mRNA. DR EMBL; BC085275; AAH85275.1; -; mRNA. DR EMBL; BC085315; AAH85315.1; -; mRNA. DR EMBL; BC091768; AAH91768.1; -; mRNA. DR EMBL; BC092252; AAH92252.1; -; mRNA. DR EMBL; BC092264; AAH92264.1; -; mRNA. DR EMBL; BC092267; AAH92267.1; -; mRNA. DR EMBL; BC092294; AAH92294.1; -; mRNA. DR EMBL; BC093508; AAH93508.1; -; mRNA. DR EMBL; BC094037; AAH94037.1; -; mRNA. DR EMBL; BC095932; AAH95932.1; -; mRNA. DR EMBL; BC096440; AAH96440.1; -; mRNA. DR EMBL; BC096590; AAH96590.1; -; mRNA. DR EMBL; BC110311; AAI10312.1; -; mRNA. DR EMBL; BC145810; AAI45811.1; -; mRNA. DR EMBL; BC145812; AAI45813.1; -; mRNA. DR EMBL; DQ403054; ABD77187.1; -; mRNA. DR PIR; JT0553; DEMSG. DR RefSeq; NP_032110.1; NM_008084.3. DR RefSeq; XP_001476757.1; XM_001476707.4. DR UniGene; Mm.304088; -. DR UniGene; Mm.309092; -. DR UniGene; Mm.317779; -. DR UniGene; Mm.343110; -. DR UniGene; Mm.392463; -. DR UniGene; Mm.458138; -. DR UniGene; Mm.458416; -. DR ProteinModelPortal; P16858; -. DR SMR; P16858; 2-333. DR BioGrid; 199829; 5. DR BioGrid; 785307; 1. DR IntAct; P16858; 17. DR MINT; MINT-1869564; -. DR PhosphoSite; P16858; -. DR REPRODUCTION-2DPAGE; P16858; -. DR REPRODUCTION-2DPAGE; Q5U410; -. DR SWISS-2DPAGE; P16858; -. DR PaxDb; P16858; -. DR PRIDE; P16858; -. DR Ensembl; ENSMUST00000073605; ENSMUSP00000073289; ENSMUSG00000057666. DR Ensembl; ENSMUST00000118875; ENSMUSP00000113213; ENSMUSG00000057666. DR GeneID; 100042025; -. DR GeneID; 14433; -. DR KEGG; mmu:100042025; -. DR KEGG; mmu:14433; -. DR UCSC; uc007igj.1; mouse. DR CTD; 2597; -. DR MGI; MGI:95640; Gapdh. DR eggNOG; COG0057; -. DR GeneTree; ENSGT00720000108591; -. DR HOVERGEN; HBG000227; -. DR InParanoid; A6H6A8; -. DR KO; K00134; -. DR OMA; FTLENMV; -. DR OrthoDB; EOG7Q5HDF; -. DR TreeFam; TF300533; -. DR SABIO-RK; P16858; -. DR UniPathway; UPA00109; UER00184. DR NextBio; 286057; -. DR PRO; PR:P16858; -. DR Bgee; P16858; -. DR CleanEx; MM_GAPDH; -. DR Genevestigator; P16858; -. DR GO; GO:0005829; C:cytosol; ISS:UniProtKB. DR GO; GO:0097452; C:GAIT complex; IDA:UniProtKB. DR GO; GO:0015630; C:microtubule cytoskeleton; ISS:UniProtKB. DR GO; GO:0005634; C:nucleus; ISS:UniProtKB. DR GO; GO:0004365; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity; IDA:UniProtKB. DR GO; GO:0008017; F:microtubule binding; ISS:UniProtKB. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR GO; GO:0050661; F:NADP binding; IEA:InterPro. DR GO; GO:0035605; F:peptidyl-cysteine S-nitrosylase activity; ISS:UniProtKB. DR GO; GO:0006096; P:glycolysis; IEA:UniProtKB-UniPathway. DR GO; GO:0000226; P:microtubule cytoskeleton organization; ISS:UniProtKB. DR GO; GO:0017148; P:negative regulation of translation; IDA:UniProtKB. DR GO; GO:0051402; P:neuron apoptotic process; ISS:UniProtKB. DR GO; GO:0035606; P:peptidyl-cysteine S-trans-nitrosylation; ISS:UniProtKB. DR GO; GO:0050821; P:protein stabilization; ISS:UniProtKB. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR020831; GlycerAld/Erythrose_P_DH. DR InterPro; IPR020830; GlycerAld_3-P_DH_AS. DR InterPro; IPR020829; GlycerAld_3-P_DH_cat. DR InterPro; IPR020828; GlycerAld_3-P_DH_NAD(P)-bd. DR InterPro; IPR006424; Glyceraldehyde-3-P_DH_1. DR InterPro; IPR016040; NAD(P)-bd_dom. DR PANTHER; PTHR10836; PTHR10836; 1. DR Pfam; PF02800; Gp_dh_C; 1. DR Pfam; PF00044; Gp_dh_N; 1. DR PIRSF; PIRSF000149; GAP_DH; 1. DR PRINTS; PR00078; G3PDHDRGNASE. DR SMART; SM00846; Gp_dh_N; 1. DR TIGRFAMs; TIGR01534; GAPDH-I; 1. DR PROSITE; PS00071; GAPDH; 1. PE 1: Evidence at protein level; KW Acetylation; ADP-ribosylation; Apoptosis; Complete proteome; KW Cytoplasm; Cytoskeleton; Direct protein sequencing; Glycolysis; KW Methylation; NAD; Nucleus; Oxidoreductase; Phosphoprotein; KW Reference proteome; S-nitrosylation; Transferase; KW Translation regulation; Ubl conjugation. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 333 Glyceraldehyde-3-phosphate dehydrogenase. FT /FTId=PRO_0000145490. FT NP_BIND 11 12 NAD (By similarity). FT REGION 2 146 Interaction with WARS (By similarity). FT REGION 149 151 Glyceraldehyde 3-phosphate binding (By FT similarity). FT REGION 209 210 Glyceraldehyde 3-phosphate binding (By FT similarity). FT ACT_SITE 150 150 Nucleophile (By similarity). FT BINDING 33 33 NAD (By similarity). FT BINDING 78 78 NAD; via carbonyl oxygen (By similarity). FT BINDING 120 120 NAD (By similarity). FT BINDING 180 180 Glyceraldehyde 3-phosphate (By FT similarity). FT BINDING 232 232 Glyceraldehyde 3-phosphate (By FT similarity). FT BINDING 314 314 NAD (By similarity). FT SITE 177 177 Activates thiol group during catalysis FT (By similarity). FT MOD_RES 3 3 N6,N6-dimethyllysine (By similarity). FT MOD_RES 7 7 Deamidated asparagine (By similarity). FT MOD_RES 40 40 Phosphotyrosine (By similarity). FT MOD_RES 59 59 N6-acetyllysine (By similarity). FT MOD_RES 62 62 Deamidated asparagine (By similarity). FT MOD_RES 64 64 N6,N6-dimethyllysine (By similarity). FT MOD_RES 68 68 Deamidated asparagine (By similarity). FT MOD_RES 73 73 Phosphothreonine (By similarity). FT MOD_RES 120 120 Phosphoserine (By similarity). FT MOD_RES 146 146 Phosphoserine (By similarity). FT MOD_RES 147 147 Deamidated asparagine (By similarity). FT MOD_RES 149 149 Phosphoserine (By similarity). FT MOD_RES 150 150 ADP-ribosylcysteine; by autocatalysis; in FT irreversibly inhibited form (By FT similarity). FT MOD_RES 150 150 Cysteine persulfide. FT MOD_RES 150 150 S-nitrosocysteine; in reversibly FT inhibited form (By similarity). FT MOD_RES 153 153 Deamidated asparagine (By similarity). FT MOD_RES 182 182 Phosphothreonine (By similarity). FT MOD_RES 192 192 N6,N6-dimethyllysine; alternate (By FT similarity). FT MOD_RES 192 192 N6-acetyllysine; alternate (By FT similarity). FT MOD_RES 192 192 N6-malonyllysine; alternate (By FT similarity). FT MOD_RES 209 209 Phosphothreonine (By similarity). FT MOD_RES 213 213 N6,N6-dimethyllysine; alternate (By FT similarity). FT MOD_RES 213 213 N6-malonyllysine; alternate (By FT similarity). FT MOD_RES 217 217 N6-acetyllysine (By similarity). FT MOD_RES 223 223 Deamidated asparagine (By similarity). FT MOD_RES 225 225 N6,N6-dimethyllysine; alternate (By FT similarity). FT MOD_RES 225 225 N6-acetyllysine; alternate (By FT similarity). FT MOD_RES 227 227 Phosphothreonine (By similarity). FT MOD_RES 235 235 Phosphothreonine (By similarity). FT MOD_RES 252 252 N6-acetyllysine (By similarity). FT MOD_RES 258 258 N6,N6-dimethyllysine (By similarity). FT MOD_RES 261 261 N6,N6-dimethyllysine (By similarity). FT MOD_RES 310 310 Phosphoserine (By similarity). FT MOD_RES 314 314 Deamidated asparagine (By similarity). FT MOD_RES 332 332 N6,N6-dimethyllysine (By similarity). FT MUTAGEN 150 150 C->S: Abolishes sulfhydration and induces FT impaired enzyme activity. FT CONFLICT 3 3 K -> E (in Ref. 2; BAE40174). FT CONFLICT 30 30 A -> V (in Ref. 4; AAH92267). FT CONFLICT 82 82 N -> S (in Ref. 2; BAE35989). FT CONFLICT 84 84 K -> E (in Ref. 2; BAE40174). FT CONFLICT 89 89 G -> S (in Ref. 2; BAE26016). FT CONFLICT 91 91 E -> K (in Ref. 2; BAE35989). FT CONFLICT 134 134 N -> D (in Ref. 4; AAH85315). FT CONFLICT 195 195 R -> C (in Ref. 4; AAH85315). FT CONFLICT 300 300 A -> S (in Ref. 4; AAH85315). SQ SEQUENCE 333 AA; 35810 MW; F25131EFFA9F2BD6 CRC64; MVKVGVNGFG RIGRLVTRAA ICSGKVEIVA INDPFIDLNY MVYMFQYDST HGKFNGTVKA ENGKLVINGK PITIFQERDP TNIKWGEAGA EYVVESTGVF TTMEKAGAHL KGGAKRVIIS APSADAPMFV MGVNHEKYDN SLKIVSNASC TTNCLAPLAK VIHDNFGIVE GLMTTVHAIT ATQKTVDGPS GKLWRDGRGA AQNIIPASTG AAKAVGKVIP ELNGKLTGMA FRVPTPNVSV VDLTCRLEKP AKYDDIKKVV KQASEGPLKG ILGYTEDQVV SCDFNSNSHS STFDAGAGIA LNDNFVKLIS WYDNEYGYSN RVVDLMAYMA SKE // ID G6PD2_MOUSE Reviewed; 513 AA. AC P97324; Q0VB18; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 19-FEB-2014, entry version 121. DE RecName: Full=Glucose-6-phosphate 1-dehydrogenase 2; DE Short=G6PD; DE EC=1.1.1.49; GN Name=G6pd2; Synonyms=G6pd-2; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, RP SUBUNIT, AND TISSUE SPECIFICITY. RC STRAIN=Swiss; RX PubMed=9169132; DOI=10.1006/geno.1997.4673; RA Hendriksen P.J.M., Hoogerbrugge J.W., Baarends W.M., de Boer P., RA Vreeburg J.T.M., Vos E.A., van der Lende T., Grootegoed A.J.; RT "Testis-specific expression of a functional retroposon encoding RT glucose-6-phosphate dehydrogenase in the mouse."; RL Genomics 41:350-359(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Testis; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: Catalyzes the rate-limiting step of the oxidative CC pentose-phosphate pathway, which represents a route for the CC dissimilation of carbohydrates besides glycolysis. The main CC function of this enzyme is to provide reducing power (NADPH) and CC pentose phosphates for fatty acid and nucleic acid synthesis. CC -!- CATALYTIC ACTIVITY: D-glucose 6-phosphate + NADP(+) = 6-phospho-D- CC glucono-1,5-lactone + NADPH. CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D- CC ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): CC step 1/3. CC -!- SUBUNIT: Homotetramer; dimer of dimers. CC -!- TISSUE SPECIFICITY: Testis. CC -!- MISCELLANEOUS: Has NADP both as cofactor (bound to the N-terminal CC domain) and as structural element bound to the C-terminal domain. CC -!- SIMILARITY: Belongs to the glucose-6-phosphate dehydrogenase CC family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; Z84471; CAB06476.1; -; Genomic_DNA. DR EMBL; BC120827; AAI20828.1; -; mRNA. DR EMBL; BC137684; AAI37685.1; -; mRNA. DR RefSeq; NP_062341.2; NM_019468.2. DR UniGene; Mm.347430; -. DR ProteinModelPortal; P97324; -. DR SMR; P97324; 28-505. DR STRING; 10090.ENSMUSP00000113269; -. DR PhosphoSite; P97324; -. DR PaxDb; P97324; -. DR PRIDE; P97324; -. DR GeneID; 14380; -. DR KEGG; mmu:14380; -. DR CTD; 14380; -. DR MGI; MGI:105977; G6pd2. DR eggNOG; COG0364; -. DR HOGENOM; HOG000046192; -. DR HOVERGEN; HBG000856; -. DR InParanoid; Q0VB18; -. DR KO; K00036; -. DR UniPathway; UPA00115; UER00408. DR NextBio; 285889; -. DR PRO; PR:P97324; -. DR CleanEx; MM_G6PD2; -. DR Genevestigator; P97324; -. DR GO; GO:0004345; F:glucose-6-phosphate dehydrogenase activity; ISS:UniProtKB. DR GO; GO:0050661; F:NADP binding; IEA:InterPro. DR GO; GO:0051156; P:glucose 6-phosphate metabolic process; ISS:UniProtKB. DR GO; GO:0006739; P:NADP metabolic process; ISS:UniProtKB. DR GO; GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.720; -; 1. DR HAMAP; MF_00966; G6PD; 1. DR InterPro; IPR001282; G6P_DH. DR InterPro; IPR022675; G6P_DH_C. DR InterPro; IPR022674; G6P_DH_NAD-bd. DR InterPro; IPR016040; NAD(P)-bd_dom. DR PANTHER; PTHR23429; PTHR23429; 1. DR Pfam; PF02781; G6PD_C; 1. DR Pfam; PF00479; G6PD_N; 1. DR PIRSF; PIRSF000110; G6PD; 1. DR PRINTS; PR00079; G6PDHDRGNASE. DR TIGRFAMs; TIGR00871; zwf; 1. PE 1: Evidence at protein level; KW Carbohydrate metabolism; Complete proteome; Glucose metabolism; NADP; KW Oxidoreductase; Reference proteome. FT CHAIN 1 513 Glucose-6-phosphate 1-dehydrogenase 2. FT /FTId=PRO_0000068086. FT NP_BIND 38 45 NADP 1 (By similarity). FT NP_BIND 401 403 NADP 2 (By similarity). FT NP_BIND 421 423 NADP 2 (By similarity). FT REGION 201 205 Substrate binding (By similarity). FT ACT_SITE 263 263 Proton acceptor (By similarity). FT BINDING 72 72 NADP 1 (By similarity). FT BINDING 147 147 NADP 1 (By similarity). FT BINDING 171 171 NADP 1; via carbonyl oxygen (By FT similarity). FT BINDING 171 171 Substrate (By similarity). FT BINDING 239 239 Substrate (By similarity). FT BINDING 258 258 Substrate (By similarity). FT BINDING 357 357 NADP 2 (By similarity). FT BINDING 360 360 Substrate (By similarity). FT BINDING 365 365 Substrate (By similarity). FT BINDING 366 366 NADP 2 (By similarity). FT BINDING 370 370 NADP 2 (By similarity). FT BINDING 393 393 NADP 2 (By similarity). FT BINDING 395 395 Substrate (By similarity). FT BINDING 487 487 NADP 2 (By similarity). FT BINDING 503 503 NADP 2 (By similarity). SQ SEQUENCE 513 AA; 59126 MW; 655830EB767B6C53 CRC64; MAEQVTLSRT QVCGILREEL YQNDAFHQAD THIFIIMGAS GDLAKKKIYP TIWWLFRDGL LPKETFIVGY ARSQLTVDDI QKQSEPFFKA TPEERPKLEE FFTRNSYVVG QYDDPASYKH LNSYINALHQ GMQANHLFYL ALPPTVYEAV TKNIQETCMS QTGFNRIIVE KPFGRDLQSS NQLSNHISSL FREDQIYRID HYLDKEMVQN LMVLRFANRI FGPIWNGDNI VCVILTFKEP FGTEGRGGYF DEFGIIRDVM QSHLLQMLCL VAMEKPATTD SDDVRNEKVK VLKCISEVET DNVILGQYVG NPNGEGEAAN GYLDDPTVPR GSTTATFAAA VLYVKNERWD GVPFILRCGK ALNERKAEVR LQFRDIPGDI FHQKCKRNEL VIRMQPNEAV YTTMMTKKPG MFFNPEESEL DLTYGNKYKN VKLPGAYERL ILDVFCGCQM HFVRTDELRE GWRIFTPLLH KIEREKPQPF PYVYGSRGPT EADELMRRVG FQYKGTYKGT HKH // ID G6PD1_MOUSE Reviewed; 515 AA. AC Q00612; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 20-MAR-2007, sequence version 3. DT 19-MAR-2014, entry version 130. DE RecName: Full=Glucose-6-phosphate 1-dehydrogenase X; DE Short=G6PD; DE EC=1.1.1.49; GN Name=G6pdx; Synonyms=G6pd, G6pd-1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=8400362; RA Zollo M.Z., D'Urso M., Schlessinger D., Chen E.Y.; RT "Sequence of mouse glucose-6-phosphate dehydrogenase cDNA."; RL DNA Seq. 3:319-322(1993). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=NOD; TISSUE=Thymus; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-40. RC STRAIN=BALB/c; RX PubMed=1874446; DOI=10.1016/0378-1119(91)90078-P; RA Toniolo D., Filippi M., Dono R., Lettieri T., Martini G.; RT "The CpG island in the 5' region of the G6PD gene of man and mouse."; RL Gene 102:197-203(1991). RN [4] RP PROTEIN SEQUENCE OF 57-71; 175-191 AND 247-257, AND MASS SPECTROMETRY. RC TISSUE=Brain, and Hippocampus; RA Lubec G., Klug S., Yang J.W., Zigmond M.; RL Submitted (JUL-2007) to UniProtKB. RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 163-214 AND 352-454. RC STRAIN=BALB/c; RX PubMed=9330624; DOI=10.1016/S0027-5107(97)00109-7; RA Kuraguchi M., Thomas G.A., Williams E.D.; RT "Somatic mutation of the glucose-6-phosphate dehydrogenase (g6pd) gene RT in colonic stem cells and crypt restricted loss of G6PD activity."; RL Mutat. Res. 379:69-75(1997). RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-507, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Mast cell; RX PubMed=17947660; RA Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., RA Kawakami T., Salomon A.R.; RT "Quantitative time-resolved phosphoproteomic analysis of mast cell RT signaling."; RL J. Immunol. 179:5864-5876(2007). CC -!- FUNCTION: Catalyzes the rate-limiting step of the oxidative CC pentose-phosphate pathway, which represents a route for the CC dissimilation of carbohydrates besides glycolysis. The main CC function of this enzyme is to provide reducing power (NADPH) and CC pentose phosphates for fatty acid and nucleic acid synthesis (By CC similarity). CC -!- CATALYTIC ACTIVITY: D-glucose 6-phosphate + NADP(+) = 6-phospho-D- CC glucono-1,5-lactone + NADPH. CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D- CC ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): CC step 1/3. CC -!- SUBUNIT: Homotetramer; dimer of dimers (By similarity). CC -!- MISCELLANEOUS: Has NADP both as cofactor (bound to the N-terminal CC domain) and as structural element bound to the C-terminal domain. CC -!- SIMILARITY: Belongs to the glucose-6-phosphate dehydrogenase CC family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; Z11911; CAA77967.1; -; mRNA. DR EMBL; AK088135; BAC40166.1; -; mRNA. DR EMBL; X53617; CAA37679.1; -; Genomic_DNA. DR EMBL; U88533; AAB52998.1; -; Genomic_DNA. DR EMBL; U88534; AAB52999.1; -; Genomic_DNA. DR PIR; A56686; A56686. DR RefSeq; NP_032088.1; NM_008062.2. DR UniGene; Mm.27210; -. DR ProteinModelPortal; Q00612; -. DR SMR; Q00612; 28-515. DR IntAct; Q00612; 3. DR MINT; MINT-4095477; -. DR PhosphoSite; Q00612; -. DR REPRODUCTION-2DPAGE; IPI00228385; -. DR REPRODUCTION-2DPAGE; Q00612; -. DR PaxDb; Q00612; -. DR PRIDE; Q00612; -. DR Ensembl; ENSMUST00000004327; ENSMUSP00000004327; ENSMUSG00000031400. DR GeneID; 14381; -. DR KEGG; mmu:14381; -. DR UCSC; uc009toy.1; mouse. DR CTD; 14381; -. DR MGI; MGI:105979; G6pdx. DR eggNOG; COG0364; -. DR HOGENOM; HOG000046192; -. DR HOVERGEN; HBG000856; -. DR InParanoid; Q00612; -. DR KO; K00036; -. DR OMA; AVVFKRA; -. DR OrthoDB; EOG7DRJ2T; -. DR TreeFam; TF300584; -. DR UniPathway; UPA00115; UER00408. DR NextBio; 285893; -. DR PRO; PR:Q00612; -. DR ArrayExpress; Q00612; -. DR Bgee; Q00612; -. DR CleanEx; MM_G6PDX; -. DR Genevestigator; Q00612; -. DR GO; GO:0004345; F:glucose-6-phosphate dehydrogenase activity; IDA:MGI. DR GO; GO:0050661; F:NADP binding; IEA:InterPro. DR GO; GO:0001998; P:angiotensin mediated vasoconstriction involved in regulation of systemic arterial blood pressure; IMP:MGI. DR GO; GO:0048821; P:erythrocyte development; IMP:MGI. DR GO; GO:0051156; P:glucose 6-phosphate metabolic process; ISS:UniProtKB. DR GO; GO:0006749; P:glutathione metabolic process; IMP:MGI. DR GO; GO:0032613; P:interleukin-10 production; IMP:MGI. DR GO; GO:0032615; P:interleukin-12 production; IMP:MGI. DR GO; GO:0006741; P:NADP biosynthetic process; IDA:MGI. DR GO; GO:0019322; P:pentose biosynthetic process; IDA:MGI. DR GO; GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-UniPathway. DR GO; GO:0040014; P:regulation of multicellular organism growth; IMP:MGI. DR GO; GO:0006979; P:response to oxidative stress; IMP:MGI. DR GO; GO:0002033; P:vasodilation by angiotensin involved in regulation of systemic arterial blood pressure; IMP:MGI. DR Gene3D; 3.40.50.720; -; 1. DR HAMAP; MF_00966; G6PD; 1. DR InterPro; IPR001282; G6P_DH. DR InterPro; IPR019796; G6P_DH_AS. DR InterPro; IPR022675; G6P_DH_C. DR InterPro; IPR022674; G6P_DH_NAD-bd. DR InterPro; IPR016040; NAD(P)-bd_dom. DR PANTHER; PTHR23429; PTHR23429; 1. DR Pfam; PF02781; G6PD_C; 1. DR Pfam; PF00479; G6PD_N; 1. DR PIRSF; PIRSF000110; G6PD; 1. DR PRINTS; PR00079; G6PDHDRGNASE. DR TIGRFAMs; TIGR00871; zwf; 1. DR PROSITE; PS00069; G6P_DEHYDROGENASE; 1. PE 1: Evidence at protein level; KW Acetylation; Carbohydrate metabolism; Complete proteome; KW Direct protein sequencing; Glucose metabolism; NADP; Oxidoreductase; KW Phosphoprotein; Reference proteome. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 515 Glucose-6-phosphate 1-dehydrogenase X. FT /FTId=PRO_0000068085. FT NP_BIND 38 45 NADP 1 (By similarity). FT NP_BIND 401 403 NADP 2 (By similarity). FT NP_BIND 421 423 NADP 2 (By similarity). FT REGION 201 205 Substrate binding (By similarity). FT ACT_SITE 263 263 Proton acceptor (By similarity). FT BINDING 72 72 NADP 1 (By similarity). FT BINDING 147 147 NADP 1 (By similarity). FT BINDING 171 171 NADP 1; via carbonyl oxygen (By FT similarity). FT BINDING 171 171 Substrate (By similarity). FT BINDING 239 239 Substrate (By similarity). FT BINDING 258 258 Substrate (By similarity). FT BINDING 357 357 NADP 2 (By similarity). FT BINDING 360 360 Substrate (By similarity). FT BINDING 365 365 Substrate (By similarity). FT BINDING 366 366 NADP 2 (By similarity). FT BINDING 370 370 NADP 2 (By similarity). FT BINDING 393 393 NADP 2 (By similarity). FT BINDING 395 395 Substrate (By similarity). FT BINDING 487 487 NADP 2 (By similarity). FT BINDING 503 503 NADP 2 (By similarity). FT BINDING 509 509 NADP 2 (By similarity). FT MOD_RES 2 2 N-acetylalanine (By similarity). FT MOD_RES 507 507 Phosphotyrosine. FT CONFLICT 24 24 D -> Y (in Ref. 3; CAA37679). SQ SEQUENCE 515 AA; 59263 MW; C8AF0D4099B7AEC3 CRC64; MAEQVALSRT QVCGILREEL YQGDAFHQAD THIFIIMGAS GDLAKKKIYP TIWWLFRDGL LPEDTFIVGY ARSRLTVDDI RKQSEPFFKA TPEERPKLEE FFARNSYVAG QYDDAASYKH LNSHMNALHQ GMQANRLFYL ALPPTVYEAV TKNIQETCMS QTGWNRIIVE KPFGRDLQSS NQLSNHISSL FREDQIYRID HYLGKEMVQN LMVLRFANRI FGPIWNRDNI ACVILTFKEP FGTEGRGGYF DEFGIIRDVM QNHLLQMLCL VAMEKPATTG SDDVRDEKVK VLKCISEVET DNVVLGQYVG NPNGEGEAAN GYLDDPTVPH GSTTATFAAA VLYVENERWD GVPFILRCGK ALNERKAEVR LQFRDVAGDI FHQQCKRNEL VIRVQPNEAV YTKMMTKKPG MFFNPEESEL DLTYGNRYKN VKLPDAYERL ILDVFCGSQM HFVRSDELRE AWRIFTPLLH KIDREKPQPI PYVYGSRGPT EADELMKRVG FQYEGTYKWV NPHKL // ID G6PE_MOUSE Reviewed; 789 AA. AC Q8CFX1; A2A7A9; B2KGW7; Q8BLH1; DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 2. DT 19-MAR-2014, entry version 87. DE RecName: Full=GDH/6PGL endoplasmic bifunctional protein; DE Includes: DE RecName: Full=Glucose 1-dehydrogenase; DE EC=1.1.1.47; DE AltName: Full=Hexose-6-phosphate dehydrogenase; DE Includes: DE RecName: Full=6-phosphogluconolactonase; DE Short=6PGL; DE EC=3.1.1.31; DE Flags: Precursor; GN Name=H6pd; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Liver; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-205 AND LYS-424, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., RA Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). CC -!- FUNCTION: Oxidizes glucose-6-phosphate and glucose, as well as CC other hexose-6-phosphates (By similarity). CC -!- CATALYTIC ACTIVITY: Beta-D-glucose + NAD(P)(+) = D-glucono-1,5- CC lactone + NAD(P)H. CC -!- CATALYTIC ACTIVITY: D-glucose 6-phosphate + NAD(P)(+) = D-glucono- CC 1,5-lactone 6-phosphate + NAD(P)H. CC -!- CATALYTIC ACTIVITY: 6-phospho-D-glucono-1,5-lactone + H(2)O = 6- CC phospho-D-gluconate. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen (By similarity). CC Note=Microsomes, endoplasmic reticulum lumen (By similarity). CC -!- SIMILARITY: In the N-terminal section; belongs to the glucose-6- CC phosphate dehydrogenase family. CC -!- SIMILARITY: In the C-terminal section; belongs to the CC glucosamine/galactosamine-6-phosphate isomerase family. 6- CC phosphogluconolactonase subfamily. CC -!- SEQUENCE CAUTION: CC Sequence=BAC32260.1; Type=Erroneous initiation; Note=Translation N-terminally shortened; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK045199; BAC32260.1; ALT_INIT; mRNA. DR EMBL; AK159373; BAE35029.1; -; mRNA. DR EMBL; AL606914; CAM16119.1; -; Genomic_DNA. DR EMBL; CU463327; CAQ51682.1; -; Genomic_DNA. DR EMBL; BC042677; AAH42677.1; -; mRNA. DR RefSeq; NP_775547.2; NM_173371.3. DR RefSeq; XP_006537123.1; XM_006537060.1. DR RefSeq; XP_006537124.1; XM_006537061.1. DR RefSeq; XP_006538523.1; XM_006538460.1. DR RefSeq; XP_006538524.1; XM_006538461.1. DR UniGene; Mm.22183; -. DR ProteinModelPortal; Q8CFX1; -. DR SMR; Q8CFX1; 25-500, 559-786. DR IntAct; Q8CFX1; 3. DR MINT; MINT-1837869; -. DR PhosphoSite; Q8CFX1; -. DR PaxDb; Q8CFX1; -. DR PRIDE; Q8CFX1; -. DR Ensembl; ENSMUST00000084117; ENSMUSP00000081134; ENSMUSG00000028980. DR GeneID; 100198; -. DR KEGG; mmu:100198; -. DR UCSC; uc008vxh.1; mouse. DR CTD; 9563; -. DR MGI; MGI:2140356; H6pd. DR eggNOG; COG0363; -. DR GeneTree; ENSGT00530000063435; -. DR HOGENOM; HOG000231077; -. DR HOVERGEN; HBG005780; -. DR InParanoid; B2KGW7; -. DR KO; K13937; -. DR OrthoDB; EOG7BW0HS; -. DR SABIO-RK; Q8CFX1; -. DR NextBio; 354313; -. DR PRO; PR:Q8CFX1; -. DR ArrayExpress; Q8CFX1; -. DR Bgee; Q8CFX1; -. DR Genevestigator; Q8CFX1; -. DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell. DR GO; GO:0017057; F:6-phosphogluconolactonase activity; IDA:MGI. DR GO; GO:0047936; F:glucose 1-dehydrogenase [NAD(P)] activity; IEA:UniProtKB-EC. DR GO; GO:0004345; F:glucose-6-phosphate dehydrogenase activity; IDA:MGI. DR GO; GO:0050661; F:NADP binding; IEA:InterPro. DR GO; GO:0006098; P:pentose-phosphate shunt; IDA:MGI. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR005900; 6-phosphogluconolactonase_DevB. DR InterPro; IPR001282; G6P_DH. DR InterPro; IPR019796; G6P_DH_AS. DR InterPro; IPR022675; G6P_DH_C. DR InterPro; IPR022674; G6P_DH_NAD-bd. DR InterPro; IPR006148; Glc/Gal-6P_isomerase. DR InterPro; IPR016040; NAD(P)-bd_dom. DR PANTHER; PTHR23429; PTHR23429; 1. DR Pfam; PF02781; G6PD_C; 1. DR Pfam; PF00479; G6PD_N; 1. DR Pfam; PF01182; Glucosamine_iso; 1. DR PRINTS; PR00079; G6PDHDRGNASE. DR TIGRFAMs; TIGR01198; pgl; 1. DR PROSITE; PS00069; G6P_DEHYDROGENASE; 1. PE 1: Evidence at protein level; KW Carbohydrate metabolism; Complete proteome; Endoplasmic reticulum; KW Glucose metabolism; Glycoprotein; Hydrolase; Multifunctional enzyme; KW NAD; NADP; Oxidoreductase; Pyrrolidone carboxylic acid; KW Reference proteome; Signal. FT SIGNAL 1 16 Potential. FT CHAIN 17 789 GDH/6PGL endoplasmic bifunctional FT protein. FT /FTId=PRO_0000236794. FT REGION 17 524 Glucose 1-dehydrogenase. FT REGION 525 538 Linker. FT REGION 539 789 6-phosphogluconolactonase. FT ACT_SITE 264 264 Proton acceptor (By similarity). FT BINDING 31 31 NADP (By similarity). FT BINDING 63 63 NADP (By similarity). FT BINDING 201 201 Substrate (By similarity). FT BINDING 205 205 Substrate (By similarity). FT MOD_RES 17 17 Pyrrolidone carboxylic acid (By FT similarity). FT MOD_RES 205 205 N6-succinyllysine. FT MOD_RES 424 424 N6-succinyllysine. FT CARBOHYD 154 154 N-linked (GlcNAc...) (Potential). FT CARBOHYD 279 279 N-linked (GlcNAc...) (Potential). FT CARBOHYD 681 681 N-linked (GlcNAc...) (Potential). FT CONFLICT 77 77 V -> A (in Ref. 1; BAE35029, 2; CAQ51682 FT and 3; AAH42677). FT CONFLICT 106 106 R -> H (in Ref. 1; BAE35029, 2; CAQ51682 FT and 3; AAH42677). FT CONFLICT 285 285 A -> T (in Ref. 1; BAE35029, 2; CAQ51682 FT and 3; AAH42677). SQ SEQUENCE 789 AA; 88928 MW; E970CE8B35D3E1E5 CRC64; MLLAAMCLAL LGCLQAQELK GHVSIILLGA TGDLAKKYLW QGLFQLYLDE AGKGHSFSFH GAALTAPQQG QKLMDKVLES LSCPKDLVPS RCDELKGQFL QLSQYRQLKT VEDYQTLNKD IETQVQQDGL WEAGRIFYFS VPPFAYADIA RNINSSCRPH PGAWLRVVFE KPFGHDHLSA QQLASELGSF FQEEEMYRVD HYLGKQAVAQ ILPFRDQNRK ALDGLWNRHH VERVEIILKE TIDAEGRASF YEEYGVIRDT LQNHLTEILT LVAMELPLNI SSSAAVLQHK LWAFQALRGL QKSSAILGQY QAYSGQVRRE LQKPDGFQSL TPTFAGVLVH IDNLRWEGVP FILMSGKALD ERVGYVRIVF KNRAYCTQSE RHWVPEQSRC LPQQIIFYIG HGELGHPAIL VSRNLFKPSL PTQKWKEVQD QPGLRLFGRP LSDYYAYRPV REQDAYSTLL SHIFHCRKES FITTENLLAS WVFWTPLLDS LAFEVPRPYP GGAENGQLLD FEFSGGQLTF SQQQLEVLIP DLGSVPKPSD FQVLGARYRQ SPLITAWPEE LISKLASDIE AAAVQAVRHF GKFHLALSGG SSPIALFQQL ATGHYSFPWA HTHLWLVDER CVPLSDPDSN FQGLQAHLLQ HVRVPYYNIH PMPVHLHQRL CAEEDQGAQT YASEISALVA NSSFDLVLLG MGTDGHTASL FPQSPTGLDG DQLVVLTESP FRPHQRMSLS LPLINRAKKV AVLVMGRTKR EITTLVSRVG HEPKKWPISG VVPLSGQLVW YMDYEAFLG // ID GCDH_MOUSE Reviewed; 438 AA. AC Q60759; Q6P8N6; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 2. DT 19-MAR-2014, entry version 113. DE RecName: Full=Glutaryl-CoA dehydrogenase, mitochondrial; DE Short=GCD; DE EC=1.3.8.6; DE Flags: Precursor; GN Name=Gcdh; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=129/Sv; TISSUE=Liver; RX PubMed=7490088; DOI=10.1006/geno.1995.1182; RA Koeller D.M., Digiulio K.A., Angeloni S.V., Dowler L.L., Frerman F.E., RA White R.A., Goodman S.I.; RT "Cloning, structure, and chromosome localization of the mouse RT glutaryl-CoA dehydrogenase gene."; RL Genomics 28:508-512(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Kidney; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Kidney; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain; RX PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200; RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., RA Burlingame A.L.; RT "Comprehensive identification of phosphorylation sites in postsynaptic RT density preparations."; RL Mol. Cell. Proteomics 5:914-922(2006). RN [5] RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-51, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., RA Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). RN [6] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-51; LYS-65 AND LYS-240, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23576753; DOI=10.1073/pnas.1302961110; RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., RA Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.; RT "Label-free quantitative proteomics of the lysine acetylome in RT mitochondria identifies substrates of SIRT3 in metabolic pathways."; RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013). CC -!- FUNCTION: Catalyzes the oxidative decarboxylation of glutaryl-CoA CC to crotonyl-CoA and CO(2) in the degradative pathway of L-lysine, CC L-hydroxylysine, and L-tryptophan metabolism. It uses electron CC transfer flavoprotein as its electron acceptor. CC -!- CATALYTIC ACTIVITY: Glutaryl-CoA + electron-transfer flavoprotein CC = crotonyl-CoA + CO(2) + reduced electron-transfer flavoprotein. CC -!- COFACTOR: FAD. CC -!- PATHWAY: Amino-acid metabolism; lysine degradation. CC -!- PATHWAY: Amino-acid metabolism; tryptophan metabolism. CC -!- SUBUNIT: Homotetramer. CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix. CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U18992; AAB04679.1; -; mRNA. DR EMBL; AK165406; BAE38166.1; -; mRNA. DR EMBL; BC061158; AAH61158.1; -; mRNA. DR RefSeq; NP_032123.3; NM_008097.2. DR UniGene; Mm.2475; -. DR ProteinModelPortal; Q60759; -. DR SMR; Q60759; 48-435. DR BioGrid; 234755; 1. DR IntAct; Q60759; 2. DR MINT; MINT-1861107; -. DR PhosphoSite; Q60759; -. DR PaxDb; Q60759; -. DR PRIDE; Q60759; -. DR Ensembl; ENSMUST00000109745; ENSMUSP00000105367; ENSMUSG00000003809. DR Ensembl; ENSMUST00000182458; ENSMUSP00000138554; ENSMUSG00000003809. DR GeneID; 270076; -. DR KEGG; mmu:270076; -. DR UCSC; uc009mnx.1; mouse. DR CTD; 2639; -. DR MGI; MGI:104541; Gcdh. DR eggNOG; COG1960; -. DR GeneTree; ENSGT00740000114853; -. DR HOGENOM; HOG000131662; -. DR HOVERGEN; HBG001939; -. DR InParanoid; Q6P8N6; -. DR KO; K00252; -. DR OMA; CYDTALR; -. DR OrthoDB; EOG7WT418; -. DR TreeFam; TF105051; -. DR UniPathway; UPA00224; -. DR UniPathway; UPA00225; -. DR NextBio; 393182; -. DR PRO; PR:Q60759; -. DR ArrayExpress; Q60759; -. DR Bgee; Q60759; -. DR CleanEx; MM_GCDH; -. DR Genevestigator; Q60759; -. DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:MGI. DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell. DR GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IEA:InterPro. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. DR GO; GO:0006568; P:tryptophan metabolic process; IEA:UniProtKB-UniPathway. DR Gene3D; 1.10.540.10; -; 1. DR Gene3D; 2.40.110.10; -; 1. DR InterPro; IPR006089; Acyl-CoA_DH_CS. DR InterPro; IPR006091; Acyl-CoA_Oxase/DH_cen-dom. DR InterPro; IPR009075; AcylCo_DH/oxidase_C. DR InterPro; IPR013786; AcylCoA_DH/ox_N. DR InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom. DR Pfam; PF00441; Acyl-CoA_dh_1; 1. DR Pfam; PF02770; Acyl-CoA_dh_M; 1. DR Pfam; PF02771; Acyl-CoA_dh_N; 1. DR SUPFAM; SSF47203; SSF47203; 1. DR SUPFAM; SSF56645; SSF56645; 1. DR PROSITE; PS00073; ACYL_COA_DH_2; 1. PE 1: Evidence at protein level; KW Acetylation; Complete proteome; FAD; Flavoprotein; Mitochondrion; KW Oxidoreductase; Reference proteome; Transit peptide. FT TRANSIT 1 44 Mitochondrion (Potential). FT CHAIN 45 438 Glutaryl-CoA dehydrogenase, FT mitochondrial. FT /FTId=PRO_0000000528. FT NP_BIND 177 186 FAD (By similarity). FT NP_BIND 177 180 FAD (By similarity). FT NP_BIND 212 214 FAD (By similarity). FT NP_BIND 387 391 FAD (By similarity). FT NP_BIND 416 418 FAD (By similarity). FT REGION 138 139 Substrate binding (By similarity). FT REGION 287 294 Substrate binding (By similarity). FT ACT_SITE 414 414 Proton acceptor (By similarity). FT BINDING 186 186 FAD (By similarity). FT BINDING 186 186 Substrate; via carbonyl oxygen (By FT similarity). FT BINDING 294 294 Substrate (By similarity). FT BINDING 319 319 FAD (By similarity). FT BINDING 330 330 FAD (By similarity). FT BINDING 415 415 Substrate; via amide nitrogen (By FT similarity). FT BINDING 416 416 FAD (By similarity). FT BINDING 434 434 FAD; via carbonyl oxygen (By similarity). FT MOD_RES 51 51 N6-acetyllysine; alternate. FT MOD_RES 51 51 N6-succinyllysine; alternate. FT MOD_RES 65 65 N6-acetyllysine. FT MOD_RES 240 240 N6-acetyllysine. FT CONFLICT 9 9 R -> Q (in Ref. 1; AAB04679). FT CONFLICT 75 75 C -> W (in Ref. 1; AAB04679). FT CONFLICT 82 82 R -> Q (in Ref. 1; AAB04679). FT CONFLICT 167 167 G -> R (in Ref. 1; AAB04679). FT CONFLICT 234 234 R -> P (in Ref. 1; AAB04679). FT CONFLICT 245 245 L -> S (in Ref. 1; AAB04679). SQ SEQUENCE 438 AA; 48606 MW; A904457D76F2BD90 CRC64; MSLRGVSARL LSRRSGLRFP RFPRTWSSAA AHTEKTQIRP AKSSRPVFDW KDPLILEEQL TADEKLIRDT FRNYCQERLM SRILLANRNE VFHRDIVYEM GELGVLGPTI KGYGCAGVSS VAYGLLTREL ERVDSGYRSM MSVQSSLVMH PIYTYGSEEQ RQKYLPGLAK GELLGCFGLT EPNHGSDPGG METRARHNPS NQSYTLSGTK TWITNSPVAD LFIVWARCED NCIRGFILEK GMRGLSAPRI EGKFSLRASA TGMIIMDSVE VPEENVLPNV SSLAGPFGCL NTARYGITWG VLGAAEFCLH TARQYALDRI QFGVPLARNQ LVQKKLADML TEITLGLHAC LQLGRLKDQD KATPEMVSML KRNNCGKALD IARQARDILG GNGISDEYHV IRHAMNLEAV NTYEGTHDIH ALILGRAITG IQAFTVGK // ID GCSP_MOUSE Reviewed; 1025 AA. AC Q91W43; DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 19-MAR-2014, entry version 94. DE RecName: Full=Glycine dehydrogenase (decarboxylating), mitochondrial; DE EC=1.4.4.2; DE AltName: Full=Glycine cleavage system P protein; DE AltName: Full=Glycine decarboxylase; DE AltName: Full=Glycine dehydrogenase (aminomethyl-transferring); DE Flags: Precursor; GN Name=Gldc; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Eye, and Retina; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [2] RP PROTEIN SEQUENCE OF 278-287; 606-615; 878-888 AND 933-942, AND MASS RP SPECTROMETRY. RC STRAIN=OF1; TISSUE=Hippocampus; RA Lubec G., Sunyer B., Chen W.-Q.; RL Submitted (JAN-2009) to UniProtKB. RN [3] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-452; LYS-519; LYS-653 AND RP LYS-669, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Liver; RX PubMed=23576753; DOI=10.1073/pnas.1302961110; RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., RA Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.; RT "Label-free quantitative proteomics of the lysine acetylome in RT mitochondria identifies substrates of SIRT3 in metabolic pathways."; RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013). CC -!- FUNCTION: The glycine cleavage system catalyzes the degradation of CC glycine. The P protein binds the alpha-amino group of glycine CC through its pyridoxal phosphate cofactor; CO(2) is released and CC the remaining methylamine moiety is then transferred to the CC lipoamide cofactor of the H protein (By similarity). CC -!- CATALYTIC ACTIVITY: Glycine + [glycine-cleavage complex H CC protein]-N(6)-lipoyl-L-lysine = [glycine-cleavage complex H CC protein]-S-aminomethyl-N(6)-dihydrolipoyl-L-lysine + CO(2). CC -!- COFACTOR: Pyridoxal phosphate (By similarity). CC -!- SUBUNIT: Homodimer. The glycine cleavage system is composed of CC four proteins: P, T, L and H (By similarity). CC -!- SUBCELLULAR LOCATION: Mitochondrion (By similarity). CC -!- SIMILARITY: Belongs to the GcvP family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BC017135; AAH17135.1; -; mRNA. DR RefSeq; NP_613061.1; NM_138595.2. DR UniGene; Mm.274852; -. DR ProteinModelPortal; Q91W43; -. DR SMR; Q91W43; 51-1010. DR IntAct; Q91W43; 1. DR MINT; MINT-1847717; -. DR STRING; 10090.ENSMUSP00000025778; -. DR PhosphoSite; Q91W43; -. DR PaxDb; Q91W43; -. DR PRIDE; Q91W43; -. DR Ensembl; ENSMUST00000025778; ENSMUSP00000025778; ENSMUSG00000024827. DR GeneID; 104174; -. DR KEGG; mmu:104174; -. DR UCSC; uc008hej.1; mouse. DR CTD; 2731; -. DR MGI; MGI:1341155; Gldc. DR eggNOG; COG1003; -. DR GeneTree; ENSGT00390000017970; -. DR HOGENOM; HOG000239369; -. DR HOVERGEN; HBG005820; -. DR InParanoid; Q91W43; -. DR KO; K00281; -. DR OMA; QTMVCDL; -. DR OrthoDB; EOG7FJGZQ; -. DR TreeFam; TF300678; -. DR NextBio; 356668; -. DR PRO; PR:Q91W43; -. DR Bgee; Q91W43; -. DR CleanEx; MM_GLDC; -. DR Genevestigator; Q91W43; -. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR GO; GO:0004375; F:glycine dehydrogenase (decarboxylating) activity; ISO:MGI. DR GO; GO:0016829; F:lyase activity; IEA:InterPro. DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro. DR GO; GO:0006546; P:glycine catabolic process; IEA:InterPro. DR Gene3D; 3.40.640.10; -; 2. DR HAMAP; MF_00711; GcvP; 1. DR InterPro; IPR001597; ArAA_b-elim_lyase/Thr_aldolase. DR InterPro; IPR020580; GDC-P_N. DR InterPro; IPR020581; GDC_P. DR InterPro; IPR003437; GDC_P_homo. DR InterPro; IPR015424; PyrdxlP-dep_Trfase. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1. DR PANTHER; PTHR11773; PTHR11773; 1. DR Pfam; PF01212; Beta_elim_lyase; 1. DR Pfam; PF02347; GDC-P; 1. DR SUPFAM; SSF53383; SSF53383; 3. DR TIGRFAMs; TIGR00461; gcvP; 1. PE 1: Evidence at protein level; KW Acetylation; Complete proteome; Direct protein sequencing; KW Mitochondrion; Oxidoreductase; Pyridoxal phosphate; KW Reference proteome; Transit peptide. FT TRANSIT 1 35 Mitochondrion (Potential). FT CHAIN 36 1025 Glycine dehydrogenase (decarboxylating), FT mitochondrial. FT /FTId=PRO_0000010741. FT MOD_RES 452 452 N6-acetyllysine. FT MOD_RES 519 519 N6-acetyllysine. FT MOD_RES 653 653 N6-acetyllysine. FT MOD_RES 669 669 N6-acetyllysine. FT MOD_RES 759 759 N6-(pyridoxal phosphate)lysine (By FT similarity). SQ SEQUENCE 1025 AA; 113267 MW; BB4A1E3459FE3495 CRC64; MQLCARAWGL RLGRGAGGGH RLARGTGLSW AQRSRDSSGG GGGGGGGDRG AAGASRLLER LLPRHDDFSR RHIGPGDKDR REMLQALGLA SIDELIEKTV PASIRLKRPL KMEDPICENE ILETLHAIAS KNQIWRSYIG MGYYNCSVPQ TILRNLLENS GWVTQYTPYQ PEVSQGRLES LLNYQTMVSD ITGLDMANAS LLDEATAAAE AMQLCHRHNK RKKFFVDPRC HPQTIAVVQT RAKYRGVLVE LKLPHEMDFS GKDVCGVLFQ YPDTEGKVED FTELVDRAHQ TGSLTCCATD LLALCILRPP GEFGVDIALG NSQRFGVPLG YGGPHAAFFA VKENLVRMMP GRMVGVTRDA TGKEVYRLAL QTREQHIRRD KATSNICTAQ ALLANMAAMF AIYHGSQGLK HIAKRVHNAT LILSEGLKRA GHQLQHDLFF DTLKVQCGCS VKEVLGRAAQ RQINFRLFDD GTLGISLDET VTEKDLDDLL WIFGCESSAE LVAEGMGEER RGLLGSSFKR TSPFLTHQVF NSYHSETNLV RYMKKLENKD ISLVHSMIPL GSCTMKLNSS SELAPITWRE FANIHPFVPL DQAQGYQQLF QGLEKDLCEI TGYDRVSFQP NSGAQGEYAG LATIRAYLDQ KGERHRTVCL IPKSAHGTNP ASAHMAGMKI QPVEVDRYGN IDVAHLKAMV DQHKENLAAI MITYPSTNGV FEENIGDVCA LIHQHGGQVY LDGANMNAQV GICRPGDFGS DVSHLNLHKT FCIPHGGGGP GMGPIGVKKH LSPFLPSHPV ISIKPTEGTW PVGTVSAAPW GSSSILPISW AYIKMMGGKG LKEATEIAIL NANYMAKRLE KHYRVLFRGA RGYVAHEFIL DTRPFKKSAN VEAVDVAKRL QDYGFHAPTM SWPVAGTLMI EPTESEDKAE LDRFCDAMIS IRQEIADIEE GRIDPRVNPL KMSPHSLTCV TSSCWDRPYS REVAAFPLPF VKPENKFWPT IARIDDIYGD QHLVCTCPPM EVYESPFSEQ KRASS // ID GFOD2_MOUSE Reviewed; 385 AA. AC Q9CYH5; DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 19-MAR-2014, entry version 90. DE RecName: Full=Glucose-fructose oxidoreductase domain-containing protein 2; DE EC=1.-.-.-; DE Flags: Precursor; GN Name=Gfod2; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Embryo, and Hippocampus; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Mammary tumor; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP SUBCELLULAR LOCATION, AND FUNCTION. RX PubMed=18757743; DOI=10.1073/pnas.0803640105; RA Manabe R., Tsutsui K., Yamada T., Kimura M., Nakano I., Shimono C., RA Sanzen N., Furutani Y., Fukuda T., Oguri Y., Shimamoto K., RA Kiyozumi D., Sato Y., Sado Y., Senoo H., Yamashina S., Fukuda S., RA Kawai J., Sugiura N., Kimata K., Hayashizaki Y., Sekiguchi K.; RT "Transcriptome-based systematic identification of extracellular matrix RT proteins."; RL Proc. Natl. Acad. Sci. U.S.A. 105:12849-12854(2008). CC -!- FUNCTION: Promotes matrix assembly. CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular CC matrix. CC -!- SIMILARITY: Belongs to the Gfo/Idh/MocA family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK017684; BAB30872.1; -; mRNA. DR EMBL; AK141521; BAE24716.1; -; mRNA. DR EMBL; BC013623; AAH13623.1; -; mRNA. DR RefSeq; NP_081745.1; NM_027469.4. DR UniGene; Mm.40954; -. DR ProteinModelPortal; Q9CYH5; -. DR SMR; Q9CYH5; 1-365. DR STRING; 10090.ENSMUSP00000013294; -. DR PhosphoSite; Q9CYH5; -. DR PaxDb; Q9CYH5; -. DR PRIDE; Q9CYH5; -. DR Ensembl; ENSMUST00000013294; ENSMUSP00000013294; ENSMUSG00000013150. DR GeneID; 70575; -. DR KEGG; mmu:70575; -. DR UCSC; uc009neb.1; mouse. DR CTD; 81577; -. DR MGI; MGI:1917825; Gfod2. DR eggNOG; COG0673; -. DR GeneTree; ENSGT00390000001507; -. DR HOGENOM; HOG000010274; -. DR HOVERGEN; HBG054911; -. DR InParanoid; Q9CYH5; -. DR OMA; RRTWDHT; -. DR OrthoDB; EOG7FJH0S; -. DR TreeFam; TF323246; -. DR NextBio; 331910; -. DR PRO; PR:Q9CYH5; -. DR ArrayExpress; Q9CYH5; -. DR Bgee; Q9CYH5; -. DR Genevestigator; Q9CYH5; -. DR GO; GO:0031012; C:extracellular matrix; IDA:MGI. DR GO; GO:0005578; C:proteinaceous extracellular matrix; IEA:UniProtKB-SubCell. DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW. DR GO; GO:0030198; P:extracellular matrix organization; IDA:MGI. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR000683; Oxidoreductase_N. DR Pfam; PF01408; GFO_IDH_MocA; 1. PE 2: Evidence at transcript level; KW Complete proteome; Extracellular matrix; Oxidoreductase; KW Reference proteome; Secreted; Signal. FT SIGNAL 1 25 Potential. FT CHAIN 26 385 Glucose-fructose oxidoreductase domain- FT containing protein 2. FT /FTId=PRO_0000282973. SQ SEQUENCE 385 AA; 42242 MW; B99702BBCFEA4210 CRC64; MKLLPGVGVF GTGSSARVLV PLLRAEGFTV EALWGKTEEE AKQLAEEMNI TFYTSRTDDV LLHQDVDLVC INIPPPLTRQ ISVKALGIGK NVVCEKAATS MDAFRMVTAS RYYPQLMSLV GNVLRFLPAF VRMKQLIAEH YVGAVMICDA RIYSGSLLSP SYGWICDELM GGGGLHTMGT YIVDLLTHLT GQKAEKVHGL LKTFVRQNAT IRGIRHVTSD DFCFFQMLMG GGVCSTVTLN FNMPGAFVHE VMVVGSAGRL VARGADLYGQ KNSAAQEELL VRDSLAVGAG LPEQGPQDVP LLYLKGMVYM VQALRQSFQG QGDRRTWDRT PVSMAASFED GLYMQSVVDA IKRSSRSGEW ETVEMLAEEP DANQNLSETL QRNNL // ID GFOD1_MOUSE Reviewed; 390 AA. AC Q3UHD2; B9EI39; DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2005, sequence version 1. DT 19-FEB-2014, entry version 62. DE RecName: Full=Glucose-fructose oxidoreductase domain-containing protein 1; DE EC=1.-.-.-; DE Flags: Precursor; GN Name=Gfod1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain, and Testis; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- SUBCELLULAR LOCATION: Secreted (Potential). CC -!- SIMILARITY: Belongs to the Gfo/Idh/MocA family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK147458; BAE27925.1; -; mRNA. DR EMBL; BC139026; AAI39027.1; -; mRNA. DR EMBL; BC139027; AAI39028.1; -; mRNA. DR RefSeq; NP_001028571.1; NM_001033399.4. DR UniGene; Mm.441399; -. DR ProteinModelPortal; Q3UHD2; -. DR SMR; Q3UHD2; 5-258. DR PhosphoSite; Q3UHD2; -. DR PaxDb; Q3UHD2; -. DR PRIDE; Q3UHD2; -. DR Ensembl; ENSMUST00000055341; ENSMUSP00000062662; ENSMUSG00000051335. DR GeneID; 328232; -. DR KEGG; mmu:328232; -. DR UCSC; uc007qfx.1; mouse. DR CTD; 54438; -. DR MGI; MGI:2145304; Gfod1. DR eggNOG; COG0673; -. DR GeneTree; ENSGT00390000001507; -. DR HOGENOM; HOG000010274; -. DR HOVERGEN; HBG054911; -. DR InParanoid; Q3UHD2; -. DR OMA; CEAQVHS; -. DR OrthoDB; EOG7FJH0S; -. DR TreeFam; TF323246; -. DR NextBio; 398178; -. DR PRO; PR:Q3UHD2; -. DR Bgee; Q3UHD2; -. DR Genevestigator; Q3UHD2; -. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR000683; Oxidoreductase_N. DR InterPro; IPR004104; OxRdtase_C. DR Pfam; PF01408; GFO_IDH_MocA; 1. DR Pfam; PF02894; GFO_IDH_MocA_C; 1. PE 2: Evidence at transcript level; KW Complete proteome; Oxidoreductase; Reference proteome; Secreted; KW Signal. FT SIGNAL 1 21 Potential. FT CHAIN 22 390 Glucose-fructose oxidoreductase domain- FT containing protein 1. FT /FTId=PRO_0000282969. SQ SEQUENCE 390 AA; 43286 MW; 718D2A2407DBE93D CRC64; MLPGVGVFGT SLTARVIIPL LKDEGFAVKA LWGRTQEEAE ELAKEMSVPF YTSRIDEVLL HQDVDLVCIN LPPPLTRQIA VKTLGIGKNV ICDRTATPLD AFRMMSAAHY YPKLMSIMGN VLRFLPAFVR MKQLIEEGYV GELLVCEVQV HSGSLLGKKY NWSCDDLMGG GGLHSVGTYI IDLLTFLTGQ KAVKVHGLLK TFVKQTDHIK GIRQITSDDF CTFQMVLEGG VCCTVTLNFN VPGEFKQDVT VVGSAGRLLA VGTDLYGQRN SAPEQELLLQ DTTSVSNSLL PEKAFSDIPS PYLRGTMKMM QAVRQAFQDQ DDRRTWDGRP LTMAATFDDC LYALCVVDTI KRSSQTGEWQ NIAIMTEEPE LSPAYLISEA MRRSRMSLYC // ID GGLO_MOUSE Reviewed; 440 AA. AC P58710; Q8K152; DT 31-JAN-2002, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 3. DT 19-MAR-2014, entry version 111. DE RecName: Full=L-gulonolactone oxidase; DE Short=LGO; DE EC=1.1.3.8; DE AltName: Full=L-gulono-gamma-lactone oxidase; DE Short=GLO; GN Name=Gulo; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR, RP AND TISSUE SPECIFICITY. RC STRAIN=C57BL/6; TISSUE=Liver; RX PubMed=14962674; DOI=10.1016/j.ygeno.2003.08.018; RA Ha M.N., Graham F.L., D'Souza C.K., Muller W.J., Igdoura S.A., RA Schellhorn H.E.; RT "Functional rescue of vitamin C synthesis deficiency in human cells RT using adenoviral-based expression of murine l-gulono-gamma-lactone RT oxidase."; RL Genomics 83:482-492(2004). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Embryo, and Placenta; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Liver; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP PROTEIN SEQUENCE OF 318-324, AND MASS SPECTROMETRY. RC STRAIN=C57BL/6; TISSUE=Brain; RA Lubec G., Kang S.U.; RL Submitted (APR-2007) to UniProtKB. CC -!- FUNCTION: Oxidizes L-gulono-1,4-lactone to hydrogen peroxide and CC L-xylo-hexulonolactone which spontaneously isomerizes to L- CC ascorbate. CC -!- CATALYTIC ACTIVITY: L-gulono-1,4-lactone + O(2) = L-ascorbate + CC H(2)O(2). CC -!- COFACTOR: FAD. CC -!- PATHWAY: Cofactor biosynthesis; L-ascorbate biosynthesis via UDP- CC alpha-D-glucuronate pathway; L-ascorbate from UDP-alpha-D- CC glucuronate: step 4/4. CC -!- SUBCELLULAR LOCATION: Microsome membrane; Single-pass membrane CC protein (By similarity). Endoplasmic reticulum membrane; Single- CC pass membrane protein (By similarity). CC -!- TISSUE SPECIFICITY: Highly expressed in liver. CC -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked CC oxidoreductase family. CC -!- SIMILARITY: Contains 1 FAD-binding PCMH-type domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AY453064; AAR15891.1; -; mRNA. DR EMBL; AK077740; BAC36988.1; -; mRNA. DR EMBL; AK167460; BAE39545.1; -; mRNA. DR EMBL; BC019856; AAH19856.1; -; mRNA. DR EMBL; BC028828; AAH28828.1; -; mRNA. DR RefSeq; NP_848862.1; NM_178747.3. DR RefSeq; XP_006519129.1; XM_006519066.1. DR UniGene; Mm.26207; -. DR ProteinModelPortal; P58710; -. DR SMR; P58710; 12-207, 308-439. DR STRING; 10090.ENSMUSP00000060912; -. DR PhosphoSite; P58710; -. DR PaxDb; P58710; -. DR PRIDE; P58710; -. DR DNASU; 268756; -. DR Ensembl; ENSMUST00000059970; ENSMUSP00000060912; ENSMUSG00000034450. DR GeneID; 268756; -. DR KEGG; mmu:268756; -. DR UCSC; uc007ujt.1; mouse. DR CTD; 268756; -. DR MGI; MGI:1353434; Gulo. DR eggNOG; COG0277; -. DR GeneTree; ENSGT00510000049722; -. DR HOGENOM; HOG000252847; -. DR HOVERGEN; HBG005834; -. DR InParanoid; Q8K152; -. DR KO; K00103; -. DR OMA; FEFYWFP; -. DR OrthoDB; EOG7N8ZV8; -. DR TreeFam; TF328994; -. DR UniPathway; UPA00991; UER00939. DR ChiTaRS; GULOP; mouse. DR NextBio; 392483; -. DR PRO; PR:P58710; -. DR ArrayExpress; P58710; -. DR Bgee; P58710; -. DR CleanEx; MM_GULO; -. DR Genevestigator; P58710; -. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0003885; F:D-arabinono-1,4-lactone oxidase activity; IEA:InterPro. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IDA:UniProtKB. DR GO; GO:0050105; F:L-gulonolactone oxidase activity; IDA:UniProtKB. DR GO; GO:0008762; F:UDP-N-acetylmuramate dehydrogenase activity; IEA:InterPro. DR GO; GO:0019853; P:L-ascorbic acid biosynthetic process; IDA:UniProtKB. DR Gene3D; 3.30.43.10; -; 1. DR Gene3D; 3.30.465.10; -; 1. DR InterPro; IPR007173; ALO. DR InterPro; IPR016169; CO_DH_flavot_FAD-bd_sub2. DR InterPro; IPR016166; FAD-bd_2. DR InterPro; IPR016167; FAD-bd_2_sub1. DR InterPro; IPR010031; FAD_lactone_oxidase. DR InterPro; IPR010032; FAD_linked_OxRdtase_bac. DR InterPro; IPR023595; LGO_GLO. DR InterPro; IPR006094; Oxid_FAD_bind_N. DR InterPro; IPR006093; Oxy_OxRdtase_FAD_BS. DR Pfam; PF04030; ALO; 1. DR Pfam; PF01565; FAD_binding_4; 1. DR PIRSF; PIRSF000136; LGO_GLO; 1. DR SUPFAM; SSF56176; SSF56176; 1. DR TIGRFAMs; TIGR01679; bact_FAD_ox; 1. DR TIGRFAMs; TIGR01678; FAD_lactone_ox; 1. DR PROSITE; PS51387; FAD_PCMH; 1. DR PROSITE; PS00862; OX2_COVAL_FAD; 1. PE 1: Evidence at protein level; KW Ascorbate biosynthesis; Complete proteome; Direct protein sequencing; KW Endoplasmic reticulum; FAD; Flavoprotein; Membrane; Microsome; KW Oxidoreductase; Reference proteome; Transmembrane; KW Transmembrane helix. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 440 L-gulonolactone oxidase. FT /FTId=PRO_0000128159. FT TRANSMEM 251 273 Helical; (Potential). FT DOMAIN 17 187 FAD-binding PCMH-type. FT MOD_RES 54 54 Pros-8alpha-FAD histidine (By FT similarity). FT CONFLICT 160 160 N -> K (in Ref. 3; AAH19856). SQ SEQUENCE 440 AA; 50478 MW; D109B480E08E773B CRC64; MVHGYKGVQF QNWAKTYGCS PEMYYQPTSV GEVREVLALA RQQNKKVKVV GGGHSPSDIA CTDGFMIHMG KMNRVLQVDK EKKQVTVEAG ILLTDLHPQL DKHGLALSNL GAVSDVTVGG VIGSGTHNTG IKHGILATQV VALTLMKADG TVLECSESSN ADVFQAARVH LGCLGVILTV TLQCVPQFHL LETSFPSTLK EVLDNLDSHL KKSEYFRFLW FPHSENVSII YQDHTNKEPS SASNWFWDYA IGFYLLEFLL WTSTYLPRLV GWINRFFFWL LFNCKKESSN LSHKIFSYEC RFKQHVQDWA IPREKTKEAL LELKAMLEAH PKVVAHYPVE VRFTRGDDIL LSPCFQRDSC YMNIIMYRPY GKDVPRLDYW LAYETIMKKF GGRPHWAKAH NCTRKDFEKM YPAFHKFCDI REKLDPTGMF LNSYLEKVFY // ID GILT_MOUSE Reviewed; 248 AA. AC Q9ESY9; G3X911; Q3U0F9; Q9EP56; DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot. DT 03-OCT-2012, sequence version 3. DT 19-FEB-2014, entry version 60. DE RecName: Full=Gamma-interferon-inducible lysosomal thiol reductase; DE EC=1.8.-.-; DE AltName: Full=Gamma-interferon-inducible protein IP-30; DE AltName: Full=Lysosomal thiol reductase IP30; DE Flags: Precursor; GN Name=Ifi30; Synonyms=Gilt, Ip30; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], SUBCELLULAR LOCATION, RP DISRUPTION PHENOTYPE, AND FUNCTION. RC STRAIN=129/SvJ, and C57BL/6; RX PubMed=11701933; DOI=10.1126/science.1065500; RA Maric M., Arunachalam B., Phan U.T., Dong C., Garrett W.S., RA Cannon K.S., Alfonso C., Karlsson L., Flavell R.A., Cresswell P.; RT "Defective antigen processing in GILT-free mice."; RL Science 294:1361-1365(2001). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Liver; RA Weber D.A., Jun J., Jensen P.E.; RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=NOD; TISSUE=Spleen; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Colon; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [7] RP DISRUPTION PHENOTYPE, AND FUNCTION IN LISTERIA MONOCYTOGENES RP INFECTION. RX PubMed=18815593; DOI=10.1038/nature07344; RA Singh R., Jamieson A., Cresswell P.; RT "GILT is a critical host factor for Listeria monocytogenes RT infection."; RL Nature 455:1244-1247(2008). RN [8] RP DISRUPTION PHENOTYPE, AND FUNCTION IN CROSS-PRESENTATION OF VIRAL RP ANTIGEN. RX PubMed=20538950; DOI=10.1126/science.1189176; RA Singh R., Cresswell P.; RT "Defective cross-presentation of viral antigens in GILT-free mice."; RL Science 328:1394-1398(2010). CC -!- FUNCTION: Lysosomal thiol reductase that can reduce protein CC disulfide bonds. May facilitate the complete unfolding of proteins CC destined for lysosomal degradation. Plays an important role in CC antigen processing. Facilitates the generation of MHC class II- CC restricted epitodes from disulfide bond-containing antigen by the CC endocytic reduction of disulfide bonds. Facilitates also MHC class CC I-restricted recognition of exogenous antigens containing CC disulfide bonds by CD8+ T-cells or crosspresentation. CC -!- SUBUNIT: Dimer; disulfide-linked (By similarity). CC -!- SUBCELLULAR LOCATION: Secreted (By similarity). Lysosome. CC -!- PTM: N-glycosylated. Sugar chains contain mannose-6-phosphate (By CC similarity). CC -!- PTM: Synthesized as a 35 kDa precursor which is then processed CC into the mature 30 kDa form via cleavage of N-terminal and C- CC terminal propeptides. Processing of the precursor is mediated by CC multiple lysosomal proteases (By similarity). CC -!- DISRUPTION PHENOTYPE: Mice lacking GILT are deficient in CC generating major histocompatibility complex class-II-restricted CC CD4(+) T-cell responses to protein antigens that contain disulfide CC bonds. Mice are partially protected from Listeria monocytogenes CC infection, they exhibit reduced bacterial replication in spleen CC and liver. Bacterial escape from the phagosome is impaired in the CC macrophages of these mice. CC -!- MISCELLANEOUS: Both precursor form and mature form have thiol CC reductase activity (By similarity). CC -!- SIMILARITY: Belongs to the GILT family. CC -!- SEQUENCE CAUTION: CC Sequence=AAG00598.1; Type=Erroneous initiation; Note=Translation N-terminally shortened; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF309649; AAG34681.1; -; mRNA. DR EMBL; AF309650; AAG34682.1; -; Genomic_DNA. DR EMBL; AF290973; AAG00598.1; ALT_INIT; mRNA. DR EMBL; AK156914; BAE33895.1; -; mRNA. DR EMBL; AC162446; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH466569; EDL28872.1; -; Genomic_DNA. DR EMBL; BC054852; AAH54852.1; -; mRNA. DR RefSeq; NP_075552.2; NM_023065.3. DR UniGene; Mm.30241; -. DR ProteinModelPortal; Q9ESY9; -. DR IntAct; Q9ESY9; 1. DR MINT; MINT-4129390; -. DR STRING; 10090.ENSMUSP00000034299; -. DR PhosphoSite; Q9ESY9; -. DR PaxDb; Q9ESY9; -. DR PRIDE; Q9ESY9; -. DR Ensembl; ENSMUST00000034299; ENSMUSP00000034299; ENSMUSG00000031838. DR GeneID; 65972; -. DR KEGG; mmu:65972; -. DR UCSC; uc009mbm.1; mouse. DR CTD; 10437; -. DR MGI; MGI:2137648; Ifi30. DR eggNOG; NOG315223; -. DR GeneTree; ENSGT00390000010450; -. DR HOGENOM; HOG000238423; -. DR HOVERGEN; HBG005837; -. DR InParanoid; Q9EP56; -. DR KO; K08059; -. DR OMA; VNVSLYY; -. DR OrthoDB; EOG71P2CG; -. DR TreeFam; TF315141; -. DR ChiTaRS; IFI30; mouse. DR NextBio; 320430; -. DR PRO; PR:Q9ESY9; -. DR Genevestigator; Q9ESY9; -. DR GO; GO:0030054; C:cell junction; IEA:Ensembl. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0005764; C:lysosome; IDA:UniProtKB. DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl. DR GO; GO:0015036; F:disulfide oxidoreductase activity; TAS:MGI. DR GO; GO:0042590; P:antigen processing and presentation of exogenous peptide antigen via MHC class I; IMP:UniProtKB. DR GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; IMP:MGI. DR GO; GO:0048147; P:negative regulation of fibroblast proliferation; IMP:MGI. DR GO; GO:0050821; P:protein stabilization; IMP:MGI. DR InterPro; IPR004911; Interferon-induced_GILT. DR PANTHER; PTHR13234; PTHR13234; 1. DR Pfam; PF03227; GILT; 1. PE 1: Evidence at protein level; KW Complete proteome; Disulfide bond; Glycoprotein; Immunity; Lysosome; KW Oxidoreductase; Redox-active center; Reference proteome; Secreted; KW Signal. FT SIGNAL 1 26 Potential. FT PROPEP 27 54 Removed in mature form (By similarity). FT /FTId=PRO_0000406221. FT CHAIN 55 230 Gamma-interferon-inducible lysosomal FT thiol reductase. FT /FTId=PRO_0000406222. FT PROPEP 231 248 Removed in mature form (By similarity). FT /FTId=PRO_0000406223. FT CARBOHYD 92 92 N-linked (GlcNAc...) (Potential). FT CARBOHYD 105 105 N-linked (GlcNAc...) (Potential). FT DISULFID 69 72 Redox-active (By similarity). FT CONFLICT 42 42 A -> V (in Ref. 1; AAG34681/AAG34682, 2; FT AAG00598 and 6; AAH54852). FT CONFLICT 112 112 F -> Y (in Ref. 3; BAE33895). FT CONFLICT 245 245 V -> C (in Ref. 2; AAG00598). SQ SEQUENCE 248 AA; 27784 MW; 41BE0390FDAADFC8 CRC64; MSWSPILPFL SLLLLLFPLE VPRAATASLS QASSEGTTTC KAHDVCLLGP RPLPPSPPVR VSLYYESLCG ACRYFLVRDL FPTWLMVMEI MNITLVPYGN AQERNVSGTW EFTCQHGELE CRLNMVEACL LDKLEKEAAF LTIVCMEEMD DMEKKLGPCL QVYAPEVSPE SIMECATGKR GTQLMHENAQ LTDALHPPHE YVPWVLVNEK PLKDPSELLS IVCQLYQGTE KPDICSSIAD SPRKVCYK // ID GLYR1_MOUSE Reviewed; 546 AA. AC Q922P9; Q3TX02; Q9CYQ1; DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 19-FEB-2014, entry version 97. DE RecName: Full=Putative oxidoreductase GLYR1; DE EC=1.-.-.-; DE AltName: Full=Glyoxylate reductase 1 homolog; DE AltName: Full=Nuclear protein NP60; GN Name=Glyr1; Synonyms=Np60; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Bone marrow, and Embryo; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Mammary tumor; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain; RX PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200; RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., RA Burlingame A.L.; RT "Comprehensive identification of phosphorylation sites in postsynaptic RT density preparations."; RL Mol. Cell. Proteomics 5:914-922(2006). CC -!- FUNCTION: May have oxidoreductase activity. Regulates p38 MAP CC kinase activity by mediating stress activation of p38alpha/MAPK14 CC and specifically regulating MAPK14 signaling. Indirectly promotes CC phosphorylation of MAPK14 and activation of ATF2. The CC phosphorylation of MAPK14 requires upstream activity of MAP2K4 and CC MAP2K6. Recruited on chromatin, recognizes and binds trimethylated CC 'Lys-36' of histone H3 (H3K36me3) (By similarity). CC -!- SUBUNIT: Interacts with MAPK14 (By similarity). CC -!- SUBCELLULAR LOCATION: Nucleus (By similarity). CC -!- DOMAIN: The A.T hook DNA-binding domain is required for the CC interaction with MAPK14 (By similarity). CC -!- DOMAIN: The PWWP domain probably mediates the binding to H3K36me3 CC (By similarity). CC -!- MISCELLANEOUS: The conserved NAD-binding sites and sequence CC similarity to plant dehydrogenases suggest that this protein may CC have oxidoreductase activity. CC -!- SIMILARITY: Belongs to the 3-hydroxyisobutyrate dehydrogenase CC family. NP60 subfamily. CC -!- SIMILARITY: Contains 1 A.T hook DNA-binding domain. CC -!- SIMILARITY: Contains 1 PWWP domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK014456; BAB29363.1; -; mRNA. DR EMBL; AK150349; BAE29486.1; -; mRNA. DR EMBL; AK152887; BAE31570.1; -; mRNA. DR EMBL; AK159476; BAE35114.1; -; mRNA. DR EMBL; BC006893; AAH06893.1; -; mRNA. DR RefSeq; NP_082996.2; NM_028720.2. DR UniGene; Mm.21652; -. DR ProteinModelPortal; Q922P9; -. DR SMR; Q922P9; 7-87, 261-546. DR IntAct; Q922P9; 3. DR MINT; MINT-4125995; -. DR PhosphoSite; Q922P9; -. DR PaxDb; Q922P9; -. DR PRIDE; Q922P9; -. DR Ensembl; ENSMUST00000023189; ENSMUSP00000023189; ENSMUSG00000022536. DR GeneID; 74022; -. DR KEGG; mmu:74022; -. DR UCSC; uc007ybm.1; mouse. DR CTD; 84656; -. DR MGI; MGI:1921272; Glyr1. DR eggNOG; COG2084; -. DR GeneTree; ENSGT00530000063270; -. DR HOGENOM; HOG000219609; -. DR OrthoDB; EOG7992RZ; -. DR ChiTaRS; GLYR1; mouse. DR NextBio; 339560; -. DR PRO; PR:Q922P9; -. DR ArrayExpress; Q922P9; -. DR Bgee; Q922P9; -. DR CleanEx; MM_3930401K13RIK; -. DR Genevestigator; Q922P9; -. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0050662; F:coenzyme binding; IEA:InterPro. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0035064; F:methylated histone residue binding; ISS:UniProtKB. DR GO; GO:0004616; F:phosphogluconate dehydrogenase (decarboxylating) activity; IEA:InterPro. DR GO; GO:0006098; P:pentose-phosphate shunt; IEA:InterPro. DR Gene3D; 1.10.1040.10; -; 1. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR008927; 6-PGluconate_DH_C-like. DR InterPro; IPR006115; 6PGDH_NADP-bd. DR InterPro; IPR017956; AT_hook_DNA-bd_motif. DR InterPro; IPR013328; DH_multihelical. DR InterPro; IPR015815; HIBADH-type. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR000313; PWWP_dom. DR PANTHER; PTHR22981; PTHR22981; 1. DR Pfam; PF03446; NAD_binding_2; 1. DR Pfam; PF00855; PWWP; 1. DR SMART; SM00384; AT_hook; 1. DR SUPFAM; SSF48179; SSF48179; 1. DR PROSITE; PS50812; PWWP; 1. PE 1: Evidence at protein level; KW Complete proteome; DNA-binding; NAD; Nucleus; Oxidoreductase; KW Phosphoprotein; Reference proteome. FT CHAIN 1 546 Putative oxidoreductase GLYR1. FT /FTId=PRO_0000312122. FT DOMAIN 8 66 PWWP. FT DNA_BIND 167 179 A.T hook. FT NP_BIND 270 284 NAD (By similarity). FT BINDING 355 355 NAD (By similarity). FT BINDING 498 498 NAD (By similarity). FT MOD_RES 130 130 Phosphoserine (By similarity). FT MOD_RES 166 166 Phosphoserine (By similarity). FT MOD_RES 533 533 Phosphoserine (By similarity). FT CONFLICT 50 51 ED -> KN (in Ref. 1; BAB29363). FT CONFLICT 109 110 NR -> DW (in Ref. 1; BAB29363). FT CONFLICT 296 296 N -> S (in Ref. 1; BAE35114). FT CONFLICT 535 535 N -> S (in Ref. 1; BAE35114). SQ SEQUENCE 546 AA; 59716 MW; F5D2090DE1F64723 CRC64; MAAVSLRLGD LVWGKLGRYP PWPGKIVNPP KDLKKPRGKK CFFVKFFGTE DHAWIKVEQL KPYHAHKEEM IKINKGKRFQ QAVDAVEEFL RRAKGKDQTS SHTSADDKNR RNSSEERSRP NSGDEKRKLS LSEGKVKKNM GEGKKRVTSG SADRGSKCLK RAQEQSPRKR GRPPKDEKDL TIPESSTVKG MMAGPMAAFK WQPTATEPVK DADPHFHHFL LSQTEKPAVC YQAITKKLKI CEEETGSTSI QAADSTAVNG SITPTDKKIG FLGLGLMGSG IVSNLLKMGH TVTVWNRTAE KEGARLGRTP AEVVSTCDIT FACVSDPKAA KDLVLGPSGV LQGIRPGKCY VDMSTVDADT VTELAQVIVS RGGRFLEAPV SGNQQLSNDG MLVILAAGDR GLYEDCSSCF QAMGKTSFFL GEVGNAAKMM LIVNMVQGSF MATIAEGLTL AQVTGQSQQT LLDILNQGQL ASIFLDQKCQ NILQGNFKPD FYLKYIQKDL RLAIALGDAV NHPTPMAAAA NEVYKRAKAL DQSDNDMSAV YRAYIH // ID GMPR1_MOUSE Reviewed; 345 AA. AC Q9DCZ1; DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 19-FEB-2014, entry version 93. DE RecName: Full=GMP reductase 1; DE EC=1.7.1.7; DE AltName: Full=Guanosine 5'-monophosphate oxidoreductase 1; DE Short=Guanosine monophosphate reductase 1; GN Name=Gmpr; Synonyms=Gmpr1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Heart, and Kidney; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Colon; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: Catalyzes the irreversible NADPH-dependent deamination CC of GMP to IMP. It functions in the conversion of nucleobase, CC nucleoside and nucleotide derivatives of G to A nucleotides, and CC in maintaining the intracellular balance of A and G nucleotides CC (By similarity). CC -!- CATALYTIC ACTIVITY: Inosine 5'-phosphate + NH(3) + NADP(+) = CC guanosine 5'-phosphate + NADPH. CC -!- SUBUNIT: Homotetramer (By similarity). CC -!- SIMILARITY: Belongs to the IMPDH/GMPR family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK002326; BAB22014.1; -; mRNA. DR EMBL; AK084508; BAC39203.1; -; mRNA. DR EMBL; BC010827; AAH10827.1; -; mRNA. DR RefSeq; NP_079784.1; NM_025508.4. DR UniGene; Mm.290802; -. DR ProteinModelPortal; Q9DCZ1; -. DR SMR; Q9DCZ1; 2-338. DR STRING; 10090.ENSMUSP00000000260; -. DR PhosphoSite; Q9DCZ1; -. DR PaxDb; Q9DCZ1; -. DR PRIDE; Q9DCZ1; -. DR Ensembl; ENSMUST00000000260; ENSMUSP00000000260; ENSMUSG00000000253. DR GeneID; 66355; -. DR KEGG; mmu:66355; -. DR UCSC; uc007qha.1; mouse. DR CTD; 2766; -. DR MGI; MGI:1913605; Gmpr. DR eggNOG; COG0516; -. DR GeneTree; ENSGT00530000062923; -. DR HOGENOM; HOG000165756; -. DR HOVERGEN; HBG051744; -. DR InParanoid; Q9DCZ1; -. DR KO; K00364; -. DR OMA; SKFPEHT; -. DR OrthoDB; EOG73804S; -. DR TreeFam; TF300378; -. DR NextBio; 321417; -. DR PRO; PR:Q9DCZ1; -. DR ArrayExpress; Q9DCZ1; -. DR Bgee; Q9DCZ1; -. DR CleanEx; MM_GMPR; -. DR Genevestigator; Q9DCZ1; -. DR GO; GO:1902560; C:GMP reductase complex; IEA:UniProtKB-EC. DR GO; GO:0003920; F:GMP reductase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0009117; P:nucleotide metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR005993; GMP_reduct1. DR InterPro; IPR015875; IMP_DH/GMP_Rdtase_CS. DR InterPro; IPR001093; IMP_DH_GMPRt. DR Pfam; PF00478; IMPDH; 1. DR PIRSF; PIRSF000235; GMP_reductase; 1. DR TIGRFAMs; TIGR01305; GMP_reduct_1; 1. DR PROSITE; PS00487; IMP_DH_GMP_RED; 1. PE 2: Evidence at transcript level; KW Complete proteome; Metal-binding; NADP; Oxidoreductase; Potassium; KW Purine metabolism; Reference proteome. FT CHAIN 1 345 GMP reductase 1. FT /FTId=PRO_0000093724. FT NP_BIND 26 27 NADP; shared with neighboring subunit (By FT similarity). FT NP_BIND 129 131 NADP (By similarity). FT NP_BIND 180 181 NADP (By similarity). FT NP_BIND 285 286 NADP (By similarity). FT NP_BIND 314 317 NADP; shared with neighboring subunit (By FT similarity). FT REGION 219 221 GMP binding (By similarity). FT REGION 242 243 GMP binding (By similarity). FT REGION 268 270 GMP binding (By similarity). FT REGION 286 290 GMP binding (By similarity). FT ACT_SITE 186 186 Thioimidate intermediate (By similarity). FT ACT_SITE 188 188 Proton donor/acceptor (By similarity). FT METAL 181 181 Potassium; via carbonyl oxygen (By FT similarity). FT METAL 183 183 Potassium; via carbonyl oxygen (By FT similarity). FT METAL 186 186 Potassium; via carbonyl oxygen (By FT similarity). FT METAL 189 189 Potassium (By similarity). FT BINDING 78 78 NADP (By similarity). FT BINDING 269 269 NADP; via carbonyl oxygen (By FT similarity). SQ SEQUENCE 345 AA; 37482 MW; 9A801692C9284D72 CRC64; MPRIDADLKL DFKDVLLRPK RSSLKSRSEV DLERTFTFRN SKQTYSGIPI IVANMDTVGT FEMAVVMSQH AMFTAVHKHY SLDDWKCFAE THPECLQHVA VSSGSGQNDL ERMSRILEAV PQVKFICLDV ANGYSEHFVE FVKLVRSKFP EHTIMAGNVV TGEMVEELIL SGADIIKVGV GPGSVCTTRT KTGVGYPQLS AVIECADSAH GLKGHIISDG GCTCPGDVAK AFGAGADFVM LGGMFSGHTE CAGEVIERNG QKLKLFYGMS SDTAMKKHAG GVAEYRASEG KTVEVPYKGD VENTILDILG GLRSTCTYVG AAKLKELSRR ATFIRVTQQH NTVFG // ID GMPR2_MOUSE Reviewed; 348 AA. AC Q99L27; Q542X2; Q8R1T5; DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 2. DT 19-MAR-2014, entry version 99. DE RecName: Full=GMP reductase 2; DE EC=1.7.1.7; DE AltName: Full=Guanosine 5'-monophosphate oxidoreductase 2; DE Short=Guanosine monophosphate reductase 2; GN Name=Gmpr2; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Pancreas, and Thymus; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: Catalyzes the irreversible NADPH-dependent deamination CC of GMP to IMP. It functions in the conversion of nucleobase, CC nucleoside and nucleotide derivatives of G to A nucleotides, and CC in maintaining the intracellular balance of A and G nucleotides CC (By similarity). CC -!- CATALYTIC ACTIVITY: Inosine 5'-phosphate + NH(3) + NADP(+) = CC guanosine 5'-phosphate + NADPH. CC -!- SUBUNIT: Homotetramer (By similarity). CC -!- SIMILARITY: Belongs to the IMPDH/GMPR family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK031004; BAC27211.1; -; mRNA. DR EMBL; AK075772; BAC35946.1; -; mRNA. DR EMBL; CH466535; EDL36258.1; -; Genomic_DNA. DR EMBL; BC003886; AAH03886.1; -; mRNA. DR EMBL; BC024109; AAH24109.1; -; mRNA. DR RefSeq; NP_818773.1; NM_177992.2. DR RefSeq; XP_006518429.1; XM_006518366.1. DR UniGene; Mm.390685; -. DR UniGene; Mm.486705; -. DR ProteinModelPortal; Q99L27; -. DR SMR; Q99L27; 10-337. DR PhosphoSite; Q99L27; -. DR PaxDb; Q99L27; -. DR PRIDE; Q99L27; -. DR Ensembl; ENSMUST00000002397; ENSMUSP00000002397; ENSMUSG00000002326. DR GeneID; 105446; -. DR KEGG; mmu:105446; -. DR UCSC; uc007uae.1; mouse. DR CTD; 51292; -. DR MGI; MGI:1917903; Gmpr2. DR eggNOG; COG0516; -. DR GeneTree; ENSGT00530000062923; -. DR HOGENOM; HOG000165756; -. DR HOVERGEN; HBG051744; -. DR InParanoid; Q542X2; -. DR KO; K00364; -. DR OMA; CSCAGDV; -. DR OrthoDB; EOG73804S; -. DR TreeFam; TF300378; -. DR NextBio; 357716; -. DR PRO; PR:Q99L27; -. DR Bgee; Q99L27; -. DR CleanEx; MM_GMPR2; -. DR Genevestigator; Q99L27; -. DR GO; GO:1902560; C:GMP reductase complex; IEA:UniProtKB-EC. DR GO; GO:0003920; F:GMP reductase activity; ISS:UniProtKB. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0046038; P:GMP catabolic process; ISA:MGI. DR GO; GO:0030224; P:monocyte differentiation; ISA:MGI. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR005993; GMP_reduct1. DR InterPro; IPR015875; IMP_DH/GMP_Rdtase_CS. DR InterPro; IPR001093; IMP_DH_GMPRt. DR Pfam; PF00478; IMPDH; 1. DR PIRSF; PIRSF000235; GMP_reductase; 1. DR TIGRFAMs; TIGR01305; GMP_reduct_1; 1. DR PROSITE; PS00487; IMP_DH_GMP_RED; 1. PE 2: Evidence at transcript level; KW Acetylation; Complete proteome; Metal-binding; NADP; Oxidoreductase; KW Potassium; Purine metabolism; Reference proteome. FT CHAIN 1 348 GMP reductase 2. FT /FTId=PRO_0000093727. FT NP_BIND 26 27 NADP; shared with neighboring subunit (By FT similarity). FT NP_BIND 129 131 NADP (By similarity). FT NP_BIND 180 181 NADP (By similarity). FT NP_BIND 285 286 NADP (By similarity). FT NP_BIND 314 317 NADP; shared with neighboring subunit (By FT similarity). FT REGION 219 221 GMP binding (By similarity). FT REGION 242 243 GMP binding (By similarity). FT REGION 268 270 GMP binding (By similarity). FT REGION 286 290 GMP binding (By similarity). FT ACT_SITE 186 186 Thioimidate intermediate (By similarity). FT ACT_SITE 188 188 Proton donor/acceptor (By similarity). FT METAL 181 181 Potassium; via carbonyl oxygen (By FT similarity). FT METAL 183 183 Potassium; via carbonyl oxygen (By FT similarity). FT METAL 186 186 Potassium; via carbonyl oxygen (By FT similarity). FT METAL 189 189 Potassium (By similarity). FT BINDING 78 78 NADP (By similarity). FT BINDING 269 269 NADP; via carbonyl oxygen (By FT similarity). FT MOD_RES 291 291 N6-acetyllysine (By similarity). FT CONFLICT 105 105 S -> T (in Ref. 3; AAH03886). SQ SEQUENCE 348 AA; 38019 MW; 83E6998193D22FC0 CRC64; MPHIDNDVKL DFKDVLLRPK RSTLKSRSEV ELTRSFSFRN SKQMYSGIPV IAANMDTVGT FEMARVLCKF SLFTAIHKHY SIHQWQEFAS QNPDCLECLA ASSGSGSADF EQLEQILEAI PQVKYICLDV ANGYSEHFVE FVKDVRKRFP QHTIMAGNVV TGEMVEELIL SGADIIKVGI GPGSVCTTRK KTGVGYPQLS AVMECADAAH GLKGHIISDG GCSCPGDVAK AFGAGADFVM LGGMLAGHSE SGGELIERDG KKYKLFYGMS SEMAMKKYSG GVAEYRASEG KIVEVPFKGD VEHTIRDILG GIRSTCTYVG AAKLKELSRR TTFIRVTQQV NPIFSNSQ // ID GPD1L_MOUSE Reviewed; 351 AA. AC Q3ULJ0; Q6A0D2; Q8BVZ7; Q8BWM5; Q8CFN6; DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot. DT 15-MAY-2007, sequence version 2. DT 19-MAR-2014, entry version 79. DE RecName: Full=Glycerol-3-phosphate dehydrogenase 1-like protein; DE EC=1.1.1.8; GN Name=Gpd1l; Synonyms=Kiaa0089; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Fetal brain; RX PubMed=15368895; DOI=10.1093/dnares/11.3.205; RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H., RA Nagase T., Ohara O., Koga H.; RT "Prediction of the coding sequences of mouse homologues of KIAA gene: RT IV. The complete nucleotide sequences of 500 mouse KIAA-homologous RT cDNAs identified by screening of terminal sequences of cDNA clones RT randomly sampled from size-fractionated libraries."; RL DNA Res. 11:205-218(2004). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC STRAIN=C57BL/6J; TISSUE=Stomach, and Thymus; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Eye; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP PROTEIN SEQUENCE OF 207-220, AND MASS SPECTROMETRY. RC TISSUE=Hippocampus; RA Lubec G., Klug S.; RL Submitted (MAR-2007) to UniProtKB. CC -!- FUNCTION: Plays a role in regulating cardiac sodium current; CC decreased enzymatic activity with resulting increased levels of CC glycerol 3-phosphate activating the DPD1L-dependent SCN5A CC phosphorylation pathway, may ultimately lead to decreased sodium CC current; cardiac sodium current may also be reduced due to CC alterations of NAD(H) balance induced by DPD1L (By similarity). CC -!- CATALYTIC ACTIVITY: sn-glycerol 3-phosphate + NAD(+) = glycerone CC phosphate + NADH. CC -!- SUBUNIT: Interacts with SCN5A (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (Potential). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q3ULJ0-1; Sequence=Displayed; CC Name=2; CC IsoId=Q3ULJ0-2; Sequence=VSP_025062; CC Note=No experimental confirmation available; CC -!- SIMILARITY: Belongs to the NAD-dependent glycerol-3-phosphate CC dehydrogenase family. CC -!- SEQUENCE CAUTION: CC Sequence=AAH37729.1; Type=Erroneous initiation; CC Sequence=BAD32164.1; Type=Erroneous initiation; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK172886; BAD32164.1; ALT_INIT; mRNA. DR EMBL; AK050572; BAC34327.1; -; mRNA. DR EMBL; AK075845; BAC36001.1; -; mRNA. DR EMBL; AK145475; BAE26458.1; -; mRNA. DR EMBL; BC037729; AAH37729.1; ALT_INIT; mRNA. DR RefSeq; NP_780589.3; NM_175380.5. DR UniGene; Mm.38198; -. DR ProteinModelPortal; Q3ULJ0; -. DR SMR; Q3ULJ0; 4-346. DR IntAct; Q3ULJ0; 1. DR MINT; MINT-4113076; -. DR PhosphoSite; Q3ULJ0; -. DR PaxDb; Q3ULJ0; -. DR PRIDE; Q3ULJ0; -. DR Ensembl; ENSMUST00000084853; ENSMUSP00000081913; ENSMUSG00000050627. [Q3ULJ0-2] DR Ensembl; ENSMUST00000146623; ENSMUSP00000117509; ENSMUSG00000050627. [Q3ULJ0-1] DR GeneID; 333433; -. DR KEGG; mmu:333433; -. DR UCSC; uc009ryj.2; mouse. [Q3ULJ0-1] DR CTD; 23171; -. DR MGI; MGI:1289257; Gpd1l. DR eggNOG; COG0240; -. DR GeneTree; ENSGT00390000003114; -. DR HOGENOM; HOG000246855; -. DR HOVERGEN; HBG003669; -. DR InParanoid; Q3ULJ0; -. DR KO; K00006; -. DR OMA; KIFCKGQ; -. DR OrthoDB; EOG7ZKSBS; -. DR TreeFam; TF300836; -. DR NextBio; 399982; -. DR PRO; PR:Q3ULJ0; -. DR ArrayExpress; Q3ULJ0; -. DR Bgee; Q3ULJ0; -. DR CleanEx; MM_GPD1L; -. DR Genevestigator; Q3ULJ0; -. DR GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:InterPro. DR GO; GO:0016020; C:membrane; IDA:BHF-UCL. DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl. DR GO; GO:0004367; F:glycerol-3-phosphate dehydrogenase [NAD+] activity; IEA:UniProtKB-EC. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR GO; GO:0017080; F:sodium channel regulator activity; IEA:Ensembl. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR GO; GO:0046168; P:glycerol-3-phosphate catabolic process; IEA:InterPro. DR GO; GO:0006734; P:NADH metabolic process; IMP:MGI. DR GO; GO:0033137; P:negative regulation of peptidyl-serine phosphorylation; IEA:Ensembl. DR GO; GO:0090038; P:negative regulation of protein kinase C signaling; IEA:Ensembl. DR GO; GO:2000010; P:positive regulation of protein localization to cell surface; IEA:Ensembl. DR GO; GO:0010765; P:positive regulation of sodium ion transport; IEA:Ensembl. DR GO; GO:0002027; P:regulation of heart rate; IEA:Ensembl. DR GO; GO:2000649; P:regulation of sodium ion transmembrane transporter activity; IEA:Ensembl. DR GO; GO:0060373; P:regulation of ventricular cardiac muscle cell membrane depolarization; IEA:Ensembl. DR GO; GO:0086005; P:ventricular cardiac muscle cell action potential; IEA:Ensembl. DR Gene3D; 1.10.1040.10; -; 1. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR008927; 6-PGluconate_DH_C-like. DR InterPro; IPR013328; DH_multihelical. DR InterPro; IPR006168; G3P_DH_NAD-dep. DR InterPro; IPR006109; G3P_DH_NAD-dep_C. DR InterPro; IPR017751; G3P_DH_NAD-dep_euk. DR InterPro; IPR011128; G3P_DH_NAD-dep_N. DR InterPro; IPR016040; NAD(P)-bd_dom. DR PANTHER; PTHR11728; PTHR11728; 1. DR Pfam; PF07479; NAD_Gly3P_dh_C; 1. DR Pfam; PF01210; NAD_Gly3P_dh_N; 1. DR PIRSF; PIRSF000114; Glycerol-3-P_dh; 1. DR PRINTS; PR00077; GPDHDRGNASE. DR SUPFAM; SSF48179; SSF48179; 1. DR TIGRFAMs; TIGR03376; glycerol3P_DH; 1. PE 1: Evidence at protein level; KW Alternative splicing; Complete proteome; Cytoplasm; KW Direct protein sequencing; NAD; Oxidoreductase; Reference proteome. FT CHAIN 1 351 Glycerol-3-phosphate dehydrogenase 1-like FT protein. FT /FTId=PRO_0000286512. FT NP_BIND 12 17 NAD (By similarity). FT REGION 271 272 Substrate binding (By similarity). FT ACT_SITE 206 206 Proton acceptor (By similarity). FT BINDING 43 43 NAD (By similarity). FT BINDING 99 99 NAD (By similarity). FT BINDING 122 122 Substrate (By similarity). FT BINDING 155 155 NAD; via amide nitrogen (By similarity). FT BINDING 271 271 NAD (By similarity). FT BINDING 298 298 NAD; via amide nitrogen (By similarity). FT BINDING 300 300 NAD (By similarity). FT VAR_SEQ 321 351 Missing (in isoform 2). FT /FTId=VSP_025062. FT CONFLICT 26 26 S -> G (in Ref. 2; BAC36001). FT CONFLICT 179 179 F -> S (in Ref. 2; BAC36001). FT CONFLICT 202 202 C -> W (in Ref. 2; BAC36001). FT CONFLICT 212 212 G -> V (in Ref. 2; BAC36001). SQ SEQUENCE 351 AA; 38226 MW; BE192D41F592E577 CRC64; MAAAPLKVCI VGSGNWGSAV AKIIGSNVKT LQKFSSTVKM WVFEETVNGR KLTDIINNDH ENVKYLPGHK LPENVVAVPN LSEAVQDADL LVFVIPHQFI HKICDEITGR VPEKALGITL IKGIDEGPDG LKLISDIIRE KMGIDISVLM GANIASEVAA EKFCETTIGS KVMQNGLLFK ELLQTPNFRI TVVDDADTVE LCGALKNIVA VGAGFCDGLR CGDNTKAAVI RLGLMEMIAF AKIFCKGQVS TATFLESCGV ADLITTCYGG RNRRVAEAFA RTGKTIEELE KELLNGQKLQ GPQTSAEVYR ILRQKGLLDK FPLFTAVYQI CYEGRPVTQM LSCLQSHPEH I // ID GPDA_MOUSE Reviewed; 349 AA. AC P13707; Q3UVM3; Q5DTS5; DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 19-MAR-2014, entry version 134. DE RecName: Full=Glycerol-3-phosphate dehydrogenase [NAD(+)], cytoplasmic; DE Short=GPD-C; DE Short=GPDH-C; DE EC=1.1.1.8; GN Name=Gpd1; Synonyms=Gdc-1, Gdc1, Kiaa4010; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=3027100; RA Dobson D.E., Groves D.L., Spiegelman B.M.; RT "Nucleotide sequence and hormonal regulation of mouse glycerophosphate RT dehydrogenase mRNA during adipocyte and muscle cell differentiation."; RL J. Biol. Chem. 262:1804-1809(1987). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=3755721; RA Ireland R.C., Kotarski M.A., Johnston L.A., Stadler U., RA Birkenmeier E., Kozak L.P.; RT "Primary structure of the mouse glycerol-3-phosphate dehydrogenase RT gene."; RL J. Biol. Chem. 261:11779-11785(1986). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=3015943; RA Phillips M., Djian P., Green H.; RT "The nucleotide sequence of three genes participating in the adipose RT differentiation of 3T3 cells."; RL J. Biol. Chem. 261:10821-10827(1986). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; RA Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O., RA Koga H.; RT "Prediction of the coding sequences of mouse homologues of KIAA gene. RT The complete nucleotide sequences of mouse KIAA-homologous cDNAs RT identified by screening of terminal sequences of cDNA clones randomly RT sampled from size-fractionated libraries."; RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Kidney, Lung, and Urinary bladder; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Liver; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [7] RP PROTEIN SEQUENCE OF 50-62; 111-130; 205-218; 230-240; 297-304 AND RP 319-340, AND MASS SPECTROMETRY. RC STRAIN=C57BL/6; TISSUE=Brain, and Hippocampus; RA Lubec G., Klug S., Kang S.U.; RL Submitted (APR-2007) to UniProtKB. RN [8] RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-289, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., RA Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). CC -!- CATALYTIC ACTIVITY: sn-glycerol 3-phosphate + NAD(+) = glycerone CC phosphate + NADH. CC -!- SUBUNIT: Homodimer. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the NAD-dependent glycerol-3-phosphate CC dehydrogenase family. CC -!- SEQUENCE CAUTION: CC Sequence=BAD90479.1; Type=Erroneous initiation; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; J02655; AAA37728.1; -; mRNA. DR EMBL; M25558; AAA37726.1; -; Genomic_DNA. DR EMBL; M13366; AAA37727.1; -; Genomic_DNA. DR EMBL; AK220445; BAD90479.1; ALT_INIT; mRNA. DR EMBL; AK137134; BAE23246.1; -; mRNA. DR EMBL; AK004565; BAB23376.1; -; mRNA. DR EMBL; AK018733; BAB31376.1; -; mRNA. DR EMBL; BC005756; AAH05756.1; -; mRNA. DR EMBL; BC019391; AAH19391.1; -; mRNA. DR PIR; A25952; A25952. DR RefSeq; NP_034401.1; NM_010271.2. DR UniGene; Mm.252391; -. DR ProteinModelPortal; P13707; -. DR SMR; P13707; 1-349. DR IntAct; P13707; 7. DR MINT; MINT-1855802; -. DR ChEMBL; CHEMBL1075171; -. DR PhosphoSite; P13707; -. DR REPRODUCTION-2DPAGE; IPI00230185; -. DR REPRODUCTION-2DPAGE; P13707; -. DR SWISS-2DPAGE; P13707; -. DR PaxDb; P13707; -. DR PRIDE; P13707; -. DR Ensembl; ENSMUST00000023760; ENSMUSP00000023760; ENSMUSG00000023019. DR GeneID; 14555; -. DR KEGG; mmu:14555; -. DR UCSC; uc007xqd.1; mouse. DR CTD; 2819; -. DR MGI; MGI:95679; Gpd1. DR eggNOG; COG0240; -. DR GeneTree; ENSGT00390000003114; -. DR HOGENOM; HOG000246855; -. DR HOVERGEN; HBG003669; -. DR InParanoid; P13707; -. DR KO; K00006; -. DR OMA; HILPFAR; -. DR OrthoDB; EOG7ZKSBS; -. DR TreeFam; TF300836; -. DR SABIO-RK; P13707; -. DR ChiTaRS; GPD1; mouse. DR NextBio; 286250; -. DR PRO; PR:P13707; -. DR ArrayExpress; P13707; -. DR Bgee; P13707; -. DR CleanEx; MM_GPD1; -. DR Genevestigator; P13707; -. DR GO; GO:0005829; C:cytosol; IEA:Ensembl. DR GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; TAS:MGI. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR GO; GO:0004367; F:glycerol-3-phosphate dehydrogenase [NAD+] activity; IDA:MGI. DR GO; GO:0004368; F:glycerol-3-phosphate dehydrogenase activity; IEA:Ensembl. DR GO; GO:0051287; F:NAD binding; IEA:Ensembl. DR GO; GO:0071320; P:cellular response to cAMP; IDA:MGI. DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IDA:MGI. DR GO; GO:0006094; P:gluconeogenesis; IMP:MGI. DR GO; GO:0046168; P:glycerol-3-phosphate catabolic process; IEA:InterPro. DR GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IMP:MGI. DR GO; GO:0046486; P:glycerolipid metabolic process; IEA:Ensembl. DR GO; GO:0006127; P:glycerophosphate shuttle; IMP:MGI. DR GO; GO:0006116; P:NADH oxidation; IEA:Ensembl. DR GO; GO:0045821; P:positive regulation of glycolysis; IMP:MGI. DR Gene3D; 1.10.1040.10; -; 1. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR008927; 6-PGluconate_DH_C-like. DR InterPro; IPR013328; DH_multihelical. DR InterPro; IPR006168; G3P_DH_NAD-dep. DR InterPro; IPR006109; G3P_DH_NAD-dep_C. DR InterPro; IPR017751; G3P_DH_NAD-dep_euk. DR InterPro; IPR011128; G3P_DH_NAD-dep_N. DR InterPro; IPR016040; NAD(P)-bd_dom. DR PANTHER; PTHR11728; PTHR11728; 1. DR Pfam; PF07479; NAD_Gly3P_dh_C; 1. DR Pfam; PF01210; NAD_Gly3P_dh_N; 1. DR PIRSF; PIRSF000114; Glycerol-3-P_dh; 1. DR PRINTS; PR00077; GPDHDRGNASE. DR SUPFAM; SSF48179; SSF48179; 1. DR TIGRFAMs; TIGR03376; glycerol3P_DH; 1. DR PROSITE; PS00957; NAD_G3PDH; 1. PE 1: Evidence at protein level; KW Complete proteome; Cytoplasm; Direct protein sequencing; NAD; KW Oxidoreductase; Reference proteome. FT CHAIN 1 349 Glycerol-3-phosphate dehydrogenase FT [NAD(+)], cytoplasmic. FT /FTId=PRO_0000138080. FT NP_BIND 10 15 NAD (By similarity). FT REGION 269 270 Substrate binding (By similarity). FT ACT_SITE 204 204 Proton acceptor (Potential). FT BINDING 41 41 NAD (By similarity). FT BINDING 97 97 NAD (By similarity). FT BINDING 120 120 Substrate (By similarity). FT BINDING 153 153 NAD; via amide nitrogen (By similarity). FT BINDING 269 269 NAD (By similarity). FT BINDING 296 296 NAD; via amide nitrogen (By similarity). FT BINDING 298 298 NAD (By similarity). FT MOD_RES 289 289 N6-succinyllysine. FT CONFLICT 218 218 G -> R (in Ref. 7; AA sequence). FT CONFLICT 246 246 T -> I (in Ref. 2; AAA37726/AAA37727 and FT 4; BAD90479). FT CONFLICT 318 318 K -> R (in Ref. 5; BAE23246). SQ SEQUENCE 349 AA; 37573 MW; F2C572DADFEA1B99 CRC64; MAGKKVCIVG SGNWGSAIAK IVGSNAGRLA HFDPRVTMWV FEEDIGGRKL TEIINTQHEN VKYLPGHKLP PNVVAIPDVV QAATGADILV FVVPHQFIGK ICDQLKGHLK ANTIGISLIK GVDEGPNGLK LISEVIGERL GIPMSVLMGA NIASEVAEEK FCETTIGCKD PAQGQLLKDL MQTPNFRITV VQEVDTVEIC GALKNIVAVG AGFCDGLGFG DNTKAAVIRL GLMEMIAFAK LFCSGTVSSA TFLESCGVAD LITTCYGGRN RKVAEAFART GKSIEQLEKE MLNGQKLQGP QTARELHSIL QHKGLVDKFP LFTAVYKVCY EGQPVGEFIR CLQNHPEHM // ID GPDM_MOUSE Reviewed; 727 AA. AC Q64521; Q3TK51; Q3UDY8; Q61507; Q8CBX6; Q8K4U5; Q8VDT0; Q9ERP0; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2007, sequence version 2. DT 19-MAR-2014, entry version 127. DE RecName: Full=Glycerol-3-phosphate dehydrogenase, mitochondrial; DE Short=GPD-M; DE Short=GPDH-M; DE EC=1.1.5.3; DE AltName: Full=Protein TISP38; DE Flags: Precursor; GN Name=Gpd2; Synonyms=Gdm1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=C57BL/6J; TISSUE=Adipocyte; RX PubMed=8951039; DOI=10.1006/abbi.1996.0536; RA Koza R.A., Kozak U.C., Brown L.J., Leiter E.H., Macdonald M.J., RA Kozak L.P.; RT "Sequence and tissue-dependent RNA expression of mouse FAD-linked RT glycerol-3-phosphate dehydrogenase."; RL Arch. Biochem. Biophys. 336:97-104(1996). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=C57BL/6; RX PubMed=8772729; DOI=10.2337/diab.45.9.1238; RA Ishihara H., Nakazaki M., Kanegae Y., Inukai K., Asano T., RA Katagiri H., Yazaki Y., Kikuchi M., Miyazaki J., Saito I., Oka Y.; RT "Effect of mitochondrial and/or cytosolic glycerol 3-phosphate RT dehydrogenase overexpression on glucose-stimulated insulin secretion RT from MIN6 and HIT cells."; RL Diabetes 45:1238-1244(1996). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Bone marrow, Diencephalon, and Lung; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Czech II; TISSUE=Mammary tumor; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP PROTEIN SEQUENCE OF 58-91; 95-110; 125-135; 167-178; 200-209; 212-254; RP 285-298; 340-348; 381-390; 392-409; 442-453; 464-473; 483-499; RP 519-538; 558-579; 598-606; 609-627 AND 635-693. RC STRAIN=C57BL/6; TISSUE=Brain, and Hippocampus; RA Lubec G., Klug S., Kang S.U.; RL Submitted (APR-2007) to UniProtKB. RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 390-686. RC STRAIN=129/Sv; TISSUE=Liver; RA Weitzel J.M.; RT "Genomic sequence of mouse mitochondrial glycerol-3-phosphate RT dehydrogenase (mGPDH)."; RL Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [MRNA] OF 611-727. RC TISSUE=Testis; RA Tamura K., Nishimune Y., Nojima H.; RT "Mus musculus TISP38 mRNA."; RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases. RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-601, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain; RX PubMed=18034455; DOI=10.1021/pr0701254; RA Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.; RT "Large-scale identification and evolution indexing of tyrosine RT phosphorylation sites from murine brain."; RL J. Proteome Res. 7:311-318(2008). CC -!- CATALYTIC ACTIVITY: sn-glycerol 3-phosphate + a quinone = CC glycerone phosphate + a quinol. CC -!- COFACTOR: FAD. CC -!- ENZYME REGULATION: Calcium-binding enhance the activity of the CC enzyme. CC -!- PATHWAY: Polyol metabolism; glycerol degradation via glycerol CC kinase pathway; glycerone phosphate from sn-glycerol 3-phosphate CC (anaerobic route): step 1/1. CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane. CC -!- SIMILARITY: Belongs to the FAD-dependent glycerol-3-phosphate CC dehydrogenase family. CC -!- SIMILARITY: Contains 2 EF-hand domains. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U60987; AAB50545.1; -; mRNA. DR EMBL; D50430; BAA08926.1; -; mRNA. DR EMBL; AK034353; BAC28685.1; -; mRNA. DR EMBL; AK144716; BAE26028.1; -; mRNA. DR EMBL; AK149851; BAE29123.1; -; mRNA. DR EMBL; AK167152; BAE39294.1; -; mRNA. DR EMBL; BC021359; AAH21359.1; -; mRNA. DR EMBL; AH009802; AAG12342.1; -; Genomic_DNA. DR EMBL; AB045714; BAB97201.1; -; mRNA. DR RefSeq; NP_001139292.1; NM_001145820.1. DR RefSeq; NP_034404.3; NM_010274.3. DR UniGene; Mm.3711; -. DR ProteinModelPortal; Q64521; -. DR SMR; Q64521; 53-716. DR IntAct; Q64521; 4. DR MINT; MINT-4119960; -. DR PhosphoSite; Q64521; -. DR REPRODUCTION-2DPAGE; Q64521; -. DR PaxDb; Q64521; -. DR PRIDE; Q64521; -. DR Ensembl; ENSMUST00000028167; ENSMUSP00000028167; ENSMUSG00000026827. DR Ensembl; ENSMUST00000169687; ENSMUSP00000130992; ENSMUSG00000026827. DR GeneID; 14571; -. DR KEGG; mmu:14571; -. DR UCSC; uc008jsc.2; mouse. DR CTD; 2820; -. DR MGI; MGI:99778; Gpd2. DR eggNOG; COG0578; -. DR GeneTree; ENSGT00390000001718; -. DR HOVERGEN; HBG005897; -. DR KO; K00111; -. DR UniPathway; UPA00618; UER00673. DR ChiTaRS; GPD2; mouse. DR NextBio; 286290; -. DR PRO; PR:Q64521; -. DR ArrayExpress; Q64521; -. DR Bgee; Q64521; -. DR CleanEx; MM_GPD2; -. DR Genevestigator; Q64521; -. DR GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; TAS:MGI. DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:MGI. DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro. DR GO; GO:0052591; F:sn-glycerol-3-phosphate:ubiquinone-8 oxidoreductase activity; IEA:UniProtKB-EC. DR GO; GO:0043010; P:camera-type eye development; IGI:MGI. DR GO; GO:0006094; P:gluconeogenesis; IMP:MGI. DR GO; GO:0019563; P:glycerol catabolic process; IEA:UniProtKB-UniPathway. DR GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IMP:MGI. DR GO; GO:0035264; P:multicellular organism growth; IGI:MGI. DR Gene3D; 1.10.238.10; -; 1. DR InterPro; IPR011992; EF-hand-dom_pair. DR InterPro; IPR018247; EF_Hand_1_Ca_BS. DR InterPro; IPR002048; EF_hand_dom. DR InterPro; IPR006076; FAD-dep_OxRdtase. DR InterPro; IPR000447; G3P_DH_FAD-dep. DR Pfam; PF01266; DAO; 1. DR Pfam; PF13499; EF-hand_7; 1. DR PRINTS; PR01001; FADG3PDH. DR SMART; SM00054; EFh; 2. DR PROSITE; PS00018; EF_HAND_1; 1. DR PROSITE; PS50222; EF_HAND_2; 2. DR PROSITE; PS00977; FAD_G3PDH_1; 1. DR PROSITE; PS00978; FAD_G3PDH_2; 1. PE 1: Evidence at protein level; KW Calcium; Complete proteome; Direct protein sequencing; FAD; KW Flavoprotein; Membrane; Metal-binding; Mitochondrion; KW Mitochondrion inner membrane; Oxidoreductase; Phosphoprotein; KW Reference proteome; Repeat; Transit peptide. FT TRANSIT 1 42 Mitochondrion (By similarity). FT CHAIN 43 727 Glycerol-3-phosphate dehydrogenase, FT mitochondrial. FT /FTId=PRO_0000010430. FT DOMAIN 623 658 EF-hand 1. FT DOMAIN 659 694 EF-hand 2. FT NP_BIND 71 99 FAD (Potential). FT CA_BIND 672 683 Potential. FT MOD_RES 601 601 Phosphotyrosine. FT CONFLICT 26 26 P -> Q (in Ref. 1; AAB50545 and 4; FT AAH21359). FT CONFLICT 42 42 Missing (in Ref. 3; BAC28685). FT CONFLICT 158 158 L -> V (in Ref. 1; AAB50545). FT CONFLICT 295 295 D -> E (in Ref. 2; BAA08926). FT CONFLICT 449 449 D -> N (in Ref. 4; AAH21359). FT CONFLICT 498 498 A -> P (in Ref. 2; BAA08926). FT CONFLICT 582 582 N -> D (in Ref. 1; AAB50545). FT CONFLICT 593 593 E -> G (in Ref. 1; AAB50545). SQ SEQUENCE 727 AA; 80954 MW; 319F52E31CFDFC44 CRC64; MAFQKAVKGT ILVGGGALAT VLGLSPFAHY RRKQVSLAYV EAAGYLTEPV NREPPSREAQ LMTLKNTPEF DILVIGGGAT GCGCALDAVT RGLKTALVER DDFSSGTSSR STKLIHGGVR YLQKAIMNLD VEQYRMVKEA LHERANLLEI APHLSAPLPI MLPLYKWWQL PYYWVGIKMY DLVAGSQCLK SSYVLSKSRA LEHFPMLQKD KLVGAIVYYD GQHNDARMNL AIALTAARYG AATANYMEVV SLLKKTDPET GKERVSGARC KDVLTGQEFD VRAKCVINAS GPFTDSVRKM DDKNVVPICQ PSAGVHIVMP GYYSPENMGL LDPATSDGRV IFFLPWEKMT IAGTTDTPTD VTHHPIPSEE DINFILNEVR NYLSSDVEVR RGDVLAAWSG IRPLVTDPKS ADTQSISRNH VVDISDSGLI TIAGGKWTTY RSMAEDTVDA AVKFHNLNAG PSRTVGLFLQ GGKDWSPTLY IRLVQDYGLE SEVAQHLAKT YGDKAFEVAK MASVTGKRWP VVGVRLVSEF PYIEAEVKYG IKEYACTAVD MISRRTRLAF LNVQAAEEAL PRIVELMGRE LNWSELRKQE ELETATRFLY YEMGYKSRTE QLTDSTEISL LPSDIDRYKK RFHKFDEDEK GFITIVDVQR VLESINVQMD ENTLHEILCE VDLNKNGQVE LHEFLQLMSA VQKGRVSGSR LAILMKTAEE NLDRRVPIPV DRSCGGL // ID GPX1_MOUSE Reviewed; 201 AA. AC P11352; P12079; Q544W3; Q5RJH8; Q9CR54; DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot. DT 26-FEB-2008, sequence version 2. DT 19-MAR-2014, entry version 143. DE RecName: Full=Glutathione peroxidase 1; DE Short=GPx-1; DE Short=GSHPx-1; DE EC=1.11.1.9; DE AltName: Full=Cellular glutathione peroxidase; DE AltName: Full=Selenium-dependent glutathione peroxidase 1; GN Name=Gpx1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SELENOCYSTEINE AT SEC-47. RC TISSUE=Erythrocyte; RX PubMed=3015592; RA Chambers I., Frampton J., Goldfarb P., Affara N., McBain W., RA Harrison P.R.; RT "The structure of the mouse glutathione peroxidase gene: the RT selenocysteine in the active site is encoded by the 'termination' RT codon, TGA."; RL EMBO J. 5:1221-1227(1986). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J, and NOD; RC TISSUE=Bone marrow, Embryonic liver, Kidney, and Liver; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6; TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP PARTIAL NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Liver; RX PubMed=2771650; DOI=10.1093/nar/17.15.6390; RA Dunn D.K., Howells D.D., Richardson J., Goldfarb P.S.; RT "A human cDNA sequence for a novel glutathione peroxidase-related RT selenopeptide, GPRP."; RL Nucleic Acids Res. 17:6390-6390(1989). RN [5] RP INTERACTION WITH MIEN1. RX PubMed=17503775; DOI=10.1021/bi602462q; RA Dikiy A., Novoselov S.V., Fomenko D.E., Sengupta A., Carlson B.A., RA Cerny R.L., Ginalski K., Grishin N.V., Hatfield D.L., Gladyshev V.N.; RT "SelT, SelW, SelH, and Rdx12: genomics and molecular insights into the RT functions of selenoproteins of a novel thioredoxin-like family."; RL Biochemistry 46:6871-6882(2007). RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=17242355; DOI=10.1073/pnas.0609836104; RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; RT "Large-scale phosphorylation analysis of mouse liver."; RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). RN [7] RP BIOPHYSICOCHEMICAL PROPERTIES, SELENOCYSTEINE AT SEC-47, PARTIAL LOSS RP OF SELENIUM IN ABSENCE OF SOD1, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RC TISSUE=Liver; RX PubMed=21420488; DOI=10.1016/j.freeradbiomed.2011.03.018; RA Wang S.K., Weaver J.D., Zhang S., Lei X.G.; RT "Knockout of SOD1 promotes conversion of selenocysteine to RT dehydroalanine in murine hepatic GPX1 protein."; RL Free Radic. Biol. Med. 51:197-204(2011). RN [8] RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-62; LYS-86; LYS-112 AND RP LYS-146, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Liver; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., RA Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). RN [9] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-62; LYS-86; LYS-112; LYS-119 RP AND LYS-146, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Liver; RX PubMed=23576753; DOI=10.1073/pnas.1302961110; RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., RA Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.; RT "Label-free quantitative proteomics of the lysine acetylome in RT mitochondria identifies substrates of SIRT3 in metabolic pathways."; RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013). CC -!- FUNCTION: Protects the hemoglobin in erythrocytes from oxidative CC breakdown. CC -!- CATALYTIC ACTIVITY: 2 glutathione + H(2)O(2) = glutathione CC disulfide + 2 H(2)O. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=14 uM for H(2)O(2) (at 25 degrees Celsius, in 0.1 M phosphate CC buffer, pH 7.0); CC KM=29 uM for tert-butylperoxide (at 25 degrees Celsius, in 0.1 M CC phosphate buffer, pH 7.0); CC Vmax=319 mM/min/mg enzyme toward H(2)O(2) (at 25 degrees CC Celsius, in 0.1 M phosphate buffer, pH 7.0); CC Vmax=182 mM/min/mg enzyme toward tert-butylperoxide (at 25 CC degrees Celsius, in 0.1 M phosphate buffer, pH 7.0); CC -!- SUBUNIT: Homotetramer. Interacts with MIEN1. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- PTM: During periods of oxidative stress, Sec-47 may react with a CC superoxide radical, irreversibly lose hydroselenide and be CC converted to dehydroalanine (PubMed:21420488). CC -!- MISCELLANEOUS: In the absence of Sod1, Gpx1 in the liver undergoes CC a 40% reduction in catalytic activity as a result of the CC decomposition of Sec-47 to dehydroalanine (PubMed:21420488). CC -!- SIMILARITY: Belongs to the glutathione peroxidase family. CC -!- CAUTION: PubMed:2771650 sequence was originally thought to CC originate from human. CC -!- SEQUENCE CAUTION: CC Sequence=CAB43535.1; Type=Miscellaneous discrepancy; Note=Number of sequencing artifacts; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X03920; CAA27558.1; -; Genomic_DNA. DR EMBL; AK002245; BAC55244.1; -; mRNA. DR EMBL; AK010999; BAC55252.1; -; mRNA. DR EMBL; AK011019; BAC55253.1; -; mRNA. DR EMBL; AK028171; BAC55257.1; -; mRNA. DR EMBL; AK150548; BAE29650.1; -; mRNA. DR EMBL; AK154833; BAE32862.1; -; mRNA. DR EMBL; AK160388; BAE35760.1; -; mRNA. DR EMBL; BC086649; AAH86649.1; -; mRNA. DR EMBL; X15667; CAB43535.1; ALT_SEQ; mRNA. DR PIR; A25106; OPMSE. DR PIR; S05317; S05317. DR RefSeq; NP_032186.2; NM_008160.6. DR UniGene; Mm.1090; -. DR ProteinModelPortal; P11352; -. DR SMR; P11352; 13-195. DR IntAct; P11352; 6. DR MINT; MINT-1855025; -. DR PeroxiBase; 3709; MmGPx01. DR PhosphoSite; P11352; -. DR REPRODUCTION-2DPAGE; IPI00319652; -. DR REPRODUCTION-2DPAGE; P11352; -. DR SWISS-2DPAGE; P11352; -. DR PaxDb; P11352; -. DR PRIDE; P11352; -. DR Ensembl; ENSMUST00000082429; ENSMUSP00000081010; ENSMUSG00000063856. DR GeneID; 14775; -. DR KEGG; mmu:14775; -. DR UCSC; uc009rpf.3; mouse. DR CTD; 2876; -. DR MGI; MGI:104887; Gpx1. DR eggNOG; COG0386; -. DR GeneTree; ENSGT00740000115226; -. DR HOGENOM; HOG000277055; -. DR HOVERGEN; HBG004333; -. DR InParanoid; P11352; -. DR KO; K00432; -. DR OMA; CEVNGEK; -. DR OrthoDB; EOG7KQ23C; -. DR TreeFam; TF105318; -. DR ChiTaRS; GPX1; mouse. DR NextBio; 286877; -. DR PRO; PR:P11352; -. DR Bgee; P11352; -. DR CleanEx; MM_GPX1; -. DR Genevestigator; P11352; -. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR GO; GO:0005634; C:nucleus; IEA:Ensembl. DR GO; GO:0004866; F:endopeptidase inhibitor activity; IEA:Ensembl. DR GO; GO:0043295; F:glutathione binding; IEA:Ensembl. DR GO; GO:0004602; F:glutathione peroxidase activity; IDA:MGI. DR GO; GO:0047066; F:phospholipid-hydroperoxide glutathione peroxidase activity; IEA:Ensembl. DR GO; GO:0008430; F:selenium binding; IEA:Ensembl. DR GO; GO:0007568; P:aging; IEA:Ensembl. DR GO; GO:0060055; P:angiogenesis involved in wound healing; IMP:MGI. DR GO; GO:0043534; P:blood vessel endothelial cell migration; IMP:MGI. DR GO; GO:0045454; P:cell redox homeostasis; IEA:Ensembl. DR GO; GO:0001885; P:endothelial cell development; IMP:MGI. DR GO; GO:0045444; P:fat cell differentiation; IMP:MGI. DR GO; GO:0006749; P:glutathione metabolic process; IEA:Ensembl. DR GO; GO:0060047; P:heart contraction; IMP:MGI. DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IMP:MGI. DR GO; GO:0051702; P:interaction with symbiont; IGI:MGI. DR GO; GO:0008631; P:intrinsic apoptotic signaling pathway in response to oxidative stress; IMP:MGI. DR GO; GO:0051450; P:myoblast proliferation; IMP:MGI. DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:MGI. DR GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IEA:Ensembl. DR GO; GO:1902042; P:negative regulation of extrinsic apoptotic signaling pathway via death domain receptors; IEA:Ensembl. DR GO; GO:0002862; P:negative regulation of inflammatory response to antigenic stimulus; IGI:MGI. DR GO; GO:1902176; P:negative regulation of intrinsic apoptotic signaling pathway in response to oxidative stress; IMP:MGI. DR GO; GO:0090201; P:negative regulation of release of cytochrome c from mitochondria; IEA:Ensembl. DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; IMP:MGI. DR GO; GO:0018158; P:protein oxidation; IMP:MGI. DR GO; GO:0040029; P:regulation of gene expression, epigenetic; IEA:Ensembl. DR GO; GO:0033599; P:regulation of mammary gland epithelial cell proliferation; IEA:Ensembl. DR GO; GO:0043523; P:regulation of neuron apoptotic process; IMP:MGI. DR GO; GO:0061136; P:regulation of proteasomal protein catabolic process; IEA:Ensembl. DR GO; GO:0032355; P:response to estradiol; IEA:Ensembl. DR GO; GO:0051593; P:response to folic acid; IEA:Ensembl. DR GO; GO:0010332; P:response to gamma radiation; IGI:MGI. DR GO; GO:0009749; P:response to glucose; IEA:Ensembl. DR GO; GO:0033194; P:response to hydroperoxide; IMP:MGI. DR GO; GO:0006982; P:response to lipid hydroperoxide; IEA:Ensembl. DR GO; GO:0035094; P:response to nicotine; IEA:Ensembl. DR GO; GO:0010269; P:response to selenium ion; IEA:Ensembl. DR GO; GO:0009609; P:response to symbiotic bacterium; IGI:MGI. DR GO; GO:0009636; P:response to toxic substance; IMP:MGI. DR GO; GO:0009410; P:response to xenobiotic stimulus; IMP:MGI. DR GO; GO:0007605; P:sensory perception of sound; IMP:MGI. DR GO; GO:0048741; P:skeletal muscle fiber development; IMP:MGI. DR GO; GO:0043403; P:skeletal muscle tissue regeneration; IMP:MGI. DR GO; GO:0001659; P:temperature homeostasis; IGI:MGI. DR GO; GO:0006641; P:triglyceride metabolic process; IMP:MGI. DR GO; GO:0009650; P:UV protection; IEA:Ensembl. DR GO; GO:0042311; P:vasodilation; IMP:MGI. DR Gene3D; 3.40.30.10; -; 1. DR InterPro; IPR000889; Glutathione_peroxidase. DR InterPro; IPR012336; Thioredoxin-like_fold. DR PANTHER; PTHR11592; PTHR11592; 1. DR Pfam; PF00255; GSHPx; 1. DR PIRSF; PIRSF000303; Glutathion_perox; 1. DR PRINTS; PR01011; GLUTPROXDASE. DR SUPFAM; SSF52833; SSF52833; 1. DR PROSITE; PS00460; GLUTATHIONE_PEROXID_1; 1. DR PROSITE; PS00763; GLUTATHIONE_PEROXID_2; 1. DR PROSITE; PS51355; GLUTATHIONE_PEROXID_3; 1. PE 1: Evidence at protein level; KW Acetylation; Complete proteome; Cytoplasm; Oxidoreductase; Peroxidase; KW Phosphoprotein; Reference proteome; Selenocysteine. FT CHAIN 1 201 Glutathione peroxidase 1. FT /FTId=PRO_0000066613. FT ACT_SITE 47 47 FT SITE 47 47 Subject to oxidation and hydroselenide FT loss to dehydroalanine. FT NON_STD 47 47 Selenocysteine. FT MOD_RES 7 7 Phosphoserine. FT MOD_RES 62 62 N6-acetyllysine; alternate. FT MOD_RES 62 62 N6-succinyllysine; alternate. FT MOD_RES 86 86 N6-acetyllysine; alternate. FT MOD_RES 86 86 N6-succinyllysine; alternate. FT MOD_RES 112 112 N6-acetyllysine; alternate. FT MOD_RES 112 112 N6-succinyllysine; alternate. FT MOD_RES 119 119 N6-acetyllysine. FT MOD_RES 146 146 N6-acetyllysine; alternate. FT MOD_RES 146 146 N6-succinyllysine; alternate. SQ SEQUENCE 201 AA; 22329 MW; 401D065165D8AF5C CRC64; MCAARLSAAA QSTVYAFSAR PLTGGEPVSL GSLRGKVLLI ENVASLUGTT IRDYTEMNDL QKRLGPRGLV VLGFPCNQFG HQENGKNEEI LNSLKYVRPG GGFEPNFTLF EKCEVNGEKA HPLFTFLRNA LPTPSDDPTA LMTDPKYIIW SPVCRNDIAW NFEKFLVGPD GVPVRRYSRR FRTIDIEPDI ETLLSQQSGN S // ID GPX2_MOUSE Reviewed; 190 AA. AC Q9JHC0; Q3V2B2; DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot. DT 26-FEB-2008, sequence version 3. DT 19-FEB-2014, entry version 101. DE RecName: Full=Glutathione peroxidase 2; DE Short=GPx-2; DE Short=GSHPx-2; DE EC=1.11.1.9; DE AltName: Full=Glutathione peroxidase-gastrointestinal; DE Short=GPx-GI; DE Short=GSHPx-GI; GN Name=Gpx2; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=129; RX PubMed=8661011; DOI=10.1006/geno.1996.0227; RA Chu F.-F., Esworthy R.S., Burmeister M.; RT "The mouse glutathione peroxidase Gpx2 gene maps to chromosome 12; its RT pseudogene Gpx2-ps maps to chromosome 7."; RL Genomics 33:516-518(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Colon; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- CATALYTIC ACTIVITY: 2 glutathione + H(2)O(2) = glutathione CC disulfide + 2 H(2)O. CC -!- SUBUNIT: Homotetramer (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the glutathione peroxidase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U62658; AAD41533.1; -; Genomic_DNA. DR EMBL; AK131940; BAE20886.1; -; mRNA. DR EMBL; BC010823; AAH10823.1; -; mRNA. DR EMBL; BC034335; AAH34335.1; -; mRNA. DR EMBL; BC039658; AAH39658.1; -; mRNA. DR EMBL; BC054848; AAH54848.2; -; mRNA. DR RefSeq; NP_109602.2; NM_030677.2. DR UniGene; Mm.441856; -. DR ProteinModelPortal; Q9JHC0; -. DR SMR; Q9JHC0; 4-187. DR PeroxiBase; 3710; MmGPx02. DR PhosphoSite; Q9JHC0; -. DR PRIDE; Q9JHC0; -. DR Ensembl; ENSMUST00000082431; ENSMUSP00000081012; ENSMUSG00000042808. DR GeneID; 14776; -. DR KEGG; mmu:14776; -. DR UCSC; uc007nys.1; mouse. DR CTD; 2877; -. DR MGI; MGI:106609; Gpx2. DR eggNOG; COG0386; -. DR GeneTree; ENSGT00740000115226; -. DR HOGENOM; HOG000277055; -. DR HOVERGEN; HBG004333; -. DR InParanoid; Q9JHC0; -. DR KO; K00432; -. DR OrthoDB; EOG7KQ23C; -. DR TreeFam; TF105318; -. DR NextBio; 286881; -. DR PRO; PR:Q9JHC0; -. DR Bgee; Q9JHC0; -. DR CleanEx; MM_GPX2; -. DR Genevestigator; Q9JHC0; -. DR GO; GO:0005829; C:cytosol; TAS:MGI. DR GO; GO:0005634; C:nucleus; IEA:Ensembl. DR GO; GO:0004602; F:glutathione peroxidase activity; IMP:MGI. DR GO; GO:0051702; P:interaction with symbiont; IGI:MGI. DR GO; GO:0002862; P:negative regulation of inflammatory response to antigenic stimulus; IGI:MGI. DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro. DR GO; GO:0009609; P:response to symbiotic bacterium; IGI:MGI. DR GO; GO:0001659; P:temperature homeostasis; IGI:MGI. DR Gene3D; 3.40.30.10; -; 1. DR InterPro; IPR000889; Glutathione_peroxidase. DR InterPro; IPR012336; Thioredoxin-like_fold. DR PANTHER; PTHR11592; PTHR11592; 1. DR Pfam; PF00255; GSHPx; 1. DR PIRSF; PIRSF000303; Glutathion_perox; 1. DR PRINTS; PR01011; GLUTPROXDASE. DR SUPFAM; SSF52833; SSF52833; 1. DR PROSITE; PS00460; GLUTATHIONE_PEROXID_1; 1. DR PROSITE; PS00763; GLUTATHIONE_PEROXID_2; 1. DR PROSITE; PS51355; GLUTATHIONE_PEROXID_3; 1. PE 2: Evidence at transcript level; KW Complete proteome; Cytoplasm; Oxidoreductase; Peroxidase; KW Reference proteome; Selenocysteine. FT CHAIN 1 190 Glutathione peroxidase 2. FT /FTId=PRO_0000066622. FT ACT_SITE 40 40 FT NON_STD 40 40 Selenocysteine. FT CONFLICT 14 14 I -> V (in Ref. 2; BAE20886). SQ SEQUENCE 190 AA; 21990 MW; F66BDD7A431E1A6D CRC64; MAYIAKSFYD LSAIGLDGEK IDFNTFRGRA VLIENVASLU GTTTRDYNQL NELQCRFPRR LVVLGFPCNQ FGHQENCQNE EILNSLKYVR PGGGYQPTFS LTQKCDVNGQ NEHPVFAYLK DKLPYPYDDP FSLMTDPKLI IWSPVRRSDV SWNFEKFLIG PEGEPFRRYS RSFQTINIEP DIKRLLKVAI // ID GPX3_MOUSE Reviewed; 226 AA. AC P46412; Q5XKR0; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 26-FEB-2008, sequence version 2. DT 19-FEB-2014, entry version 122. DE RecName: Full=Glutathione peroxidase 3; DE Short=GPx-3; DE Short=GSHPx-3; DE EC=1.11.1.9; DE AltName: Full=Plasma glutathione peroxidase; DE Short=GPx-P; DE Short=GSHPx-P; DE Flags: Precursor; GN Name=Gpx3; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=C57BL/6J; TISSUE=Kidney; RX PubMed=7929449; RA Maser R.L., Magenheimer B.S., Calvet J.P.; RT "Mouse plasma glutathione peroxidase. cDNA sequence analysis and renal RT proximal tubular expression and secretion."; RL J. Biol. Chem. 269:27066-27073(1994). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Heart, Kidney, and Liver; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N, and NMRI; TISSUE=Colon, Kidney, and Mammary tumor; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-29. RX PubMed=8566787; DOI=10.1016/0378-1119(95)00551-X; RA Schwaab V., Baud E., Ghyselinck N.B., Mattei M.-G., Dufaure J.-P., RA Drevet J.R.; RT "Cloning of the mouse gene encoding plasma glutathione peroxidase: RT organization, sequence and chromosomal localization."; RL Gene 167:25-31(1995). CC -!- FUNCTION: Protects cells and enzymes from oxidative damage, by CC catalyzing the reduction of hydrogen peroxide, lipid peroxides and CC organic hydroperoxide, by glutathione. CC -!- CATALYTIC ACTIVITY: 2 glutathione + H(2)O(2) = glutathione CC disulfide + 2 H(2)O. CC -!- SUBUNIT: Homotetramer. CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- TISSUE SPECIFICITY: Secreted in plasma. CC -!- SIMILARITY: Belongs to the glutathione peroxidase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U13705; AAA62283.2; -; mRNA. DR EMBL; AK002219; BAC55243.1; -; mRNA. DR EMBL; AK004942; BAC55250.1; -; mRNA. DR EMBL; AK146760; BAE27413.1; -; mRNA. DR EMBL; BC003339; AAH03339.1; -; mRNA. DR EMBL; BC037027; AAH37027.1; -; mRNA. DR EMBL; BC049235; AAH49235.1; -; mRNA. DR EMBL; BC061950; AAH61950.1; -; mRNA. DR EMBL; X84742; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR PIR; A55086; A55086. DR RefSeq; NP_032187.2; NM_008161.3. DR UniGene; Mm.200916; -. DR ProteinModelPortal; P46412; -. DR SMR; P46412; 36-221. DR IntAct; P46412; 3. DR MINT; MINT-4096578; -. DR STRING; 10090.ENSMUSP00000081011; -. DR PeroxiBase; 3711; MmGPx03. DR PaxDb; P46412; -. DR PRIDE; P46412; -. DR Ensembl; ENSMUST00000082430; ENSMUSP00000081011; ENSMUSG00000018339. DR GeneID; 14778; -. DR KEGG; mmu:14778; -. DR UCSC; uc007iyk.2; mouse. DR CTD; 2878; -. DR MGI; MGI:105102; Gpx3. DR eggNOG; COG0386; -. DR GeneTree; ENSGT00740000115226; -. DR HOGENOM; HOG000277055; -. DR HOVERGEN; HBG004333; -. DR InParanoid; P46412; -. DR KO; K00432; -. DR OMA; WYHRTTV; -. DR TreeFam; TF105318; -. DR ChiTaRS; GPX3; mouse. DR NextBio; 286887; -. DR PRO; PR:P46412; -. DR Bgee; P46412; -. DR CleanEx; MM_GPX3; -. DR Genevestigator; P46412; -. DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB. DR GO; GO:0004602; F:glutathione peroxidase activity; ISS:UniProtKB. DR GO; GO:0008430; F:selenium binding; ISS:UniProtKB. DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IDA:MGI. DR GO; GO:0051289; P:protein homotetramerization; ISS:UniProtKB. DR Gene3D; 3.40.30.10; -; 1. DR InterPro; IPR000889; Glutathione_peroxidase. DR InterPro; IPR012336; Thioredoxin-like_fold. DR PANTHER; PTHR11592; PTHR11592; 1. DR Pfam; PF00255; GSHPx; 1. DR PIRSF; PIRSF000303; Glutathion_perox; 1. DR PRINTS; PR01011; GLUTPROXDASE. DR SUPFAM; SSF52833; SSF52833; 1. DR PROSITE; PS00460; GLUTATHIONE_PEROXID_1; 1. DR PROSITE; PS00763; GLUTATHIONE_PEROXID_2; 1. DR PROSITE; PS51355; GLUTATHIONE_PEROXID_3; 1. PE 2: Evidence at transcript level; KW Complete proteome; Oxidoreductase; Peroxidase; Reference proteome; KW Secreted; Selenocysteine; Signal. FT SIGNAL 1 24 Potential. FT CHAIN 25 226 Glutathione peroxidase 3. FT /FTId=PRO_0000013063. FT ACT_SITE 73 73 FT NON_STD 73 73 Selenocysteine. FT CONFLICT 6 7 RA -> Q (in Ref. 4). FT CONFLICT 21 21 P -> A (in Ref. 4). FT CONFLICT 24 29 GQEKSK -> DKRSLR (in Ref. 4). SQ SEQUENCE 226 AA; 25424 MW; D9706574929E3F86 CRC64; MARILRASCL LSLLLAGFVP PGRGQEKSKT DCHGGMSGTI YEYGALTIDG EEYIPFKQYA GKYILFVNVA SYUGLTDQYL ELNALQEELG PFGLVILGFP SNQFGKQEPG ENSEILPSLK YVRPGGGFVP NFQLFEKGDV NGEKEQKFYT FLKNSCPPTA ELLGSPGRLF WEPMKIHDIR WNFEKFLVGP DGIPVMRWYH RTTVSNVKMD ILSYMRRQAA LSARGK // ID GPX42_MOUSE Reviewed; 253 AA. AC Q91XR9; Q8K4U8; DT 23-MAY-2003, integrated into UniProtKB/Swiss-Prot. DT 26-FEB-2008, sequence version 3. DT 19-MAR-2014, entry version 93. DE RecName: Full=Phospholipid hydroperoxide glutathione peroxidase, nuclear; DE EC=1.11.1.12; DE AltName: Full=Glutathione peroxidase 4; DE Short=GPx-4; DE Short=GSHPx-4; GN Name=Gpx4; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RC TISSUE=Testis; RX PubMed=11344099; RA Pfeifer H., Conrad M., Roethlein D., Kyriakopoulos A., Brielmeier M., RA Bornkamm G.W., Behne D.; RT "Identification of a specific sperm nuclei selenoenzyme necessary for RT protamine thiol cross-linking during sperm maturation."; RL FASEB J. 15:1236-1238(2001). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=129/SvJ; TISSUE=Liver; RX PubMed=12745070; DOI=10.1016/S0006-291X(03)00734-4; RA Imai H., Hirao F., Sakamoto T., Sekine K., Mizukura Y., Saito M., RA Kitamoto T., Hayasaka M., Hanaoka K., Nakagawa Y.; RT "Early embryonic lethality caused by targeted disruption of the mouse RT PHGPx gene."; RL Biochem. Biophys. Res. Commun. 305:278-286(2003). RN [3] RP FUNCTION. RX PubMed=12566075; DOI=10.1016/S0891-5849(02)01360-6; RA Yant L.J., Ran Q., Rao L., Van Remmen H., Shibatani T., Belter J.G., RA Motta L., Richardson A., Prolla T.A.; RT "The selenoprotein GPX4 is essential for mouse development and RT protects from radiation and oxidative damage insults."; RL Free Radic. Biol. Med. 34:496-502(2003). CC -!- FUNCTION: Could play a major role in protecting mammals from the CC toxicity of ingested lipid hydroperoxides. Essential for embryonic CC development. Protects from radiation and oxidative damage. CC Stabilizes the condensed chromatin in sperm nuclei and is CC necessary for male fertility. CC -!- CATALYTIC ACTIVITY: 2 glutathione + a lipid hydroperoxide = CC glutathione disulfide + lipid + 2 H(2)O. CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=Nuclear; CC IsoId=Q91XR9-1; Sequence=Displayed; CC Name=Mitochondrial; CC IsoId=O70325-1; Sequence=External; CC Name=Cytoplasmic; CC IsoId=O70325-2; Sequence=External; CC Note=Produced by alternative initiation at Met-28 of isoform CC Mitochondrial; CC -!- TISSUE SPECIFICITY: Expressed exclusively in sperm. CC -!- SIMILARITY: Belongs to the glutathione peroxidase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF274027; AAK74112.1; -; mRNA. DR EMBL; AB030643; BAC06509.1; -; Genomic_DNA. DR RefSeq; NP_001032830.2; NM_001037741.3. DR UniGene; Mm.359573; -. DR ProteinModelPortal; Q91XR9; -. DR SMR; Q91XR9; 89-253. DR STRING; 10090.ENSMUSP00000094863; -. DR PeroxiBase; 3865; MmGPx04-B. DR PhosphoSite; Q91XR9; -. DR PRIDE; Q91XR9; -. DR GeneID; 625249; -. DR KEGG; mmu:625249; -. DR CTD; 2879; -. DR MGI; MGI:104767; Gpx4. DR HOGENOM; HOG000277054; -. DR HOVERGEN; HBG004333; -. DR InParanoid; Q91XR9; -. DR KO; K05361; -. DR ChiTaRS; GPX4; mouse. DR NextBio; 418158; -. DR PRO; PR:Q91XR9; -. DR CleanEx; MM_GPX4; -. DR Genevestigator; Q91XR9; -. DR GO; GO:0005829; C:cytosol; IDA:MGI. DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:MGI. DR GO; GO:0005635; C:nuclear envelope; IDA:MGI. DR GO; GO:0004602; F:glutathione peroxidase activity; IDA:MGI. DR GO; GO:0047066; F:phospholipid-hydroperoxide glutathione peroxidase activity; IEA:UniProtKB-EC. DR GO; GO:0006325; P:chromatin organization; IDA:MGI. DR GO; GO:0007275; P:multicellular organismal development; IEA:UniProtKB-KW. DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro. DR GO; GO:0007283; P:spermatogenesis; IDA:MGI. DR Gene3D; 3.40.30.10; -; 1. DR InterPro; IPR000889; Glutathione_peroxidase. DR InterPro; IPR012336; Thioredoxin-like_fold. DR PANTHER; PTHR11592; PTHR11592; 1. DR Pfam; PF00255; GSHPx; 1. DR PRINTS; PR01011; GLUTPROXDASE. DR SUPFAM; SSF52833; SSF52833; 1. DR PROSITE; PS00460; GLUTATHIONE_PEROXID_1; 1. DR PROSITE; PS00763; GLUTATHIONE_PEROXID_2; 1. DR PROSITE; PS51355; GLUTATHIONE_PEROXID_3; 1. PE 2: Evidence at transcript level; KW Alternative splicing; Complete proteome; Developmental protein; KW Nucleus; Oxidoreductase; Peroxidase; Reference proteome; KW Selenocysteine. FT CHAIN 1 253 Phospholipid hydroperoxide glutathione FT peroxidase, nuclear. FT /FTId=PRO_0000066625. FT ACT_SITE 129 129 By similarity. FT NON_STD 129 129 Selenocysteine (By similarity). SQ SEQUENCE 253 AA; 29252 MW; C55E282753231653 CRC64; MGRAAARKRG RCRQRGGSPR GRRRRGPGRQ SPRKRPGPRR RKARARRRRR ARPRRMEPIP EPFNPGPLLQ EPPQYCNSSE FLGLCASRDD WRCARSMHEF SAKDIDGHMV CLDKYRGFVC IVTNVASQUG KTDVNYTQLV DLHARYAECG LRILAFPCNQ FGRQEPGSNQ EIKEFAAGYN VKFDMYSKIC VNGDDAHPLW KWMKVQPKGR GMLGNAIKWN FTKFLIDKNG CEVKRYGPME EPQVIERDLP CYL // ID GPX41_MOUSE Reviewed; 197 AA. AC O70325; O35560; Q9JK35; DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot. DT 26-FEB-2008, sequence version 4. DT 19-MAR-2014, entry version 131. DE RecName: Full=Phospholipid hydroperoxide glutathione peroxidase, mitochondrial; DE Short=PHGPx; DE EC=1.11.1.12; DE AltName: Full=Glutathione peroxidase 4; DE Short=GPx-4; DE Short=GSHPx-4; DE Flags: Precursor; GN Name=Gpx4; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=CD-1; TISSUE=Testis; RX PubMed=9370288; DOI=10.1016/S0378-1119(97)00321-1; RA Nam S.-Y., Nakamuta N., Kurohmaru M., Hayashi Y.; RT "Cloning and sequencing of the cDNA encoding a phospholipid RT hydroperoxide glutathione peroxidase."; RL Gene 198:245-249(1997). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=C57BL/6N; RX PubMed=10100845; DOI=10.1016/S0014-5793(99)00221-5; RA Borchert A., Schnurr K., Thiele B.J., Kuehn H.; RT "Cloning of the mouse phospholipid hydroperoxide glutathione RT peroxidase gene."; RL FEBS Lett. 446:223-227(1999). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. RC STRAIN=BALB/c, and C57BL/6J; TISSUE=Myocardium, and Testis; RX PubMed=10341094; DOI=10.1007/s003359901053; RA Knopp E.A., Arndt T.L., Eng K.L., Caldwell M., LeBoeuf R.C., RA Deeb S.S., O'Brien K.D.; RT "Murine phospholipid hydroperoxide glutathione peroxidase: cDNA RT sequence, tissue expression, and mapping."; RL Mamm. Genome 10:601-605(1999). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=129/SvJ; TISSUE=Liver; RX PubMed=12745070; DOI=10.1016/S0006-291X(03)00734-4; RA Imai H., Hirao F., Sakamoto T., Sekine K., Mizukura Y., Saito M., RA Kitamoto T., Hayasaka M., Hanaoka K., Nakagawa Y.; RT "Early embryonic lethality caused by targeted disruption of the mouse RT PHGPx gene."; RL Biochem. Biophys. Res. Commun. 305:278-286(2003). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Testis; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [6] RP FUNCTION. RX PubMed=12566075; DOI=10.1016/S0891-5849(02)01360-6; RA Yant L.J., Ran Q., Rao L., Van Remmen H., Shibatani T., Belter J.G., RA Motta L., Richardson A., Prolla T.A.; RT "The selenoprotein GPX4 is essential for mouse development and RT protects from radiation and oxidative damage insults."; RL Free Radic. Biol. Med. 34:496-502(2003). RN [7] RP DISRUPTION PHENOTYPE, AND FUNCTION. RX PubMed=18762024; DOI=10.1016/j.cmet.2008.07.005; RA Seiler A., Schneider M., Foerster H., Roth S., Wirth E.K., Culmsee C., RA Plesnila N., Kremmer E., Raadmark O., Wurst W., Bornkamm G.W., RA Schweizer U., Conrad M.; RT "Glutathione peroxidase 4 senses and translates oxidative stress into RT 12/15-lipoxygenase dependent- and AIF-mediated cell death."; RL Cell Metab. 8:237-248(2008). RN [8] RP DISRUPTION PHENOTYPE, FUNCTION, AND TISSUE SPECIFICITY. RX PubMed=19417079; DOI=10.1096/fj.09-132795; RA Schneider M., Forster H., Boersma A., Seiler A., Wehnes H., RA Sinowatz F., Neumueller C., Deutsch M.J., Walch A., RA Hrabe de Angelis M., Wurst W., Ursini F., Roveri A., Maleszewski M., RA Maiorino M., Conrad M.; RT "Mitochondrial glutathione peroxidase 4 disruption causes male RT infertility."; RL FASEB J. 23:3233-3242(2009). CC -!- FUNCTION: Protects cells against membrane lipid peroxidation and CC cell death. Isoform mitochondrial is required for normal sperm CC development and male fertility. Could play a major role in CC protecting mammals from the toxicity of ingested lipid CC hydroperoxides. Essential for embryonic development. Protects from CC radiation and oxidative damage. CC -!- CATALYTIC ACTIVITY: 2 glutathione + a lipid hydroperoxide = CC glutathione disulfide + lipid + 2 H(2)O. CC -!- SUBUNIT: Monomer (By similarity). CC -!- SUBCELLULAR LOCATION: Mitochondrion. Cytoplasm. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing, Alternative initiation; Named isoforms=3; CC Name=Mitochondrial; CC IsoId=O70325-1; Sequence=Displayed; CC Name=Nuclear; CC IsoId=Q91XR9-1; Sequence=External; CC Name=Cytoplasmic; CC IsoId=O70325-2; Sequence=VSP_018743; CC Note=Produced by alternative initiation at Met-28 of isoform CC Mitochondrial; CC -!- TISSUE SPECIFICITY: Detected in testis and sperm midpiece (at CC protein level). Present primarily in testis. CC -!- DISRUPTION PHENOTYPE: Embryonic lethality. The embryos die after CC about 7.5 days of development. Causes neurodegeneration. Selective CC disruption of isoform mitochondrial causes sperm abnormalities and CC male infertility. CC -!- SIMILARITY: Belongs to the glutathione peroxidase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; D87896; BAA22780.1; -; mRNA. DR EMBL; AJ012104; CAB42657.2; -; Genomic_DNA. DR EMBL; AF045768; AAC15832.1; -; mRNA. DR EMBL; AF045769; AAC15833.1; -; mRNA. DR EMBL; AF044056; AAC14560.1; -; Genomic_DNA. DR EMBL; AB030643; BAC06507.1; -; Genomic_DNA. DR EMBL; AB030643; BAC06508.1; -; Genomic_DNA. DR EMBL; AB030728; BAC06511.1; -; Genomic_DNA. DR EMBL; AK006441; BAC55251.1; -; mRNA. DR RefSeq; NP_032188.3; NM_008162.3. DR UniGene; Mm.359573; -. DR ProteinModelPortal; O70325; -. DR SMR; O70325; 33-197. DR IntAct; O70325; 1. DR PeroxiBase; 3714; MmGPx04-A. DR PeroxiBase; 3867; MmGPx04-C. DR PaxDb; O70325; -. DR PRIDE; O70325; -. DR Ensembl; ENSMUST00000105372; ENSMUSP00000101011; ENSMUSG00000075706. [O70325-1] DR GeneID; 625249; -. DR KEGG; mmu:625249; -. DR UCSC; uc007gbk.1; mouse. [O70325-1] DR CTD; 2879; -. DR MGI; MGI:104767; Gpx4. DR eggNOG; COG0386; -. DR GeneTree; ENSGT00740000115371; -. DR HOGENOM; HOG000277054; -. DR HOVERGEN; HBG004333; -. DR KO; K05361; -. DR OMA; HAGDILW; -. DR OrthoDB; EOG7B5WZH; -. DR ChiTaRS; GPX4; mouse. DR NextBio; 418158; -. DR PRO; PR:O70325; -. DR Bgee; O70325; -. DR CleanEx; MM_GPX4; -. DR Genevestigator; O70325; -. DR GO; GO:0005829; C:cytosol; IDA:MGI. DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:MGI. DR GO; GO:0005635; C:nuclear envelope; IDA:MGI. DR GO; GO:0004602; F:glutathione peroxidase activity; IDA:MGI. DR GO; GO:0047066; F:phospholipid-hydroperoxide glutathione peroxidase activity; IEA:UniProtKB-EC. DR GO; GO:0006325; P:chromatin organization; IDA:MGI. DR GO; GO:0007275; P:multicellular organismal development; IEA:UniProtKB-KW. DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro. DR GO; GO:0007283; P:spermatogenesis; IDA:MGI. DR Gene3D; 3.40.30.10; -; 1. DR InterPro; IPR000889; Glutathione_peroxidase. DR InterPro; IPR012336; Thioredoxin-like_fold. DR PANTHER; PTHR11592; PTHR11592; 1. DR Pfam; PF00255; GSHPx; 1. DR PIRSF; PIRSF000303; Glutathion_perox; 1. DR PRINTS; PR01011; GLUTPROXDASE. DR SUPFAM; SSF52833; SSF52833; 1. DR PROSITE; PS00460; GLUTATHIONE_PEROXID_1; 1. DR PROSITE; PS00763; GLUTATHIONE_PEROXID_2; 1. DR PROSITE; PS51355; GLUTATHIONE_PEROXID_3; 1. PE 1: Evidence at protein level; KW Alternative initiation; Alternative splicing; Complete proteome; KW Cytoplasm; Developmental protein; Mitochondrion; Oxidoreductase; KW Peroxidase; Reference proteome; Selenocysteine; Transit peptide. FT TRANSIT 1 ? Mitochondrion (Potential). FT CHAIN ? 197 Phospholipid hydroperoxide glutathione FT peroxidase, mitochondrial. FT /FTId=PRO_0000013069. FT ACT_SITE 73 73 FT NON_STD 73 73 Selenocysteine. FT VAR_SEQ 1 27 Missing (in isoform Cytoplasmic). FT /FTId=VSP_018743. FT CONFLICT 39 39 R -> A (in Ref. 1; BAA22780). SQ SEQUENCE 197 AA; 22229 MW; 5CED4991A484F31C CRC64; MSWGRLSRLL KPALLCGALA APGLAGTMCA SRDDWRCARS MHEFSAKDID GHMVCLDKYR GFVCIVTNVA SQUGKTDVNY TQLVDLHARY AECGLRILAF PCNQFGRQEP GSNQEIKEFA AGYNVKFDMY SKICVNGDDA HPLWKWMKVQ PKGRGMLGNA IKWNFTKFLI DKNGCVVKRY GPMEEPQVIE KDLPCYL // ID GPX5_MOUSE Reviewed; 221 AA. AC P21765; E9QK84; DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot. DT 03-OCT-2012, sequence version 3. DT 19-MAR-2014, entry version 112. DE RecName: Full=Epididymal secretory glutathione peroxidase; DE EC=1.11.1.9; DE AltName: Full=Epididymis-specific glutathione peroxidase-like protein; DE Short=EGLP; DE AltName: Full=Glutathione peroxidase 5; DE Short=GPx-5; DE Short=GSHPx-5; DE AltName: Full=Major androgen-regulated protein; DE AltName: Full=arMEP24; DE Flags: Precursor; GN Name=Gpx5; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC TISSUE=Epididymis; RX PubMed=1913244; RA Ghyselinck N.B., Rigaudiere N., Dufaure J.-P.; RT "Androgen-dependent protein secreted by mouse caput epididymis shows RT high homologies with different glutathione peroxidases."; RL C. R. Acad. Sci. III, Sci. Vie 313:1-6(1991). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=8469239; DOI=10.1210/me.7.2.258; RA Ghyselinck N.B., Dufaure I., Lareyre J.J., Rigaudiere N., RA Mattei M.-G., Dufaure J.-P.; RT "Structural organization and regulation of the gene for the androgen- RT dependent glutathione peroxidase-like protein specific to the mouse RT epididymis."; RL Mol. Endocrinol. 7:258-272(1993). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] OF 47-221. RC TISSUE=Epididymis; RX PubMed=2263479; DOI=10.1093/nar/18.23.7144; RA Ghyselinck N.B., Dufaure J.-P.; RT "A mouse cDNA sequence for epididymal androgen-regulated proteins RT related to glutathione peroxidase."; RL Nucleic Acids Res. 18:7144-7144(1990). CC -!- FUNCTION: Protects cells and enzymes from oxidative damage, by CC catalyzing the reduction of hydrogen peroxide, lipid peroxides and CC organic hydroperoxide, by glutathione. May constitute a CC glutathione peroxidase-like protective system against peroxide CC damage in sperm membrane lipids. CC -!- CATALYTIC ACTIVITY: 2 glutathione + H(2)O(2) = glutathione CC disulfide + 2 H(2)O. CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- TISSUE SPECIFICITY: Epididymis. CC -!- SIMILARITY: Belongs to the glutathione peroxidase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M68896; AAA37729.1; -; Genomic_DNA. DR EMBL; AC124460; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; X53780; CAA37796.1; -; mRNA. DR PIR; A47367; A47367. DR RefSeq; NP_034473.2; NM_010343.2. DR UniGene; Mm.1332; -. DR ProteinModelPortal; P21765; -. DR SMR; P21765; 31-218. DR PeroxiBase; 5578; MmGPx05. DR PaxDb; P21765; -. DR PRIDE; P21765; -. DR Ensembl; ENSMUST00000004456; ENSMUSP00000004456; ENSMUSG00000004344. DR GeneID; 14780; -. DR KEGG; mmu:14780; -. DR CTD; 2880; -. DR MGI; MGI:104886; Gpx5. DR eggNOG; COG0386; -. DR GeneTree; ENSGT00740000115226; -. DR HOGENOM; HOG000277055; -. DR HOVERGEN; HBG004333; -. DR InParanoid; P21765; -. DR KO; K00432; -. DR NextBio; 286893; -. DR PRO; PR:P21765; -. DR ArrayExpress; P21765; -. DR CleanEx; MM_GPX5; -. DR Genevestigator; P21765; -. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0004602; F:glutathione peroxidase activity; IEA:UniProtKB-EC. DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro. DR Gene3D; 3.40.30.10; -; 1. DR InterPro; IPR000889; Glutathione_peroxidase. DR InterPro; IPR012336; Thioredoxin-like_fold. DR PANTHER; PTHR11592; PTHR11592; 1. DR Pfam; PF00255; GSHPx; 1. DR PIRSF; PIRSF000303; Glutathion_perox; 1. DR PRINTS; PR01011; GLUTPROXDASE. DR SUPFAM; SSF52833; SSF52833; 1. DR PROSITE; PS00460; GLUTATHIONE_PEROXID_1; 1. DR PROSITE; PS00763; GLUTATHIONE_PEROXID_2; 1. DR PROSITE; PS51355; GLUTATHIONE_PEROXID_3; 1. PE 2: Evidence at transcript level; KW Complete proteome; Oxidoreductase; Peroxidase; Reference proteome; KW Secreted; Signal. FT SIGNAL 1 21 Potential. FT CHAIN 22 221 Epididymal secretory glutathione FT peroxidase. FT /FTId=PRO_0000013078. FT ACT_SITE 73 73 By similarity. FT CONFLICT 53 53 H -> D (in Ref. 2; AAA37729). FT CONFLICT 60 60 A -> R (in Ref. 2; AAA37729 and 4; FT CAA37796). FT CONFLICT 170 170 F -> S (in Ref. 2; AAA37729 and 4; FT CAA37796). FT CONFLICT 193 193 I -> V (in Ref. 2; AAA37729 and 4; FT CAA37796). SQ SEQUENCE 221 AA; 25393 MW; 99FF8A2FECABFC9E CRC64; MVTELRVFYL VPLLLASYVQ TTPRPEKMKM DCYKDVKGTI YDYEALSLNG KEHIPFKQYA GKHVLFVNVA TYCGLTIQYP ELNALQEDLK PFGLVILGFP CNQFGKQEPG DNLEILPGLK YVRPGKGFLP NFQLFAKGDV NGENEQKIFT FLKRSCPHPS ETVVMSKHTF WEPIKVHDIR WNFEKFLVGP DGIPVMRWFH QAPVSTVKSD IMAYLSHFKT I // ID GPX6_MOUSE Reviewed; 221 AA. AC Q91WR8; F2Z3U8; DT 04-AUG-2003, integrated into UniProtKB/Swiss-Prot. DT 03-OCT-2012, sequence version 2. DT 19-MAR-2014, entry version 89. DE RecName: Full=Glutathione peroxidase 6; DE Short=GPx-6; DE Short=GSHPx-6; DE EC=1.11.1.9; DE Flags: Precursor; GN Name=Gpx6; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Kidney; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- CATALYTIC ACTIVITY: 2 glutathione + H(2)O(2) = glutathione CC disulfide + 2 H(2)O. CC -!- SUBCELLULAR LOCATION: Secreted (By similarity). CC -!- SIMILARITY: Belongs to the glutathione peroxidase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AC124460; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC013526; AAH13526.1; -; mRNA. DR RefSeq; NP_663426.2; NM_145451.3. DR UniGene; Mm.46195; -. DR ProteinModelPortal; Q91WR8; -. DR SMR; Q91WR8; 38-219. DR STRING; 10090.ENSMUSP00000004453; -. DR PeroxiBase; 3719; MmGPx06. DR PRIDE; Q91WR8; -. DR Ensembl; ENSMUST00000004453; ENSMUSP00000004453; ENSMUSG00000004341. DR GeneID; 75512; -. DR KEGG; mmu:75512; -. DR CTD; 257202; -. DR MGI; MGI:1922762; Gpx6. DR eggNOG; COG0386; -. DR GeneTree; ENSGT00740000115226; -. DR HOGENOM; HOG000277055; -. DR HOVERGEN; HBG004333; -. DR InParanoid; Q91WR8; -. DR KO; K00432; -. DR OMA; FQQYAGK; -. DR OrthoDB; EOG7KQ23C; -. DR TreeFam; TF105318; -. DR NextBio; 343218; -. DR PRO; PR:Q91WR8; -. DR CleanEx; MM_GPX6; -. DR Genevestigator; Q91WR8; -. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0004602; F:glutathione peroxidase activity; IEA:UniProtKB-EC. DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro. DR Gene3D; 3.40.30.10; -; 1. DR InterPro; IPR000889; Glutathione_peroxidase. DR InterPro; IPR012336; Thioredoxin-like_fold. DR PANTHER; PTHR11592; PTHR11592; 1. DR Pfam; PF00255; GSHPx; 1. DR PIRSF; PIRSF000303; Glutathion_perox; 1. DR PRINTS; PR01011; GLUTPROXDASE. DR SUPFAM; SSF52833; SSF52833; 1. DR PROSITE; PS00460; GLUTATHIONE_PEROXID_1; 1. DR PROSITE; PS00763; GLUTATHIONE_PEROXID_2; 1. DR PROSITE; PS51355; GLUTATHIONE_PEROXID_3; 1. PE 2: Evidence at transcript level; KW Complete proteome; Oxidoreductase; Peroxidase; Reference proteome; KW Secreted; Signal. FT SIGNAL 1 19 Potential. FT CHAIN 20 221 Glutathione peroxidase 6. FT /FTId=PRO_0000013082. FT ACT_SITE 73 73 By similarity. FT CONFLICT 52 52 E -> G (in Ref. 2; AAH13526). FT CONFLICT 176 176 V -> I (in Ref. 2; AAH13526). SQ SEQUENCE 221 AA; 24903 MW; 39577A18B4C99BCA CRC64; MAQKLWGSCL FSLFMAALAQ ETLNPQKSKV DCNKGVTGTV YEYGANTIDG GEFVNFQQYA GKHILFVNVA SFCGLTATYP ELNTLQEELK PFNVTVLGFP CNQFGKQEPG KNSEILLGLK YVRPGGGYVP NFQLFEKGDV NGDNEQKVFS FLKNSCPPTS ELFGSPEHLF WDPMKVHDIR WNFEKFLVGP DGVPVMRWFH HTPVRIVQSD IMEYLNQTST Q // ID GPX7_MOUSE Reviewed; 186 AA. AC Q99LJ6; DT 04-AUG-2003, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 19-FEB-2014, entry version 95. DE RecName: Full=Glutathione peroxidase 7; DE Short=GPx-7; DE Short=GSHPx-7; DE EC=1.11.1.9; DE Flags: Precursor; GN Name=Gpx7; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: It protects esophageal epithelia from hydrogen peroxide- CC induced oxidative stress. It suppresses acidic bile acid-induced CC reactive oxigen species (ROS) and protects against oxidative DNA CC damage and double-strand breaks (By similarity). CC -!- CATALYTIC ACTIVITY: 2 glutathione + H(2)O(2) = glutathione CC disulfide + 2 H(2)O. CC -!- SUBCELLULAR LOCATION: Secreted (Potential). CC -!- SIMILARITY: Belongs to the glutathione peroxidase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BC003228; AAH03228.1; -; mRNA. DR RefSeq; NP_077160.1; NM_024198.3. DR UniGene; Mm.20164; -. DR ProteinModelPortal; Q99LJ6; -. DR SMR; Q99LJ6; 22-175. DR IntAct; Q99LJ6; 1. DR MINT; MINT-4096598; -. DR PeroxiBase; 3720; MmGPx07. DR PaxDb; Q99LJ6; -. DR PRIDE; Q99LJ6; -. DR Ensembl; ENSMUST00000030332; ENSMUSP00000030332; ENSMUSG00000028597. DR GeneID; 67305; -. DR KEGG; mmu:67305; -. DR UCSC; uc008ubc.1; mouse. DR CTD; 2882; -. DR MGI; MGI:1914555; Gpx7. DR eggNOG; COG0386; -. DR GeneTree; ENSGT00740000115371; -. DR HOGENOM; HOG000277054; -. DR HOVERGEN; HBG004333; -. DR InParanoid; Q99LJ6; -. DR KO; K00432; -. DR OMA; FYTFKVV; -. DR OrthoDB; EOG757CZF; -. DR TreeFam; TF331942; -. DR NextBio; 324182; -. DR PRO; PR:Q99LJ6; -. DR ArrayExpress; Q99LJ6; -. DR Bgee; Q99LJ6; -. DR CleanEx; MM_GPX7; -. DR Genevestigator; Q99LJ6; -. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0004602; F:glutathione peroxidase activity; IEA:UniProtKB-EC. DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro. DR Gene3D; 3.40.30.10; -; 1. DR InterPro; IPR013376; Glut_perox_Gpx7. DR InterPro; IPR000889; Glutathione_peroxidase. DR InterPro; IPR012336; Thioredoxin-like_fold. DR PANTHER; PTHR11592; PTHR11592; 1. DR Pfam; PF00255; GSHPx; 1. DR PIRSF; PIRSF000303; Glutathion_perox; 1. DR PRINTS; PR01011; GLUTPROXDASE. DR SUPFAM; SSF52833; SSF52833; 1. DR TIGRFAMs; TIGR02540; gpx7; 1. DR PROSITE; PS00460; GLUTATHIONE_PEROXID_1; 1. DR PROSITE; PS00763; GLUTATHIONE_PEROXID_2; 1. DR PROSITE; PS51355; GLUTATHIONE_PEROXID_3; 1. PE 2: Evidence at transcript level; KW Complete proteome; Oxidoreductase; Peroxidase; Reference proteome; KW Secreted; Signal. FT SIGNAL 1 18 Potential. FT CHAIN 19 186 Glutathione peroxidase 7. FT /FTId=PRO_0000013085. FT ACT_SITE 56 56 By similarity. SQ SEQUENCE 186 AA; 21061 MW; D20211218380A1BA CRC64; MVAAVATAWL LLWAAACAQS EQDFYDFKAV NIRGKLVSLE KYRGSVSLVV NVASECGFTD QNYRALQQLQ RDLGPHHFNV LAFPCNQFGQ QEPDTNREIE NFARRTYSVS FPMFSKIAVT GTGAHPAFKY LTQTSGKEPT WNFWKYLVDP DGKVVGAWDP TVPVAEIKPR ITEQVMKLIL RKREDL // ID GPX8_MOUSE Reviewed; 209 AA. AC Q9D7B7; Q8VE68; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 19-FEB-2014, entry version 97. DE RecName: Full=Probable glutathione peroxidase 8; DE Short=GPx-8; DE Short=GSHPx-8; DE EC=1.11.1.9; GN Name=Gpx8; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Tongue; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Czech II; TISSUE=Mammary tumor; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- CATALYTIC ACTIVITY: 2 glutathione + H(2)O(2) = glutathione CC disulfide + 2 H(2)O. CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein CC (Potential). CC -!- SIMILARITY: Belongs to the glutathione peroxidase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK009378; BAB26254.1; -; mRNA. DR EMBL; BC019664; AAH19664.1; -; mRNA. DR RefSeq; NP_081403.1; NM_027127.2. DR UniGene; Mm.12715; -. DR ProteinModelPortal; Q9D7B7; -. DR SMR; Q9D7B7; 39-209. DR PhosphoSite; Q9D7B7; -. DR PaxDb; Q9D7B7; -. DR PRIDE; Q9D7B7; -. DR Ensembl; ENSMUST00000022282; ENSMUSP00000022282; ENSMUSG00000021760. DR GeneID; 69590; -. DR KEGG; mmu:69590; -. DR UCSC; uc007rxb.1; mouse. DR CTD; 493869; -. DR MGI; MGI:1916840; Gpx8. DR eggNOG; COG0386; -. DR GeneTree; ENSGT00740000115371; -. DR HOGENOM; HOG000277054; -. DR HOVERGEN; HBG004333; -. DR InParanoid; Q9D7B7; -. DR KO; K00432; -. DR OMA; TAYPLRC; -. DR OrthoDB; EOG757CZF; -. DR TreeFam; TF331942; -. DR NextBio; 329860; -. DR PRO; PR:Q9D7B7; -. DR Bgee; Q9D7B7; -. DR Genevestigator; Q9D7B7; -. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004602; F:glutathione peroxidase activity; IEA:UniProtKB-EC. DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro. DR Gene3D; 3.40.30.10; -; 1. DR InterPro; IPR013376; Glut_perox_Gpx7. DR InterPro; IPR000889; Glutathione_peroxidase. DR InterPro; IPR012336; Thioredoxin-like_fold. DR PANTHER; PTHR11592; PTHR11592; 1. DR Pfam; PF00255; GSHPx; 1. DR PIRSF; PIRSF000303; Glutathion_perox; 1. DR PRINTS; PR01011; GLUTPROXDASE. DR SUPFAM; SSF52833; SSF52833; 1. DR TIGRFAMs; TIGR02540; gpx7; 1. DR PROSITE; PS00763; GLUTATHIONE_PEROXID_2; 1. DR PROSITE; PS51355; GLUTATHIONE_PEROXID_3; 1. PE 2: Evidence at transcript level; KW Acetylation; Complete proteome; Membrane; Oxidoreductase; Peroxidase; KW Reference proteome; Transmembrane; Transmembrane helix. FT CHAIN 1 209 Probable glutathione peroxidase 8. FT /FTId=PRO_0000317757. FT TRANSMEM 18 40 Helical; (Potential). FT ACT_SITE 79 79 By similarity. FT MOD_RES 1 1 N-acetylmethionine (By similarity). FT CONFLICT 88 88 T -> I (in Ref. 2; AAH19664). SQ SEQUENCE 209 AA; 24148 MW; 8DA93ED11B4ECF21 CRC64; MEPFAAYPLK CSGPKAKIFA VLLSMVLCTV MLFLLQLKFL KPRTNSFYSF EVKDAKGRTV SLEKFKGKAS LVVNVASDCR FTDKSYQTLR ELHKEFGPYH FNVLAFPCNQ FGESEPKSSK EVESFARQNY GVTFPIFHKI KILGPEAEPA FRFIVDSSKK EPRWNFWKYL VNPEGQVVKF WRPEEPLEAI RPHVSQMIGQ IILKKKEDL // ID GRHPR_MOUSE Reviewed; 328 AA. AC Q91Z53; DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 19-FEB-2014, entry version 96. DE RecName: Full=Glyoxylate reductase/hydroxypyruvate reductase; DE EC=1.1.1.79; DE EC=1.1.1.81; GN Name=Grhpr; Synonyms=Glxr; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=129/SvEv; TISSUE=Liver; RA Cramer S.D.; RT "Identification of the mouse GRHPR cDNA from liver."; RL Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Mammary tumor; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP PROTEIN SEQUENCE OF 44-58 AND 303-318, AND MASS SPECTROMETRY. RC TISSUE=Hippocampus; RA Lubec G., Klug S.; RL Submitted (MAR-2007) to UniProtKB. CC -!- FUNCTION: Enzyme with hydroxy-pyruvate reductase, glyoxylate CC reductase and D-glycerate dehydrogenase enzymatic activities. CC Reduces hydroxypyruvate to D-glycerate, glyoxylate to glycolate CC oxidizes D-glycerate to hydroxypyruvate (By similarity). CC -!- CATALYTIC ACTIVITY: Glycolate + NADP(+) = glyoxylate + NADPH. CC -!- CATALYTIC ACTIVITY: D-glycerate + NAD(P)(+) = hydroxypyruvate + CC NAD(P)H. CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid CC dehydrogenase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AY113690; AAM52985.1; -; mRNA. DR EMBL; BC010194; AAH10194.1; -; mRNA. DR RefSeq; NP_525028.1; NM_080289.1. DR UniGene; Mm.196574; -. DR ProteinModelPortal; Q91Z53; -. DR SMR; Q91Z53; 5-328. DR IntAct; Q91Z53; 4. DR MINT; MINT-1868690; -. DR PhosphoSite; Q91Z53; -. DR REPRODUCTION-2DPAGE; Q91Z53; -. DR PaxDb; Q91Z53; -. DR PRIDE; Q91Z53; -. DR Ensembl; ENSMUST00000045078; ENSMUSP00000047218; ENSMUSG00000035637. DR GeneID; 76238; -. DR KEGG; mmu:76238; -. DR UCSC; uc008ssb.1; mouse. DR CTD; 9380; -. DR MGI; MGI:1923488; Grhpr. DR eggNOG; COG1052; -. DR GeneTree; ENSGT00510000046913; -. DR HOGENOM; HOG000136700; -. DR HOVERGEN; HBG051838; -. DR InParanoid; Q91Z53; -. DR KO; K00049; -. DR OMA; ERSMKPS; -. DR OrthoDB; EOG7K3TMJ; -. DR TreeFam; TF324791; -. DR NextBio; 344835; -. DR PRO; PR:Q91Z53; -. DR ArrayExpress; Q91Z53; -. DR Bgee; Q91Z53; -. DR CleanEx; MM_GRHPR; -. DR Genevestigator; Q91Z53; -. DR GO; GO:0005829; C:cytosol; IEA:Ensembl. DR GO; GO:0031406; F:carboxylic acid binding; IEA:Ensembl. DR GO; GO:0008465; F:glycerate dehydrogenase activity; IEA:Ensembl. DR GO; GO:0030267; F:glyoxylate reductase (NADP) activity; IEA:UniProtKB-EC. DR GO; GO:0016618; F:hydroxypyruvate reductase activity; IEA:UniProtKB-EC. DR GO; GO:0051287; F:NAD binding; IEA:Ensembl. DR GO; GO:0070402; F:NADPH binding; IEA:Ensembl. DR GO; GO:0043648; P:dicarboxylic acid metabolic process; IEA:Ensembl. DR GO; GO:0007588; P:excretion; IEA:Ensembl. DR GO; GO:0051259; P:protein oligomerization; IEA:Ensembl. DR Gene3D; 3.40.50.720; -; 2. DR InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom. DR InterPro; IPR006140; D-isomer_2_OHA_DH_NAD-bd. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Pfam; PF00389; 2-Hacid_dh; 1. DR Pfam; PF02826; 2-Hacid_dh_C; 1. DR PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1. PE 1: Evidence at protein level; KW Complete proteome; Direct protein sequencing; NADP; Oxidoreductase; KW Reference proteome. FT CHAIN 1 328 Glyoxylate reductase/hydroxypyruvate FT reductase. FT /FTId=PRO_0000075945. FT NP_BIND 162 164 NADP (By similarity). FT NP_BIND 185 188 NADP (By similarity). FT REGION 83 84 Substrate binding (By similarity). FT REGION 293 296 Substrate binding (By similarity). FT ACT_SITE 293 293 Proton donor (By similarity). FT BINDING 217 217 NADP (By similarity). FT BINDING 243 243 NADP; via carbonyl oxygen (By FT similarity). FT BINDING 245 245 Substrate (By similarity). FT BINDING 269 269 Substrate (By similarity). FT BINDING 295 295 NADP; via amide nitrogen (By similarity). FT SITE 274 274 Raises pKa of active site His (By FT similarity). SQ SEQUENCE 328 AA; 35329 MW; BDEC1ADEC1E18153 CRC64; MKPARLMKVF VTGPLPAEGR AALAQAADCE VEQWNSDDPI PRKDLEQGVV GAHGLLCRLS DRVDKKLLDA AGANLRVIST LSVGVDHLAL DEIKKRGIRV GYTPGVLTDA TAELAVSLLL TTCRRLPEAI EEVKNGGWSS WSPLWMCGYG LSQSTVGIVG LGRIGQAIAR RLKPFGVQRF LYTGRQPRPQ EAAEFQAEFV PIAQLAAESD FIVVSCSLTP DTMGLCSKDF FQKMKNTAIF INISRGDVVN QEDLYQALAS GQIAAAGLDV TTPEPLPPSH PLLTLKNCVI LPHIGSATYK TRNTMSLLAA NNLLAGLRGE AMPSELKL // ID GSHR_MOUSE Reviewed; 500 AA. AC P47791; Q7TNC2; Q8BN97; Q8C9Z6; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 21-JUN-2004, sequence version 3. DT 19-MAR-2014, entry version 141. DE RecName: Full=Glutathione reductase, mitochondrial; DE Short=GR; DE Short=GRase; DE EC=1.8.1.7; DE Flags: Precursor; GN Name=Gsr; Synonyms=Gr1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND ALTERNATIVE INITIATION. RX PubMed=9268726; DOI=10.1006/bbrc.1997.7153; RA Tamura T., McMicken H.W., Smith C.V., Hansen T.N.; RT "Gene structure for mouse glutathione reductase, including a putative RT mitochondrial targeting signal."; RL Biochem. Biophys. Res. Commun. 237:419-422(1997). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], AND SEQUENCE REVISION. RA Werner D.; RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases. RN [3] RP PARTIAL NUCLEOTIDE SEQUENCE. RX PubMed=2185014; DOI=10.1111/j.1432-1033.1990.tb15431.x; RA Tutic M., Lu X.A., Schirmer R.H., Werner D.; RT "Cloning and sequencing of mammalian glutathione reductase cDNA."; RL Eur. J. Biochem. 188:523-528(1990). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Eye, and Thymus; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6; TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-75, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23576753; DOI=10.1073/pnas.1302961110; RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., RA Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.; RT "Label-free quantitative proteomics of the lysine acetylome in RT mitochondria identifies substrates of SIRT3 in metabolic pathways."; RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013). CC -!- FUNCTION: Maintains high levels of reduced glutathione in the CC cytosol. CC -!- CATALYTIC ACTIVITY: 2 glutathione + NADP(+) = glutathione CC disulfide + NADPH. CC -!- COFACTOR: Binds 1 FAD per subunit (By similarity). CC -!- SUBUNIT: Homodimer; disulfide-linked. CC -!- SUBCELLULAR LOCATION: Isoform Mitochondrial: Mitochondrion. CC -!- SUBCELLULAR LOCATION: Isoform Cytoplasmic: Cytoplasm. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative initiation; Named isoforms=2; CC Name=Mitochondrial; CC IsoId=P47791-1; Sequence=Displayed; CC Name=Cytoplasmic; CC IsoId=P47791-2; Sequence=VSP_018973; CC -!- DOMAIN: Each subunit can be divided into 4 domains that are CC consecutive along the polypeptide chain. Domains 1 and 2 bind FAD CC and NADPH, respectively. Domain 4 forms the interface. CC -!- MISCELLANEOUS: The active site is a redox-active disulfide bond. CC -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide CC oxidoreductase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X76341; CAA53959.3; -; mRNA. DR EMBL; AK040136; BAC30518.1; -; mRNA. DR EMBL; AK084328; BAC39162.1; -; mRNA. DR EMBL; BC056357; AAH56357.1; -; mRNA. DR EMBL; BC057325; AAH57325.1; -; mRNA. DR PIR; PC4370; PC4370. DR PIR; S39494; S39494. DR RefSeq; NP_034474.4; NM_010344.4. DR UniGene; Mm.283573; -. DR ProteinModelPortal; P47791; -. DR SMR; P47791; 41-500. DR IntAct; P47791; 3. DR MINT; MINT-1869660; -. DR PhosphoSite; P47791; -. DR PaxDb; P47791; -. DR PRIDE; P47791; -. DR Ensembl; ENSMUST00000033992; ENSMUSP00000033992; ENSMUSG00000031584. [P47791-1] DR GeneID; 14782; -. DR KEGG; mmu:14782; -. DR UCSC; uc009lkf.1; mouse. [P47791-1] DR CTD; 2936; -. DR MGI; MGI:95804; Gsr. DR eggNOG; COG1249; -. DR GeneTree; ENSGT00390000007578; -. DR HOGENOM; HOG000276712; -. DR HOVERGEN; HBG004959; -. DR InParanoid; P47791; -. DR KO; K00383; -. DR OMA; HRQPCKM; -. DR OrthoDB; EOG7HHWS0; -. DR TreeFam; TF105353; -. DR ChiTaRS; GSR; mouse. DR NextBio; 286899; -. DR PRO; PR:P47791; -. DR ArrayExpress; P47791; -. DR Bgee; P47791; -. DR CleanEx; MM_GSR; -. DR Genevestigator; P47791; -. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. DR GO; GO:0004362; F:glutathione-disulfide reductase activity; IDA:MGI. DR GO; GO:0050661; F:NADP binding; IEA:InterPro. DR GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro. DR GO; GO:0006749; P:glutathione metabolic process; IC:MGI. DR Gene3D; 3.30.390.30; -; 1. DR InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer. DR InterPro; IPR013027; FAD_pyr_nucl-diS_OxRdtase. DR InterPro; IPR006322; Glutathione_Rdtase_euk/bac. DR InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer. DR InterPro; IPR023753; Pyr_nucl-diS_OxRdtase_FAD/NAD. DR InterPro; IPR012999; Pyr_OxRdtase_I_AS. DR InterPro; IPR001327; Pyr_OxRdtase_NAD-bd_dom. DR Pfam; PF00070; Pyr_redox; 1. DR Pfam; PF07992; Pyr_redox_2; 1. DR Pfam; PF02852; Pyr_redox_dim; 1. DR PRINTS; PR00368; FADPNR. DR SUPFAM; SSF55424; SSF55424; 1. DR TIGRFAMs; TIGR01421; gluta_reduc_1; 1. DR PROSITE; PS00076; PYRIDINE_REDOX_1; 1. PE 1: Evidence at protein level; KW Acetylation; Alternative initiation; Complete proteome; Cytoplasm; KW Disulfide bond; FAD; Flavoprotein; Mitochondrion; NADP; KW Oxidoreductase; Redox-active center; Reference proteome; KW Transit peptide. FT TRANSIT 1 26 Mitochondrion (Potential). FT CHAIN 27 500 Glutathione reductase, mitochondrial. FT /FTId=PRO_0000030278. FT NP_BIND 72 80 FAD (By similarity). FT ACT_SITE 489 489 Proton acceptor (By similarity). FT MOD_RES 75 75 N6-acetyllysine. FT DISULFID 80 85 Redox-active (By similarity). FT DISULFID 112 112 Interchain (By similarity). FT VAR_SEQ 1 26 Missing (in isoform Cytoplasmic). FT /FTId=VSP_018973. FT CONFLICT 26 26 A -> T (in Ref. 2; CAA53959). FT CONFLICT 255 255 N -> K (in Ref. 2; CAA53959). FT CONFLICT 300 300 M -> V (in Ref. 2; CAA53959). FT CONFLICT 312 312 G -> R (in Ref. 5; AAH56357/AAH57325). SQ SEQUENCE 500 AA; 53663 MW; A2E6F629B5CC0B7B CRC64; MALLPRALGV GAAPSLRRAA RALTCAMASP GEPQPPAPDT SSFDYLVIGG GSGGLASARR AAELGARAAV VESHKLGGTC VNVGCVPKKV MWNTAVHSEF MHDHVDYGFQ SCEGKFSWHV IKQKRDAYVS RLNTIYQNNL TKSHIEIIHG YATFADGPRP TVEVNGKKFT APHILIATGG VPTVPHESQI PGASLGITSD GFFQLEDLPS RSVIVGAGYI AVEIAGILSA LGSKTSLMIR HDKVLRNFDS LISSNCTEEL ENAGVEVLKF TQVKEVKKTS SGLELQVVTS VPGRKPTTTM IPDVDCLLWA IGRDPNSKGL NLNKVGIQTD EKGHILVDEF QNTNVKGVYA VGDVCGKALL TPVAIAAGRK LAHRLFECKQ DSKLDYDNIP TVVFSHPPIG TVGLTEDEAV HKYGKDNVKI YSTAFTPMYH AVTTRKTKCV MKMVCANKEE KVVGIHMQGI GCDEMLQGFA VAVKMGATKA DFDNTVAIHP TSSEELVTLR // ID GSTO1_MOUSE Reviewed; 240 AA. AC O09131; Q3TH87; DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1998, sequence version 2. DT 19-FEB-2014, entry version 117. DE RecName: Full=Glutathione S-transferase omega-1; DE Short=GSTO-1; DE EC=2.5.1.18; DE AltName: Full=Glutathione S-transferase omega 1-1; DE Short=GSTO 1-1; DE AltName: Full=Glutathione-dependent dehydroascorbate reductase; DE EC=1.8.5.1; DE AltName: Full=Monomethylarsonic acid reductase; DE Short=MMA(V) reductase; DE EC=1.20.4.2; DE AltName: Full=S-(Phenacyl)glutathione reductase; DE Short=SPG-R; DE AltName: Full=p28; GN Name=Gsto1; Synonyms=Gstx, Gtsttl; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=9988762; DOI=10.1074/jbc.274.8.5131; RA Kodym R., Calkins P., Story M.D.; RT "The cloning and characterization of a new stress response protein. A RT mammalian member of a family of theta class glutathione s-transferase- RT like proteins."; RL J. Biol. Chem. 274:5131-5137(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Amnion; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6; TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: Exhibits glutathione-dependent thiol transferase and CC dehydroascorbate reductase activities. Has S-(phenacyl)glutathione CC reductase activity. Has also glutathione S-transferase activity. CC Participates in the biotransformation of inorganic arsenic and CC reduces monomethylarsonic acid (MMA) and dimethylarsonic acid (By CC similarity). CC -!- CATALYTIC ACTIVITY: RX + glutathione = HX + R-S-glutathione. CC -!- CATALYTIC ACTIVITY: 2 glutathione + dehydroascorbate = glutathione CC disulfide + ascorbate. CC -!- CATALYTIC ACTIVITY: Methylarsonate + 2 glutathione = CC methylarsonite + glutathione disulfide + H(2)O. CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol (By similarity). CC -!- SIMILARITY: Belongs to the GST superfamily. Omega family. CC -!- SIMILARITY: Contains 1 GST C-terminal domain. CC -!- SIMILARITY: Contains 1 GST N-terminal domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U80819; AAB70110.1; -; mRNA. DR EMBL; AK027922; BAC25667.1; -; mRNA. DR EMBL; AK146834; BAE27469.1; -; mRNA. DR EMBL; AK168383; BAE40311.1; -; mRNA. DR EMBL; BC085165; AAH85165.1; -; mRNA. DR RefSeq; NP_034492.1; NM_010362.2. DR UniGene; Mm.378931; -. DR ProteinModelPortal; O09131; -. DR SMR; O09131; 3-240. DR IntAct; O09131; 2. DR MINT; MINT-1868625; -. DR STRING; 10090.ENSMUSP00000026050; -. DR PhosphoSite; O09131; -. DR REPRODUCTION-2DPAGE; IPI00114285; -. DR PaxDb; O09131; -. DR PRIDE; O09131; -. DR Ensembl; ENSMUST00000026050; ENSMUSP00000026050; ENSMUSG00000025068. DR GeneID; 14873; -. DR KEGG; mmu:14873; -. DR UCSC; uc008hvq.1; mouse. DR CTD; 9446; -. DR MGI; MGI:1342273; Gsto1. DR eggNOG; COG0625; -. DR GeneTree; ENSGT00390000005479; -. DR HOGENOM; HOG000006560; -. DR HOVERGEN; HBG051853; -. DR InParanoid; O09131; -. DR KO; K00799; -. DR OMA; MAGSTKS; -. DR OrthoDB; EOG71CFNG; -. DR TreeFam; TF105325; -. DR NextBio; 287145; -. DR PRO; PR:O09131; -. DR Bgee; O09131; -. DR CleanEx; MM_GSTO1; -. DR Genevestigator; O09131; -. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell. DR GO; GO:0045174; F:glutathione dehydrogenase (ascorbate) activity; ISS:UniProtKB. DR GO; GO:0004364; F:glutathione transferase activity; ISS:UniProtKB. DR GO; GO:0050610; F:methylarsonate reductase activity; IEA:UniProtKB-EC. DR GO; GO:0071243; P:cellular response to arsenic-containing substance; ISS:UniProtKB. DR GO; GO:0019852; P:L-ascorbic acid metabolic process; ISS:UniProtKB. DR GO; GO:0060315; P:negative regulation of ryanodine-sensitive calcium-release channel activity; IEA:Ensembl. DR GO; GO:0060316; P:positive regulation of ryanodine-sensitive calcium-release channel activity; IEA:Ensembl. DR GO; GO:0010880; P:regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum; IEA:Ensembl. DR GO; GO:0042178; P:xenobiotic catabolic process; ISS:UniProtKB. DR Gene3D; 1.20.1050.10; -; 1. DR Gene3D; 3.40.30.10; -; 1. DR InterPro; IPR010987; Glutathione-S-Trfase_C-like. DR InterPro; IPR004045; Glutathione_S-Trfase_N. DR InterPro; IPR004046; GST_C. DR InterPro; IPR005442; GST_omega. DR InterPro; IPR012336; Thioredoxin-like_fold. DR Pfam; PF00043; GST_C; 1. DR Pfam; PF13417; GST_N_3; 1. DR PRINTS; PR01625; GSTRNSFRASEO. DR SUPFAM; SSF47616; SSF47616; 1. DR SUPFAM; SSF52833; SSF52833; 1. DR PROSITE; PS50405; GST_CTER; 1. DR PROSITE; PS50404; GST_NTER; 1. PE 2: Evidence at transcript level; KW Acetylation; Complete proteome; Cytoplasm; Oxidoreductase; KW Reference proteome; Transferase. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 240 Glutathione S-transferase omega-1. FT /FTId=PRO_0000185885. FT DOMAIN 22 101 GST N-terminal. FT DOMAIN 106 227 GST C-terminal. FT REGION 85 86 Glutathione binding (By similarity). FT ACT_SITE 32 32 Nucleophile (By similarity). FT BINDING 59 59 Glutathione (By similarity). FT BINDING 72 72 Glutathione; via amide nitrogen and FT carbonyl oxygen (By similarity). FT MOD_RES 2 2 N-acetylserine (By similarity). FT MOD_RES 57 57 N6-acetyllysine (By similarity). FT MOD_RES 152 152 N6-acetyllysine (By similarity). SQ SEQUENCE 240 AA; 27498 MW; 17FEB52DB4BBE506 CRC64; MSGESSRSLG KGSAPPGPVP EGQIRVYSMR FCPFAQRTLM VLKAKGIRHE VININLKNKP EWFFEKNPLG LVPVLENSQG HLVTESVITC EYLDEAYPEK KLFPDDPYKK ARQKMTLESF SKVPPLIASF VRSKRKEDSP NLREALENEF KKLEEGMDNY KSFLGGDSPS MVDYLTWPWF QRLEALELKE CLAHTPKLKL WMAAMQQDPV ASSHKIDAKT YREYLNLYLQ DSPEACDYGL // ID GSTO2_MOUSE Reviewed; 248 AA. AC Q8K2Q2; DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2002, sequence version 1. DT 19-FEB-2014, entry version 86. DE RecName: Full=Glutathione S-transferase omega-2; DE Short=GSTO-2; DE EC=2.5.1.18; DE AltName: Full=Glutathione S-transferase omega 2-2; DE Short=GSTO 2-2; DE AltName: Full=Glutathione-dependent dehydroascorbate reductase; DE EC=1.8.5.1; DE AltName: Full=Monomethylarsonic acid reductase; DE Short=MMA(V) reductase; DE EC=1.20.4.2; GN Name=Gsto2; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Testis; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N-3; TISSUE=Mammary tumor; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: Exhibits glutathione-dependent thiol transferase CC activity. Has high dehydroascorbate reductase activity and may CC contribute to the recycling of ascorbic acid. Participates in the CC biotransformation of inorganic arsenic and reduces CC monomethylarsonic acid (MMA) (By similarity). CC -!- CATALYTIC ACTIVITY: RX + glutathione = HX + R-S-glutathione. CC -!- CATALYTIC ACTIVITY: 2 glutathione + dehydroascorbate = glutathione CC disulfide + ascorbate. CC -!- CATALYTIC ACTIVITY: Methylarsonate + 2 glutathione = CC methylarsonite + glutathione disulfide + H(2)O. CC -!- SIMILARITY: Belongs to the GST superfamily. Omega family. CC -!- SIMILARITY: Contains 1 GST C-terminal domain. CC -!- SIMILARITY: Contains 1 GST N-terminal domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK077086; BAC36604.1; -; mRNA. DR EMBL; BC030371; AAH30371.1; -; mRNA. DR RefSeq; NP_080895.2; NM_026619.2. DR RefSeq; NP_084327.1; NM_030051.1. DR UniGene; Mm.63791; -. DR ProteinModelPortal; Q8K2Q2; -. DR SMR; Q8K2Q2; 7-239. DR PhosphoSite; Q8K2Q2; -. DR PaxDb; Q8K2Q2; -. DR PRIDE; Q8K2Q2; -. DR Ensembl; ENSMUST00000056159; ENSMUSP00000052592; ENSMUSG00000025069. DR Ensembl; ENSMUST00000120645; ENSMUSP00000113409; ENSMUSG00000025069. DR GeneID; 68214; -. DR KEGG; mmu:68214; -. DR UCSC; uc008hvs.1; mouse. DR CTD; 119391; -. DR MGI; MGI:1915464; Gsto2. DR eggNOG; COG0625; -. DR GeneTree; ENSGT00390000005479; -. DR HOGENOM; HOG000006560; -. DR HOVERGEN; HBG051853; -. DR InParanoid; Q8K2Q2; -. DR KO; K00799; -. DR OMA; FCNLEEI; -. DR OrthoDB; EOG71CFNG; -. DR TreeFam; TF105325; -. DR NextBio; 326722; -. DR PRO; PR:Q8K2Q2; -. DR ArrayExpress; Q8K2Q2; -. DR Bgee; Q8K2Q2; -. DR CleanEx; MM_GSTO2; -. DR Genevestigator; Q8K2Q2; -. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0045174; F:glutathione dehydrogenase (ascorbate) activity; ISS:UniProtKB. DR GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-EC. DR GO; GO:0050610; F:methylarsonate reductase activity; IEA:UniProtKB-EC. DR GO; GO:0071243; P:cellular response to arsenic-containing substance; ISS:UniProtKB. DR GO; GO:0019852; P:L-ascorbic acid metabolic process; ISS:UniProtKB. DR GO; GO:0006805; P:xenobiotic metabolic process; ISS:UniProtKB. DR Gene3D; 1.20.1050.10; -; 1. DR Gene3D; 3.40.30.10; -; 1. DR InterPro; IPR010987; Glutathione-S-Trfase_C-like. DR InterPro; IPR004045; Glutathione_S-Trfase_N. DR InterPro; IPR005442; GST_omega. DR InterPro; IPR012336; Thioredoxin-like_fold. DR Pfam; PF13417; GST_N_3; 1. DR PRINTS; PR01625; GSTRNSFRASEO. DR SUPFAM; SSF47616; SSF47616; 1. DR SUPFAM; SSF52833; SSF52833; 1. DR PROSITE; PS50405; GST_CTER; 1. DR PROSITE; PS50404; GST_NTER; 1. PE 2: Evidence at transcript level; KW Complete proteome; Oxidoreductase; Reference proteome; Transferase. FT CHAIN 1 248 Glutathione S-transferase omega-2. FT /FTId=PRO_0000239141. FT DOMAIN 22 101 GST N-terminal. FT DOMAIN 106 231 GST C-terminal. FT REGION 85 86 Glutathione binding (By similarity). FT ACT_SITE 32 32 Nucleophile (By similarity). FT BINDING 59 59 Glutathione (By similarity). FT BINDING 72 72 Glutathione; via amide nitrogen and FT carbonyl oxygen (By similarity). SQ SEQUENCE 248 AA; 28599 MW; ADB9FCFCA9F0FE48 CRC64; MSGDLSRCLG KGSCPPGPVP EGVIRIYSMR FCPYSHRARL VLKAKGIRHE VININLKSKP DWYYTKHPFG QIPVLENSQC QLVYESVIAC EYLDDVYPGR KLFPYDPYER ARQKMLLELF CKVPPLSKEC LIALRCGRDC TDLKVALRQE LCNMEEILEY QNTTFFGGDC ISMIDYLVWP WFERLDVYGL ADCVNHTPML RLWIASMKQD PAVCALHTDK SVFLGFLNLY FQNNPCAFDF GLCNPIIR // ID H17B6_MOUSE Reviewed; 317 AA. AC Q9R092; DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 19-MAR-2014, entry version 110. DE RecName: Full=17-beta-hydroxysteroid dehydrogenase type 6; DE Short=17-beta-HSD 6; DE Short=17-beta-HSD6; DE EC=1.1.1.105; DE EC=1.1.1.239; DE EC=1.1.1.62; DE AltName: Full=17-beta-HSD9; DE AltName: Full=3-alpha->beta-hydroxysteroid epimerase; DE Short=3-alpha->beta-HSE; DE AltName: Full=Oxidative 3-alpha hydroxysteroid dehydrogenase; DE Flags: Precursor; GN Name=Hsd17b6; Synonyms=Gm182, Hsd17b9, Rdh8; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE RP SPECIFICITY. RC TISSUE=Liver; RX PubMed=10537158; DOI=10.1210/en.140.11.5275; RA Su J., Lin M., Napoli J.L.; RT "Complementary deoxyribonucleic acid cloning and enzymatic RT characterization of a novel 17beta/3alpha-hydroxysteroid/retinoid RT short chain dehydrogenase/reductase."; RL Endocrinology 140:5275-5284(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Small intestine; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Liver; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: NAD-dependent oxidoreductase with broad substrate CC specificity that shows both oxidative and reductive activity (in CC vitro). Has 17-beta-hydroxysteroid dehydrogenase activity towards CC various steroids (in vitro). Converts 5-alpha-androstan-3- CC alpha,17-beta-diol to androsterone and estradiol to estrone (in CC vitro). Has 3-alpha-hydroxysteroid dehydrogenase activity towards CC androsterone (in vitro). Has retinol dehydrogenase activity CC towards all-trans-retinol (in vitro). CC -!- CATALYTIC ACTIVITY: 17-beta-estradiol + NAD(P)(+) = estrone + CC NAD(P)H. CC -!- CATALYTIC ACTIVITY: Testosterone + NAD(+) = androstenedione + CC NADH. CC -!- CATALYTIC ACTIVITY: All-trans-retinol-[cellular-retinol-binding- CC protein] + NAD(+) = all-trans-retinal-[cellular-retinol-binding- CC protein] + NADH. CC -!- SUBCELLULAR LOCATION: Microsome membrane; Peripheral membrane CC protein; Lumenal side. Early endosome membrane; Peripheral CC membrane protein; Lumenal side (Potential). CC -!- TISSUE SPECIFICITY: Detected in liver. CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases CC (SDR) family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF103797; AAF04761.1; -; mRNA. DR EMBL; AK008212; BAB25536.1; -; mRNA. DR EMBL; BC021836; AAH21836.1; -; mRNA. DR RefSeq; NP_038814.1; NM_013786.2. DR UniGene; Mm.26719; -. DR ProteinModelPortal; Q9R092; -. DR SMR; Q9R092; 25-299. DR IntAct; Q9R092; 2. DR MINT; MINT-1864897; -. DR STRING; 10090.ENSMUSP00000026462; -. DR PhosphoSite; Q9R092; -. DR PaxDb; Q9R092; -. DR PRIDE; Q9R092; -. DR DNASU; 27400; -. DR Ensembl; ENSMUST00000026462; ENSMUSP00000026462; ENSMUSG00000025396. DR GeneID; 27400; -. DR KEGG; mmu:27400; -. DR UCSC; uc007hky.1; mouse. DR CTD; 8630; -. DR MGI; MGI:1351670; Hsd17b6. DR eggNOG; COG1028; -. DR GeneTree; ENSGT00620000087655; -. DR HOVERGEN; HBG005482; -. DR InParanoid; Q9R092; -. DR KO; K13369; -. DR OMA; LCATHAR; -. DR OrthoDB; EOG7FXZZX; -. DR TreeFam; TF325617; -. DR ChiTaRS; HSD17B6; mouse. DR NextBio; 305388; -. DR PRO; PR:Q9R092; -. DR Bgee; Q9R092; -. DR CleanEx; MM_HSD17B6; -. DR Genevestigator; Q9R092; -. DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW. DR GO; GO:0004303; F:estradiol 17-beta-dehydrogenase activity; IEA:UniProtKB-EC. DR GO; GO:0004745; F:retinol dehydrogenase activity; IEA:UniProtKB-EC. DR GO; GO:0047035; F:testosterone dehydrogenase (NAD+) activity; IEA:UniProtKB-EC. DR GO; GO:0008202; P:steroid metabolic process; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR002198; DH_sc/Rdtase_SDR. DR InterPro; IPR002347; Glc/ribitol_DH. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR020904; Sc_DH/Rdtase_CS. DR Pfam; PF00106; adh_short; 1. DR PRINTS; PR00081; GDHRDH. DR PRINTS; PR00080; SDRFAMILY. DR PROSITE; PS00061; ADH_SHORT; 1. PE 2: Evidence at transcript level; KW Complete proteome; Endoplasmic reticulum; Endosome; Glycoprotein; KW Lipid metabolism; Membrane; Microsome; NAD; Oxidoreductase; KW Reference proteome; Signal; Steroid metabolism. FT SIGNAL 1 17 Potential. FT CHAIN 18 317 17-beta-hydroxysteroid dehydrogenase type FT 6. FT /FTId=PRO_0000303212. FT NP_BIND 33 57 NAD (By similarity). FT ACT_SITE 176 176 Proton acceptor (By similarity). FT BINDING 164 164 Substrate (Potential). FT CARBOHYD 71 71 N-linked (GlcNAc...) (Potential). FT CARBOHYD 161 161 N-linked (GlcNAc...) (Potential). SQ SEQUENCE 317 AA; 36103 MW; 7B09D741424D3881 CRC64; MWFYLVTLVG LYHLLRWYRE RQVVSHLQDK YVFITGCDSG FGNLLARQLD RRGMRVLAAC LTEKGAEELR NKTSDRLETV ILDVTKTESI VAATQWVKER VGDRGLWGLV NNAGVLQPFA YIEWYRPEDY MPIFQVNLIG LTQVTISMLF LVKKARGRIV NVSSALGRVA LFGGFYSCSK YGVEAFSDVL RHEVQDFGVK VSIIEPGSFK TEMTDAELTI ERTKKVWEAA PEHIKESYGQ QFFDDFCSTT KRELMKCSRN LSLVTDCMEH ALTSTHPRTR YSAGWDAKFF FIPLSYLPAS LVDYLLAISR GKPAQAA // ID HAOX2_MOUSE Reviewed; 353 AA. AC Q9NYQ2; Q9JHS7; Q9JI00; DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 19-MAR-2014, entry version 119. DE RecName: Full=Hydroxyacid oxidase 2; DE Short=HAOX2; DE EC=1.1.3.15; DE AltName: Full=(S)-2-hydroxy-acid oxidase, peroxisomal; DE AltName: Full=Medium chain alpha-hydroxy acid oxidase; DE AltName: Full=Medium-chain L-2-hydroxy acid oxidase; GN Name=Hao2; Synonyms=Hao3, Haox2; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=10777549; DOI=10.1074/jbc.275.17.12590; RA Jones J.M., Morrell J.C., Gould S.J.; RT "Identification and characterization of HAOX1, HAOX2, and HAOX3, three RT human peroxisomal 2-hydroxy acid oxidases."; RL J. Biol. Chem. 275:12590-12597(2000). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Spielbauer B., Conzelmann E.; RT "Mus musculus long-chain L-2-hydroxy acid oxidase."; RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Van Veldhoven P.P.; RT "Search for PTS1-containing protein in mammals."; RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Cecum; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). CC -!- FUNCTION: Has 2-hydroxyacid oxidase activity. Most active on CC medium-chain substrates. CC -!- CATALYTIC ACTIVITY: (S)-2-hydroxy acid + O(2) = 2-oxo acid + CC H(2)O(2). CC -!- COFACTOR: FMN. CC -!- SUBUNIT: Homotetramer or homooctamer (By similarity). CC -!- SUBCELLULAR LOCATION: Peroxisome. CC -!- TISSUE SPECIFICITY: Pancreas. CC -!- SIMILARITY: Belongs to the FMN-dependent alpha-hydroxy acid CC dehydrogenase family. CC -!- SIMILARITY: Contains 1 FMN hydroxy acid dehydrogenase domain. CC -!- CAUTION: Was originally (PubMed:10777549) thought to originate CC from human. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF231918; AAF40201.1; -; mRNA. DR EMBL; AF272947; AAF81795.1; -; mRNA. DR EMBL; AJ251820; CAB96380.1; -; mRNA. DR EMBL; AK078908; BAC37452.1; -; mRNA. DR RefSeq; NP_062418.3; NM_019545.4. DR UniGene; Mm.281874; -. DR ProteinModelPortal; Q9NYQ2; -. DR SMR; Q9NYQ2; 3-352. DR STRING; 10090.ENSMUSP00000029464; -. DR PhosphoSite; Q9NYQ2; -. DR PaxDb; Q9NYQ2; -. DR PRIDE; Q9NYQ2; -. DR Ensembl; ENSMUST00000029464; ENSMUSP00000029464; ENSMUSG00000027870. DR GeneID; 56185; -. DR KEGG; mmu:56185; -. DR UCSC; uc008qqj.2; mouse. DR CTD; 51179; -. DR MGI; MGI:96012; Hao2. DR eggNOG; COG1304; -. DR GeneTree; ENSGT00390000018717; -. DR HOGENOM; HOG000217463; -. DR HOVERGEN; HBG051881; -. DR InParanoid; Q9NYQ2; -. DR KO; K11517; -. DR OMA; KEXIDAL; -. DR OrthoDB; EOG7B5WW0; -. DR TreeFam; TF313363; -. DR ChiTaRS; HAO2; mouse. DR NextBio; 311970; -. DR PRO; PR:Q9NYQ2; -. DR Bgee; Q9NYQ2; -. DR CleanEx; MM_HAO3; -. DR Genevestigator; Q9NYQ2; -. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell. DR GO; GO:0010181; F:FMN binding; IEA:Ensembl. DR GO; GO:0052853; F:long-chain-(S)-2-hydroxy-long-chain-acid oxidase activity; IEA:UniProtKB-EC. DR GO; GO:0052854; F:medium-chain-(S)-2-hydroxy-acid oxidase activity; IEA:UniProtKB-EC. DR GO; GO:0052852; F:very-long-chain-(S)-2-hydroxy-acid oxidase activity; IEA:UniProtKB-EC. DR GO; GO:0019395; P:fatty acid oxidation; IEA:Ensembl. DR GO; GO:0018924; P:mandelate metabolic process; IEA:Ensembl. DR GO; GO:0051260; P:protein homooligomerization; IEA:Ensembl. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR012133; Alpha-hydoxy_acid_DH_FMN. DR InterPro; IPR000262; FMN-dep_DH. DR InterPro; IPR008259; FMN_hydac_DH_AS. DR Pfam; PF01070; FMN_dh; 1. DR PIRSF; PIRSF000138; Al-hdrx_acd_dh; 1. DR PROSITE; PS00557; FMN_HYDROXY_ACID_DH_1; 1. DR PROSITE; PS51349; FMN_HYDROXY_ACID_DH_2; 1. PE 2: Evidence at transcript level; KW Complete proteome; Flavoprotein; FMN; Oxidoreductase; Peroxisome; KW Reference proteome. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 353 Hydroxyacid oxidase 2. FT /FTId=PRO_0000206321. FT DOMAIN 2 353 FMN hydroxy acid dehydrogenase. FT NP_BIND 279 303 FMN (By similarity). FT MOTIF 351 353 Microbody targeting signal (Potential). FT ACT_SITE 248 248 Proton acceptor (By similarity). FT BINDING 106 106 FMN (By similarity). FT BINDING 128 128 FMN (By similarity). FT BINDING 130 130 Substrate (By similarity). FT BINDING 156 156 FMN (By similarity). FT BINDING 165 165 Substrate (By similarity). FT BINDING 224 224 FMN (By similarity). FT BINDING 251 251 Substrate (Potential). FT BINDING 303 303 FMN (By similarity). FT CONFLICT 164 164 N -> H (in Ref. 3; CAB96380). SQ SEQUENCE 353 AA; 38700 MW; 0604D529F69DE3C7 CRC64; MSLLCLADFK AQAQKQLSKT SWDFIEGEAD DGITYNDNLA AFRRIRLRPR YLRDVSKIDT RTTIQGQEIN APICISPTAF HSIAWADGEK STAKAAQKAN ICYVISSYAS YTVEDIVAAA PGGLHWFQLY VQPDWDINKQ MVQRIEALGF KALVVTVDAP VLGNRRGNKR SLLDLEANIK LKDLRSPGES KSGLPTPLSM PSSSSCWNDL PLLQSMTRLP IILKGILTKE DAELAVKHNI RGIIVSNHGG RQLDEVPASI DALREVVAAV NGKIEVYMDG GVRTGNDVLK ALALGARCIF LGRPIIWGLA CKGEDGVKEV LDILKEELHT CMALSGCRSV AEISPDLIQF SRL // ID HAOX1_MOUSE Reviewed; 370 AA. AC Q9WU19; DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 19-MAR-2014, entry version 102. DE RecName: Full=Hydroxyacid oxidase 1; DE Short=HAOX1; DE EC=1.1.3.15; DE AltName: Full=Glycolate oxidase; DE Short=GOX; GN Name=Hao1; Synonyms=Gox1, Hao-1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY. RC TISSUE=Liver; RX PubMed=9891009; DOI=10.1074/jbc.274.4.2401; RA Kohler S.A., Menotti E., Kuhn L.C.; RT "Molecular cloning of mouse glycolate oxidase. High evolutionary RT conservation and presence of an iron-responsive element-like sequence RT in the mRNA."; RL J. Biol. Chem. 274:2401-2407(1999). RN [2] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-194, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=17242355; DOI=10.1073/pnas.0609836104; RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; RT "Large-scale phosphorylation analysis of mouse liver."; RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). RN [3] RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-184, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., RA Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). CC -!- FUNCTION: Has 2-hydroxyacid oxidase activity. Most active on the CC 2-carbon substrate glycolate, but is also active on 2-hydroxy CC fatty acids, with high activity towards 2-hydroxy palmitate and 2- CC hydroxy octanoate (By similarity). CC -!- CATALYTIC ACTIVITY: (S)-2-hydroxy acid + O(2) = 2-oxo acid + CC H(2)O(2). CC -!- COFACTOR: FMN. CC -!- PATHWAY: Organic acid metabolism; glycolate degradation; 3- CC phospho-D-glycerate from glycolate: step 1/4. CC -!- SUBCELLULAR LOCATION: Peroxisome. CC -!- TISSUE SPECIFICITY: Liver. CC -!- SIMILARITY: Belongs to the FMN-dependent alpha-hydroxy acid CC dehydrogenase family. CC -!- SIMILARITY: Contains 1 FMN hydroxy acid dehydrogenase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF104312; AAD25332.1; -; mRNA. DR RefSeq; NP_034533.1; NM_010403.2. DR UniGene; Mm.26634; -. DR ProteinModelPortal; Q9WU19; -. DR SMR; Q9WU19; 3-362. DR IntAct; Q9WU19; 2. DR MINT; MINT-1848223; -. DR PhosphoSite; Q9WU19; -. DR PaxDb; Q9WU19; -. DR PRIDE; Q9WU19; -. DR Ensembl; ENSMUST00000028704; ENSMUSP00000028704; ENSMUSG00000027261. DR GeneID; 15112; -. DR KEGG; mmu:15112; -. DR UCSC; uc008mns.1; mouse. DR CTD; 54363; -. DR MGI; MGI:96011; Hao1. DR eggNOG; COG1304; -. DR GeneTree; ENSGT00390000018717; -. DR HOGENOM; HOG000217463; -. DR HOVERGEN; HBG051881; -. DR InParanoid; Q9WU19; -. DR KO; K11517; -. DR OMA; IDPSINW; -. DR OrthoDB; EOG7B5WW0; -. DR TreeFam; TF313363; -. DR UniPathway; UPA00864; UER00830. DR ChiTaRS; HAO1; mouse. DR NextBio; 287518; -. DR PRO; PR:Q9WU19; -. DR ArrayExpress; Q9WU19; -. DR Bgee; Q9WU19; -. DR CleanEx; MM_HAO1; -. DR Genevestigator; Q9WU19; -. DR GO; GO:0005777; C:peroxisome; IDA:HGNC. DR GO; GO:0010181; F:FMN binding; ISS:UniProtKB. DR GO; GO:0008891; F:glycolate oxidase activity; ISS:UniProtKB. DR GO; GO:0052853; F:long-chain-(S)-2-hydroxy-long-chain-acid oxidase activity; IEA:UniProtKB-EC. DR GO; GO:0052854; F:medium-chain-(S)-2-hydroxy-acid oxidase activity; IEA:UniProtKB-EC. DR GO; GO:0052852; F:very-long-chain-(S)-2-hydroxy-acid oxidase activity; IEA:UniProtKB-EC. DR GO; GO:0001561; P:fatty acid alpha-oxidation; ISS:UniProtKB. DR GO; GO:0046296; P:glycolate catabolic process; ISS:UniProtKB. DR GO; GO:0006979; P:response to oxidative stress; IEA:Ensembl. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR012133; Alpha-hydoxy_acid_DH_FMN. DR InterPro; IPR000262; FMN-dep_DH. DR InterPro; IPR008259; FMN_hydac_DH_AS. DR Pfam; PF01070; FMN_dh; 1. DR PIRSF; PIRSF000138; Al-hdrx_acd_dh; 1. DR PROSITE; PS00557; FMN_HYDROXY_ACID_DH_1; 1. DR PROSITE; PS51349; FMN_HYDROXY_ACID_DH_2; 1. PE 1: Evidence at protein level; KW Complete proteome; Flavoprotein; FMN; Oxidoreductase; Peroxisome; KW Phosphoprotein; Reference proteome. FT CHAIN 1 370 Hydroxyacid oxidase 1. FT /FTId=PRO_0000206319. FT DOMAIN 1 365 FMN hydroxy acid dehydrogenase. FT NP_BIND 291 315 FMN (By similarity). FT MOTIF 368 370 Microbody targeting signal (Potential). FT ACT_SITE 260 260 Proton acceptor (By similarity). FT BINDING 26 26 Substrate (Potential). FT BINDING 108 108 FMN (By similarity). FT BINDING 130 130 FMN (By similarity). FT BINDING 132 132 Substrate (By similarity). FT BINDING 158 158 FMN (By similarity). FT BINDING 167 167 Substrate (By similarity). FT BINDING 236 236 FMN (By similarity). FT BINDING 263 263 Substrate (Potential). FT BINDING 315 315 FMN (By similarity). FT MOD_RES 184 184 N6-succinyllysine. FT MOD_RES 194 194 Phosphoserine. SQ SEQUENCE 370 AA; 41001 MW; 97339211AF9FC19C CRC64; MLPRLVCISD YEQHVRSVLQ KSVYDYYRSG ANDQETLADN IQAFSRWKLY PRMLRNVADI DLSTSVLGQR VSMPICVGAT AMQCMAHVDG ELATVRACQT MGTGMMLSSW ATSSIEEVAE AGPEALRWMQ LYIYKDREIS RQIVKRAEKQ GYKAIFVTVD TPYLGNRIDD VRNRFKLPPQ LRMKNFETND LAFSPKGNFG DNSGLAEYVA QAIDPSLSWD DITWLRRLTS LPIVVKGILR GDDAKEAVKH GVDGILVSNH GARQLDGVPA TIDVLPEIVE AVEGKVEVFL DGGVRKGTDV LKALALGAKA VFVGRPIIWG LAFQGEKGVQ DVLEILKEEF RLAMALSGCQ NVKVIDKTLV RKNPLAVSKI // ID HCD2_MOUSE Reviewed; 261 AA. AC O08756; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 4. DT 19-MAR-2014, entry version 117. DE RecName: Full=3-hydroxyacyl-CoA dehydrogenase type-2; DE EC=1.1.1.35; DE AltName: Full=17-beta-hydroxysteroid dehydrogenase 10; DE Short=17-beta-HSD 10; DE EC=1.1.1.51; DE AltName: Full=3-hydroxy-2-methylbutyryl-CoA dehydrogenase; DE EC=1.1.1.178; DE AltName: Full=3-hydroxyacyl-CoA dehydrogenase type II; DE AltName: Full=Endoplasmic reticulum-associated amyloid beta-peptide-binding protein; DE AltName: Full=Mitochondrial ribonuclease P protein 2; DE Short=Mitochondrial RNase P protein 2; DE AltName: Full=Type II HADH; GN Name=Hsd17b10; Synonyms=Erab, Hadh2; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=C57BL/6 X CBA; RA Fu J., Chen X., Stern D., Yan S.D.; RL Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases. RN [2] RP PROTEIN SEQUENCE OF 2-6; 193-212 AND 215-226, CLEAVAGE OF INITIATOR RP METHIONINE, ACETYLATION AT ALA-2, AND MASS SPECTROMETRY. RC STRAIN=C57BL/6; TISSUE=Liver; RA Bienvenut W.V.; RL Submitted (JUL-2005) to UniProtKB. RN [3] RP PROTEIN SEQUENCE OF 70-79 AND 131-147, AND MASS SPECTROMETRY. RC STRAIN=C57BL/6; TISSUE=Brain; RA Lubec G., Kang S.U.; RL Submitted (APR-2007) to UniProtKB. RN [4] RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-53; LYS-107 AND LYS-212, RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic fibroblast, and Liver; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., RA Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). RN [5] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-53; LYS-69; LYS-99; LYS-105; RP LYS-107 AND LYS-212, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE RP SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23576753; DOI=10.1073/pnas.1302961110; RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., RA Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.; RT "Label-free quantitative proteomics of the lysine acetylome in RT mitochondria identifies substrates of SIRT3 in metabolic pathways."; RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013). CC -!- FUNCTION: Functions in mitochondrial tRNA maturation. Part of CC mitochondrial ribonuclease P, an enzyme composed of MRPP1/TRMT10C, CC MRPP2/HSD17B10 and MRPP3/KIAA0391, which cleaves tRNA molecules in CC their 5'-ends. Catalyzes the beta-oxidation at position 17 of CC androgens and estrogens and has 3-alpha-hydroxysteroid CC dehydrogenase activity with androsterone. Catalyzes the third step CC in the beta-oxidation of fatty acids. Carries out oxidative CC conversions of 7-alpha-OH and 7-beta-OH bile acids. Also exhibits CC 20-beta-OH and 21-OH dehydrogenase activities with C21 steroids CC (By similarity). CC -!- CATALYTIC ACTIVITY: (S)-3-hydroxyacyl-CoA + NAD(+) = 3-oxoacyl-CoA CC + NADH. CC -!- CATALYTIC ACTIVITY: (2S,3S)-3-hydroxy-2-methylbutanoyl-CoA + CC NAD(+) = 2-methylacetoacetyl-CoA + NADH. CC -!- CATALYTIC ACTIVITY: Testosterone + NAD(P)(+) = androst-4-ene-3,17- CC dione + NAD(P)H. CC -!- SUBUNIT: Homotetramer. Interacts with MRPP1/TRMT10C and CC MRPP3/KIAA0391 (By similarity). CC -!- SUBCELLULAR LOCATION: Mitochondrion (By similarity). CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases CC (SDR) family. CC -!- SEQUENCE CAUTION: CC Sequence=AAB57689.1; Type=Erroneous initiation; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U96116; AAB57689.1; ALT_INIT; mRNA. DR UniGene; Mm.6994; -. DR ProteinModelPortal; O08756; -. DR SMR; O08756; 7-261. DR IntAct; O08756; 2. DR MINT; MINT-1861176; -. DR PhosphoSite; O08756; -. DR SWISS-2DPAGE; O08756; -. DR PaxDb; O08756; -. DR PRIDE; O08756; -. DR MGI; MGI:1333871; Hsd17b10. DR eggNOG; COG1028; -. DR HOVERGEN; HBG002145; -. DR ChiTaRS; HSD17B10; mouse. DR PMAP-CutDB; O08756; -. DR PRO; PR:O08756; -. DR CleanEx; MM_HSD17B10; -. DR Genevestigator; O08756; -. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI. DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:MGI. DR GO; GO:0047015; F:3-hydroxy-2-methylbutyryl-CoA dehydrogenase activity; IEA:UniProtKB-EC. DR GO; GO:0003857; F:3-hydroxyacyl-CoA dehydrogenase activity; IEA:UniProtKB-EC. DR GO; GO:0030283; F:testosterone dehydrogenase [NAD(P)] activity; IEA:UniProtKB-EC. DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR002198; DH_sc/Rdtase_SDR. DR InterPro; IPR002347; Glc/ribitol_DH. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR020904; Sc_DH/Rdtase_CS. DR Pfam; PF00106; adh_short; 1. DR PRINTS; PR00081; GDHRDH. DR PRINTS; PR00080; SDRFAMILY. DR PROSITE; PS00061; ADH_SHORT; 1. PE 1: Evidence at protein level; KW Acetylation; Complete proteome; Direct protein sequencing; KW Mitochondrion; NAD; Oxidoreductase; Reference proteome; KW tRNA processing. FT INIT_MET 1 1 Removed. FT CHAIN 2 261 3-hydroxyacyl-CoA dehydrogenase type-2. FT /FTId=PRO_0000054811. FT NP_BIND 12 37 NAD (By similarity). FT ACT_SITE 168 168 Proton acceptor (By similarity). FT BINDING 155 155 Substrate (By similarity). FT MOD_RES 2 2 N-acetylalanine. FT MOD_RES 53 53 N6-acetyllysine; alternate. FT MOD_RES 53 53 N6-succinyllysine; alternate. FT MOD_RES 69 69 N6-acetyllysine. FT MOD_RES 99 99 N6-acetyllysine. FT MOD_RES 105 105 N6-acetyllysine. FT MOD_RES 107 107 N6-acetyllysine; alternate. FT MOD_RES 107 107 N6-succinyllysine; alternate. FT MOD_RES 212 212 N6-acetyllysine; alternate. FT MOD_RES 212 212 N6-succinyllysine; alternate. SQ SEQUENCE 261 AA; 27419 MW; 61213B13E2839D41 CRC64; MAAAVRSVKG LVAVVTGGAS GPWLATAKRL VGQGATAVLL DVPDSEGESQ AKKLGESCIF APANVTSEKE IQAALTLAKE KFGRIDVAVN CAGIAVAIKT YHQKKNKIHT LEDFQRVINV NLIGTFNVIR LVAGEMGQNE PDQGGQRGVI INTASVAAFE GQVGQAAYSA SKGGIDGMTL PIARDLAPTG IRVVTIAPGL FATPLLTTLP EKVRNFLASQ VPFPSRLGDP AEYAHLVQTI IENPFLNGEV IRLDGAIRMQ P // ID HCDH_MOUSE Reviewed; 314 AA. AC Q61425; Q3TF75; Q3THK8; Q3UFI0; Q8K149; Q925U9; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 06-JUN-2002, sequence version 2. DT 19-MAR-2014, entry version 126. DE RecName: Full=Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial; DE Short=HCDH; DE EC=1.1.1.35; DE AltName: Full=Medium and short-chain L-3-hydroxyacyl-coenzyme A dehydrogenase; DE AltName: Full=Short-chain 3-hydroxyacyl-CoA dehydrogenase; DE Flags: Precursor; GN Name=Hadh; Synonyms=Hadhsc, Mschad, Schad; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=7642117; DOI=10.1016/0378-1119(95)00205-K; RA Nomura M., Takihara Y., Shimada K.; RT "Isolation of a cDNA clone encoding mouse 3-hydroxyacyl CoA RT dehydrogenase."; RL Gene 160:309-310(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA O'Brien L.K., Sims H.F., Strauss A.W.; RT "Mouse medium and short chain L-3-hydroxyacyl-coenzyme A dehydrogenase RT gene."; RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; RC TISSUE=Amnion, Extraembryonic tissue, Pancreas, and Placenta; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Kidney, and Liver; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP SUCCINYLATION AT LYS-81, DESUCCINYLATION BY SIRT5, ACETYLATION [LARGE RP SCALE ANALYSIS] AT LYS-241, SUCCINYLATION [LARGE SCALE ANALYSIS] AT RP LYS-80; LYS-81; LYS-87; LYS-136; LYS-185; LYS-192; LYS-202; LYS-206; RP LYS-212; LYS-241 AND LYS-312, AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic fibroblast, and Liver; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., RA Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). RN [6] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-75; LYS-81; LYS-87; LYS-125; RP LYS-136; LYS-179; LYS-185; LYS-192; LYS-202; LYS-212 AND LYS-241, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23576753; DOI=10.1073/pnas.1302961110; RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., RA Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.; RT "Label-free quantitative proteomics of the lysine acetylome in RT mitochondria identifies substrates of SIRT3 in metabolic pathways."; RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013). CC -!- FUNCTION: Plays an essential role in the mitochondrial beta- CC oxidation of short chain fatty acids. Exerts it highest activity CC toward 3-hydroxybutyryl-CoA. CC -!- CATALYTIC ACTIVITY: (S)-3-hydroxyacyl-CoA + NAD(+) = 3-oxoacyl-CoA CC + NADH. CC -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation. CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix. CC -!- PTM: Succinylation at Lys-81, adjacent to a coenzyme A binding CC site. Desuccinylated by SIRT5. CC -!- SIMILARITY: Belongs to the 3-hydroxyacyl-CoA dehydrogenase family. CC -!- SEQUENCE CAUTION: CC Sequence=BAA06122.1; Type=Erroneous initiation; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; D29639; BAA06122.1; ALT_INIT; mRNA. DR EMBL; AF375597; AAK54642.1; -; Genomic_DNA. DR EMBL; AF375596; AAK54642.1; JOINED; Genomic_DNA. DR EMBL; AK132260; BAE21064.1; -; mRNA. DR EMBL; AK148486; BAE28581.1; -; mRNA. DR EMBL; AK167024; BAE39197.1; -; mRNA. DR EMBL; AK168238; BAE40188.1; -; mRNA. DR EMBL; AK168877; BAE40695.1; -; mRNA. DR EMBL; AK169261; BAE41023.1; -; mRNA. DR EMBL; BC028833; AAH28833.1; -; mRNA. DR EMBL; BC064712; AAH64712.1; -; mRNA. DR PIR; JC4210; JC4210. DR RefSeq; NP_032238.2; NM_008212.4. DR UniGene; Mm.260164; -. DR ProteinModelPortal; Q61425; -. DR SMR; Q61425; 23-314. DR IntAct; Q61425; 4. DR MINT; MINT-1859897; -. DR PhosphoSite; Q61425; -. DR REPRODUCTION-2DPAGE; Q61425; -. DR SWISS-2DPAGE; Q61425; -. DR PaxDb; Q61425; -. DR PRIDE; Q61425; -. DR Ensembl; ENSMUST00000029610; ENSMUSP00000029610; ENSMUSG00000027984. DR GeneID; 15107; -. DR KEGG; mmu:15107; -. DR UCSC; uc008rjl.1; mouse. DR CTD; 3033; -. DR MGI; MGI:96009; Hadh. DR eggNOG; COG1250; -. DR GeneTree; ENSGT00720000108673; -. DR HOGENOM; HOG000141498; -. DR HOVERGEN; HBG000832; -. DR InParanoid; Q61425; -. DR KO; K00022; -. DR OMA; AGFVTTR; -. DR OrthoDB; EOG7K3TMS; -. DR TreeFam; TF300886; -. DR UniPathway; UPA00659; -. DR ChiTaRS; HADH; mouse. DR NextBio; 287498; -. DR PRO; PR:Q61425; -. DR Bgee; Q61425; -. DR CleanEx; MM_HADH; -. DR Genevestigator; Q61425; -. DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:MGI. DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell. DR GO; GO:0003857; F:3-hydroxyacyl-CoA dehydrogenase activity; IDA:MGI. DR GO; GO:0070403; F:NAD+ binding; IEA:InterPro. DR GO; GO:0006635; P:fatty acid beta-oxidation; IEA:UniProtKB-UniPathway. DR GO; GO:0046676; P:negative regulation of insulin secretion; IEA:Ensembl. DR GO; GO:0014823; P:response to activity; IEA:Ensembl. DR GO; GO:0042493; P:response to drug; IEA:Ensembl. DR GO; GO:0032868; P:response to insulin; IEA:Ensembl. DR Gene3D; 1.10.1040.10; -; 1. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR022694; 3-OHacyl-CoA_DH. DR InterPro; IPR006180; 3-OHacyl-CoA_DH_CS. DR InterPro; IPR006176; 3-OHacyl-CoA_DH_NAD-bd. DR InterPro; IPR006108; 3HC_DH_C. DR InterPro; IPR008927; 6-PGluconate_DH_C-like. DR InterPro; IPR013328; DH_multihelical. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Pfam; PF00725; 3HCDH; 1. DR Pfam; PF02737; 3HCDH_N; 1. DR PIRSF; PIRSF000105; HCDH; 1. DR SUPFAM; SSF48179; SSF48179; 1. DR PROSITE; PS00067; 3HCDH; 1. PE 1: Evidence at protein level; KW Acetylation; Complete proteome; Fatty acid metabolism; KW Lipid metabolism; Mitochondrion; NAD; Oxidoreductase; KW Reference proteome; Transit peptide. FT TRANSIT 1 12 Mitochondrion (By similarity). FT CHAIN 13 314 Hydroxyacyl-coenzyme A dehydrogenase, FT mitochondrial. FT /FTId=PRO_0000007407. FT NP_BIND 34 39 NAD (By similarity). FT BINDING 57 57 NAD (By similarity). FT BINDING 73 73 Coenzyme A (By similarity). FT BINDING 80 80 Coenzyme A (By similarity). FT BINDING 122 122 NAD (By similarity). FT BINDING 127 127 NAD (By similarity). FT BINDING 149 149 Coenzyme A (By similarity). FT BINDING 149 149 NAD (By similarity). FT BINDING 173 173 NAD (By similarity). FT BINDING 305 305 NAD (By similarity). FT SITE 170 170 Important for catalytic activity (By FT similarity). FT MOD_RES 75 75 N6-acetyllysine. FT MOD_RES 80 80 N6-succinyllysine. FT MOD_RES 81 81 N6-acetyllysine; alternate. FT MOD_RES 81 81 N6-succinyllysine; alternate. FT MOD_RES 87 87 N6-acetyllysine; alternate. FT MOD_RES 87 87 N6-succinyllysine; alternate. FT MOD_RES 125 125 N6-acetyllysine. FT MOD_RES 136 136 N6-acetyllysine; alternate. FT MOD_RES 136 136 N6-succinyllysine; alternate. FT MOD_RES 179 179 N6-acetyllysine. FT MOD_RES 185 185 N6-acetyllysine; alternate. FT MOD_RES 185 185 N6-succinyllysine; alternate. FT MOD_RES 192 192 N6-acetyllysine; alternate. FT MOD_RES 192 192 N6-succinyllysine; alternate. FT MOD_RES 202 202 N6-acetyllysine; alternate. FT MOD_RES 202 202 N6-succinyllysine; alternate. FT MOD_RES 206 206 N6-succinyllysine. FT MOD_RES 212 212 N6-acetyllysine; alternate. FT MOD_RES 212 212 N6-succinyllysine; alternate. FT MOD_RES 241 241 N6-acetyllysine; alternate. FT MOD_RES 241 241 N6-succinyllysine; alternate. FT MOD_RES 312 312 N6-acetyllysine; alternate (By FT similarity). FT MOD_RES 312 312 N6-succinyllysine; alternate. FT CONFLICT 11 11 S -> Y (in Ref. 3; BAE40188). FT CONFLICT 56 56 V -> M (in Ref. 3; BAE41023). FT CONFLICT 111 111 H -> D (in Ref. 1; BAA06122). FT CONFLICT 146 146 S -> G (in Ref. 3; BAE40188). FT CONFLICT 211 211 C -> S (in Ref. 1; BAA06122). SQ SEQUENCE 314 AA; 34464 MW; 366A4C075F708BC1 CRC64; MAFVTRQFLR SMSSSSSASA AAKKILIKHV TVIGGGLMGA GIAQVAAATG HTVVLVDQTE DILAKSKKGI EESLKRMAKK KFTENPKAGD EFVEKTLSCL STSTDAASVV HSTDLVVEAI VENLKLKNEL FQRLDKFAAE HTIFASNTSS LQITNIANAT TRQDRFAGLH FFNPVPMMKL VEVIKTPMTS QKTFESLVDF CKTLGKHPVS CKDTPGFIVN RLLVPYLIEA VRLHERGDAS KEDIDTAMKL GAGYPMGPFE LLDYVGLDTT KFILDGWHEM EPENPLFQPS PSMNNLVAQK KLGKKTGEGF YKYK // ID HEM6_MOUSE Reviewed; 443 AA. AC P36552; Q7TQ36; Q8VD08; DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot. DT 21-JUN-2004, sequence version 2. DT 19-MAR-2014, entry version 125. DE RecName: Full=Coproporphyrinogen-III oxidase, mitochondrial; DE Short=COX; DE Short=Coprogen oxidase; DE Short=Coproporphyrinogenase; DE EC=1.3.3.3; DE Flags: Precursor; GN Name=Cpox; Synonyms=Cpo; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=8407975; RA Kohno H., Furukawa T., Yoshinaga T., Tokunaga R., Taketani S.; RT "Coproporphyrinogen oxidase. Purification, molecular cloning, and RT induction of mRNA during erythroid differentiation."; RL J. Biol. Chem. 268:21359-21363(1993). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Kidney; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-139. RX PubMed=15482256; DOI=10.1042/BJ20040570; RA Dailey T.A., Woodruff J.H., Dailey H.A.; RT "Examination of mitochondrial protein targeting of haem synthetic RT enzymes: in vivo identification of three functional haem-responsive RT motifs in 5-aminolaevulinate synthase."; RL Biochem. J. 386:381-386(2005). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-144. RX PubMed=12862310; DOI=10.1620/tjem.200.39; RA Susa S., Daimon M., Ono H., Li S., Yoshida T., Kato T.; RT "The long, but not the short, presequence of human coproporphyrinogen RT oxidase is essential for its import and sorting to mitochondria."; RL Tohoku J. Exp. Med. 200:39-45(2003). RN [5] RP PROTEIN SEQUENCE OF 99-125 AND 248-258. RX PubMed=8159699; DOI=10.1073/pnas.91.8.3024; RA Martasek P., Camadro J.-M., Delfau-Larue M.H., Dumas J.B., RA Montagne J.J., de Verneuil H., Labbe P., Grandchamp B.; RT "Molecular cloning, sequencing, and functional expression of a cDNA RT encoding human coproporphyrinogen oxidase."; RL Proc. Natl. Acad. Sci. U.S.A. 91:3024-3028(1994). RN [6] RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-393, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., RA Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). RN [7] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-393, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23576753; DOI=10.1073/pnas.1302961110; RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., RA Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.; RT "Label-free quantitative proteomics of the lysine acetylome in RT mitochondria identifies substrates of SIRT3 in metabolic pathways."; RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013). CC -!- FUNCTION: Key enzyme in heme biosynthesis. Catalyzes the oxidative CC decarboxylation of propionic acid side chains of rings A and B of CC coproporphyrinogen III (By similarity). CC -!- CATALYTIC ACTIVITY: Coproporphyrinogen-III + O(2) + 2 H(+) = CC protoporphyrinogen-IX + 2 CO(2) + 2 H(2)O. CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin- CC IX biosynthesis; protoporphyrinogen-IX from coproporphyrinogen-III CC (O2 route): step 1/1. CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space. CC -!- TISSUE SPECIFICITY: Erythroid cells and non erythroid cells such CC as liver. CC -!- PTM: Acetylation of Lys-360 is observed in liver mitochondria from CC fasted mice but not from fed mice. CC -!- SIMILARITY: Belongs to the aerobic coproporphyrinogen-III oxidase CC family. CC -!- SEQUENCE CAUTION: CC Sequence=AAH17680.2; Type=Erroneous initiation; CC Sequence=BAA03840.1; Type=Frameshift; Positions=22, 43, 76; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; D16333; BAA03840.1; ALT_FRAME; mRNA. DR EMBL; BC017680; AAH17680.2; ALT_INIT; mRNA. DR EMBL; AY382578; AAQ88103.1; -; Genomic_DNA. DR EMBL; AB099924; BAC79229.1; -; Genomic_DNA. DR PIR; A48049; A48049. DR RefSeq; NP_031783.2; NM_007757.2. DR UniGene; Mm.291519; -. DR ProteinModelPortal; P36552; -. DR SMR; P36552; 110-442. DR IntAct; P36552; 1. DR MINT; MINT-1844590; -. DR PhosphoSite; P36552; -. DR PaxDb; P36552; -. DR PRIDE; P36552; -. DR Ensembl; ENSMUST00000060077; ENSMUSP00000055455; ENSMUSG00000022742. DR GeneID; 12892; -. DR KEGG; mmu:12892; -. DR UCSC; uc007znz.2; mouse. DR CTD; 1371; -. DR MGI; MGI:104841; Cpox. DR eggNOG; COG0408; -. DR GeneTree; ENSGT00390000017311; -. DR HOGENOM; HOG000262768; -. DR HOVERGEN; HBG051897; -. DR InParanoid; P36552; -. DR KO; K00228; -. DR OMA; QRPEAKG; -. DR OrthoDB; EOG7BZVSG; -. DR TreeFam; TF300703; -. DR UniPathway; UPA00251; UER00322. DR ChiTaRS; CPOX; mouse. DR NextBio; 282498; -. DR PRO; PR:P36552; -. DR ArrayExpress; P36552; -. DR Bgee; P36552; -. DR CleanEx; MM_CPOX; -. DR Genevestigator; P36552; -. DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:Ensembl. DR GO; GO:0005758; C:mitochondrial intermembrane space; IEA:UniProtKB-SubCell. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR GO; GO:0004109; F:coproporphyrinogen oxidase activity; IDA:MGI. DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB. DR GO; GO:0005391; F:sodium:potassium-exchanging ATPase activity; TAS:MGI. DR GO; GO:0005212; F:structural constituent of eye lens; IMP:MGI. DR GO; GO:0006783; P:heme biosynthetic process; IDA:MGI. DR GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0046685; P:response to arsenic-containing substance; IEA:Ensembl. DR GO; GO:0017085; P:response to insecticide; IEA:Ensembl. DR GO; GO:0010039; P:response to iron ion; IEA:Ensembl. DR GO; GO:0010288; P:response to lead ion; IEA:Ensembl. DR GO; GO:0051597; P:response to methylmercury; IEA:Ensembl. DR Gene3D; 3.40.1500.10; -; 1. DR InterPro; IPR001260; Coprogen_oxidase_aer. DR InterPro; IPR018375; Coprogen_oxidase_CS. DR PANTHER; PTHR10755; PTHR10755; 1. DR Pfam; PF01218; Coprogen_oxidas; 1. DR PRINTS; PR00073; COPRGNOXDASE. DR SUPFAM; SSF102886; SSF102886; 1. DR PROSITE; PS01021; COPROGEN_OXIDASE; 1. PE 1: Evidence at protein level; KW Acetylation; Complete proteome; Direct protein sequencing; KW Heme biosynthesis; Mitochondrion; Oxidoreductase; KW Porphyrin biosynthesis; Reference proteome; Transit peptide. FT TRANSIT 1 98 Mitochondrion. FT CHAIN 99 443 Coproporphyrinogen-III oxidase, FT mitochondrial. FT /FTId=PRO_0000006030. FT REGION 182 191 Important for dimerization (By FT similarity). FT REGION 249 251 Substrate binding (By similarity). FT REGION 381 417 Important for dimerization (By FT similarity). FT REGION 400 405 Substrate binding (By similarity). FT ACT_SITE 247 247 Proton donor (By similarity). FT BINDING 233 233 Substrate (By similarity). FT SITE 316 316 Important for dimerization (By FT similarity). FT MOD_RES 393 393 N6-acetyllysine; alternate. FT MOD_RES 393 393 N6-succinyllysine; alternate. FT CONFLICT 7 7 R -> P (in Ref. 1; BAA03840). FT CONFLICT 101 101 S -> T (in Ref. 5; AA sequence). FT CONFLICT 116 117 CS -> SD (in Ref. 5; AA sequence). FT CONFLICT 122 122 S -> T (in Ref. 5; AA sequence). FT CONFLICT 124 124 V -> P (in Ref. 5; AA sequence). FT CONFLICT 138 138 K -> N (in Ref. 3; BAC79229). FT CONFLICT 275 275 T -> R (in Ref. 1; BAA03840). SQ SEQUENCE 443 AA; 49715 MW; 9F3D5E8E420645F0 CRC64; MALRLGRLGS DPWWRAVLGD YAQLRAASPR CASARVCQLP GTAGPQPRRG LGYGPWARGG SGLGTRLAAT LAGLAGLAAA AFGHVQRAEM VPKSSGARSP SPGRREEDGD ELARRCSTFM SSPVTELREL RRRPEDMKTK MELMIMETQA QVCRALAQVD GVADFTVDRW ERKEGGGGIT CVLQDGRVFE KAGVSISVVH GNLSEEAANQ MRGRGKTLKT KDSKLPFTAM GVSSVIHPKN PYAPTMHFNY RYFEVEEADG NTHWWFGGGC DLTPTYLNQE DAVHFHRTLK EACDQHGPDI YPKFKKWCDD YFFIVHRGER RGIGGIFFDD LDSPSKEEAF RFVKTCAEAV VPSYVPIVKK HCDDSYTPRD KLWQQLRRGR YVEFNLLYDR GTKFGLFTPG SRIESILMSL PLTARWEYMH SPPENSKEAE ILEVLRHPKD WVH // ID HEPH_MOUSE Reviewed; 1157 AA. AC Q9Z0Z4; A2AI63; Q6ZQ65; Q80Y80; Q8C4S2; DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 3. DT 19-MAR-2014, entry version 103. DE RecName: Full=Hephaestin; DE EC=1.-.-.-; DE Flags: Precursor; GN Name=Heph; Synonyms=Kiaa0698; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC STRAIN=C57BL/6J; RX PubMed=9988272; DOI=10.1038/5979; RA Vulpe C.D., Kuo Y.M., Murphy T.L., Cowley L., Askwith C., Libina N., RA Gitschier J., Anderson G.J.; RT "Hephaestin, a ceruloplasmin homologue implicated in intestinal iron RT transport, is defective in the sla mouse."; RL Nat. Genet. 21:195-199(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Embryonic tail; RX PubMed=14621295; DOI=10.1093/dnares/10.4.167; RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., RA Saga Y., Nagase T., Ohara O., Koga H.; RT "Prediction of the coding sequences of mouse homologues of KIAA gene: RT III. The complete nucleotide sequences of 500 mouse KIAA-homologous RT cDNAs identified by screening of terminal sequences of cDNA clones RT randomly sampled from size-fractionated libraries."; RL DNA Res. 10:167-180(2003). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC STRAIN=FVB/N; TISSUE=Colon; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-889. RC STRAIN=C57BL/6J; TISSUE=Head; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). CC -!- FUNCTION: May function as a ferroxidase for ferrous (II) to ferric CC ion (III) conversion and may be involved in copper transport and CC homeostasis. Implicated in iron homeostasis and may mediate iron CC efflux associated to ferroportin 1. CC -!- COFACTOR: Binds 6 copper ions per monomer (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane CC protein (Potential). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9Z0Z4-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9Z0Z4-2; Sequence=VSP_011628; CC -!- DISEASE: Note=Defects in Heph are a cause of the sex-linked anemia CC (sla) that is characterized by moderate to severe microcytic CC hypochronic anemia. CC -!- SIMILARITY: Belongs to the multicopper oxidase family. CC -!- SIMILARITY: Contains 6 plastocyanin-like domains. CC -!- SEQUENCE CAUTION: CC Sequence=BAC98004.1; Type=Erroneous initiation; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF082567; AAD16035.1; -; mRNA. DR EMBL; AK129194; BAC98004.1; ALT_INIT; mRNA. DR EMBL; AL732365; CAM22078.1; -; Genomic_DNA. DR EMBL; CH466564; EDL14216.1; -; Genomic_DNA. DR EMBL; BC048237; AAH48237.1; -; mRNA. DR EMBL; BC054442; AAH54442.1; -; mRNA. DR EMBL; AK081330; BAC38197.1; -; mRNA. DR RefSeq; NP_001153099.1; NM_001159627.1. DR RefSeq; NP_001153100.1; NM_001159628.1. DR RefSeq; NP_034547.2; NM_010417.2. DR RefSeq; NP_851790.1; NM_181273.4. DR RefSeq; XP_006527900.1; XM_006527837.1. DR RefSeq; XP_006527901.1; XM_006527838.1. DR UniGene; Mm.277092; -. DR ProteinModelPortal; Q9Z0Z4; -. DR SMR; Q9Z0Z4; 24-1065. DR PhosphoSite; Q9Z0Z4; -. DR PaxDb; Q9Z0Z4; -. DR PRIDE; Q9Z0Z4; -. DR Ensembl; ENSMUST00000033553; ENSMUSP00000033553; ENSMUSG00000031209. [Q9Z0Z4-1] DR Ensembl; ENSMUST00000113838; ENSMUSP00000109469; ENSMUSG00000031209. [Q9Z0Z4-1] DR GeneID; 15203; -. DR KEGG; mmu:15203; -. DR UCSC; uc009tuk.2; mouse. [Q9Z0Z4-1] DR UCSC; uc009tul.2; mouse. [Q9Z0Z4-2] DR CTD; 9843; -. DR MGI; MGI:1332240; Heph. DR eggNOG; NOG276067; -. DR GeneTree; ENSGT00550000074552; -. DR HOGENOM; HOG000231499; -. DR HOVERGEN; HBG003674; -. DR InParanoid; A2AI63; -. DR KO; K14735; -. DR OMA; LIHLKNF; -. DR OrthoDB; EOG7V49XN; -. DR TreeFam; TF329807; -. DR NextBio; 287747; -. DR PRO; PR:Q9Z0Z4; -. DR ArrayExpress; Q9Z0Z4; -. DR Bgee; Q9Z0Z4; -. DR CleanEx; MM_HEPH; -. DR Genevestigator; Q9Z0Z4; -. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl. DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl. DR GO; GO:0005507; F:copper ion binding; IEA:InterPro. DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW. DR GO; GO:0006879; P:cellular iron ion homeostasis; IEA:InterPro. DR GO; GO:0006825; P:copper ion transport; IEA:UniProtKB-KW. DR GO; GO:0006826; P:iron ion transport; TAS:MGI. DR Gene3D; 2.60.40.420; -; 6. DR InterPro; IPR011706; Cu-oxidase_2. DR InterPro; IPR011707; Cu-oxidase_3. DR InterPro; IPR002355; Cu_oxidase_Cu_BS. DR InterPro; IPR008972; Cupredoxin. DR InterPro; IPR027154; HEPH. DR PANTHER; PTHR10127:SF54; PTHR10127:SF54; 1. DR Pfam; PF07731; Cu-oxidase_2; 1. DR Pfam; PF07732; Cu-oxidase_3; 3. DR SUPFAM; SSF49503; SSF49503; 6. DR PROSITE; PS00079; MULTICOPPER_OXIDASE1; 3. DR PROSITE; PS00080; MULTICOPPER_OXIDASE2; 1. PE 2: Evidence at transcript level; KW Alternative splicing; Complete proteome; Copper; Copper transport; KW Disulfide bond; Glycoprotein; Ion transport; Iron; Iron transport; KW Membrane; Metal-binding; Oxidoreductase; Reference proteome; Repeat; KW Signal; Transmembrane; Transmembrane helix; Transport. FT SIGNAL 1 18 Potential. FT CHAIN 19 1157 Hephaestin. FT /FTId=PRO_0000002916. FT TOPO_DOM 19 1109 Extracellular (Potential). FT TRANSMEM 1110 1130 Helical; (Potential). FT TOPO_DOM 1131 1157 Cytoplasmic (Potential). FT DOMAIN 24 206 Plastocyanin-like 1. FT DOMAIN 218 366 Plastocyanin-like 2. FT DOMAIN 379 559 Plastocyanin-like 3. FT DOMAIN 569 717 Plastocyanin-like 4. FT DOMAIN 730 902 Plastocyanin-like 5. FT DOMAIN 910 1086 Plastocyanin-like 6. FT METAL 126 126 Copper 1; type 2 (By similarity). FT METAL 128 128 Copper 2; type 3 (By similarity). FT METAL 186 186 Copper 2; type 3 (By similarity). FT METAL 188 188 Copper 3; type 3 (By similarity). FT METAL 304 304 Copper 4; type 1 (By similarity). FT METAL 347 347 Copper 4; type 1 (By similarity). FT METAL 352 352 Copper 4; type 1 (By similarity). FT METAL 655 655 Copper 5; type 1 (By similarity). FT METAL 698 698 Copper 5; type 1 (By similarity). FT METAL 703 703 Copper 5; type 1 (By similarity). FT METAL 708 708 Copper 5; type 1 (By similarity). FT METAL 999 999 Copper 6; type 1 (By similarity). FT METAL 1002 1002 Copper 1; type 2 (By similarity). FT METAL 1004 1004 Copper 3; type 3 (By similarity). FT METAL 1044 1044 Copper 3; type 3 (By similarity). FT METAL 1045 1045 Copper 6; type 1 (By similarity). FT METAL 1046 1046 Copper 2; type 3 (By similarity). FT METAL 1050 1050 Copper 6; type 1 (By similarity). FT METAL 1055 1055 Copper 6; type 1 (By similarity). FT CARBOHYD 49 49 N-linked (GlcNAc...) (Potential). FT CARBOHYD 54 54 N-linked (GlcNAc...) (Potential). FT CARBOHYD 164 164 N-linked (GlcNAc...) (Potential). FT CARBOHYD 236 236 N-linked (GlcNAc...) (Potential). FT CARBOHYD 587 587 N-linked (GlcNAc...) (Potential). FT CARBOHYD 713 713 N-linked (GlcNAc...) (Potential). FT CARBOHYD 757 757 N-linked (GlcNAc...) (Potential). FT CARBOHYD 930 930 N-linked (GlcNAc...) (Potential). FT DISULFID 180 206 Potential. FT DISULFID 285 366 Potential. FT DISULFID 533 559 Potential. FT DISULFID 636 717 Potential. FT DISULFID 876 902 Potential. FT VAR_SEQ 1081 1081 Missing (in isoform 2). FT /FTId=VSP_011628. FT CONFLICT 501 542 Missing (in Ref. 6; BAC38197). FT CONFLICT 593 593 N -> S (in Ref. 2; BAC98004 and 5; FT AAH48237/AAH54442). FT CONFLICT 856 889 VLTYQWNIPERSGPGPSDSACVSWIYYSAVDPIK -> LEH FT LMKRQRLYNPFTLVFWFIPFNILHSWAGQVT (in Ref. FT 6; BAC38197). FT CONFLICT 1068 1068 F -> Y (in Ref. 1; AAD16035). SQ SEQUENCE 1157 AA; 129666 MW; 41055EC4DA11DC12 CRC64; MKAGHLLWAL LLMHSLWSIP TDGAIRNYYL GIQDMQWNYA PKGRNVITNQ TLNNDTVASS FLKSGKNRIG SSYKKTVYKE YSDGTYTEEI AKPAWLGFLG PLLQAEVGDV ILIHLKNFAS RPYTIHPHGV FYEKDSEGSL YPDGSSGYLK ADDSVPPGGS HVYNWSIPES HAPTEADPAC LTWIYHSHVD APRDIATGLI GPLITCKRGT LDGNSPPQRK DVDHNFFLLF SVIDENLSWH LDDNIATYCS DPASVDKEDG AFQDSNRMHA INGFVFGNLP ELSMCAQKHV AWHLFGMGNE IDVHTAFFHG QMLSIRGHHT DVANIFPATF VTAEMVPQKS GTWLISCEVN SHLRSGMQAF YKVDSCSMDP PVDQLTGKVR QYFIQAHEIQ WDYGPIGYDG RTGKSLREPG SGPDKYFQKS SSRIGGTYWK VRYEAFQDET FQERVHQEEE THLGILGPVI RAEVGDTIQV VFYNRASQPF SIQPHGVFYE KNSEGTVYND GTSHPKVAKS FEKVTYYWTV PPHAGPTAQD PACLTWMYFS AADPTRDTNS GLVGPLLVCK AGALGADGKQ KGVDKEFFLL FTVFDENESW YNNANQAAGM LDSRLLSEDV EGFQDSNRMH AINGFLFSNL PRLDMCKGDT VAWHLLGLGT ETDVHGVMFE GNTVQLQGMR KGAVMLFPHT FVTAIMQPDN PGIFEIYCQA GSHREEGMQA IYNVSQCSSH QDSPRQHYQA SRVYYIMAEE IEWDYCPDRS WELEWHNTSE KDSYGHVFLS NKDGLLGSKY KKAVFREYTD GTFRIPRPRS GPEEHLGILG PLIRGEVGDI LTVVFKNKAS RPYSIHAHGV LESNTGGPQA AEPGEVLTYQ WNIPERSGPG PSDSACVSWI YYSAVDPIKD MYSGLVGPLV ICRNGILEPN GGRNDMDREF ALLFLIFDEN QSWYLKENIA TYGPQESSHV NLKDATFLES NKMHAINGKL YANLRGLTVY QGERVAWYML AMGQDTDIHT VHFHAESFLY QNGQSYRADV VDLFPGTFEV VEMVASNPGT WLMHCHVTDH VHAGMETIFT VLSHEEHFST MTTITKEIGK AVILRDIGGD NVKMLGMNIP IKDVEILSSA LIAICVLLLL IALALGGVVW YQHRQRKLRR NRRSILDDSF KLLSLKQ // ID HGD_MOUSE Reviewed; 445 AA. AC O09173; Q7TPP2; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 2. DT 19-MAR-2014, entry version 108. DE RecName: Full=Homogentisate 1,2-dioxygenase; DE EC=1.13.11.5; DE AltName: Full=Homogentisate oxygenase; DE AltName: Full=Homogentisic acid oxidase; DE AltName: Full=Homogentisicase; GN Name=Hgd; Synonyms=Aku, Hgo; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE. RC STRAIN=C57BL/6 X CBA; TISSUE=Liver; RX PubMed=9069115; DOI=10.1007/s003359900383; RA Schmidt S.R., Gehrig A., Koehler M.R., Schmid M., Mueller C.R., RA Kress W.; RT "Cloning of the homogentisate 1,2-dioxygenase gene, the key enzyme of RT alkaptonuria in mouse."; RL Mamm. Genome 8:168-171(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Liver; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP CHARACTERIZATION. RC TISSUE=Liver; RX PubMed=7705358; DOI=10.1111/j.1432-1033.1995.00425.x; RA Schmidt S.R., Muller C.R., Kress W.; RT "Murine liver homogentisate 1,2-dioxygenase. Purification to RT homogeneity and novel biochemical properties."; RL Eur. J. Biochem. 228:425-430(1995). RN [5] RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-414, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., RA Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). CC -!- CATALYTIC ACTIVITY: Homogentisate + O(2) = 4-maleylacetoacetate. CC -!- COFACTOR: Iron. CC -!- PATHWAY: Amino-acid degradation; L-phenylalanine degradation; CC acetoacetate and fumarate from L-phenylalanine: step 4/6. CC -!- SUBUNIT: Homohexamer arranged as a dimer of trimers (By CC similarity). CC -!- DISEASE: Note=Defects in Hgd are the cause of alkaptonuria (aku). CC Aku is an autosomal recessive error of metabolism which is CC characterized by an increase in the level of homogentisic acid. CC -!- SIMILARITY: Belongs to the homogentisate dioxygenase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U58988; AAC53224.1; -; mRNA. DR EMBL; CH466521; EDK97961.1; -; Genomic_DNA. DR EMBL; BC055029; AAH55029.1; -; mRNA. DR RefSeq; NP_038575.2; NM_013547.3. DR UniGene; Mm.157442; -. DR ProteinModelPortal; O09173; -. DR SMR; O09173; 2-440. DR IntAct; O09173; 5. DR MINT; MINT-1857911; -. DR STRING; 10090.ENSMUSP00000023519; -. DR PhosphoSite; O09173; -. DR PaxDb; O09173; -. DR PRIDE; O09173; -. DR Ensembl; ENSMUST00000160847; ENSMUSP00000125492; ENSMUSG00000022821. DR GeneID; 15233; -. DR KEGG; mmu:15233; -. DR UCSC; uc007zeg.2; mouse. DR CTD; 3081; -. DR MGI; MGI:96078; Hgd. DR eggNOG; COG3508; -. DR GeneTree; ENSGT00390000004601; -. DR HOGENOM; HOG000139824; -. DR HOVERGEN; HBG005965; -. DR InParanoid; Q7TPP2; -. DR KO; K00451; -. DR OMA; CWEPLKS; -. DR OrthoDB; EOG7PP58Z; -. DR TreeFam; TF300490; -. DR SABIO-RK; O09173; -. DR UniPathway; UPA00139; UER00339. DR NextBio; 287827; -. DR PRO; PR:O09173; -. DR Bgee; O09173; -. DR CleanEx; MM_HGD; -. DR Genevestigator; O09173; -. DR GO; GO:0004411; F:homogentisate 1,2-dioxygenase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006520; P:cellular amino acid metabolic process; IMP:MGI. DR GO; GO:0006559; P:L-phenylalanine catabolic process; IEA:UniProtKB-UniPathway. DR GO; GO:0006572; P:tyrosine catabolic process; IEA:UniProtKB-KW. DR Gene3D; 2.60.120.10; -; 2. DR InterPro; IPR005708; Homogentis_dOase. DR InterPro; IPR014710; RmlC-like_jellyroll. DR InterPro; IPR011051; RmlC_Cupin. DR PANTHER; PTHR11056; PTHR11056; 1. DR Pfam; PF04209; HgmA; 1. DR SUPFAM; SSF51182; SSF51182; 1. DR TIGRFAMs; TIGR01015; hmgA; 1. PE 1: Evidence at protein level; KW Acetylation; Complete proteome; Dioxygenase; KW Direct protein sequencing; Iron; Metal-binding; Oxidoreductase; KW Phenylalanine catabolism; Reference proteome; Tyrosine catabolism. FT CHAIN 1 445 Homogentisate 1,2-dioxygenase. FT /FTId=PRO_0000220241. FT METAL 335 335 Iron (By similarity). FT METAL 341 341 Iron (By similarity). FT METAL 371 371 Iron (By similarity). FT MOD_RES 98 98 N6-acetyllysine (By similarity). FT MOD_RES 414 414 N6-succinyllysine. FT CONFLICT 267 267 A -> T (in Ref. 1; AAC53224). SQ SEQUENCE 445 AA; 49960 MW; 27DEB34D38DB1C25 CRC64; MAELKYISGF GNECASEDPR CPGSLPKGQN NPQVCPYNLY AEQLSGSAFT CPRNTNKRSW LYRILPSVSH KPFESIDQGH VTHNWDEVGP DPNQLRWKPF EIPKASEKKV DFVSGLYTLC GAGDIKSNNG LAVHIFLCNS SMENRCFYNS DGDFLIVPQK GKLLIYTEFG KMSLQPNEIC VIQRGMRFSV DVFEETRGYI LEVYGVHFEL PDLGPIGANG LANPRDFLIP VAWYEDRRVP GGYTVINKFQ GKLFACKQDV SPFNVVAWHG NYTPYKYNLE NFMVINAVAF DHADPSIFTV LTAKSLRPGV AIADFVIFPP RWGVADKTFR PPYYHRNCMS EFMGLIKGHY EAKQGGFLPG GGSLHSAMTP HGPDADCFEK ASKAKLEPER IADGTMAFMF ESSLSLAVTK WGLKTCSCLD ENYYKCWEPL RSHFTPNSRS PTEPK // ID HIF1N_MOUSE Reviewed; 349 AA. AC Q8BLR9; A1L3B7; Q3U3G4; DT 16-JUN-2003, integrated into UniProtKB/Swiss-Prot. DT 07-MAR-2006, sequence version 2. DT 19-MAR-2014, entry version 93. DE RecName: Full=Hypoxia-inducible factor 1-alpha inhibitor; DE EC=1.14.11.30; DE EC=1.14.11.n4; DE AltName: Full=Hypoxia-inducible factor asparagine hydroxylase; GN Name=Hif1an; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC STRAIN=C57BL/6J, and NOD; TISSUE=Brain cortex; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP FUNCTION, AND INTERACTION WITH ASB4. RX PubMed=17636018; DOI=10.1128/MCB.00511-07; RA Ferguson J.E. III, Wu Y., Smith K., Charles P., Powers K., Wang H., RA Patterson C.; RT "ASB4 is a hydroxylation substrate of FIH and promotes vascular RT differentiation via an oxygen-dependent mechanism."; RL Mol. Cell. Biol. 27:6407-6419(2007). CC -!- FUNCTION: Hydroxylates HIF-1 alpha at 'Asp-799' in the C-terminal CC transactivation domain (CAD). Functions as an oxygen sensor and, CC under normoxic conditions, the hydroxylation prevents interaction CC of HIF-1 with transcriptional coactivators including Cbp/p300- CC interacting transactivator. Involved in transcriptional repression CC through interaction with HIF1A, VHL and histone deacetylases. CC Hydroxylates specific Asn residues within ankyrin repeat domains CC (ARD) of NFKB1, NFKBIA, NOTCH1, ASB4, PPP1R12A and several other CC ARD-containing proteins. Also hydroxylates Asp and His residues CC within ARDs of ANK1 and TNKS2, respectively. Negatively regulates CC NOTCH1 activity, accelerating myogenic differentiation (By CC similarity). Positively regulates ASB4 activity, promoting CC vascular differentiation. CC -!- CATALYTIC ACTIVITY: Hypoxia-inducible factor-L-asparagine + 2- CC oxoglutarate + O(2) = hypoxia-inducible factor-(3S)-3-hydroxy-L- CC asparagine + succinate + CO(2). CC -!- CATALYTIC ACTIVITY: Ankyrin-repeat-L-histidine + 2-oxoglutarate + CC O(2) = ankyrin-repeat-(3S)-3-hydroxy-L-histidine + succinate + CC CO(2). CC -!- COFACTOR: Fe(2+) ion (By similarity). CC -!- SUBUNIT: Homodimer; homodimerization is essential for catalytic CC activity. Interacts with VHL and HIF1A. Part of a complex with CC VHL, HIF1A and HDAC1 or HDAC2 or HDAC3. Interacts with NFKB1 and CC NFKBIA. Interacts with NOTCH1, NOTCH2 and NOTCH3 but not with CC NOTCH4. Interacts with ABPA3. Interacts with TNKS2. Interacts with CC PPP1R12A (By similarity). Interacts with UBE3A (By similarity). CC Interacts with ASB4. CC -!- SUBCELLULAR LOCATION: Nucleus (By similarity). Cytoplasm (By CC similarity). Cytoplasm, perinuclear region (By similarity). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q8BLR9-1; Sequence=Displayed; CC Name=2; CC IsoId=Q8BLR9-2; Sequence=VSP_017537, VSP_017538; CC Note=No experimental confirmation available; CC -!- SIMILARITY: Contains 1 JmjC domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK043636; BAC31602.1; -; mRNA. DR EMBL; AK154774; BAE32822.1; -; mRNA. DR EMBL; BC130013; AAI30014.1; -; mRNA. DR RefSeq; NP_795932.2; NM_176958.3. DR UniGene; Mm.145278; -. DR ProteinModelPortal; Q8BLR9; -. DR SMR; Q8BLR9; 10-349. DR BioGrid; 235386; 2. DR PhosphoSite; Q8BLR9; -. DR PaxDb; Q8BLR9; -. DR PRIDE; Q8BLR9; -. DR Ensembl; ENSMUST00000040455; ENSMUSP00000035326; ENSMUSG00000036450. [Q8BLR9-1] DR GeneID; 319594; -. DR KEGG; mmu:319594; -. DR UCSC; uc008hpx.1; mouse. [Q8BLR9-2] DR UCSC; uc008hpy.1; mouse. [Q8BLR9-1] DR CTD; 55662; -. DR MGI; MGI:2442345; Hif1an. DR eggNOG; NOG71927; -. DR GeneTree; ENSGT00530000062914; -. DR HOGENOM; HOG000008146; -. DR HOVERGEN; HBG051903; -. DR InParanoid; Q8BLR9; -. DR KO; K00476; -. DR OMA; MIKGRYD; -. DR OrthoDB; EOG72NRQ4; -. DR TreeFam; TF329609; -. DR NextBio; 395052; -. DR PRO; PR:Q8BLR9; -. DR Bgee; Q8BLR9; -. DR Genevestigator; Q8BLR9; -. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0071532; F:ankyrin repeat binding; ISS:UniProtKB. DR GO; GO:0031406; F:carboxylic acid binding; IEA:Ensembl. DR GO; GO:0048037; F:cofactor binding; IEA:Ensembl. DR GO; GO:0005506; F:iron ion binding; IEA:Ensembl. DR GO; GO:0005112; F:Notch binding; ISS:UniProtKB. DR GO; GO:0036140; F:peptidyl-asparagine 3-dioxygenase activity; ISS:UniProtKB. DR GO; GO:0036139; F:peptidyl-histidine dioxygenase activity; ISS:UniProtKB. DR GO; GO:0008270; F:zinc ion binding; IEA:Ensembl. DR GO; GO:0045746; P:negative regulation of Notch signaling pathway; ISS:UniProtKB. DR GO; GO:0061428; P:negative regulation of transcription from RNA polymerase II promoter in response to hypoxia; ISS:UniProtKB. DR GO; GO:0042265; P:peptidyl-asparagine hydroxylation; ISS:UniProtKB. DR GO; GO:0042264; P:peptidyl-aspartic acid hydroxylation; ISS:UniProtKB. DR GO; GO:0036138; P:peptidyl-histidine hydroxylation; ISS:UniProtKB. DR GO; GO:0045663; P:positive regulation of myoblast differentiation; ISS:UniProtKB. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.287.1010; -; 1. DR InterPro; IPR027452; FIH-1_domII. DR InterPro; IPR003347; JmjC_dom. DR SMART; SM00558; JmjC; 1. DR PROSITE; PS51184; JMJC; 1. PE 1: Evidence at protein level; KW Acetylation; Alternative splicing; Complete proteome; Cytoplasm; KW Dioxygenase; Iron; Metal-binding; Nucleus; Oxidoreductase; KW Reference proteome; Transcription; Transcription regulation; Zinc. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 349 Hypoxia-inducible factor 1-alpha FT inhibitor. FT /FTId=PRO_0000083975. FT DOMAIN 142 307 JmjC. FT REGION 2 125 Interaction with VHL (By similarity). FT REGION 181 183 Substrate binding (By similarity). FT REGION 201 203 Substrate binding (By similarity). FT REGION 238 239 Substrate binding (By similarity). FT METAL 199 199 Iron; via tele nitrogen; catalytic (By FT similarity). FT METAL 199 199 Zinc; via tele nitrogen (By similarity). FT METAL 201 201 Iron; via tele nitrogen; catalytic (By FT similarity). FT METAL 201 201 Zinc; via tele nitrogen (By similarity). FT METAL 279 279 Iron; via tele nitrogen; catalytic (By FT similarity). FT METAL 279 279 Zinc; via tele nitrogen (By similarity). FT BINDING 145 145 2-oxoglutarate (By similarity). FT BINDING 152 152 Substrate (By similarity). FT BINDING 196 196 2-oxoglutarate (By similarity). FT BINDING 205 205 2-oxoglutarate (By similarity). FT BINDING 214 214 2-oxoglutarate (By similarity). FT BINDING 294 294 2-oxoglutarate (By similarity). FT BINDING 300 300 Substrate; via amide nitrogen (By FT similarity). FT BINDING 321 321 Substrate (By similarity). FT SITE 340 340 Important for dimer formation (By FT similarity). FT MOD_RES 2 2 N-acetylalanine (By similarity). FT VAR_SEQ 241 263 QVDFDNPDYERFPNFRNVVGYET -> GVKRRDQAKRETIA FT KEKYTKQNK (in isoform 2). FT /FTId=VSP_017537. FT VAR_SEQ 264 349 Missing (in isoform 2). FT /FTId=VSP_017538. FT CONFLICT 177 177 R -> L (in Ref. 2; AAI30014). SQ SEQUENCE 349 AA; 40241 MW; ED5C2B875EBCE76E CRC64; MAATAAEVAA SGSGEAREEA EAPGPAWDES QLRSYSFPTR PIPRLSQSDP RAEELIENEE PVVLTDTNLV YPALKWDLEY LQENIGNGDF SVYSASTHKF LYYDEKKMGN FQNFKPRSNR EEIKFHEFVE KLQAIQQRGG EERLYLQQTL NDTVGRKIVM DFLGFNWNWI NKQQGKRGWG QLTSNLLLIG MEGNVTPAHY DEQQNFFAQI KGHKRCILFP PDQFECLYPY PVHHPCDRQS QVDFDNPDYE RFPNFRNVVG YETVVGPGDV LYIPMYWWHH IESLLNGGIT ITVNFWYKGA PTPKRIEYPL KAHQKVAIMR NIEKMLGEAL GNPQEVGPLL NTMIKGRYN // ID HMDH_MOUSE Reviewed; 887 AA. AC Q01237; G3X8U5; Q5U4I2; DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot. DT 03-OCT-2012, sequence version 3. DT 19-MAR-2014, entry version 126. DE RecName: Full=3-hydroxy-3-methylglutaryl-coenzyme A reductase; DE Short=HMG-CoA reductase; DE EC=1.1.1.34; GN Name=Hmgcr; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Mammary tumor; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] OF 664-887. RX PubMed=2258621; RA Helmberg A., Faessler R., Geley S., Joehrer K., Kroemer G., Boeck G., RA Kofler R.; RT "Glucocorticoid-regulated gene expression in the immune system. RT Analysis of glucocorticoid-regulated transcripts from the mouse RT macrophage-like cell line P388D1."; RL J. Immunol. 145:4332-4337(1990). CC -!- FUNCTION: Transmembrane glycoprotein that is the rate-limiting CC enzyme in cholesterol biosynthesis as well as in the biosynthesis CC of nonsterol isoprenoids that are essential for normal cell CC function including ubiquinone and geranylgeranyl proteins. CC -!- CATALYTIC ACTIVITY: (R)-mevalonate + CoA + 2 NADP(+) = (S)-3- CC hydroxy-3-methylglutaryl-CoA + 2 NADPH. CC -!- ENZYME REGULATION: Regulated by a negative feedback mechanism CC through sterols and non-sterol metabolites derived from CC mevalonate. CC -!- PATHWAY: Metabolic intermediate biosynthesis; (R)-mevalonate CC biosynthesis; (R)-mevalonate from acetyl-CoA: step 3/3. CC -!- SUBUNIT: Homodimer. Interacts with INSIG1 (via its SSD); the CC interaction, accelerated by sterols, leads to the recruitment of CC HMGCR to AMFR/gp78 for its ubiquitination by the sterol-mediated CC ERAD pathway. Interacts with UBIAD1 (By similarity). CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass CC membrane protein (By similarity). CC -!- PTM: N-glycosylated (By similarity). Deglycosylated by NGLY1 on CC release from the endoplasmic reticulum (ER) in a sterol-mediated CC manner (By similarity). CC -!- PTM: Undergoes sterol-mediated ubiquitination and ER-association CC degradation (ERAD). Accumulation of sterols in the endoplasmic CC reticulum (ER) membrane, triggers binding of the reductase to the CC ER membrane protein INSIG1. This INSIG binding leads to the CC recruitment of the ubiquitin ligase, AMFR/gp78, initiating CC ubiquitination of the reductase. The ubiquitinated reductase is CC then extracted from the ER membrane and delivered to cytosolic 26S CC proteosomes by a mechanism probably mediated by the ATPase CC Valosin-containing protein VCP/p97. Lys-248 is the main site of CC ubiquitination. Ubiquitination is enhanced by the presence of a CC geranylgeranylated protein (By similarity). CC -!- SIMILARITY: Belongs to the HMG-CoA reductase family. CC -!- SIMILARITY: Contains 1 SSD (sterol-sensing) domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AC154851; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH466567; EDL00884.1; -; Genomic_DNA. DR EMBL; BC085083; AAH85083.1; -; mRNA. DR EMBL; M62766; AAA37819.1; -; mRNA. DR PIR; A43533; A43533. DR RefSeq; NP_032281.2; NM_008255.2. DR RefSeq; XP_006517594.1; XM_006517531.1. DR RefSeq; XP_006517595.1; XM_006517532.1. DR UniGene; Mm.316652; -. DR ProteinModelPortal; Q01237; -. DR SMR; Q01237; 440-862. DR ChEMBL; CHEMBL2764; -. DR GuidetoPHARMACOLOGY; 639; -. DR PhosphoSite; Q01237; -. DR PaxDb; Q01237; -. DR PRIDE; Q01237; -. DR Ensembl; ENSMUST00000022176; ENSMUSP00000022176; ENSMUSG00000021670. DR GeneID; 15357; -. DR KEGG; mmu:15357; -. DR UCSC; uc007rnm.3; mouse. DR CTD; 3156; -. DR MGI; MGI:96159; Hmgcr. DR eggNOG; COG1257; -. DR GeneTree; ENSGT00390000006426; -. DR HOGENOM; HOG000183489; -. DR HOVERGEN; HBG000453; -. DR InParanoid; Q01237; -. DR KO; K00021; -. DR OMA; PNEECLQ; -. DR OrthoDB; EOG7GXP9T; -. DR TreeFam; TF105362; -. DR SABIO-RK; Q01237; -. DR UniPathway; UPA00058; UER00103. DR ChiTaRS; Hmgcr; mouse. DR NextBio; 287972; -. DR PRO; PR:Q01237; -. DR ArrayExpress; Q01237; -. DR CleanEx; MM_HMGCR; -. DR Genevestigator; Q01237; -. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005778; C:peroxisomal membrane; IEA:Ensembl. DR GO; GO:0004420; F:hydroxymethylglutaryl-CoA reductase (NADPH) activity; IDA:MGI. DR GO; GO:0042282; F:hydroxymethylglutaryl-CoA reductase activity; IEA:Ensembl. DR GO; GO:0070402; F:NADPH binding; IEA:Ensembl. DR GO; GO:0007568; P:aging; IEA:Ensembl. DR GO; GO:0006695; P:cholesterol biosynthetic process; IDA:MGI. DR GO; GO:0015936; P:coenzyme A metabolic process; IEA:InterPro. DR GO; GO:0009790; P:embryo development; IMP:MGI. DR GO; GO:0008299; P:isoprenoid biosynthetic process; IEA:Ensembl. DR GO; GO:0045445; P:myoblast differentiation; IEA:Ensembl. DR GO; GO:0061179; P:negative regulation of insulin secretion involved in cellular response to glucose stimulus; IEA:Ensembl. DR GO; GO:0043407; P:negative regulation of MAP kinase activity; IGI:MGI. DR GO; GO:0010664; P:negative regulation of striated muscle cell apoptotic process; IEA:Ensembl. DR GO; GO:0045908; P:negative regulation of vasodilation; IEA:Ensembl. DR GO; GO:0061045; P:negative regulation of wound healing; IEA:Ensembl. DR GO; GO:0010666; P:positive regulation of cardiac muscle cell apoptotic process; IEA:Ensembl. DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IEA:Ensembl. DR GO; GO:0048643; P:positive regulation of skeletal muscle tissue development; IEA:Ensembl. DR GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; IEA:Ensembl. DR GO; GO:0032874; P:positive regulation of stress-activated MAPK cascade; IEA:Ensembl. DR GO; GO:0051262; P:protein tetramerization; IEA:Ensembl. DR GO; GO:0045471; P:response to ethanol; IEA:Ensembl. DR GO; GO:0007584; P:response to nutrient; IEA:Ensembl. DR GO; GO:0006743; P:ubiquinone metabolic process; IEA:Ensembl. DR GO; GO:0008542; P:visual learning; IGI:MGI. DR Gene3D; 1.10.3270.10; -; 1. DR Gene3D; 3.30.70.420; -; 1. DR Gene3D; 3.90.770.10; -; 2. DR InterPro; IPR002202; HMG_CoA_Rdtase. DR InterPro; IPR023074; HMG_CoA_Rdtase_cat. DR InterPro; IPR023076; HMG_CoA_Rdtase_CS. DR InterPro; IPR004554; HMG_CoA_Rdtase_eu_arc. DR InterPro; IPR004816; HMG_CoA_Rdtase_metazoan. DR InterPro; IPR023282; HMG_CoA_Rdtase_N. DR InterPro; IPR009023; HMG_CoA_Rdtase_NAD(P)-bd. DR InterPro; IPR009029; HMG_CoA_Rdtase_sub-bd. DR InterPro; IPR000731; SSD. DR PANTHER; PTHR10572; PTHR10572; 1. DR Pfam; PF00368; HMG-CoA_red; 1. DR PRINTS; PR00071; HMGCOARDTASE. DR SUPFAM; SSF55035; SSF55035; 1. DR SUPFAM; SSF56542; SSF56542; 2. DR TIGRFAMs; TIGR00920; 2A060605; 1. DR TIGRFAMs; TIGR00533; HMG_CoA_R_NADP; 1. DR PROSITE; PS00066; HMG_COA_REDUCTASE_1; 1. DR PROSITE; PS00318; HMG_COA_REDUCTASE_2; 1. DR PROSITE; PS01192; HMG_COA_REDUCTASE_3; 1. DR PROSITE; PS50065; HMG_COA_REDUCTASE_4; 1. DR PROSITE; PS50156; SSD; 1. PE 2: Evidence at transcript level; KW Cholesterol biosynthesis; Cholesterol metabolism; Complete proteome; KW Endoplasmic reticulum; Glycoprotein; Isopeptide bond; KW Lipid biosynthesis; Lipid metabolism; Membrane; NADP; Oxidoreductase; KW Phosphoprotein; Reference proteome; Steroid biosynthesis; KW Steroid metabolism; Sterol biosynthesis; Sterol metabolism; KW Transmembrane; Transmembrane helix; Ubl conjugation. FT CHAIN 1 887 3-hydroxy-3-methylglutaryl-coenzyme A FT reductase. FT /FTId=PRO_0000114421. FT TRANSMEM 10 39 Helical; (Potential). FT TRANSMEM 57 78 Helical; (Potential). FT TRANSMEM 90 114 Helical; (Potential). FT TRANSMEM 124 149 Helical; (Potential). FT TRANSMEM 160 187 Helical; (Potential). FT TRANSMEM 192 220 Helical; (Potential). FT TRANSMEM 315 339 Helical; (Potential). FT DOMAIN 61 218 SSD. FT REGION 340 449 Linker. FT REGION 450 887 Catalytic. FT MOTIF 75 78 INSIG-binding motif (By similarity). FT COMPBIAS 243 246 Poly-Glu. FT ACT_SITE 558 558 Charge relay system (By similarity). FT ACT_SITE 690 690 Charge relay system (By similarity). FT ACT_SITE 766 766 Charge relay system (By similarity). FT ACT_SITE 865 865 Proton donor (By similarity). FT MOD_RES 871 871 Phosphoserine; by AMPK (By similarity). FT CARBOHYD 281 281 N-linked (GlcNAc...) (Potential). FT CARBOHYD 517 517 N-linked (GlcNAc...) (Potential). FT CARBOHYD 869 869 N-linked (GlcNAc...) (Potential). FT CROSSLNK 89 89 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in ubiquitin) (By FT similarity). FT CROSSLNK 248 248 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in ubiquitin) (By FT similarity). FT CONFLICT 258 258 M -> I (in Ref. 3; AAH85083). SQ SEQUENCE 887 AA; 97040 MW; DD77B40CE66ABF92 CRC64; MLSRLFRMHG LFVASHPWEV IVGTVTLTIC MMSMNMFTGN NKICGWNYEC PKFEEDVLSS DIIILTITRC IAILYIYFQF QNLRQLGSKY ILGIAGLFTI FSSFVFSTVV IHFLDKELTG LNEALPFFLL LIDLSRASAL AKFALSSNSQ DEVRENIARG MAILGPTFTL DALVECLVIG VGTMSGVRQL EIMCCFGCMS VLANYFVFMT FFPACVSLVL ELSRESREGR PIWQLSHFAR VLEEEENKPN PVTQRVKMIM SLGLVLVHAH SRWIADPSPQ NSTAEQAKVS LGLDEDVSKR IEPSVSLWQF YLSKMISMDI EQVITLSLAF LLAVKYIFFE QAETESTLSL KNPITSPVVT SKKAQDNCCR REPLLVRRNQ KLSSVEEDPG ANQERKVEVI KPLVVEAETT SRATFVLGAS VASPPSALGT QEPGIELPIE PRPNEECLQI LENAEKGAKF LSDAEIIQLV NAKHIPAYKL ETLMETHERG VSIRRQLLST KLAEPSSLQY LPYRDYNYSL VMGACCENVI GYMPIPVGVA GPLCLDGKEY QVPMATTEGC LVASTNRGCR AISLGGGASS RVLADGMTRG PVVRLPRACD SAEVKTWLET PEGFAVIKEA FDSTSRFARL QKLHVTMAGR NLYIRFQSRT GDAMGMNMIS KGTEKALLKL QEFFPDMQIL AVSGNYCTDK KPAAINWIEG RGKTVVCEAV IPAKVVREVL KTTTEAMVDV NINKNLVGSA MAGSIGGYNA HAANIVTAIY IACGQDAAQN VGSSNCITLM EASGPTNEDL YISCTMPSIE IGTVGGGTNL LPQQACLQML GVQGACKDNP GENARQLARI VCGTVMAGEL SLMAALAAGH LVRSHMVHNR SKINLQDLQG TCTKKAA // ID HMOX2_MOUSE Reviewed; 315 AA. AC O70252; O70626; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1998, sequence version 1. DT 19-FEB-2014, entry version 108. DE RecName: Full=Heme oxygenase 2; DE Short=HO-2; DE EC=1.14.99.3; GN Name=Hmox2; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=CD-1; RA Mount D.B.; RT "Sequence of mouse heme oxygenase-2."; RL Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=9795203; DOI=10.1016/S0378-1119(98)00477-6; RA Gibbs L., Willis D., Morgan M.J.; RT "The identification and expression of heme oxygenase-2 alternative RT transcripts in the mouse."; RL Gene 221:171-177(1998). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Mammary gland; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: Heme oxygenase cleaves the heme ring at the alpha CC methene bridge to form biliverdin. Biliverdin is subsequently CC converted to bilirubin by biliverdin reductase. Under CC physiological conditions, the activity of heme oxygenase is CC highest in the spleen, where senescent erythrocytes are CC sequestrated and destroyed. Heme oxygenase 2 could be implicated CC in the production of carbon monoxide in brain where it could act CC as a neurotransmitter. CC -!- CATALYTIC ACTIVITY: Protoheme + 3 AH(2) + 3 O(2) = biliverdin + CC Fe(2+) + CO + 3 A + 3 H(2)O. CC -!- SUBCELLULAR LOCATION: Microsome. Endoplasmic reticulum. CC -!- SIMILARITY: Belongs to the heme oxygenase family. CC -!- SIMILARITY: Contains 2 HRM (heme regulatory motif) repeats. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF029874; AAC17981.1; -; mRNA. DR EMBL; AF054670; AAC82364.1; -; mRNA. DR EMBL; AF054669; AAC82363.1; -; mRNA. DR EMBL; BC002011; AAH02011.1; -; mRNA. DR PIR; JC5149; JC5149. DR RefSeq; NP_001129538.1; NM_001136066.2. DR RefSeq; NP_034573.2; NM_010443.2. DR UniGene; Mm.272866; -. DR ProteinModelPortal; O70252; -. DR SMR; O70252; 29-247. DR IntAct; O70252; 3. DR MINT; MINT-1847819; -. DR PhosphoSite; O70252; -. DR PaxDb; O70252; -. DR PRIDE; O70252; -. DR Ensembl; ENSMUST00000004172; ENSMUSP00000004172; ENSMUSG00000004070. DR Ensembl; ENSMUST00000118885; ENSMUSP00000113110; ENSMUSG00000004070. DR Ensembl; ENSMUST00000120232; ENSMUSP00000112397; ENSMUSG00000004070. DR GeneID; 15369; -. DR KEGG; mmu:15369; -. DR UCSC; uc007yag.2; mouse. DR CTD; 3163; -. DR MGI; MGI:109373; Hmox2. DR eggNOG; COG5398; -. DR HOGENOM; HOG000233221; -. DR HOVERGEN; HBG005982; -. DR InParanoid; O70252; -. DR KO; K00510; -. DR OMA; KKSHTMA; -. DR TreeFam; TF314786; -. DR NextBio; 288002; -. DR PRO; PR:O70252; -. DR ArrayExpress; O70252; -. DR Bgee; O70252; -. DR CleanEx; MM_HMOX2; -. DR Genevestigator; O70252; -. DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl. DR GO; GO:0004392; F:heme oxygenase (decyclizing) activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006788; P:heme oxidation; IEA:InterPro. DR GO; GO:0001666; P:response to hypoxia; IEA:Ensembl. DR GO; GO:0006979; P:response to oxidative stress; IEA:Ensembl. DR Gene3D; 1.20.910.10; -; 1. DR InterPro; IPR002051; Haem_Oase. DR InterPro; IPR016053; Haem_Oase-like. DR InterPro; IPR016084; Haem_Oase-like_multi-hlx. DR InterPro; IPR018207; Haem_oxygenase_CS. DR PANTHER; PTHR10720; PTHR10720; 1. DR Pfam; PF01126; Heme_oxygenase; 1. DR PIRSF; PIRSF000343; Haem_Oase; 1. DR PRINTS; PR00088; HAEMOXYGNASE. DR SUPFAM; SSF48613; SSF48613; 1. DR PROSITE; PS00593; HEME_OXYGENASE; 1. PE 2: Evidence at transcript level; KW Acetylation; Complete proteome; Endoplasmic reticulum; Heme; Iron; KW Metal-binding; Microsome; Oxidoreductase; Reference proteome; Repeat. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 315 Heme oxygenase 2. FT /FTId=PRO_0000209692. FT REPEAT 263 268 HRM 1. FT REPEAT 280 285 HRM 2. FT METAL 44 44 Iron (heme axial ligand) (By similarity). FT MOD_RES 2 2 N-acetylserine (By similarity). FT CONFLICT 172 174 RAL -> SSS (in Ref. 2; AAC82364/ FT AAC82363). SQ SEQUENCE 315 AA; 35739 MW; EA382EB2C7CED6D1 CRC64; MSSEVETSEG VDESEKNSMA PEKENHTKMA DLSELLKEGT KEAHDRAENT QFVKDFLKGN IKKELFKLAT TALYFTYSAL EEEMDRNKDH PAFAPLYFPT ELHRKAALIK DMKYFFGENW EEQVKCSEAA QKYVDRIHYV GQNEPELLVA HAYTRYMGDL SGGQVLKKVA QRALKLPSTG EGTQFYLFEH VDNAQQFKQF YRARMNALDL NLKTKERIVE EANKAFEYNM QIFSELDQAG SMLARETLED GLPVHDGKGD IRKCPFYAAQ PDKGTLGGSN CPFQTTVAVL RKPSLQLILA ASVALVAGLL AWYYM // ID HMOX1_MOUSE Reviewed; 289 AA. AC P14901; DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1990, sequence version 1. DT 19-FEB-2014, entry version 117. DE RecName: Full=Heme oxygenase 1; DE Short=HO-1; DE EC=1.14.99.3; DE AltName: Full=P32 protein; GN Name=Hmox1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=BALB/c; TISSUE=Fibroblast; RX PubMed=3409220; RA Kageyama H., Hiwasa T., Tokunaga K., Sakiyama S.; RT "Isolation and characterization of a complementary DNA clone for a Mr RT 32,000 protein which is induced with tumor promoters in BALB/c 3T3 RT cells."; RL Cancer Res. 48:4795-4798(1988). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=8288554; RA Alam J., Cai J., Smith A.; RT "Isolation and characterization of the mouse heme oxygenase-1 gene. RT Distal 5' sequences are required for induction by heme or heavy RT metals."; RL J. Biol. Chem. 269:1001-1009(1994). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Kidney; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP INDUCTION BY M.TUBERCULOSIS. RX PubMed=18474359; DOI=10.1016/j.chom.2008.03.007; RA Shiloh M.U., Manzanillo P., Cox J.S.; RT "Mycobacterium tuberculosis senses host-derived carbon monoxide during RT macrophage infection."; RL Cell Host Microbe 3:323-330(2008). RN [5] RP INDUCTION IN MACROPHAGES AND LUNGS BY M.TUBERCULOSIS. RC STRAIN=C3Heb/FeJ, and C57BL/6 X FVB; TISSUE=Lung, and Macrophage; RX PubMed=18400743; DOI=10.1074/jbc.M802274200; RA Kumar A., Deshane J.S., Crossman D.K., Bolisetty S., Yan B.S., RA Kramnik I., Agarwal A., Steyn A.J.; RT "Heme oxygenase-1-derived carbon monoxide induces the Mycobacterium RT tuberculosis dormancy regulon."; RL J. Biol. Chem. 283:18032-18039(2008). CC -!- FUNCTION: Heme oxygenase cleaves the heme ring at the alpha CC methene bridge to form biliverdin. Biliverdin is subsequently CC converted to bilirubin by biliverdin reductase. Under CC physiological conditions, the activity of heme oxygenase is CC highest in the spleen, where senescent erythrocytes are CC sequestrated and destroyed. Exhibits cytoprotective effects since CC excess of free heme sensitizes cells to undergo apoptosis. CC -!- CATALYTIC ACTIVITY: Protoheme + 3 AH(2) + 3 O(2) = biliverdin + CC Fe(2+) + CO + 3 A + 3 H(2)O. CC -!- SUBCELLULAR LOCATION: Microsome. Endoplasmic reticulum membrane CC (By similarity); Peripheral membrane protein; Cytoplasmic side. CC -!- INDUCTION: Heme oxygenase 1 activity is highly inducible by its CC substrate heme and by various non-heme substances such as heavy CC metals, bromobenzene, and endotoxin. It is also induced in CC macrophages, liver and the lungs upon infection with CC M.tuberculosis (at protein level). Data is conflicting as to CC whether macrophage induction is independent of the nitric oxide CC (NO) signaling pathway (PubMed:18400743), or dependent on NO CC (PubMed:18474359). CC -!- SIMILARITY: Belongs to the heme oxygenase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M33203; AAA39872.1; -; mRNA. DR EMBL; X13356; CAA31732.1; -; mRNA. DR EMBL; X56824; CAA40159.1; -; Genomic_DNA. DR EMBL; X56825; CAA40159.1; JOINED; Genomic_DNA. DR EMBL; X56826; CAA40159.1; JOINED; Genomic_DNA. DR EMBL; X56827; CAA40159.1; JOINED; Genomic_DNA. DR EMBL; BC010757; AAH10757.1; -; mRNA. DR PIR; I48409; I48409. DR RefSeq; NP_034572.1; NM_010442.2. DR UniGene; Mm.276389; -. DR ProteinModelPortal; P14901; -. DR SMR; P14901; 30-225. DR IntAct; P14901; 3. DR MINT; MINT-4097595; -. DR ChEMBL; CHEMBL4434; -. DR PhosphoSite; P14901; -. DR PaxDb; P14901; -. DR PRIDE; P14901; -. DR Ensembl; ENSMUST00000005548; ENSMUSP00000005548; ENSMUSG00000005413. DR GeneID; 15368; -. DR KEGG; mmu:15368; -. DR UCSC; uc009mhc.2; mouse. DR CTD; 3162; -. DR MGI; MGI:96163; Hmox1. DR eggNOG; COG5398; -. DR HOGENOM; HOG000233221; -. DR HOVERGEN; HBG005982; -. DR InParanoid; P14901; -. DR KO; K00510; -. DR OMA; YAPLYFP; -. DR OrthoDB; EOG7JQBNR; -. DR TreeFam; TF314786; -. DR NextBio; 287998; -. DR PRO; PR:P14901; -. DR ArrayExpress; P14901; -. DR Bgee; P14901; -. DR CleanEx; MM_HMOX1; -. DR Genevestigator; P14901; -. DR GO; GO:0005901; C:caveola; IEA:Ensembl. DR GO; GO:0005829; C:cytosol; IEA:Ensembl. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005730; C:nucleolus; IEA:Ensembl. DR GO; GO:0005634; C:nucleus; IDA:BHF-UCL. DR GO; GO:0020037; F:heme binding; IEA:Ensembl. DR GO; GO:0004392; F:heme oxygenase (decyclizing) activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004630; F:phospholipase D activity; IEA:Ensembl. DR GO; GO:0004871; F:signal transducer activity; IEA:Ensembl. DR GO; GO:0001525; P:angiogenesis; IEA:Ensembl. DR GO; GO:0071243; P:cellular response to arsenic-containing substance; IDA:MGI. DR GO; GO:0071276; P:cellular response to cadmium ion; IDA:MGI. DR GO; GO:0071456; P:cellular response to hypoxia; IEA:Ensembl. DR GO; GO:0031670; P:cellular response to nutrient; IEA:Ensembl. DR GO; GO:0034101; P:erythrocyte homeostasis; IEA:Ensembl. DR GO; GO:0042167; P:heme catabolic process; IEA:Ensembl. DR GO; GO:0042168; P:heme metabolic process; IDA:MGI. DR GO; GO:0006788; P:heme oxidation; IEA:InterPro. DR GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IEA:Ensembl. DR GO; GO:0055072; P:iron ion homeostasis; IEA:Ensembl. DR GO; GO:0043392; P:negative regulation of DNA binding; IEA:Ensembl. DR GO; GO:1902042; P:negative regulation of extrinsic apoptotic signaling pathway via death domain receptors; IEA:Ensembl. DR GO; GO:0032764; P:negative regulation of mast cell cytokine production; IEA:Ensembl. DR GO; GO:0043305; P:negative regulation of mast cell degranulation; IEA:Ensembl. DR GO; GO:0010656; P:negative regulation of muscle cell apoptotic process; IEA:Ensembl. DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IEA:Ensembl. DR GO; GO:0043433; P:negative regulation of sequence-specific DNA binding transcription factor activity; IEA:Ensembl. DR GO; GO:0048662; P:negative regulation of smooth muscle cell proliferation; IEA:Ensembl. DR GO; GO:0045766; P:positive regulation of angiogenesis; IEA:Ensembl. DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IEA:Ensembl. DR GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; IEA:Ensembl. DR GO; GO:0051260; P:protein homooligomerization; IEA:Ensembl. DR GO; GO:0008217; P:regulation of blood pressure; IEA:Ensembl. DR GO; GO:0043619; P:regulation of transcription from RNA polymerase II promoter in response to oxidative stress; IEA:Ensembl. DR GO; GO:0043627; P:response to estrogen; IEA:Ensembl. DR GO; GO:0042542; P:response to hydrogen peroxide; IEA:Ensembl. DR GO; GO:0035094; P:response to nicotine; IEA:Ensembl. DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:Ensembl. DR GO; GO:0002246; P:wound healing involved in inflammatory response; IEA:Ensembl. DR Gene3D; 1.20.910.10; -; 1. DR InterPro; IPR002051; Haem_Oase. DR InterPro; IPR016053; Haem_Oase-like. DR InterPro; IPR016084; Haem_Oase-like_multi-hlx. DR InterPro; IPR018207; Haem_oxygenase_CS. DR PANTHER; PTHR10720; PTHR10720; 1. DR Pfam; PF01126; Heme_oxygenase; 1. DR PIRSF; PIRSF000343; Haem_Oase; 1. DR PRINTS; PR00088; HAEMOXYGNASE. DR SUPFAM; SSF48613; SSF48613; 1. DR PROSITE; PS00593; HEME_OXYGENASE; 1. PE 1: Evidence at protein level; KW Apoptosis; Complete proteome; Endoplasmic reticulum; Heme; Iron; KW Membrane; Metal-binding; Microsome; Oxidoreductase; Phosphoprotein; KW Reference proteome. FT CHAIN 1 289 Heme oxygenase 1. FT /FTId=PRO_0000209688. FT METAL 25 25 Iron (heme axial ligand) (By similarity). FT BINDING 18 18 Heme (By similarity). FT BINDING 134 134 Heme (By similarity). FT BINDING 183 183 Heme (By similarity). FT MOD_RES 229 229 Phosphoserine (By similarity). SQ SEQUENCE 289 AA; 32929 MW; 19DB0DCCD574044B CRC64; MERPQPDSMP QDLSEALKEA TKEVHIQAEN AEFMKNFQKG QVSREGFKLV MASLYHIYTA LEEEIERNKQ NPVYAPLYFP EELHRRAALE QDMAFWYGPH WQEIIPCTPA TQHYVKRLHE VGRTHPELLV AHAYTRYLGD LSGGQVLKKI AQKAMALPSS GEGLAFFTFP NIDSPTKFKQ LYRARMNTLE MTPEVKHRVT EEAKTAFLLN IELFEELQVM LTEEHKDQSP SQMASLRQRP ASLVQDTAPA ETPRGKPQIS TSSSQTPLLQ WVLTLSFLLA TVAVGIYAM // ID HOT_MOUSE Reviewed; 465 AA. AC Q8R0N6; Q78SV3; Q8BYP0; DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 2. DT 19-MAR-2014, entry version 82. DE RecName: Full=Hydroxyacid-oxoacid transhydrogenase, mitochondrial; DE Short=HOT; DE EC=1.1.99.24; DE AltName: Full=Alcohol dehydrogenase iron-containing protein 1; DE Short=ADHFe1; DE Flags: Precursor; GN Name=Adhfe1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC STRAIN=C57BL/6J; TISSUE=Hypothalamus, and Liver; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC STRAIN=FVB/N; TISSUE=Kidney; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION. RX PubMed=17559793; DOI=10.1016/j.abb.2007.04.018; RA Kim J.Y., Tillison K.S., Zhou S., Lee J.H., Smas C.M.; RT "Differentiation-dependent expression of Adhfe1 in adipogenesis."; RL Arch. Biochem. Biophys. 464:100-111(2007). RN [4] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-443, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23576753; DOI=10.1073/pnas.1302961110; RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., RA Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.; RT "Label-free quantitative proteomics of the lysine acetylome in RT mitochondria identifies substrates of SIRT3 in metabolic pathways."; RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013). CC -!- FUNCTION: Catalyzes the cofactor-independent reversible oxidation CC of gamma-hydroxybutyrate (GHB) to succinic semialdehyde (SSA) CC coupled to reduction of 2-ketoglutarate (2-KG) to D-2- CC hydroxyglutarate (D-2-HG). L-3-hydroxybutyrate (L-3-OHB) is also a CC substrate for HOT when using 2-KG as hydrogen acceptor, resulting CC in the formation of D-2-HG (By similarity). CC -!- CATALYTIC ACTIVITY: (S)-3-hydroxybutanoate + 2-oxoglutarate = CC acetoacetate + (R)-2-hydroxyglutarate. CC -!- CATALYTIC ACTIVITY: 4-hydroxybutanoate + 2-oxoglutarate = succinic CC semialdehyde + (R)-2-hydroxyglutarate. CC -!- SUBCELLULAR LOCATION: Mitochondrion. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q8R0N6-1; Sequence=Displayed; CC Name=2; CC IsoId=Q8R0N6-2; Sequence=VSP_031987; CC -!- TISSUE SPECIFICITY: Expressed in white and brown adipose tissues, CC liver, and kidney. Expression is differentiation-dependent during CC in vitro brown and white adipogenesis. CC -!- INDUCTION: Down-regulated of 40% in white adipose tissue of ob/ob CC obese mice. CC -!- SIMILARITY: Belongs to the iron-containing alcohol dehydrogenase CC family. Hydroxyacid-oxoacid transhydrogenase subfamily. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK038853; BAC30151.1; -; mRNA. DR EMBL; AK050178; BAC34108.1; -; mRNA. DR EMBL; BC026584; AAH26584.2; -; mRNA. DR RefSeq; NP_780445.1; NM_175236.4. DR RefSeq; XP_006495649.1; XM_006495586.1. DR UniGene; Mm.28514; -. DR ProteinModelPortal; Q8R0N6; -. DR SMR; Q8R0N6; 55-458. DR IntAct; Q8R0N6; 2. DR MINT; MINT-4118408; -. DR PhosphoSite; Q8R0N6; -. DR PaxDb; Q8R0N6; -. DR PRIDE; Q8R0N6; -. DR Ensembl; ENSMUST00000144177; ENSMUSP00000116627; ENSMUSG00000025911. [Q8R0N6-1] DR GeneID; 76187; -. DR KEGG; mmu:76187; -. DR UCSC; uc007agl.2; mouse. [Q8R0N6-1] DR CTD; 137872; -. DR MGI; MGI:1923437; Adhfe1. DR eggNOG; COG1454; -. DR GeneTree; ENSGT00390000003849; -. DR HOGENOM; HOG000243335; -. DR HOVERGEN; HBG057032; -. DR InParanoid; Q8R0N6; -. DR KO; K11173; -. DR OMA; RAACQCP; -. DR OrthoDB; EOG77WWC7; -. DR TreeFam; TF105710; -. DR SABIO-RK; Q8R0N6; -. DR ChiTaRS; ADHFE1; mouse. DR NextBio; 344737; -. DR PRO; PR:Q8R0N6; -. DR ArrayExpress; Q8R0N6; -. DR Bgee; Q8R0N6; -. DR CleanEx; MM_ADHFE1; -. DR Genevestigator; Q8R0N6; -. DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB. DR GO; GO:0047988; F:hydroxyacid-oxoacid transhydrogenase activity; ISS:UniProtKB. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0015993; P:molecular hydrogen transport; ISS:UniProtKB. DR InterPro; IPR001670; ADH_Fe. DR Pfam; PF00465; Fe-ADH; 1. PE 1: Evidence at protein level; KW Acetylation; Alternative splicing; Complete proteome; Mitochondrion; KW Oxidoreductase; Reference proteome; Transit peptide. FT TRANSIT 1 ? Mitochondrion (Potential). FT CHAIN ? 465 Hydroxyacid-oxoacid transhydrogenase, FT mitochondrial. FT /FTId=PRO_0000322997. FT MOD_RES 443 443 N6-acetyllysine. FT VAR_SEQ 1 46 Missing (in isoform 2). FT /FTId=VSP_031987. SQ SEQUENCE 465 AA; 49937 MW; CD1463685F788C2A CRC64; MAAAARARVT HLLRHLQSTA CQCPTHSHTY SQAPGPSGKT ADYAFEMAVS NIRYGAGVTK EVGMDLQNMG AKNVCLMTDK NLSQLPPVQI VMDSLSKNGI SFQVYDDVRV EPTDGSFMDA IEFAKKGAFD AYVAVGGGST MDTCKAANLY ASSPHSEFLD YVNAPIGKGK PVTVPLKPLI AVPTTSGTGS ETTGVAIFDY EHLKVKTGIA SRAIKPTLGL VDPLHTLHMP CQVVANSGFD VLCHALESYT AIPYSMRSPC PSNPIQRPAY QGSNPISDIW AVHALQIVAK YLKRAVRNPD DLEARSKMHL ASAFAGIGFG NAGVHLCHGM SYPISGLVKT YKAKEYNVDH PLVPHGLSVV LTSPAVFTFT AQMFPERHLE TAGILGANIR TARIQDAGLV LADALRKFLF DLNVDDGLAA LGYSKDDIPS LVKGTLPQER VTKLAPRAQS EEDLSALFEA SMKLY // ID HPDL_MOUSE Reviewed; 371 AA. AC Q8K248; DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2002, sequence version 1. DT 19-MAR-2014, entry version 81. DE RecName: Full=4-hydroxyphenylpyruvate dioxygenase-like protein; DE EC=1.13.-.-; DE AltName: Full=Glyoxalase domain-containing protein 1; GN Name=Hpdl; Synonyms=Gloxd1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Brain cortex, and Cecum; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Mammary tumor; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: May have dioxygenase activity (Potential). CC -!- COFACTOR: Binds 1 iron ion per subunit (By similarity). CC -!- SIMILARITY: Belongs to the 4HPPD family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK043902; BAC31697.1; -; mRNA. DR EMBL; AK049217; BAC33615.1; -; mRNA. DR EMBL; AK078929; BAC37467.1; -; mRNA. DR EMBL; BC034099; AAH34099.1; -; mRNA. DR RefSeq; NP_666368.1; NM_146256.3. DR UniGene; Mm.279897; -. DR ProteinModelPortal; Q8K248; -. DR SMR; Q8K248; 4-367. DR PhosphoSite; Q8K248; -. DR PRIDE; Q8K248; -. DR Ensembl; ENSMUST00000055436; ENSMUSP00000062327; ENSMUSG00000043155. DR GeneID; 242642; -. DR KEGG; mmu:242642; -. DR UCSC; uc008uho.1; mouse. DR CTD; 84842; -. DR MGI; MGI:2444646; Hpdl. DR eggNOG; COG3185; -. DR GeneTree; ENSGT00530000063474; -. DR HOGENOM; HOG000231418; -. DR HOVERGEN; HBG059537; -. DR InParanoid; Q8K248; -. DR OMA; PGKERQI; -. DR OrthoDB; EOG7BS49H; -. DR TreeFam; TF300622; -. DR NextBio; 385462; -. DR PRO; PR:Q8K248; -. DR Bgee; Q8K248; -. DR CleanEx; MM_HPDL; -. DR Genevestigator; Q8K248; -. DR GO; GO:0003868; F:4-hydroxyphenylpyruvate dioxygenase activity; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0009072; P:aromatic amino acid family metabolic process; IEA:InterPro. DR InterPro; IPR005956; 4OHPhenylPyrv_dOase. DR PANTHER; PTHR11959; PTHR11959; 1. DR PIRSF; PIRSF009283; HPP_dOase; 1. PE 2: Evidence at transcript level; KW Complete proteome; Dioxygenase; Iron; Metal-binding; Oxidoreductase; KW Reference proteome. FT CHAIN 1 371 4-hydroxyphenylpyruvate dioxygenase-like FT protein. FT /FTId=PRO_0000271120. FT METAL 163 163 Iron (By similarity). FT METAL 258 258 Iron (By similarity). FT METAL 339 339 Iron (By similarity). SQ SEQUENCE 371 AA; 39909 MW; 88D5D47644EC8F4E CRC64; MTAPARRLCH IAFHVPAGQP LARDLHRVFG FQPLAVREAG GWRQLALRSG DAVFLVNEGT GPQEPLYSLD PHHSVPSATN LCFDVEDVDG AARALAARGC IMPVPPTRVR DAQGTATYTV LSSPAGNLSL TLLQRAGYRG SFLPGFRPLP CTPGPGWVSH VDHLTLACTS GSSPMLMRWF HDCLGFHHLP LSPGEDPEMG LKVAAGSGRG GLRLTALQTP PNNTVPTLVL AESLPGLNSK QDQVEQFLTR HGGPGLQHVG LYTPNIIDAS EGMAKAGCRL LTPPEAYYQQ PGKEEQILAA GHKPGLLERQ GILLDGDKDE FLLQVFTKSL FAEDTFFLEL IQRQGATGFG QNNIRALWQS VQEEAARAQG A // ID HPHL1_MOUSE Reviewed; 1159 AA. AC Q3V1H3; DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot. DT 02-SEP-2008, sequence version 2. DT 19-MAR-2014, entry version 72. DE RecName: Full=Hephaestin-like protein 1; DE EC=1.-.-.-; DE Flags: Precursor; GN Name=Hephl1; Synonyms=Gm509; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Skin; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). CC -!- FUNCTION: May function as a ferroxidase and may be involved in CC copper transport and homeostasis (By similarity). CC -!- COFACTOR: Binds 6 copper ions per monomer (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane CC protein (Potential). CC -!- SIMILARITY: Belongs to the multicopper oxidase family. CC -!- SIMILARITY: Contains 6 plastocyanin-like domains. CC -!- SEQUENCE CAUTION: CC Sequence=BAE21178.1; Type=Erroneous initiation; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK132457; BAE21178.1; ALT_INIT; mRNA. DR EMBL; AC154295; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC156500; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; NP_001158269.1; NM_001164797.1. DR UniGene; Mm.325134; -. DR ProteinModelPortal; Q3V1H3; -. DR SMR; Q3V1H3; 24-1067. DR STRING; 10090.ENSMUSP00000034412; -. DR PhosphoSite; Q3V1H3; -. DR PRIDE; Q3V1H3; -. DR Ensembl; ENSMUST00000159985; ENSMUSP00000124518; ENSMUSG00000031936. DR GeneID; 244698; -. DR KEGG; mmu:244698; -. DR UCSC; uc009ofj.2; mouse. DR CTD; 341208; -. DR MGI; MGI:2685355; Hephl1. DR eggNOG; NOG276067; -. DR GeneTree; ENSGT00550000074552; -. DR HOGENOM; HOG000231499; -. DR HOVERGEN; HBG003674; -. DR InParanoid; Q3V1H3; -. DR OMA; MHAVNGY; -. DR OrthoDB; EOG7V49XN; -. DR TreeFam; TF329807; -. DR NextBio; 386395; -. DR PRO; PR:Q3V1H3; -. DR Bgee; Q3V1H3; -. DR Genevestigator; Q3V1H3; -. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005507; F:copper ion binding; IEA:InterPro. DR GO; GO:0004322; F:ferroxidase activity; IEA:Ensembl. DR GO; GO:0006825; P:copper ion transport; IEA:UniProtKB-KW. DR GO; GO:0055114; P:oxidation-reduction process; ISO:MGI. DR Gene3D; 2.60.40.420; -; 6. DR InterPro; IPR011706; Cu-oxidase_2. DR InterPro; IPR011707; Cu-oxidase_3. DR InterPro; IPR002355; Cu_oxidase_Cu_BS. DR InterPro; IPR008972; Cupredoxin. DR Pfam; PF07731; Cu-oxidase_2; 2. DR Pfam; PF07732; Cu-oxidase_3; 3. DR SUPFAM; SSF49503; SSF49503; 6. DR PROSITE; PS00079; MULTICOPPER_OXIDASE1; 3. DR PROSITE; PS00080; MULTICOPPER_OXIDASE2; 1. PE 2: Evidence at transcript level; KW Complete proteome; Copper; Copper transport; Disulfide bond; KW Glycoprotein; Ion transport; Membrane; Metal-binding; Oxidoreductase; KW Reference proteome; Repeat; Signal; Transmembrane; KW Transmembrane helix; Transport. FT SIGNAL 1 23 Potential. FT CHAIN 24 1159 Hephaestin-like protein 1. FT /FTId=PRO_0000346772. FT TOPO_DOM 24 1114 Extracellular (Potential). FT TRANSMEM 1115 1135 Helical; (Potential). FT TOPO_DOM 1136 1159 Cytoplasmic (Potential). FT DOMAIN 24 206 Plastocyanin-like 1. FT DOMAIN 217 365 Plastocyanin-like 2. FT DOMAIN 378 560 Plastocyanin-like 3. FT DOMAIN 570 718 Plastocyanin-like 4. FT DOMAIN 730 906 Plastocyanin-like 5. FT DOMAIN 914 1092 Plastocyanin-like 6. FT COMPBIAS 1122 1127 Poly-Leu. FT METAL 126 126 Copper 1; type 2 (By similarity). FT METAL 128 128 Copper 2; type 3 (By similarity). FT METAL 186 186 Copper 2; type 3 (By similarity). FT METAL 188 188 Copper 3; type 3 (By similarity). FT METAL 303 303 Copper 4; type 1 (By similarity). FT METAL 346 346 Copper 4; type 1 (By similarity). FT METAL 351 351 Copper 4; type 1 (By similarity). FT METAL 656 656 Copper 5; type 1 (By similarity). FT METAL 699 699 Copper 5; type 1 (By similarity). FT METAL 704 704 Copper 5; type 1 (By similarity). FT METAL 709 709 Copper 5; type 1 (By similarity). FT METAL 1002 1002 Copper 6; type 1 (By similarity). FT METAL 1005 1005 Copper 1; type 2 (By similarity). FT METAL 1007 1007 Copper 3; type 3 (By similarity). FT METAL 1047 1047 Copper 3; type 3 (By similarity). FT METAL 1048 1048 Copper 6; type 1 (By similarity). FT METAL 1049 1049 Copper 2; type 3 (By similarity). FT METAL 1053 1053 Copper 6; type 1 (By similarity). FT METAL 1058 1058 Copper 6; type 1 (By similarity). FT CARBOHYD 160 160 N-linked (GlcNAc...) (Potential). FT CARBOHYD 235 235 N-linked (GlcNAc...) (Potential). FT CARBOHYD 406 406 N-linked (GlcNAc...) (Potential). FT CARBOHYD 588 588 N-linked (GlcNAc...) (Potential). FT CARBOHYD 771 771 N-linked (GlcNAc...) (Potential). FT CARBOHYD 934 934 N-linked (GlcNAc...) (Potential). FT DISULFID 180 206 Potential. FT DISULFID 284 365 Potential. FT DISULFID 534 560 Potential. FT DISULFID 637 718 Potential. FT DISULFID 880 906 Potential. SQ SEQUENCE 1159 AA; 130888 MW; 3EC317CFF861E96C CRC64; MFLKQPGGCI LLQFLGLLGL VGAVTRTYYI GIVEEYWNYV PQGKDVITGK SFSEDKLATL FLERGPNRIG GIYKKAVYRH FTDGSYSTEI PKPPWLGFLG PILRAEVGDV IVIHLMNFAS RPFSLHPHGV FYDKDSEGAL YPDGTSGRNK EDDMVPPGKN YTYVWPVREE YAPAPADANC LTWVYHSHID APKDICSGLI GPLLVCKEGV LNRYSGMRTD VDREFVIMFT LVDENQSWYL DDNIKQFCTN PNSVDKSDAV FQRSNKMHAL NGFLFGNMPE PEMCVGESVS WHLFGMGNEI DIHSIYFYGN TFITRGHRAD VVNLFPATFL TTEMIVENPG KWMITCQVSD HLQAGMLGQY SVGNCRGNAP HPKVQGQQRR YFIAAEKVLW DYGPQGYDKF TGFPLNTSGS DSAVYFTQAD NRIGGKYWKA RYTEYVDATF SRRKMPSDSE AHLGILGPVI KAEVGDILLV TFANKADKVY SILPHGVFYD KASDAAPNVD GFLKPGAHVK PGETFTYRWT VPESVSPTDE DPPCLTYLYF SAVQPIKDTS AGLVGPLLVC KKGTLNADGT QKGIDKEFYL LFTVFDENFS SYLDENIKKF TWHPFSVDKE DKEFVKSNRM HAVNGYMYGS QPGLSMCKKD RVSWHLIGMG TDTDMHGVYF QGNTIHLRGT HRDSLALFPH MATTAYMQPD HSGIFKVFCS TLPHFTRGMG QIYEISSCGN RDPSEPPYGM LRTFFIAAEE VEWDYAPNKN WEFEKQHLDA GGERHGDIFM NHTENWIGSQ YRKVVYREYT NGEFVEIKAR PPQEEHLQLL GPMIHAEVGD SILIIFKNKA SRPYSIAAQG VEDSNNGKLL NVPVTKPGEI KTYRWNVPKR SGPGPSDPNC IPWVYFSTAN FVKDTYSGLM GPLITCREGV LNEKGRRSDV DYEFALLFLV FNENESWYLD DNIKKYLNKD PRDFKHTDDF EESNKMHAIN GKIFGNLPGL IMTEDSMTNW YLLGIGSEVD IHTIHYHAES FLFKIDKSYR EDVYDLFPGT FQTIELFADH PGTWLLHCHV SDHIHAGMET TYTVLRNIDN RIPYSTKTPS GAGSHAVTVP SQEQPGKEEL YFFGKNLRPR GAKAALVILF ILGLLLLVAT VVLALRLRSS RRQMAYREVQ SCALPTDAL // ID HPPD_MOUSE Reviewed; 393 AA. AC P49429; P97322; Q3UEQ0; Q91WV9; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 19-MAR-2014, entry version 117. DE RecName: Full=4-hydroxyphenylpyruvate dioxygenase; DE EC=1.13.11.27; DE AltName: Full=4-hydroxyphenylpyruvic acid oxidase; DE Short=4HPPD; DE Short=HPD; DE Short=HPPDase; DE AltName: Full=F Alloantigen; DE Short=F protein; GN Name=Hpd; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=BALB/c; TISSUE=Liver; RX PubMed=7774914; DOI=10.1016/0888-7543(95)80122-3; RA Endo F., Awata H., Katoh H., Matsuda I.; RT "A nonsense mutation in the 4-hydroxyphenylpyruvic acid dioxygenase RT gene (Hpd) causes skipping of the constitutive exon and RT hypertyrosinemia in mouse strain III."; RL Genomics 25:164-169(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Liver; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Salivary gland; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-379, AND VARIANT ASN-104. RC STRAIN=CBA; TISSUE=Liver; RX PubMed=1709870; DOI=10.1002/eji.1830210521; RA Schofield J.P., Vijayakumar R.K., Oliveira D.B.G.; RT "Sequences of the mouse F protein alleles and identification of a T RT cell epitope."; RL Eur. J. Immunol. 21:1235-1240(1991). RN [5] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-211; SER-226 AND RP SER-250, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Liver; RX PubMed=17242355; DOI=10.1073/pnas.0609836104; RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; RT "Large-scale phosphorylation analysis of mouse liver."; RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). RN [6] RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-132, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., RA Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). CC -!- FUNCTION: Key enzyme in the degradation of tyrosine (By CC similarity). CC -!- CATALYTIC ACTIVITY: 4-hydroxyphenylpyruvate + O(2) = homogentisate CC + CO(2). CC -!- COFACTOR: Binds 1 iron ion per subunit (By similarity). CC -!- PATHWAY: Amino-acid degradation; L-phenylalanine degradation; CC acetoacetate and fumarate from L-phenylalanine: step 3/6. CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Membrane; CC Peripheral membrane protein (By similarity). CC -!- POLYMORPHISM: There are two alleles (F1 and F2), F2 has Asp-104 CC and F1 has Asn-104. Mice are completely tolerant to the self form CC of the protein, but make a good antibody response to immunization CC with the non-self form. CC -!- DISEASE: Note=Defects in Hpd are the cause of tyrosinemia type CC III. CC -!- SIMILARITY: Belongs to the 4HPPD family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; D29987; BAA06267.1; -; mRNA. DR EMBL; AK149416; BAE28861.1; -; mRNA. DR EMBL; BC013343; AAH13343.1; -; mRNA. DR EMBL; X59530; CAA42111.1; -; mRNA. DR PIR; A60236; A60236. DR RefSeq; NP_032303.1; NM_008277.2. DR UniGene; Mm.439709; -. DR ProteinModelPortal; P49429; -. DR SMR; P49429; 10-384. DR IntAct; P49429; 3. DR MINT; MINT-1869831; -. DR PhosphoSite; P49429; -. DR PaxDb; P49429; -. DR PRIDE; P49429; -. DR Ensembl; ENSMUST00000031398; ENSMUSP00000031398; ENSMUSG00000029445. DR GeneID; 15445; -. DR KEGG; mmu:15445; -. DR UCSC; uc008znj.1; mouse. DR CTD; 3242; -. DR MGI; MGI:96213; Hpd. DR eggNOG; COG3185; -. DR GeneTree; ENSGT00530000063474; -. DR HOGENOM; HOG000188687; -. DR HOVERGEN; HBG005987; -. DR InParanoid; P49429; -. DR KO; K00457; -. DR OMA; NAKQAAH; -. DR OrthoDB; EOG75F4D7; -. DR TreeFam; TF300622; -. DR SABIO-RK; P49429; -. DR UniPathway; UPA00139; UER00362. DR NextBio; 288240; -. DR PRO; PR:P49429; -. DR ArrayExpress; P49429; -. DR Bgee; P49429; -. DR CleanEx; MM_HPD; -. DR Genevestigator; P49429; -. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:Ensembl. DR GO; GO:0000139; C:Golgi membrane; IEA:Ensembl. DR GO; GO:0003868; F:4-hydroxyphenylpyruvate dioxygenase activity; ISS:UniProtKB. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006559; P:L-phenylalanine catabolic process; IEA:UniProtKB-UniPathway. DR GO; GO:0006572; P:tyrosine catabolic process; ISS:UniProtKB. DR InterPro; IPR005956; 4OHPhenylPyrv_dOase. DR InterPro; IPR004360; Glyas_Fos-R_dOase_dom. DR PANTHER; PTHR11959; PTHR11959; 1. DR Pfam; PF00903; Glyoxalase; 2. DR PIRSF; PIRSF009283; HPP_dOase; 1. DR TIGRFAMs; TIGR01263; 4HPPD; 1. PE 1: Evidence at protein level; KW Acetylation; Complete proteome; Cytoplasm; Dioxygenase; Iron; KW Membrane; Metal-binding; Oxidoreductase; Phenylalanine catabolism; KW Phosphoprotein; Polymorphism; Reference proteome; Tyrosine catabolism. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 393 4-hydroxyphenylpyruvate dioxygenase. FT /FTId=PRO_0000088389. FT METAL 183 183 Iron (By similarity). FT METAL 266 266 Iron (By similarity). FT METAL 349 349 Iron (By similarity). FT MOD_RES 2 2 N-acetylthreonine (By similarity). FT MOD_RES 132 132 N6-succinyllysine. FT MOD_RES 211 211 Phosphoserine. FT MOD_RES 226 226 Phosphoserine. FT MOD_RES 250 250 Phosphoserine. FT VARIANT 104 104 D -> N (in allele F1). FT CONFLICT 2 6 TTYNN -> VDYWD (in Ref. 4; CAA42111). FT CONFLICT 64 64 Q -> R (in Ref. 1; BAA06267). FT CONFLICT 120 121 EP -> DA (in Ref. 4; CAA42111). FT CONFLICT 206 206 F -> S (in Ref. 2; BAE28861). SQ SEQUENCE 393 AA; 45054 MW; 70B42A4E4744744A CRC64; MTTYNNKGPK PERGRFLHFH SVTFWVGNAK QAASFYCNKM GFEPLAYRGL ETGSREVVSH VIKQGKIVFV LCSALNPWNK EMGDHLVKHG DGVKDIAFEV EDCDHIVQKA RERGAKIVRE PWVEQDKFGK VKFAVLQTYG DTTHTLVEKI NYTGRFLPGF EAPTYKDTLL PKLPRCNLEI IDHIVGNQPD QEMQSASEWY LKNLQFHRFW SVDDTQVHTE YSSLRSIVVT NYEESIKMPI NEPAPGRKKS QIQEYVDYNG GAGVQHIALK TEDIITAIRH LRERGTEFLA APSSYYKLLR ENLKSAKIQV KESMDVLEEL HILVDYDEKG YLLQIFTKPM QDRPTLFLEV IQRHNHQGFG AGNFNSLFKA FEEEQALRGN LTDLEPNGVR SGM // ID HSDL2_MOUSE Reviewed; 490 AA. AC Q2TPA8; Q3ULY5; Q3UVZ3; Q8C3H3; Q99LV2; DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 24-JAN-2006, sequence version 1. DT 19-MAR-2014, entry version 68. DE RecName: Full=Hydroxysteroid dehydrogenase-like protein 2; DE EC=1.-.-.-; GN Name=Hsdl2; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INDUCTION. RC STRAIN=C57BL/6; RX PubMed=16240713; RA Dai J., Li P., Ji C., Feng C., Gui M., Sun Y., Zhang J., Zhu J., RA Dou C., Gu S.; RT "Cloning and characterization of a novel mouse short-chain RT dehydrogenase/reductases cDNA mHsdl2, encoding a protein with a SDR RT domain and a SCP2 domain."; RL Mol. Biol. (Mosk.) 39:799-805(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Diencephalon, Heart, and Mammary gland; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Mammary tumor; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-390, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., RA Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). RN [6] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-116, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23576753; DOI=10.1073/pnas.1302961110; RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., RA Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.; RT "Label-free quantitative proteomics of the lysine acetylome in RT mitochondria identifies substrates of SIRT3 in metabolic pathways."; RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013). CC -!- FUNCTION: Has apparently no steroid dehydrogenase activity (By CC similarity). CC -!- SUBCELLULAR LOCATION: Peroxisome (By similarity). CC -!- TISSUE SPECIFICITY: Widely expressed. CC -!- INDUCTION: Up-regulated by cholesterol-rich food. CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases CC (SDR) family. CC -!- SIMILARITY: Contains 1 SCP2 domain. CC -!- SEQUENCE CAUTION: CC Sequence=BAC39563.1; Type=Frameshift; Positions=336; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AY725196; AAU11505.1; -; mRNA. DR EMBL; AK085899; BAC39563.1; ALT_FRAME; mRNA. DR EMBL; AK136773; BAE23126.1; -; mRNA. DR EMBL; AK145230; BAE26313.1; -; mRNA. DR EMBL; AL806512; CAM21909.1; -; Genomic_DNA. DR EMBL; BX005031; CAM21909.1; JOINED; Genomic_DNA. DR EMBL; BX005031; CAM26657.1; -; Genomic_DNA. DR EMBL; AL806512; CAM26657.1; JOINED; Genomic_DNA. DR EMBL; BC002211; AAH02211.1; -; mRNA. DR RefSeq; NP_077217.2; NM_024255.3. DR UniGene; Mm.272905; -. DR ProteinModelPortal; Q2TPA8; -. DR SMR; Q2TPA8; 1-276, 383-483. DR IntAct; Q2TPA8; 2. DR MINT; MINT-1860458; -. DR PhosphoSite; Q2TPA8; -. DR REPRODUCTION-2DPAGE; Q2TPA8; -. DR PaxDb; Q2TPA8; -. DR PRIDE; Q2TPA8; -. DR DNASU; 72479; -. DR Ensembl; ENSMUST00000030078; ENSMUSP00000030078; ENSMUSG00000028383. DR GeneID; 72479; -. DR KEGG; mmu:72479; -. DR UCSC; uc008szy.2; mouse. DR CTD; 84263; -. DR MGI; MGI:1919729; Hsdl2. DR eggNOG; COG1028; -. DR GeneTree; ENSGT00730000111071; -. DR HOVERGEN; HBG107982; -. DR InParanoid; Q2TPA8; -. DR OMA; WFKNHTA; -. DR OrthoDB; EOG77T155; -. DR TreeFam; TF101523; -. DR NextBio; 336312; -. DR PRO; PR:Q2TPA8; -. DR ArrayExpress; Q2TPA8; -. DR Bgee; Q2TPA8; -. DR CleanEx; MM_HSDL2; -. DR Genevestigator; Q2TPA8; -. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell. DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW. DR GO; GO:0032934; F:sterol binding; IEA:InterPro. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR002198; DH_sc/Rdtase_SDR. DR InterPro; IPR002347; Glc/ribitol_DH. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR003033; SCP2_sterol-bd_dom. DR Pfam; PF00106; adh_short; 1. DR Pfam; PF02036; SCP2; 1. DR PRINTS; PR00081; GDHRDH. DR SUPFAM; SSF55718; SSF55718; 1. PE 1: Evidence at protein level; KW Acetylation; Complete proteome; NADP; Oxidoreductase; Peroxisome; KW Reference proteome. FT CHAIN 1 490 Hydroxysteroid dehydrogenase-like protein FT 2. FT /FTId=PRO_0000319889. FT DOMAIN 380 487 SCP2. FT NP_BIND 17 23 NADP (By similarity). FT COMPBIAS 300 375 Gln/Glu/Pro-rich. FT ACT_SITE 168 168 Proton acceptor (Potential). FT BINDING 42 42 NADP (By similarity). FT BINDING 74 74 NADP (By similarity). FT BINDING 172 172 NADP (By similarity). FT MOD_RES 116 116 N6-acetyllysine. FT MOD_RES 390 390 N6-succinyllysine. FT CONFLICT 307 307 L -> V (in Ref. 2; BAE23126). FT CONFLICT 328 328 K -> KPQLQEKPQLQEQ (in Ref. 2; BAE26313). FT CONFLICT 333 333 E -> EQPQLQQ (in Ref. 4; AAH02211). FT CONFLICT 334 334 Q -> K (in Ref. 2; BAE26313). FT CONFLICT 353 353 P -> Q (in Ref. 2; BAE26313). SQ SEQUENCE 490 AA; 54208 MW; 700958CDA46905DB CRC64; MLPNTGKLAG CTVFITGASR GIGKAIALKA AKDGANIVIA AKTTQKHPKL LGTIYTAAEE IEAAGGTALP CVVDVRDEQQ INSAVEKAVE KFGGIDILVN NASAISLTNT LDTPTKRVDL MMNVNTRGTY LTSKACIPFL KKSKVGHILN LSPPLNLNPL WFKQHCAYTI AKYGMSMCVL GMAEEFRGEI AVNALWPRTA IHTAAMDMLG GSGVENQCRK VDIIADAAYS IFKRPKSFTG NFIIDENILK EEGIKNFDVY AIAPGHPLLP DFFLDEHPDA VMEEKESNDS VPEVKEEKLQ LQEESQLQKQ PQLQEQPQLQ EKPQLQEKPQ LQEQPQLQEK PQLQEQPQQR EQPQLQQQPR PRQQPQPFVQ SMLPQKPHFG AVEETFRIVK DSLSDEVVRA TQAVYQFELS GEDGGTWFLD LKSKGGKVGH GEPSDRADVV MSMATDDFVK MFSGKLKPTM AFMSGKLKIK GNIALAIKLE KLMTQMNSRL // ID HTAI2_MOUSE Reviewed; 242 AA. AC Q9Z2G9; Q810Y5; Q99KN6; Q9D5F8; Q9D804; DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot. DT 03-OCT-2012, sequence version 3. DT 19-MAR-2014, entry version 86. DE RecName: Full=Oxidoreductase HTATIP2; DE EC=1.1.1.-; GN Name=Htatip2; Synonyms=Cc3, Tip30; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND DISRUPTION RP PHENOTYPE. RX PubMed=14695192; RA Ito M., Jiang C., Krumm K., Zhang X., Pecha J., Zhao J., Guo Y., RA Roeder R.G., Xiao H.; RT "TIP30 deficiency increases susceptibility to tumorigenesis."; RL Cancer Res. 63:8763-8767(2003). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=129/SvJ; RA Hauser L.J., Webb L.S., Dhar M.S., Mural R.M., Larimer F.W., RA Johnson D.K.; RT "Genomic organization, chromosomal mapping, and expression analysis of RT the murine Prmt3 and Htatip2 genes."; RL Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC STRAIN=C57BL/6J; TISSUE=Lung, Stomach, and Testis; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Czech II, and FVB/N; TISSUE=Mammary tumor; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [7] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 7-242. RG Joint center for structural genomics (JCSG); RT "Crystal structure of Tat-interacting protein 30 kDa (HIV-1 Tat- RT interactive protein 2, 30 kDa homolog) (human) (16924205) from Mus RT musculus at 2.30 A resolution."; RL Submitted (FEB-2006) to the PDB data bank. CC -!- FUNCTION: Oxidoreductase required for tumor suppression. NAPDH- CC bound form inhibits nuclear import by competing with nuclear CC import substrates for binding to a subset of nuclear transport CC receptors. May act as a redox sensor linked to transcription CC through regulation of nuclear import. CC -!- SUBUNIT: Monomer. Binds nuclear transport receptors XPO4, CC IPO5/RANBP5, IPO7, IPO9 and KPNB1 as well as GCN1L1/GCN1 and CC LRPPRC probably through their HEAT repeats. Binds NCOA5/CIA (By CC similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus envelope CC (By similarity). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; Synonyms=TIP30, CC3; CC IsoId=Q9Z2G9-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9Z2G9-2; Sequence=VSP_051866, VSP_051867; CC Note=No experimental confirmation available; CC -!- DISRUPTION PHENOTYPE: Mice are haploinsufficient for tumor CC suppression. 50% develop tumors within their second year. 30% of CC the tumors are hepatocellular carcinomas. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF061972; AAC69617.1; -; mRNA. DR EMBL; AY151050; AAN84531.1; -; Genomic_DNA. DR EMBL; AK008630; BAB25792.1; -; mRNA. DR EMBL; AK015389; BAB29825.1; -; mRNA. DR EMBL; AK144837; BAE26091.1; -; mRNA. DR EMBL; AC124775; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH466603; EDL22975.1; -; Genomic_DNA. DR EMBL; CH466603; EDL22976.1; -; Genomic_DNA. DR EMBL; CH466603; EDL22977.1; -; Genomic_DNA. DR EMBL; BC004083; AAH04083.1; -; mRNA. DR EMBL; BC017372; AAH17372.1; -; mRNA. DR RefSeq; NP_001139521.1; NM_001146049.1. DR RefSeq; NP_001139522.1; NM_001146050.1. DR RefSeq; NP_001139524.1; NM_001146052.1. DR RefSeq; NP_001139525.1; NM_001146053.1. DR UniGene; Mm.20801; -. DR PDB; 2FMU; X-ray; 2.30 A; A=7-242. DR PDBsum; 2FMU; -. DR ProteinModelPortal; Q9Z2G9; -. DR SMR; Q9Z2G9; 5-235. DR STRING; 10090.ENSMUSP00000082374; -. DR PhosphoSite; Q9Z2G9; -. DR PaxDb; Q9Z2G9; -. DR PRIDE; Q9Z2G9; -. DR DNASU; 53415; -. DR Ensembl; ENSMUST00000085272; ENSMUSP00000082374; ENSMUSG00000039745. [Q9Z2G9-1] DR GeneID; 53415; -. DR KEGG; mmu:53415; -. DR UCSC; uc009hbo.2; mouse. [Q9Z2G9-2] DR UCSC; uc009hbq.2; mouse. DR CTD; 10553; -. DR MGI; MGI:1859271; Htatip2. DR eggNOG; COG0702; -. DR GeneTree; ENSGT00390000008184; -. DR HOVERGEN; HBG052833; -. DR InParanoid; Q9Z2G9; -. DR KO; K17290; -. DR OMA; PRDKQME; -. DR OrthoDB; EOG7GJ6GJ; -. DR TreeFam; TF312849; -. DR EvolutionaryTrace; Q9Z2G9; -. DR NextBio; 310233; -. DR PRO; PR:Q9Z2G9; -. DR ArrayExpress; Q9Z2G9; -. DR CleanEx; MM_HTATIP2; -. DR Genevestigator; Q9Z2G9; -. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. DR GO; GO:0005635; C:nuclear envelope; ISS:UniProtKB. DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW. DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW. DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW. DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW. DR GO; GO:0051170; P:nuclear import; ISS:UniProtKB. DR GO; GO:0045765; P:regulation of angiogenesis; ISS:UniProtKB. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR016040; NAD(P)-bd_dom. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Angiogenesis; KW Apoptosis; Complete proteome; Cytoplasm; Developmental protein; KW Differentiation; NADP; Nucleus; Oxidoreductase; Reference proteome; KW Tumor suppressor. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 242 Oxidoreductase HTATIP2. FT /FTId=PRO_0000072545. FT NP_BIND 19 52 NADP (By similarity). FT ACT_SITE 143 143 Proton acceptor (By similarity). FT ACT_SITE 147 147 By similarity. FT BINDING 131 131 Substrate (By similarity). FT MOD_RES 2 2 N-acetylalanine (By similarity). FT VAR_SEQ 102 105 EGFV -> VSKK (in isoform 2). FT /FTId=VSP_051866. FT VAR_SEQ 106 242 Missing (in isoform 2). FT /FTId=VSP_051867. FT CONFLICT 8 8 P -> R (in Ref. 1; AAC69617). FT CONFLICT 10 10 L -> P (in Ref. 3; BAB29825). FT CONFLICT 27 27 S -> T (in Ref. 3; BAB29825). FT CONFLICT 39 39 L -> V (in Ref. 1; AAC69617). FT CONFLICT 77 77 V -> G (in Ref. 2; AAN84531). FT CONFLICT 213 213 N -> S (in Ref. 1; AAC69617). FT CONFLICT 235 235 K -> I (in Ref. 3; BAB25792). FT HELIX 7 16 FT STRAND 20 24 FT HELIX 29 41 FT STRAND 45 53 FT STRAND 66 69 FT HELIX 72 82 FT STRAND 86 90 FT HELIX 101 108 FT HELIX 110 121 FT STRAND 126 130 FT HELIX 142 156 FT STRAND 160 166 FT STRAND 168 171 FT HELIX 195 199 FT STRAND 200 202 FT HELIX 203 215 FT STRAND 219 226 FT HELIX 227 233 SQ SEQUENCE 242 AA; 26870 MW; 034F02137D3BF22A CRC64; MADKEALPKL REDFKMQNKS VFILGASGET GKVLLKEILG QNLFSKVTLI GRRKLTFEEE AYKNVNQEVV DFEKLDVYAS AFQGHDVGFC CLGTTRSKAG AEGFVRVDRD YVLKSAELAK AGGCKHFNLL SSRGADKSSS FLYLQVKGEV EAKVEELKFD RLSVFRPGVL LCDRQESRPG EWLARKFFGS LPDSWASGYA VPVVTVVRAM LNNLVSPSSG QMELLENKAI LHLGKDRDVP KL // ID I23O2_MOUSE Reviewed; 398 AA. AC Q8R0V5; E9QKA9; DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot. DT 03-OCT-2012, sequence version 2. DT 19-MAR-2014, entry version 78. DE RecName: Full=Indoleamine 2,3-dioxygenase 2; DE Short=IDO-2; DE EC=1.13.11.-; DE AltName: Full=Indoleamine 2,3-dioxygenase-like protein 1; DE AltName: Full=Indoleamine-pyrrole 2,3-dioxygenase-like protein 1; GN Name=Ido2; Synonyms=Indol1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Liver; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP FUNCTION, CATALYTIC ACTIVITY, AND TISSUE SPECIFICITY. RX PubMed=17499941; DOI=10.1016/j.gene.2007.04.010; RA Ball H.J., Sanchez-Perez A., Weiser S., Austin C.J.D., Astelbauer F., RA Miu J., McQuillan J.A., Stocker R., Jermiin L.S., Hunt N.H.; RT "Characterization of an indoleamine 2,3-dioxygenase-like protein found RT in humans and mice."; RL Gene 396:203-213(2007). RN [4] RP BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=18026683; DOI=10.1007/s00239-007-9049-1; RA Yuasa H.J., Takubo M., Takahashi A., Hasegawa T., Noma H., Suzuki T.; RT "Evolution of vertebrate indoleamine 2,3-dioxygenases."; RL J. Mol. Evol. 65:705-714(2007). CC -!- FUNCTION: Catalyzes the first and rate-limiting step in the CC kynurenine pathway of tryptophan catabolism. CC -!- CATALYTIC ACTIVITY: L-tryptophan + O(2) = N-formyl-L-kynurenine. CC -!- COFACTOR: Binds 1 heme group per subunit (By similarity). CC -!- ENZYME REGULATION: Activity is inhibited by D-1MT (1-methyl-D- CC tryptophan) and MTH-trp (methylthiohydantoin-DL-tryptophan) but CC not L-1MT (1-methyl-L-tryptophan) (By similarity). CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=38.85 mM for L-tryptophan; CC Note=Do not accept D-tryptophan as substrate; CC -!- PATHWAY: Amino-acid degradation; L-tryptophan degradation via CC kynurenine pathway; L-kynurenine from L-tryptophan: step 1/2. CC -!- TISSUE SPECIFICITY: Highest in kidney, followed by epididymis and CC liver (at protein level). Detected in the tails of the spermatozoa CC in the testis and in the kidney tubules (at protein level). CC -!- SIMILARITY: Belongs to the indoleamine 2,3-dioxygenase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AC114602; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC026393; AAH26393.1; -; mRNA. DR UniGene; Mm.219580; -. DR ProteinModelPortal; Q8R0V5; -. DR SMR; Q8R0V5; 12-397. DR IntAct; Q8R0V5; 1. DR MINT; MINT-1869768; -. DR ChEMBL; CHEMBL2189159; -. DR PhosphoSite; Q8R0V5; -. DR PaxDb; Q8R0V5; -. DR PRIDE; Q8R0V5; -. DR Ensembl; ENSMUST00000033953; ENSMUSP00000033953; ENSMUSG00000031549. DR MGI; MGI:2142489; Ido2. DR eggNOG; NOG73554; -. DR GeneTree; ENSGT00390000002154; -. DR HOGENOM; HOG000190192; -. DR InParanoid; Q8R0V5; -. DR UniPathway; UPA00333; UER00453. DR PRO; PR:Q8R0V5; -. DR ArrayExpress; Q8R0V5; -. DR CleanEx; MM_INDOL1; -. DR Genevestigator; Q8R0V5; -. DR GO; GO:0005737; C:cytoplasm; IDA:MGI. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0033754; F:indoleamine 2,3-dioxygenase activity; IDA:MGI. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0019441; P:tryptophan catabolic process to kynurenine; IDA:MGI. DR InterPro; IPR000898; Indolamine_dOase. DR Pfam; PF01231; IDO; 1. PE 1: Evidence at protein level; KW Complete proteome; Dioxygenase; Heme; Iron; Metal-binding; KW Oxidoreductase; Reference proteome. FT CHAIN 1 398 Indoleamine 2,3-dioxygenase 2. FT /FTId=PRO_0000285263. FT METAL 340 340 Iron (heme proximal ligand) (By FT similarity). FT CONFLICT 249 249 V -> A (in Ref. 2; AAH26393). SQ SEQUENCE 398 AA; 44468 MW; 8916CCFE1E8B8B35 CRC64; MTLEVPLSLG RYHISEEYGF LLPNPLEALP DHYKPWMEIA LRLPHLIENR QLRAHVYRMP LLDCRFLKSY REQRLAHMAL AAITMGFVWQ EGEGQPQKVL PRSLAIPFVE VSRNLGLPPI LVHSDLVLTN WTKRNPEGPL EISNLETIIS FPGGESLRGF ILVTVLVEKA AVPGLKALVQ GMEAIRQHSQ DTLLEALQQL RLSIQDITRA LAQMHDYVDP DIFYSVIRIF LSGWKDNPAM PVGLVYEGVA TEPLKYSGGS AAQSSVLHAF DEFLGIEHCK ESVGFLHRMR DYMPPSHKAF LEDLHVAPSL RDYILASGPG DCLMAYNQCV EALGELRSYH INVVARYIIS AATRARSRGL TNPSPHALED RGTGGTAMLS FLKSVREKTM EALLCPGA // ID I23O1_MOUSE Reviewed; 407 AA. AC P28776; DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-1992, sequence version 1. DT 19-FEB-2014, entry version 109. DE RecName: Full=Indoleamine 2,3-dioxygenase 1; DE Short=IDO-1; DE EC=1.13.11.52; DE AltName: Full=Indoleamine-pyrrole 2,3-dioxygenase; GN Name=Ido1; Synonyms=Ido, Indo; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE. RX PubMed=1937018; DOI=10.1016/0378-1119(91)90154-4; RA Habara-Ohkubo A., Takikawa O., Yoshida R.; RT "Cloning and expression of a cDNA encoding mouse indoleamine 2,3- RT dioxygenase."; RL Gene 105:221-227(1991). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=NMRI; TISSUE=Mammary gland; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP TISSUE SPECIFICITY. RX PubMed=17499941; DOI=10.1016/j.gene.2007.04.010; RA Ball H.J., Sanchez-Perez A., Weiser S., Austin C.J.D., Astelbauer F., RA Miu J., McQuillan J.A., Stocker R., Jermiin L.S., Hunt N.H.; RT "Characterization of an indoleamine 2,3-dioxygenase-like protein found RT in humans and mice."; RL Gene 396:203-213(2007). RN [4] RP BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=18026683; DOI=10.1007/s00239-007-9049-1; RA Yuasa H.J., Takubo M., Takahashi A., Hasegawa T., Noma H., Suzuki T.; RT "Evolution of vertebrate indoleamine 2,3-dioxygenases."; RL J. Mol. Evol. 65:705-714(2007). CC -!- FUNCTION: Catalyzes the cleavage of the pyrrol ring of tryptophan CC and incorporates both atoms of a molecule of oxygen (By CC similarity). CC -!- CATALYTIC ACTIVITY: D-tryptophan + O(2) = N-formyl-D-kynurenine. CC -!- CATALYTIC ACTIVITY: L-tryptophan + O(2) = N-formyl-L-kynurenine. CC -!- COFACTOR: Binds 1 heme group per subunit. CC -!- ENZYME REGULATION: Activity is inhibited by and MTH-trp CC (methylthiohydantoin-DL-tryptophan), modestly inhibited by L-1MT CC (1-methyl-L-tryptophan) but not D-1MT (1-methyl-D-tryptophan) (By CC similarity). CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=28.1 uM for L-tryptophan; CC KM=2.87 mM for D-tryptophan; CC Note=Catalytic efficiency for L-tryptophan is 90 times higher CC than for D-tryptophan; CC -!- INTERACTION: CC P35235:Ptpn11; NbExp=5; IntAct=EBI-4410822, EBI-397236; CC -!- TISSUE SPECIFICITY: Detected in the apical cells of the caput CC epididymis and in the kidney blood vessels (at protein level). CC -!- INDUCTION: By interferon gamma. CC -!- SIMILARITY: Belongs to the indoleamine 2,3-dioxygenase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M69109; AAA37872.1; -; mRNA. DR EMBL; BC049931; AAH49931.1; -; mRNA. DR PIR; JH0492; JH0492. DR RefSeq; NP_032350.1; NM_008324.1. DR UniGene; Mm.392; -. DR ProteinModelPortal; P28776; -. DR SMR; P28776; 15-404. DR BioGrid; 200512; 2. DR DIP; DIP-48663N; -. DR IntAct; P28776; 2. DR STRING; 10090.ENSMUSP00000033956; -. DR ChEMBL; CHEMBL1075294; -. DR PhosphoSite; P28776; -. DR PRIDE; P28776; -. DR DNASU; 15930; -. DR Ensembl; ENSMUST00000033956; ENSMUSP00000033956; ENSMUSG00000031551. DR GeneID; 15930; -. DR KEGG; mmu:15930; -. DR UCSC; uc009lfa.1; mouse. DR CTD; 3620; -. DR MGI; MGI:96416; Ido1. DR eggNOG; NOG73554; -. DR GeneTree; ENSGT00390000002154; -. DR HOGENOM; HOG000190192; -. DR InParanoid; P28776; -. DR KO; K00463; -. DR OMA; QIVAKYI; -. DR TreeFam; TF330978; -. DR BRENDA; 1.13.11.11; 3474. DR SABIO-RK; P28776; -. DR NextBio; 288648; -. DR PRO; PR:P28776; -. DR ArrayExpress; P28776; -. DR Bgee; P28776; -. DR CleanEx; MM_INDO; -. DR Genevestigator; P28776; -. DR GO; GO:0030485; C:smooth muscle contractile fiber; IDA:MGI. DR GO; GO:0032421; C:stereocilium bundle; IDA:MGI. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0033754; F:indoleamine 2,3-dioxygenase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004833; F:tryptophan 2,3-dioxygenase activity; IDA:MGI. DR GO; GO:0002534; P:cytokine production involved in inflammatory response; IMP:MGI. DR GO; GO:0034276; P:kynurenic acid biosynthetic process; IMP:MGI. DR GO; GO:0033555; P:multicellular organismal response to stress; IMP:MGI. DR GO; GO:0046007; P:negative regulation of activated T cell proliferation; IMP:MGI. DR GO; GO:0032693; P:negative regulation of interleukin-10 production; IMP:MGI. DR GO; GO:0070233; P:negative regulation of T cell apoptotic process; IMP:MGI. DR GO; GO:0043065; P:positive regulation of apoptotic process; IMP:MGI. DR GO; GO:0002678; P:positive regulation of chronic inflammatory response; IMP:MGI. DR GO; GO:0032735; P:positive regulation of interleukin-12 production; IMP:MGI. DR GO; GO:0002666; P:positive regulation of T cell tolerance induction; IMP:MGI. DR GO; GO:0002830; P:positive regulation of type 2 immune response; IMP:MGI. DR GO; GO:0032496; P:response to lipopolysaccharide; IMP:MGI. DR GO; GO:0036269; P:swimming behavior; IMP:MGI. DR GO; GO:0019441; P:tryptophan catabolic process to kynurenine; IDA:MGI. DR InterPro; IPR000898; Indolamine_dOase. DR Pfam; PF01231; IDO; 1. DR PROSITE; PS00876; IDO_1; 1. DR PROSITE; PS00877; IDO_2; 1. PE 1: Evidence at protein level; KW Complete proteome; Dioxygenase; Direct protein sequencing; Heme; Iron; KW Metal-binding; Oxidoreductase; Reference proteome; KW Tryptophan catabolism. FT CHAIN 1 407 Indoleamine 2,3-dioxygenase 1. FT /FTId=PRO_0000215205. FT METAL 350 350 Iron (heme proximal ligand) (By FT similarity). SQ SEQUENCE 407 AA; 45641 MW; 317681EABF96A727 CRC64; MALSKISPTE GSRRILEDHH IDEDVGFALP HPLVELPDAY SPWVLVARNL PVLIENGQLR EEVEKLPTLS TDGLRGHRLQ RLAHLALGYI TMAYVWNRGD DDVRKVLPRN IAVPYCELSE KLGLPPILSY ADCVLANWKK KDPNGPMTYE NMDILFSFPG GDCDKGFFLV SLLVEIAASP AIKAIPTVSS AVERQDLKAL EKALHDIATS LEKAKEIFKR MRDFVDPDTF FHVLRIYLSG WKCSSKLPEG LLYEGVWDTP KMFSGGSAGQ SSIFQSLDVL LGIKHEAGKE SPAEFLQEMR EYMPPAHRNF LFFLESAPPV REFVISRHNE DLTKAYNECV NGLVSVRKFH LAIVDTYIMK PSKKKPTDGD KSEEPSNVES RGTGGTNPMT FLRSVKDTTE KALLSWP // ID IDH3A_MOUSE Reviewed; 366 AA. AC Q9D6R2; Q3UAM8; Q8C8A1; Q9D1L1; DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 19-MAR-2014, entry version 113. DE RecName: Full=Isocitrate dehydrogenase [NAD] subunit alpha, mitochondrial; DE EC=1.1.1.41; DE AltName: Full=Isocitric dehydrogenase subunit alpha; DE AltName: Full=NAD(+)-specific ICDH subunit alpha; DE Flags: Precursor; GN Name=Idh3a; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC STRAIN=C57BL/6J, and DBA/2; RC TISSUE=Bone marrow, Heart, Tongue, Visual cortex, and Wolffian duct; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC STRAIN=FVB/N; TISSUE=Liver; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP PROTEIN SEQUENCE OF 59-85; 101-188; 206-214 AND 300-336, AND MASS RP SPECTROMETRY. RC STRAIN=C57BL/6, and OF1; TISSUE=Brain, and Hippocampus; RA Lubec G., Kang S.U., Klug S., Yang J.W., Zigmond M., Sunyer B., RA Chen W.-Q.; RL Submitted (JAN-2009) to UniProtKB. RN [4] RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-77; LYS-343 AND LYS-350, RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic fibroblast, and Liver; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., RA Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). RN [5] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-223, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23576753; DOI=10.1073/pnas.1302961110; RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., RA Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.; RT "Label-free quantitative proteomics of the lysine acetylome in RT mitochondria identifies substrates of SIRT3 in metabolic pathways."; RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013). CC -!- CATALYTIC ACTIVITY: Isocitrate + NAD(+) = 2-oxoglutarate + CO(2) + CC NADH. CC -!- COFACTOR: Binds 1 magnesium or manganese ion per subunit (By CC similarity). CC -!- SUBUNIT: Heterooligomer of subunits alpha, beta, and gamma in the CC apparent ratio of 2:1:1 (By similarity). CC -!- SUBCELLULAR LOCATION: Mitochondrion (By similarity). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9D6R2-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9D6R2-2; Sequence=VSP_014517; CC -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate CC dehydrogenases family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK003393; BAB22760.1; -; mRNA. DR EMBL; AK010065; BAB26679.1; -; mRNA. DR EMBL; AK032787; BAC28021.1; -; mRNA. DR EMBL; AK047951; BAC33199.1; -; mRNA. DR EMBL; AK150618; BAE29708.1; -; mRNA. DR EMBL; AK151304; BAE30286.1; -; mRNA. DR EMBL; AK152353; BAE31145.1; -; mRNA. DR EMBL; AK153459; BAE32011.1; -; mRNA. DR EMBL; AK158646; BAE34596.1; -; mRNA. DR EMBL; AK159051; BAE34785.1; -; mRNA. DR EMBL; AK168049; BAE40031.1; -; mRNA. DR EMBL; AK168149; BAE40114.1; -; mRNA. DR EMBL; AK169152; BAE40931.1; -; mRNA. DR EMBL; BC034273; AAH34273.1; -; mRNA. DR EMBL; BC049956; AAH49956.1; -; mRNA. DR RefSeq; NP_083849.1; NM_029573.2. DR UniGene; Mm.279195; -. DR ProteinModelPortal; Q9D6R2; -. DR SMR; Q9D6R2; 30-362. DR IntAct; Q9D6R2; 8. DR MINT; MINT-1861233; -. DR PhosphoSite; Q9D6R2; -. DR REPRODUCTION-2DPAGE; Q9D6R2; -. DR UCD-2DPAGE; Q9D6R2; -. DR PaxDb; Q9D6R2; -. DR PRIDE; Q9D6R2; -. DR Ensembl; ENSMUST00000167866; ENSMUSP00000127526; ENSMUSG00000032279. [Q9D6R2-1] DR GeneID; 67834; -. DR KEGG; mmu:67834; -. DR UCSC; uc009prg.1; mouse. [Q9D6R2-1] DR CTD; 3419; -. DR MGI; MGI:1915084; Idh3a. DR eggNOG; COG0473; -. DR GeneTree; ENSGT00550000074918; -. DR HOGENOM; HOG000021113; -. DR HOVERGEN; HBG052080; -. DR InParanoid; Q9D6R2; -. DR KO; K00030; -. DR OMA; EGMYSGL; -. DR OrthoDB; EOG75B85R; -. DR TreeFam; TF105692; -. DR NextBio; 325657; -. DR PRO; PR:Q9D6R2; -. DR Bgee; Q9D6R2; -. DR CleanEx; MM_IDH3A; -. DR Genevestigator; Q9D6R2; -. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR GO; GO:0004449; F:isocitrate dehydrogenase (NAD+) activity; IEA:UniProtKB-EC. DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW. DR Gene3D; 3.40.718.10; -; 1. DR InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS. DR InterPro; IPR001804; Isocitrate/isopropylmalate_DH. DR InterPro; IPR004434; Isocitrate_DH_NAD. DR InterPro; IPR024084; IsoPropMal-DH-like_dom. DR PANTHER; PTHR11835; PTHR11835; 1. DR Pfam; PF00180; Iso_dh; 1. DR TIGRFAMs; TIGR00175; mito_nad_idh; 1. DR PROSITE; PS00470; IDH_IMDH; 1. PE 1: Evidence at protein level; KW Acetylation; Alternative splicing; Complete proteome; KW Direct protein sequencing; Magnesium; Manganese; Metal-binding; KW Mitochondrion; NAD; Oxidoreductase; Reference proteome; KW Transit peptide; Tricarboxylic acid cycle. FT TRANSIT 1 27 Mitochondrion (By similarity). FT CHAIN 28 366 Isocitrate dehydrogenase [NAD] subunit FT alpha, mitochondrial. FT /FTId=PRO_0000014438. FT METAL 233 233 Magnesium or manganese (By similarity). FT METAL 257 257 Magnesium or manganese (By similarity). FT METAL 261 261 Magnesium or manganese (By similarity). FT BINDING 115 115 Substrate (By similarity). FT BINDING 125 125 Substrate (By similarity). FT BINDING 146 146 Substrate (By similarity). FT BINDING 233 233 Substrate (By similarity). FT SITE 153 153 Critical for catalysis (By similarity). FT SITE 200 200 Critical for catalysis (By similarity). FT MOD_RES 77 77 N6-succinyllysine. FT MOD_RES 223 223 N6-acetyllysine. FT MOD_RES 343 343 N6-acetyllysine; alternate (By FT similarity). FT MOD_RES 343 343 N6-succinyllysine; alternate. FT MOD_RES 350 350 N6-succinyllysine. FT VAR_SEQ 1 78 Missing (in isoform 2). FT /FTId=VSP_014517. FT CONFLICT 306 306 A -> T (in Ref. 1; BAC33199). SQ SEQUENCE 366 AA; 39639 MW; 9F1D68C269376955 CRC64; MAGSAWVSKV SRLLGAFHNT KQVTRGFAGG VQTVTLIPGD GIGPEISASV MKIFDAAKAP IQWEERNVTA IQGPGGKWMI PPEAKESMDK NKMGLKGPLK TPIAAGHPSM NLLLRKTFDL YANVRPCVSI EGYKTPYTDV NIVTIRENTE GEYSGIEHVI VDGVVQSIKL ITEEASKRIA EFAFEYARNN HRSNVTAVHK ANIMRMSDGL FLQKCREVAE NCKDIKFNEM YLDTVCLNMV QDPSQFDVLV MPNLYGDILS DLCAGLIGGL GVTPSGNIGA NGVAIFESVH GTAPDIAGKD MANPTALLLS AVMMLRHMGL FDHAAKIEAA CFATIKDGKS LTKDLGGNAK CSDFTEEICR RVKDLD // ID IDHC_MOUSE Reviewed; 414 AA. AC O88844; Q3UAV7; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 2. DT 19-MAR-2014, entry version 110. DE RecName: Full=Isocitrate dehydrogenase [NADP] cytoplasmic; DE Short=IDH; DE EC=1.1.1.42; DE AltName: Full=Cytosolic NADP-isocitrate dehydrogenase; DE AltName: Full=IDP; DE AltName: Full=NADP(+)-specific ICDH; DE AltName: Full=Oxalosuccinate decarboxylase; GN Name=Idh1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=9866202; RA Nekrutenko A., Hillis D.M., Patton J.C., Bradley R.D., Baker R.J.; RT "Cytosolic isocitrate dehydrogenase in humans, mice, and voles and RT phylogenetic analysis of the enzyme family."; RL Mol. Biol. Evol. 15:1674-1684(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Bone marrow, Embryo, and Sympathetic ganglion; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP PROTEIN SEQUENCE OF 30-49. RC TISSUE=Brain; RA Lubec G., Yang J.W., Zigmond M.; RL Submitted (JUL-2007) to UniProtKB. RN [5] RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-126 AND LYS-400, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic fibroblast, and Liver; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., RA Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). RN [6] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-81; LYS-224; LYS-233 AND RP LYS-243, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Liver; RX PubMed=23576753; DOI=10.1073/pnas.1302961110; RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., RA Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.; RT "Label-free quantitative proteomics of the lysine acetylome in RT mitochondria identifies substrates of SIRT3 in metabolic pathways."; RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013). CC -!- CATALYTIC ACTIVITY: Isocitrate + NADP(+) = 2-oxoglutarate + CO(2) CC + NADPH. CC -!- COFACTOR: Binds 1 magnesium or manganese ion per subunit (By CC similarity). CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- PTM: Acetylation at Lys-374 dramatically reduces catalytic CC activity (By similarity). CC -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate CC dehydrogenases family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF020039; AAD02919.1; -; mRNA. DR EMBL; AK149019; BAE28720.1; -; mRNA. DR EMBL; AK151212; BAE30207.1; -; mRNA. DR EMBL; AK159173; BAE34873.1; -; mRNA. DR EMBL; AK160896; BAE36075.1; -; mRNA. DR EMBL; AK167158; BAE39299.1; -; mRNA. DR EMBL; CH466548; EDL00223.1; -; Genomic_DNA. DR EMBL; CH466548; EDL00225.1; -; Genomic_DNA. DR RefSeq; NP_001104790.1; NM_001111320.1. DR RefSeq; NP_034627.3; NM_010497.3. DR UniGene; Mm.9925; -. DR PDB; 2CMJ; X-ray; 1.99 A; A/B=4-413. DR PDB; 2CMV; X-ray; 2.52 A; A/B=4-413. DR PDBsum; 2CMJ; -. DR PDBsum; 2CMV; -. DR ProteinModelPortal; O88844; -. DR SMR; O88844; 4-413. DR IntAct; O88844; 5. DR MINT; MINT-1859161; -. DR PhosphoSite; O88844; -. DR COMPLUYEAST-2DPAGE; O88844; -. DR REPRODUCTION-2DPAGE; O88844; -. DR SWISS-2DPAGE; O88844; -. DR PaxDb; O88844; -. DR PRIDE; O88844; -. DR Ensembl; ENSMUST00000097709; ENSMUSP00000095316; ENSMUSG00000025950. DR Ensembl; ENSMUST00000169032; ENSMUSP00000127307; ENSMUSG00000025950. DR GeneID; 15926; -. DR KEGG; mmu:15926; -. DR UCSC; uc007bhn.2; mouse. DR CTD; 3417; -. DR MGI; MGI:96413; Idh1. DR eggNOG; COG0538; -. DR GeneTree; ENSGT00390000012547; -. DR HOGENOM; HOG000019858; -. DR HOVERGEN; HBG006119; -. DR KO; K00031; -. DR OMA; KELSFFA; -. DR OrthoDB; EOG7QNVKS; -. DR TreeFam; TF300428; -. DR EvolutionaryTrace; O88844; -. DR NextBio; 288640; -. DR PRO; PR:O88844; -. DR ArrayExpress; O88844; -. DR Bgee; O88844; -. DR CleanEx; MM_IDH1; -. DR Genevestigator; O88844; -. DR GO; GO:0005829; C:cytosol; IDA:MGI. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR GO; GO:0005777; C:peroxisome; IEA:Ensembl. DR GO; GO:0004450; F:isocitrate dehydrogenase (NADP+) activity; ISS:UniProtKB. DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR GO; GO:0050661; F:NADP binding; IEA:Ensembl. DR GO; GO:0006103; P:2-oxoglutarate metabolic process; ISS:UniProtKB. DR GO; GO:0008585; P:female gonad development; IEA:Ensembl. DR GO; GO:0006749; P:glutathione metabolic process; IMP:MGI. DR GO; GO:0006097; P:glyoxylate cycle; IEA:UniProtKB-KW. DR GO; GO:0006102; P:isocitrate metabolic process; ISS:UniProtKB. DR GO; GO:0006979; P:response to oxidative stress; IDA:MGI. DR GO; GO:0048545; P:response to steroid hormone; IEA:Ensembl. DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW. DR Gene3D; 3.40.718.10; -; 1. DR InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS. DR InterPro; IPR004790; Isocitrate_DH_NADP. DR InterPro; IPR024084; IsoPropMal-DH-like_dom. DR PANTHER; PTHR11822; PTHR11822; 1. DR Pfam; PF00180; Iso_dh; 1. DR PIRSF; PIRSF000108; IDH_NADP; 1. DR TIGRFAMs; TIGR00127; nadp_idh_euk; 1. DR PROSITE; PS00470; IDH_IMDH; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Complete proteome; Cytoplasm; KW Direct protein sequencing; Glyoxylate bypass; Magnesium; Manganese; KW Metal-binding; NADP; Oxidoreductase; Reference proteome; KW Tricarboxylic acid cycle. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 414 Isocitrate dehydrogenase [NADP] FT cytoplasmic. FT /FTId=PRO_0000083578. FT NP_BIND 75 77 NADP (By similarity). FT NP_BIND 310 315 NADP (By similarity). FT REGION 94 100 Substrate binding (By similarity). FT METAL 252 252 Magnesium or manganese (By similarity). FT METAL 275 275 Magnesium or manganese (By similarity). FT BINDING 77 77 Substrate (By similarity). FT BINDING 82 82 NADP (By similarity). FT BINDING 109 109 Substrate (By similarity). FT BINDING 132 132 Substrate (By similarity). FT BINDING 260 260 NADP (By similarity). FT BINDING 328 328 NADP; via amide nitrogen and carbonyl FT oxygen (By similarity). FT SITE 139 139 Critical for catalysis (By similarity). FT SITE 212 212 Critical for catalysis (By similarity). FT MOD_RES 2 2 N-acetylserine (By similarity). FT MOD_RES 81 81 N6-acetyllysine. FT MOD_RES 126 126 N6-succinyllysine. FT MOD_RES 224 224 N6-acetyllysine. FT MOD_RES 233 233 N6-acetyllysine. FT MOD_RES 243 243 N6-acetyllysine. FT MOD_RES 321 321 N6-acetyllysine (By similarity). FT MOD_RES 400 400 N6-succinyllysine. FT CONFLICT 243 243 K -> N (in Ref. 1; AAD02919). FT STRAND 5 14 FT HELIX 17 30 FT TURN 31 34 FT STRAND 35 43 FT HELIX 46 51 FT TURN 52 54 FT HELIX 55 67 FT STRAND 68 72 FT HELIX 80 86 FT HELIX 95 103 FT STRAND 106 111 FT STRAND 128 133 FT HELIX 137 140 FT STRAND 142 146 FT STRAND 148 162 FT STRAND 165 172 FT STRAND 177 185 FT HELIX 186 203 FT STRAND 207 211 FT TURN 213 215 FT HELIX 219 234 FT HELIX 236 241 FT STRAND 246 250 FT HELIX 251 260 FT STRAND 265 269 FT HELIX 271 285 FT STRAND 290 296 FT STRAND 303 306 FT HELIX 313 320 FT HELIX 330 347 FT HELIX 350 368 FT HELIX 374 381 FT HELIX 383 385 FT HELIX 388 390 FT HELIX 394 412 SQ SEQUENCE 414 AA; 46674 MW; C7FEF315D042C44C CRC64; MSRKIQGGSV VEMQGDEMTR IIWELIKEKL ILPYVELDLH SYDLGIENRD ATNDQVTKDA AEAIKKYNVG VKCATITPDE KRVEEFKLKQ MWKSPNGTIR NILGGTVFRE AIICKNIPRL VTGWVKPIII GRHAYGDQYR ATDFVVPGPG KVEITYTPKD GTQKVTYMVH DFEEGGGVAM GMYNQDKSIE DFAHSSFQMA LSKGWPLYLS TKNTILKKYD GRFKDIFQEI YDKKYKSQFE AQKICYEHRL IDDMVAQAMK SEGGFIWACK NYDGDVQSDS VAQGYGSLGM MTSVLICPDG KTVEAEAAHG TVTRHYRMYQ KGQETSTNPI ASIFAWSRGL AHRAKLDNNT ELSFFAKALE DVCIETIEAG FMTKDLAACI KGLPNVQRSD YLNTFEFMDK LGENLKAKLA QAKL // ID IDHG2_MOUSE Reviewed; 396 AA. AC Q8BPC6; DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 19-MAR-2014, entry version 85. DE RecName: Full=Probable isocitrate dehydrogenase [NAD] gamma 2, mitochondrial; DE EC=1.1.1.41; DE AltName: Full=Isocitric dehydrogenase subunit gamma 2; DE AltName: Full=NAD(+)-specific ICDH subunit gamma 2; DE Flags: Precursor; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Testis; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Testis; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. RX PubMed=18614015; DOI=10.1016/j.cell.2008.06.016; RA Pagliarini D.J., Calvo S.E., Chang B., Sheth S.A., Vafai S.B., RA Ong S.E., Walford G.A., Sugiana C., Boneh A., Chen W.K., Hill D.E., RA Vidal M., Evans J.G., Thorburn D.R., Carr S.A., Mootha V.K.; RT "A mitochondrial protein compendium elucidates complex I disease RT biology."; RL Cell 134:112-123(2008). CC -!- CATALYTIC ACTIVITY: Isocitrate + NAD(+) = 2-oxoglutarate + CO(2) + CC NADH. CC -!- COFACTOR: Binds 1 magnesium or manganese ion per subunit (By CC similarity). CC -!- SUBUNIT: Heterooligomer of subunits alpha, beta, and gamma in the CC apparent ratio of 2:1:1 (By similarity). CC -!- SUBCELLULAR LOCATION: Mitochondrion. CC -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate CC dehydrogenases family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK077105; BAC36614.1; -; mRNA. DR EMBL; CH466603; EDL22983.1; -; Genomic_DNA. DR EMBL; BC060958; AAH60958.1; -; mRNA. DR RefSeq; NP_766489.1; NM_172901.2. DR UniGene; Mm.443270; -. DR ProteinModelPortal; Q8BPC6; -. DR SMR; Q8BPC6; 47-382. DR PRIDE; Q8BPC6; -. DR Ensembl; ENSMUST00000119710; ENSMUSP00000138215; ENSMUSG00000084234. DR GeneID; 243996; -. DR KEGG; mmu:243996; -. DR UCSC; uc009hca.1; mouse. DR MGI; MGI:2142174; 4933405O20Rik. DR GeneTree; ENSGT00590000083091; -. DR HOVERGEN; HBG052080; -. DR KO; K00030; -. DR NextBio; 386086; -. DR Genevestigator; Q8BPC6; -. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004449; F:isocitrate dehydrogenase (NAD+) activity; IEA:UniProtKB-EC. DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW. DR Gene3D; 3.40.718.10; -; 1. DR InterPro; IPR001804; Isocitrate/isopropylmalate_DH. DR InterPro; IPR004434; Isocitrate_DH_NAD. DR InterPro; IPR024084; IsoPropMal-DH-like_dom. DR PANTHER; PTHR11835; PTHR11835; 1. DR Pfam; PF00180; Iso_dh; 1. DR TIGRFAMs; TIGR00175; mito_nad_idh; 1. PE 2: Evidence at transcript level; KW ATP-binding; Complete proteome; Magnesium; Manganese; Metal-binding; KW Mitochondrion; NAD; Nucleotide-binding; Oxidoreductase; KW Reference proteome; Transit peptide; Tricarboxylic acid cycle. FT TRANSIT 1 25 Mitochondrion (Potential). FT CHAIN 26 396 Probable isocitrate dehydrogenase [NAD] FT gamma 2, mitochondrial. FT /FTId=PRO_0000401933. FT NP_BIND 53 81 NAD (Potential). FT NP_BIND 306 313 ATP (Potential). FT METAL 251 251 Magnesium or manganese (By similarity). FT BINDING 133 133 Substrate (By similarity). FT BINDING 164 164 Substrate (By similarity). FT BINDING 251 251 Substrate (By similarity). FT SITE 171 171 Critical for catalysis (By similarity). FT SITE 218 218 Critical for catalysis (By similarity). SQ SEQUENCE 396 AA; 43850 MW; 1B5D708D2D265398 CRC64; MLAVTSCSMK TVLQYAVFLG HSREVVCELV TSFRSFCSHC AVPPSPKYGG RHTVAMIPGD GIGPELMVHV KKIFRSNCVP VDFEEVWVTS TSNEEEINNA LMAIRRNRVA LKGNIATNHN LPARYKSHNT KFRTILDLYA SVVHFKTFPG VMTRHKDIDI LVVRENTEGE YTNLEHESVK GVVESLKIVT KTKSVRIADY AFKLAQKMGR KKVTVVHKAN IMKLGDGLFL QCCKDVAAHY PQITLESMII DNTTMQLVSK PQQFDVMVMP NLYGNIINSI CTGLVGGSGI VPGANYGDSY AIFEMGSKEI GKDLAHRNIA NPVAMLLTSC IMLDYLDLQP YATHIRSAVM ASLQNKAVCT PDIGGQGNTA STVEYILHHM KEQTSGCHPN FFLQFT // ID IDHP_MOUSE Reviewed; 452 AA. AC P54071; Q8C2R9; Q9EQK1; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 11-SEP-2007, sequence version 3. DT 19-MAR-2014, entry version 109. DE RecName: Full=Isocitrate dehydrogenase [NADP], mitochondrial; DE Short=IDH; DE EC=1.1.1.42; DE AltName: Full=ICD-M; DE AltName: Full=IDP; DE AltName: Full=NADP(+)-specific ICDH; DE AltName: Full=Oxalosuccinate decarboxylase; DE Flags: Precursor; GN Name=Idh2; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=BALB/c; TISSUE=Heart; RX PubMed=8867815; RX DOI=10.1002/(SICI)1097-4644(19960301)60:3<400::AID-JCB11>3.3.CO;2-2; RA Yang L., Luo H., Vinay P., Wu J.; RT "Molecular cloning of the cDNA of mouse mitochondrial NADP-dependent RT isocitrate dehydrogenase and the expression of the gene during RT lymphocyte activation."; RL J. Cell. Biochem. 60:400-410(1996). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INDUCTION. RX PubMed=11278619; DOI=10.1074/jbc.M010120200; RA Jo S.-H., Son M.-K., Koh H.-J., Lee S.-M., Song I.-H., Kim Y.-O., RA Lee Y.-S., Jeong K.-S., Kim W.B., Park J.-W., Song B.J., Huhe T.-L.; RT "Control of mitochondrial redox balance and cellular defense against RT oxidative damage by mitochondrial NADP+-dependent isocitrate RT dehydrogenase."; RL J. Biol. Chem. 276:16168-16176(2001). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J, and NOD; TISSUE=Embryo, Heart, and Thymus; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N-3; TISSUE=Mammary tumor; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP PROTEIN SEQUENCE OF 44-60 AND 81-89, AND MASS SPECTROMETRY. RC STRAIN=C57BL/6; TISSUE=Brain; RA Lubec G., Kang S.U.; RL Submitted (APR-2007) to UniProtKB. RN [6] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-263, SUCCINYLATION [LARGE RP SCALE ANALYSIS] AT LYS-80; LYS-106; LYS-166; LYS-180; LYS-193; RP LYS-256; LYS-282 AND LYS-384, AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic fibroblast, and Liver; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., RA Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). RN [7] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-45; LYS-48; LYS-69; LYS-80; RP LYS-106; LYS-155; LYS-166; LYS-180; LYS-193; LYS-199; LYS-256; RP LYS-263; LYS-272; LYS-280; LYS-282; LYS-384; LYS-400 AND LYS-442, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23576753; DOI=10.1073/pnas.1302961110; RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., RA Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.; RT "Label-free quantitative proteomics of the lysine acetylome in RT mitochondria identifies substrates of SIRT3 in metabolic pathways."; RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013). CC -!- FUNCTION: Plays a role in intermediary metabolism and energy CC production. It may tightly associate or interact with the pyruvate CC dehydrogenase complex. CC -!- CATALYTIC ACTIVITY: Isocitrate + NADP(+) = 2-oxoglutarate + CO(2) CC + NADPH. CC -!- COFACTOR: Binds 1 magnesium or manganese ion per subunit (By CC similarity). CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SUBCELLULAR LOCATION: Mitochondrion. CC -!- TISSUE SPECIFICITY: Heart > kidney >> other tissues. CC -!- INDUCTION: By oxidative stress (at protein level). CC -!- PTM: Acetylation at Lys-413 dramatically reduces catalytic CC activity. Deacetylated by SIRT3 (By similarity). CC -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate CC dehydrogenases family. CC -!- SEQUENCE CAUTION: CC Sequence=AAC52473.1; Type=Frameshift; Positions=5, 11; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U51167; AAC52473.1; ALT_FRAME; mRNA. DR EMBL; AF212319; AAG43538.1; -; mRNA. DR EMBL; AK088110; BAC40149.1; -; mRNA. DR EMBL; AK145753; BAE26628.1; -; mRNA. DR EMBL; AK161640; BAE36505.1; -; mRNA. DR EMBL; AK169395; BAE41142.1; -; mRNA. DR EMBL; BC060030; AAH60030.1; -; mRNA. DR RefSeq; NP_766599.2; NM_173011.2. DR UniGene; Mm.246432; -. DR UniGene; Mm.290925; -. DR ProteinModelPortal; P54071; -. DR SMR; P54071; 40-452. DR BioGrid; 234733; 2. DR IntAct; P54071; 4. DR MINT; MINT-4114220; -. DR ChEMBL; CHEMBL2176829; -. DR PhosphoSite; P54071; -. DR PaxDb; P54071; -. DR PRIDE; P54071; -. DR Ensembl; ENSMUST00000107384; ENSMUSP00000103007; ENSMUSG00000030541. DR GeneID; 269951; -. DR KEGG; mmu:269951; -. DR UCSC; uc009hzm.2; mouse. DR CTD; 3418; -. DR MGI; MGI:96414; Idh2. DR eggNOG; COG0538; -. DR GeneTree; ENSGT00390000012547; -. DR HOGENOM; HOG000019858; -. DR HOVERGEN; HBG006119; -. DR KO; K00031; -. DR OMA; GSGPTWA; -. DR OrthoDB; EOG7QNVKS; -. DR TreeFam; TF300428; -. DR ChiTaRS; IDH2; mouse. DR NextBio; 393111; -. DR PRO; PR:P54071; -. DR ArrayExpress; P54071; -. DR Bgee; P54071; -. DR CleanEx; MM_IDH2; -. DR Genevestigator; P54071; -. DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:MGI. DR GO; GO:0004450; F:isocitrate dehydrogenase (NADP+) activity; ISS:UniProtKB. DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR GO; GO:0006103; P:2-oxoglutarate metabolic process; ISS:UniProtKB. DR GO; GO:0006097; P:glyoxylate cycle; IEA:UniProtKB-KW. DR GO; GO:0006102; P:isocitrate metabolic process; ISS:UniProtKB. DR GO; GO:0006950; P:response to stress; IEA:UniProtKB-KW. DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW. DR Gene3D; 3.40.718.10; -; 1. DR InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS. DR InterPro; IPR004790; Isocitrate_DH_NADP. DR InterPro; IPR024084; IsoPropMal-DH-like_dom. DR PANTHER; PTHR11822; PTHR11822; 1. DR Pfam; PF00180; Iso_dh; 1. DR PIRSF; PIRSF000108; IDH_NADP; 1. DR TIGRFAMs; TIGR00127; nadp_idh_euk; 1. DR PROSITE; PS00470; IDH_IMDH; 1. PE 1: Evidence at protein level; KW Acetylation; Complete proteome; Direct protein sequencing; KW Glyoxylate bypass; Magnesium; Manganese; Metal-binding; Mitochondrion; KW NADP; Oxidoreductase; Reference proteome; Stress response; KW Transit peptide; Tricarboxylic acid cycle. FT TRANSIT 1 39 Mitochondrion (By similarity). FT CHAIN 40 452 Isocitrate dehydrogenase [NADP], FT mitochondrial. FT /FTId=PRO_0000014421. FT NP_BIND 115 117 NADP (By similarity). FT NP_BIND 349 354 NADP (By similarity). FT REGION 134 140 Substrate binding (By similarity). FT METAL 291 291 Magnesium or manganese (By similarity). FT METAL 314 314 Magnesium or manganese (By similarity). FT BINDING 117 117 Substrate (By similarity). FT BINDING 122 122 NADP (By similarity). FT BINDING 149 149 Substrate (By similarity). FT BINDING 172 172 Substrate (By similarity). FT BINDING 299 299 NADP (By similarity). FT BINDING 367 367 NADP; via amide nitrogen and carbonyl FT oxygen (By similarity). FT SITE 179 179 Critical for catalysis (By similarity). FT SITE 251 251 Critical for catalysis (By similarity). FT MOD_RES 45 45 N6-acetyllysine. FT MOD_RES 48 48 N6-acetyllysine. FT MOD_RES 67 67 N6-acetyllysine (By similarity). FT MOD_RES 69 69 N6-acetyllysine. FT MOD_RES 80 80 N6-acetyllysine; alternate. FT MOD_RES 80 80 N6-succinyllysine; alternate. FT MOD_RES 106 106 N6-acetyllysine; alternate. FT MOD_RES 106 106 N6-succinyllysine; alternate. FT MOD_RES 155 155 N6-acetyllysine. FT MOD_RES 166 166 N6-acetyllysine; alternate. FT MOD_RES 166 166 N6-succinyllysine; alternate. FT MOD_RES 180 180 N6-acetyllysine; alternate. FT MOD_RES 180 180 N6-succinyllysine; alternate. FT MOD_RES 193 193 N6-acetyllysine; alternate. FT MOD_RES 193 193 N6-succinyllysine; alternate. FT MOD_RES 199 199 N6-acetyllysine. FT MOD_RES 256 256 N6-acetyllysine; alternate. FT MOD_RES 256 256 N6-succinyllysine; alternate. FT MOD_RES 263 263 N6-acetyllysine. FT MOD_RES 272 272 N6-acetyllysine. FT MOD_RES 275 275 N6-acetyllysine (By similarity). FT MOD_RES 280 280 N6-acetyllysine. FT MOD_RES 282 282 N6-acetyllysine; alternate. FT MOD_RES 282 282 N6-succinyllysine; alternate. FT MOD_RES 384 384 N6-acetyllysine; alternate. FT MOD_RES 384 384 N6-succinyllysine; alternate. FT MOD_RES 400 400 N6-acetyllysine. FT MOD_RES 413 413 N6-acetyllysine (By similarity). FT MOD_RES 442 442 N6-acetyllysine. FT CONFLICT 104 104 T -> A (in Ref. 1; AAC52473). FT CONFLICT 109 109 V -> M (in Ref. 1; AAC52473). FT CONFLICT 152 152 I -> S (in Ref. 1; AAC52473). FT CONFLICT 200 200 D -> N (in Ref. 1; AAC52473). FT CONFLICT 214 214 A -> G (in Ref. 1; AAC52473). FT CONFLICT 280 280 K -> R (in Ref. 1; AAC52473 and 2; FT AAG43538). FT CONFLICT 322 323 QG -> SR (in Ref. 1; AAC52473). FT CONFLICT 367 368 NP -> KG (in Ref. 1; AAC52473). FT CONFLICT 398 398 L -> R (in Ref. 1; AAC52473). FT CONFLICT 408 408 Missing (in Ref. 1; AAC52473). SQ SEQUENCE 452 AA; 50906 MW; 19BB5CF78512ECAB CRC64; MAGYLRAVSS LCRASGSART WAPAALTVPS WPEQPRRHYA EKRIKVEKPV VEMDGDEMTR IIWQFIKEKL ILPHVDVQLK YFDLGLPNRD QTNDQVTIDS ALATQKYSVA VKCATITPDE ARVEEFKLKK MWKSPNGTIR NILGGTVFRE PIICKNIPRL VPGWTKPITI GRHAHGDQYK ATDFVVDRAG TFKLVFTPKD GSSAKEWEVY NFPAGGVGMG MYNTDESISG FAHSCFQYSI QKKWPLYLST KNTILKAYDG RFKDIFQEIF DKHYKTDFDK NKIWYEHRLI DDMVAQVLKS SGGFVWACKN YDGDVQSDIL AQGFGSLGLM TSVLVCPDGK TIEAEAAHGT VTRHYREHQK GRPTSTNPIA SIFAWTRGLE HRGKLDGNQD LIRFAQTLEK VCVQTVESGA MTKDLAGCIH GLSNVKLNEH FLNTTDFLDT IKSNLDRALG KQ // ID IDHG1_MOUSE Reviewed; 393 AA. AC P70404; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 19-MAR-2014, entry version 121. DE RecName: Full=Isocitrate dehydrogenase [NAD] subunit gamma 1, mitochondrial; DE EC=1.1.1.41; DE AltName: Full=Isocitric dehydrogenase subunit gamma; DE AltName: Full=NAD(+)-specific ICDH subunit gamma; DE Flags: Precursor; GN Name=Idh3g; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=9286695; DOI=10.1006/geno.1997.4822; RA Brenner V., Nyakatura G., Rosenthal A., Platzer M.; RT "Genomic organization of two novel genes on human Xq28: compact head RT to head arrangement of IDH gamma and TRAP delta is conserved in rat RT and mouse."; RL Genomics 44:8-14(1997). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Platzer M., Brenner V., Reichwald K., Wiehe T., Oksche A., RA Rosenthal A.; RT "Comparative sequence analysis of the mouse L1cam locus and the RT corresponding region of human Xq28."; RL Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases. RN [3] RP PROTEIN SEQUENCE OF 70-108; 116-129; 137-190 AND 227-237, AND MASS RP SPECTROMETRY. RC STRAIN=C57BL/6, and OF1; TISSUE=Brain, and Hippocampus; RA Lubec G., Kang S.U., Sunyer B., Chen W.-Q.; RL Submitted (JAN-2009) to UniProtKB. RN [4] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain; RX PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200; RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., RA Burlingame A.L.; RT "Comprehensive identification of phosphorylation sites in postsynaptic RT density preparations."; RL Mol. Cell. Proteomics 5:914-922(2006). RN [5] RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-226, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic fibroblast; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., RA Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). RN [6] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-206, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23576753; DOI=10.1073/pnas.1302961110; RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., RA Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.; RT "Label-free quantitative proteomics of the lysine acetylome in RT mitochondria identifies substrates of SIRT3 in metabolic pathways."; RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013). CC -!- CATALYTIC ACTIVITY: Isocitrate + NAD(+) = 2-oxoglutarate + CO(2) + CC NADH. CC -!- COFACTOR: Binds 1 magnesium or manganese ion per subunit (By CC similarity). CC -!- ENZYME REGULATION: Activated by increasing ADP/ATP ratios and by CC Ca(2+) (By similarity). CC -!- SUBUNIT: Heterooligomer of subunits alpha, beta, and gamma in the CC apparent ratio of 2:1:1 (By similarity). CC -!- SUBCELLULAR LOCATION: Mitochondrion. CC -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate CC dehydrogenases family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U68564; AAC53340.1; -; mRNA. DR EMBL; AF133093; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; NP_032349.1; NM_008323.1. DR UniGene; Mm.14825; -. DR ProteinModelPortal; P70404; -. DR SMR; P70404; 50-383. DR BioGrid; 200511; 1. DR IntAct; P70404; 4. DR MINT; MINT-1861482; -. DR PhosphoSite; P70404; -. DR PaxDb; P70404; -. DR PRIDE; P70404; -. DR Ensembl; ENSMUST00000052761; ENSMUSP00000056502; ENSMUSG00000002010. DR GeneID; 15929; -. DR KEGG; mmu:15929; -. DR UCSC; uc009tmp.1; mouse. DR CTD; 3421; -. DR MGI; MGI:1099463; Idh3g. DR eggNOG; COG0473; -. DR HOVERGEN; HBG052080; -. DR InParanoid; P70404; -. DR KO; K00030; -. DR OMA; NETRLHT; -. DR OrthoDB; EOG75B85R; -. DR TreeFam; TF315033; -. DR NextBio; 288644; -. DR PRO; PR:P70404; -. DR ArrayExpress; P70404; -. DR Bgee; P70404; -. DR CleanEx; MM_IDH3G; -. DR Genevestigator; P70404; -. DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB. DR GO; GO:0005730; C:nucleolus; IEA:Ensembl. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004449; F:isocitrate dehydrogenase (NAD+) activity; ISS:UniProtKB. DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR GO; GO:0006102; P:isocitrate metabolic process; ISS:UniProtKB. DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW. DR Gene3D; 3.40.718.10; -; 1. DR InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS. DR InterPro; IPR001804; Isocitrate/isopropylmalate_DH. DR InterPro; IPR004434; Isocitrate_DH_NAD. DR InterPro; IPR024084; IsoPropMal-DH-like_dom. DR PANTHER; PTHR11835; PTHR11835; 1. DR Pfam; PF00180; Iso_dh; 1. DR TIGRFAMs; TIGR00175; mito_nad_idh; 1. DR PROSITE; PS00470; IDH_IMDH; 1. PE 1: Evidence at protein level; KW Acetylation; ATP-binding; Complete proteome; KW Direct protein sequencing; Magnesium; Manganese; Metal-binding; KW Mitochondrion; NAD; Nucleotide-binding; Oxidoreductase; KW Reference proteome; Transit peptide; Tricarboxylic acid cycle. FT TRANSIT 1 39 Mitochondrion (By similarity). FT CHAIN 40 393 Isocitrate dehydrogenase [NAD] subunit FT gamma 1, mitochondrial. FT /FTId=PRO_0000014451. FT NP_BIND 56 84 NAD (Potential). FT NP_BIND 309 316 ATP (Potential). FT METAL 254 254 Magnesium or manganese (By similarity). FT BINDING 136 136 Substrate (By similarity). FT BINDING 167 167 Substrate (By similarity). FT BINDING 254 254 Substrate (By similarity). FT SITE 174 174 Critical for catalysis (By similarity). FT SITE 221 221 Critical for catalysis (By similarity). FT MOD_RES 206 206 N6-acetyllysine. FT MOD_RES 226 226 N6-succinyllysine. SQ SEQUENCE 393 AA; 42785 MW; 4023560C44C1F4D3 CRC64; MALKVAIAAG GAAKAMLKPT LLCRPWEVLA AHVAPRRSIS SQQTIPPSAK YGGRHTVTMI PGDGIGPELM LHVKSVFRHA CVPVDFEEVH VSSNADEEDI RNAIMAIRRN RVALKGNIET NHNLPPSHKS RNNILRTSLD LYANVIHCKS LPGVVTRHKD IDILIVRENT EGEYSSLEHE SVAGVVESLK IITKAKSLRI AEYAFKLAQE SGRKKVTAVH KANIMKLGDG LFLQCCREVA AHYPQITFDS MIVDNTTMQL VSRPQQFDVM VMPNLYGNIV NNVCAGLVGG PGLVAGANYG HVYAVFETAT RNTGKSIANK NIANPTATLL ASCMMLDHLK LHSYATSIRK AVLASMDNEN MHTPDIGGQG TTSQAIQDII RHIRIINGRA VEA // ID IMDH2_MOUSE Reviewed; 514 AA. AC P24547; Q61734; Q91Z11; DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot. DT 03-OCT-2003, sequence version 2. DT 19-FEB-2014, entry version 143. DE RecName: Full=Inosine-5'-monophosphate dehydrogenase 2; DE Short=IMP dehydrogenase 2; DE Short=IMPD 2; DE Short=IMPDH 2; DE EC=1.1.1.205; DE AltName: Full=IMPDH-II; GN Name=Impdh2; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=1671845; DOI=10.1016/0378-1119(91)90065-J; RA Tiedeman A.A., Smith J.M.; RT "Isolation and sequence of a cDNA encoding mouse IMP dehydrogenase."; RL Gene 97:289-293(1991). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS MYCOPHENOLIC ACID RESISTANT. RC TISSUE=Brain; RX PubMed=7906545; DOI=10.1016/0167-4781(94)90029-9; RA Lightfoot T., Snyder F.F.; RT "Gene amplification and dual point mutations of mouse IMP RT dehydrogenase associated with cellular resistance to mycophenolic RT acid."; RL Biochim. Biophys. Acta 1217:156-162(1994). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C3H/He, and Czech II; TISSUE=Mammary gland, and Osteoblast; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP PROTEIN SEQUENCE OF 125-133; 182-194; 289-290; 439-449; 456-466 AND RP 475-478. RX PubMed=2572589; RA Hodges S.D., Fung E., McKay D.J., Renaux B.S., Snyder F.F.; RT "Increased activity, amount, and altered kinetic properties of IMP RT dehydrogenase from mycophenolic acid-resistant neuroblastoma cells."; RL J. Biol. Chem. 264:18137-18141(1989). RN [5] RP PROTEIN SEQUENCE OF 137-149. RC TISSUE=Brain; RA Lubec G., Yang J.W., Zigmond M.; RL Submitted (JUL-2007) to UniProtKB. CC -!- FUNCTION: Catalyzes the conversion of inosine 5'-phosphate (IMP) CC to xanthosine 5'-phosphate (XMP), the first committed and rate- CC limiting step in the de novo synthesis of guanine nucleotides, and CC therefore plays an important role in the regulation of cell CC growth. Could also have a single-stranded nucleic acid-binding CC activity and could play a role in RNA and/or DNA metabolism (By CC similarity). It may also have a role in the development of CC malignancy and the growth progression of some tumors. CC -!- CATALYTIC ACTIVITY: Inosine 5'-phosphate + NAD(+) + H(2)O = CC xanthosine 5'-phosphate + NADH. CC -!- COFACTOR: Potassium (By similarity). CC -!- ENZYME REGULATION: Mycophenolic acid (MPA) is a non-competitive CC inhibitor that prevents formation of the closed enzyme CC conformation by binding to the same site as the amobile flap. In CC contrast, mizoribine monophosphate (MZP) is a competitive CC inhibitor that induces the closed conformation. MPA is a potent CC inhibitor of mammalian IMPDHs but a poor inhibitor of the CC bacterial enzymes. MZP is a more potent inhibitor of bacterial CC IMPDH (By similarity). CC -!- PATHWAY: Purine metabolism; XMP biosynthesis via de novo pathway; CC XMP from IMP: step 1/1. CC -!- SUBUNIT: Homotetramer. CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By CC similarity). CC -!- SIMILARITY: Belongs to the IMPDH/GMPR family. CC -!- SIMILARITY: Contains 2 CBS domains. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M33934; AAA39311.1; -; mRNA. DR EMBL; M98333; AAA20181.1; -; mRNA. DR EMBL; BC010314; AAH10314.1; -; mRNA. DR EMBL; BC052671; AAH52671.1; -; mRNA. DR PIR; JT0565; JT0565. DR RefSeq; NP_035960.2; NM_011830.3. DR UniGene; Mm.6065; -. DR ProteinModelPortal; P24547; -. DR SMR; P24547; 10-514. DR BioGrid; 204792; 1. DR IntAct; P24547; 2. DR MINT; MINT-1869864; -. DR BindingDB; P24547; -. DR ChEMBL; CHEMBL3169; -. DR PhosphoSite; P24547; -. DR REPRODUCTION-2DPAGE; P24547; -. DR PaxDb; P24547; -. DR PRIDE; P24547; -. DR Ensembl; ENSMUST00000081111; ENSMUSP00000079888; ENSMUSG00000062867. DR GeneID; 23918; -. DR KEGG; mmu:23918; -. DR UCSC; uc009rqg.1; mouse. DR CTD; 3615; -. DR MGI; MGI:109367; Impdh2. DR eggNOG; COG0517; -. DR HOGENOM; HOG000165752; -. DR HOVERGEN; HBG052122; -. DR InParanoid; P24547; -. DR KO; K00088; -. DR OMA; FQAKARH; -. DR OrthoDB; EOG7VTDMM; -. DR TreeFam; TF300378; -. DR UniPathway; UPA00601; UER00295. DR ChiTaRS; IMPDH2; mouse. DR NextBio; 303689; -. DR PRO; PR:P24547; -. DR ArrayExpress; P24547; -. DR Bgee; P24547; -. DR CleanEx; MM_IMPDH2; -. DR Genevestigator; P24547; -. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. DR GO; GO:0005634; C:nucleus; ISS:UniProtKB. DR GO; GO:0030554; F:adenyl nucleotide binding; IEA:InterPro. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0003938; F:IMP dehydrogenase activity; IDA:MGI. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0000166; F:nucleotide binding; ISS:UniProtKB. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW. DR GO; GO:0071353; P:cellular response to interleukin-4; IDA:MGI. DR GO; GO:0006177; P:GMP biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0046651; P:lymphocyte proliferation; IMP:MGI. DR GO; GO:0051289; P:protein homotetramerization; IEA:Ensembl. DR GO; GO:0006164; P:purine nucleotide biosynthetic process; IMP:MGI. DR GO; GO:0060041; P:retina development in camera-type eye; IEA:Ensembl. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_01964; IMPDH; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000644; CBS_dom. DR InterPro; IPR005990; IMP_DH. DR InterPro; IPR015875; IMP_DH/GMP_Rdtase_CS. DR InterPro; IPR001093; IMP_DH_GMPRt. DR PANTHER; PTHR11911:SF6; PTHR11911:SF6; 1. DR Pfam; PF00571; CBS; 2. DR Pfam; PF00478; IMPDH; 1. DR PIRSF; PIRSF000130; IMPDH; 1. DR SMART; SM00116; CBS; 2. DR TIGRFAMs; TIGR01302; IMP_dehydrog; 1. DR PROSITE; PS51371; CBS; 2. DR PROSITE; PS00487; IMP_DH_GMP_RED; 1. PE 1: Evidence at protein level; KW Acetylation; CBS domain; Complete proteome; Cytoplasm; KW Direct protein sequencing; DNA-binding; GMP biosynthesis; KW Metal-binding; NAD; Nucleus; Oxidoreductase; Phosphoprotein; KW Potassium; Purine biosynthesis; Reference proteome; Repeat; KW RNA-binding. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 514 Inosine-5'-monophosphate dehydrogenase 2. FT /FTId=PRO_0000093674. FT DOMAIN 114 173 CBS 1. FT DOMAIN 179 237 CBS 2. FT NP_BIND 274 276 NAD (By similarity). FT NP_BIND 324 326 NAD (By similarity). FT REGION 364 366 IMP binding (By similarity). FT REGION 387 388 IMP binding (By similarity). FT REGION 411 415 IMP binding (By similarity). FT ACT_SITE 331 331 Thioimidate intermediate (By similarity). FT METAL 326 326 Potassium; via carbonyl oxygen (By FT similarity). FT METAL 328 328 Potassium; via carbonyl oxygen (By FT similarity). FT METAL 331 331 Potassium; via carbonyl oxygen (By FT similarity). FT METAL 500 500 Potassium; via carbonyl oxygen; shared FT with tetrameric partner (By similarity). FT METAL 501 501 Potassium; via carbonyl oxygen; shared FT with tetrameric partner (By similarity). FT METAL 502 502 Potassium; via carbonyl oxygen; shared FT with tetrameric partner (By similarity). FT BINDING 329 329 IMP (By similarity). FT BINDING 441 441 IMP (By similarity). FT MOD_RES 122 122 Phosphoserine (By similarity). FT MOD_RES 400 400 Phosphotyrosine (By similarity). FT MOD_RES 416 416 Phosphoserine (By similarity). FT MOD_RES 511 511 N6-acetyllysine (By similarity). FT VARIANT 333 333 T -> I (in mycophenolic acid resistant FT cells). FT VARIANT 351 351 S -> Y (in mycophenolic acid resistant FT cells). FT CONFLICT 458 458 P -> L (in Ref. 4; AA sequence). FT CONFLICT 465 465 Q -> S (in Ref. 4; AA sequence). FT CONFLICT 483 483 M -> T (in Ref. 1; AAA39311). SQ SEQUENCE 514 AA; 55815 MW; 17D25A5C5EBCC439 CRC64; MADYLISGGT SYVPDDGLTA QQLFNCGDGL TYNDFLILPG YIDFTADQVD LTSALTKKIT LKTPLVSSPM DTVTEAGMAI AMALTGGIGF IHHNCTPEFQ ANEVRKVKKY EQGFITDPVV LSPKDRVRDV FEAKARHGFC GIPITDTGRM GSRLVGIISS RDIDFLKEEE HDRFLEEIMT KREDLVVAPA GVTLKEANEI LQRSKKGKLP IVNENDELVA IIARTDLKKN RDYPLASKDA KKQLLCGAAI GTHEDDKYRL DLLALAGVDV VVLDSSQGNS IFQINMIKYI KEKYPSLQVI GGNVVTAAQA KNLIDAGVDA LRVGMGSGSI CITQEVLACG RPQATAVYKV SEYARRFGVP VIADGGIQNV GHIAKALALG ASTVMMGSLL AATTEAPGEY FFSDGIRLKK YRGMGSLDAM DKHLSSQNRY FSEADKIKVA QGVSGAVQDK GSIHKFVPYL IAGIQHSCQD IGAKSLTQVR AMMYSGELKF EKRTSSAQVE GGVHSLHSYE KRLF // ID IMDH1_MOUSE Reviewed; 514 AA. AC P50096; Q7TSG7; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 2. DT 19-FEB-2014, entry version 119. DE RecName: Full=Inosine-5'-monophosphate dehydrogenase 1; DE Short=IMP dehydrogenase 1; DE Short=IMPD 1; DE Short=IMPDH 1; DE EC=1.1.1.205; DE AltName: Full=IMPDH-I; GN Name=Impdh1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Leukemia; RX PubMed=7690562; DOI=10.1006/bbrc.1993.2129; RA Dayton J.S., Mitchell B.S.; RT "Type I inosine monophosphate dehydrogenase: evidence for a single RT functional gene in mammalian species."; RL Biochem. Biophys. Res. Commun. 195:897-901(1993). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=NOD; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: Catalyzes the conversion of inosine 5'-phosphate (IMP) CC to xanthosine 5'-phosphate (XMP), the first committed and rate- CC limiting step in the de novo synthesis of guanine nucleotides, and CC therefore plays an important role in the regulation of cell CC growth. Could also have a single-stranded nucleic acid-binding CC activity and could play a role in RNA and/or DNA metabolism. It CC may also have a role in the development of malignancy and the CC growth progression of some tumors (By similarity). CC -!- CATALYTIC ACTIVITY: Inosine 5'-phosphate + NAD(+) + H(2)O = CC xanthosine 5'-phosphate + NADH. CC -!- COFACTOR: Potassium (By similarity). CC -!- ENZYME REGULATION: Mycophenolic acid (MPA) is a non-competitive CC inhibitor that prevents formation of the closed enzyme CC conformation by binding to the same site as the amobile flap. In CC contrast, mizoribine monophosphate (MZP) is a competitive CC inhibitor that induces the closed conformation. MPA is a potent CC inhibitor of mammalian IMPDHs but a poor inhibitor of the CC bacterial enzymes. MZP is a more potent inhibitor of bacterial CC IMPDH (By similarity). CC -!- PATHWAY: Purine metabolism; XMP biosynthesis via de novo pathway; CC XMP from IMP: step 1/1. CC -!- SUBUNIT: Homotetramer. CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By CC similarity). CC -!- SIMILARITY: Belongs to the IMPDH/GMPR family. CC -!- SIMILARITY: Contains 2 CBS domains. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00978; AAA18285.1; -; mRNA. DR EMBL; AK171139; BAE42272.1; -; mRNA. DR EMBL; CH466533; EDL13790.1; -; Genomic_DNA. DR EMBL; BC053416; AAH53416.1; -; mRNA. DR RefSeq; NP_035959.2; NM_011829.2. DR UniGene; Mm.260707; -. DR ProteinModelPortal; P50096; -. DR SMR; P50096; 10-514. DR BioGrid; 204791; 2. DR IntAct; P50096; 1. DR MINT; MINT-4098666; -. DR STRING; 10090.ENSMUSP00000077289; -. DR BindingDB; P50096; -. DR PhosphoSite; P50096; -. DR PaxDb; P50096; -. DR PRIDE; P50096; -. DR Ensembl; ENSMUST00000078155; ENSMUSP00000077289; ENSMUSG00000003500. DR Ensembl; ENSMUST00000159124; ENSMUSP00000124931; ENSMUSG00000003500. DR Ensembl; ENSMUST00000162099; ENSMUSP00000124541; ENSMUSG00000003500. DR GeneID; 23917; -. DR KEGG; mmu:23917; -. DR UCSC; uc009bda.1; mouse. DR CTD; 3614; -. DR MGI; MGI:96567; Impdh1. DR eggNOG; COG0517; -. DR GeneTree; ENSGT00530000062923; -. DR HOGENOM; HOG000165752; -. DR HOVERGEN; HBG052122; -. DR InParanoid; Q7TSG7; -. DR KO; K00088; -. DR TreeFam; TF300378; -. DR UniPathway; UPA00601; UER00295. DR NextBio; 303685; -. DR PRO; PR:P50096; -. DR ArrayExpress; P50096; -. DR Bgee; P50096; -. DR CleanEx; MM_IMPDH1; -. DR Genevestigator; P50096; -. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. DR GO; GO:0005634; C:nucleus; ISS:UniProtKB. DR GO; GO:0030554; F:adenyl nucleotide binding; IEA:InterPro. DR GO; GO:0003677; F:DNA binding; ISS:UniProtKB. DR GO; GO:0003938; F:IMP dehydrogenase activity; IDA:MGI. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006177; P:GMP biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0046651; P:lymphocyte proliferation; IMP:MGI. DR GO; GO:0006164; P:purine nucleotide biosynthetic process; IMP:MGI. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_01964; IMPDH; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000644; CBS_dom. DR InterPro; IPR005990; IMP_DH. DR InterPro; IPR015875; IMP_DH/GMP_Rdtase_CS. DR InterPro; IPR001093; IMP_DH_GMPRt. DR PANTHER; PTHR11911:SF6; PTHR11911:SF6; 1. DR Pfam; PF00571; CBS; 2. DR Pfam; PF00478; IMPDH; 1. DR PIRSF; PIRSF000130; IMPDH; 1. DR SMART; SM00116; CBS; 2. DR TIGRFAMs; TIGR01302; IMP_dehydrog; 1. DR PROSITE; PS51371; CBS; 2. DR PROSITE; PS00487; IMP_DH_GMP_RED; 1. PE 2: Evidence at transcript level; KW CBS domain; Complete proteome; Cytoplasm; GMP biosynthesis; KW Metal-binding; NAD; Nucleus; Oxidoreductase; Potassium; KW Purine biosynthesis; Reference proteome; Repeat. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 514 Inosine-5'-monophosphate dehydrogenase 1. FT /FTId=PRO_0000093671. FT DOMAIN 114 173 CBS 1. FT DOMAIN 179 237 CBS 2. FT NP_BIND 274 276 NAD (By similarity). FT NP_BIND 324 326 NAD (By similarity). FT REGION 364 366 IMP binding (By similarity). FT REGION 387 388 IMP binding (By similarity). FT REGION 411 415 IMP binding (By similarity). FT ACT_SITE 331 331 Thioimidate intermediate (By similarity). FT METAL 326 326 Potassium; via carbonyl oxygen (By FT similarity). FT METAL 328 328 Potassium; via carbonyl oxygen (By FT similarity). FT METAL 331 331 Potassium; via carbonyl oxygen (By FT similarity). FT METAL 500 500 Potassium; via carbonyl oxygen; shared FT with tetrameric partner (By similarity). FT METAL 501 501 Potassium; via carbonyl oxygen; shared FT with tetrameric partner (By similarity). FT METAL 502 502 Potassium; via carbonyl oxygen; shared FT with tetrameric partner (By similarity). FT BINDING 329 329 IMP (By similarity). FT BINDING 441 441 IMP (By similarity). FT CONFLICT 21 22 QQ -> HE (in Ref. 1; AAA18285). FT CONFLICT 273 273 L -> H (in Ref. 1; AAA18285). FT CONFLICT 414 414 M -> I (in Ref. 1; AAA18285). SQ SEQUENCE 514 AA; 55279 MW; 69E2DD40F03701F2 CRC64; MADYLISGGT GYVPEDGLTA QQLFANADGL TYNDFLILPG FIDFIADEVD LTSALTRKIT LKTPLISSPM DTVTEADMAI AMALMGGIGF IHHNCTPEFQ ANEVRKVKKF EQGFITDPVV LSPSHTVGDV LEAKIQHGFS GIPITATGTM GSKLVGIVTS RDIDFLAEKD HTTLLSEVMT PRVELVVAPA GVTLKEANEI LQRSKKGKLP IVNDQDELVA IIARTDLKKN RDYPLASKDS HKQLLCGAAV GTREDDKYRL DLLTQAGADV IVLDSSQGNS VYQIAMVHYI KQKYPHLQVI GGNVVTAAQA KNLIDAGVDG LRVGMGCGSI CITQEVMACG RPQGTAVYKV AEYARRFGVP VIADGGIQTV GHVVKALALG ASTVMMGSLL AATTEAPGEY FFSDGVRLKK YRGMGSLDAM EKSSSSQKRY FSEGDKVKIA QGVSGSIQDK GSIQKFVPYL IAGIQHGCQD IGAQSLSVLR SMMYSGELKF EKRTMSAQIE GGVHGLHSYE KRLY // ID IOD1_MOUSE Reviewed; 257 AA. AC Q61153; Q05CY5; Q5FW63; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 26-FEB-2008, sequence version 3. DT 19-MAR-2014, entry version 104. DE RecName: Full=Type I iodothyronine deiodinase; DE EC=1.97.1.10; DE AltName: Full=5DI; DE AltName: Full=DIOI; DE AltName: Full=Type 1 DI; DE AltName: Full=Type-I 5'-deiodinase; GN Name=Dio1; Synonyms=Itdi1, Txdi1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=C57BL/6J; RX PubMed=7476994; DOI=10.1210/me.9.8.969; RA Maia A.L., Berry M.J., Sabbag R., Harney J.W., Larsen P.R.; RT "Structural and functional differences in the dio1 gene in mice with RT inherited type 1 deiodinase deficiency."; RL Mol. Endocrinol. 9:969-980(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Liver; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: Responsible for the deiodination of T4 (3,5,3',5'- CC tetraiodothyronine) into T3 (3,5,3'-triiodothyronine) and of T3 CC into T2 (3,3'-diiodothyronine). CC -!- CATALYTIC ACTIVITY: 3,5,3'-triiodo-L-thyronine + iodide + A + H(+) CC = L-thyroxine + AH(2). CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass CC membrane protein (By similarity). CC -!- SIMILARITY: Belongs to the iodothyronine deiodinase family. CC -!- SEQUENCE CAUTION: CC Sequence=AAB00228.1; Type=Erroneous termination; Positions=126; Note=Translated as Sec; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U49861; AAB00228.1; ALT_SEQ; mRNA. DR EMBL; BC019786; AAH19786.1; -; mRNA. DR EMBL; BC089608; AAH89608.1; -; mRNA. DR RefSeq; NP_031886.3; NM_007860.3. DR UniGene; Mm.148342; -. DR ProteinModelPortal; Q61153; -. DR SMR; Q61153; 88-247. DR STRING; 10090.ENSMUSP00000081007; -. DR PaxDb; Q61153; -. DR PRIDE; Q61153; -. DR Ensembl; ENSMUST00000082426; ENSMUSP00000081007; ENSMUSG00000034785. DR Ensembl; ENSMUST00000150974; ENSMUSP00000117751; ENSMUSG00000034785. DR GeneID; 13370; -. DR KEGG; mmu:13370; -. DR UCSC; uc008tzq.1; mouse. DR CTD; 1733; -. DR MGI; MGI:94896; Dio1. DR eggNOG; NOG67608; -. DR GeneTree; ENSGT00740000115645; -. DR HOGENOM; HOG000169547; -. DR HOVERGEN; HBG000099; -. DR InParanoid; Q61153; -. DR KO; K01562; -. DR OrthoDB; EOG751NHS; -. DR TreeFam; TF329721; -. DR BioCyc; MetaCyc:MONOMER-16138; -. DR SABIO-RK; Q61153; -. DR NextBio; 283716; -. DR PRO; PR:Q61153; -. DR ArrayExpress; Q61153; -. DR Bgee; Q61153; -. DR CleanEx; MM_DIO1; -. DR Genevestigator; Q61153; -. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0008430; F:selenium binding; IDA:MGI. DR GO; GO:0004800; F:thyroxine 5'-deiodinase activity; IDA:UniProtKB. DR GO; GO:0042446; P:hormone biosynthetic process; IEA:UniProtKB-KW. DR Gene3D; 3.40.30.10; -; 1. DR InterPro; IPR000643; Iodothyronine_deiodinase. DR InterPro; IPR008261; Iodothyronine_deiodinase_AS. DR InterPro; IPR027252; Iodothyronine_deiodinase_I/III. DR InterPro; IPR012336; Thioredoxin-like_fold. DR PANTHER; PTHR11781; PTHR11781; 1. DR Pfam; PF00837; T4_deiodinase; 1. DR PIRSF; PIRSF001330; IOD; 1. DR PIRSF; PIRSF500144; IODI_III; 1. DR SUPFAM; SSF52833; SSF52833; 1. DR PROSITE; PS01205; T4_DEIODINASE; 1. PE 2: Evidence at transcript level; KW Complete proteome; Endoplasmic reticulum; Membrane; Oxidoreductase; KW Reference proteome; Selenocysteine; Thyroid hormones biosynthesis; KW Transmembrane; Transmembrane helix. FT CHAIN 1 257 Type I iodothyronine deiodinase. FT /FTId=PRO_0000154312. FT TRANSMEM 13 33 Helical; (Potential). FT ACT_SITE 126 126 FT NON_STD 126 126 Selenocysteine. FT CONFLICT 167 167 N -> K (in Ref. 1; AAB00228). FT CONFLICT 171 171 I -> V (in Ref. 1; AAB00228). FT CONFLICT 186 186 L -> M (in Ref. 1; AAB00228 and 2; FT AAH89608). FT CONFLICT 193 193 Q -> R (in Ref. 2; AAH19786). FT CONFLICT 225 225 C -> R (in Ref. 2; AAH19786). FT CONFLICT 240 240 V -> L (in Ref. 1; AAB00228). SQ SEQUENCE 257 AA; 29568 MW; DF569BDFF7A4257A CRC64; MGLPQLWLWL KRLVIFLQVA LEVAVGKVLM TLFPGRVKQS ILAMGQKTGM ARNPRFAPDN WVPTFFSIQY FWFVLKVRWQ RLEDRAEFGG LAPNCTVVCL SGQKCNIWDF IQGSRPLVLN FGSCTUPSFL LKFDQFKRLV DDFASTADFL IIYIEEAHAT DGWAFKNNVD IRQHRSLQER VRAARLLLAR SPQCPVVVDT MQNQSSQLYA ALPERLYVIQ EGRICYKGKA GPWNYNPEEV RAVLEKLCTP PRHVPQL // ID IOD2_MOUSE Reviewed; 266 AA. AC Q9Z1Y9; Q05A70; Q9JHH1; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 26-FEB-2008, sequence version 4. DT 19-MAR-2014, entry version 110. DE RecName: Full=Type II iodothyronine deiodinase; DE EC=1.97.1.10; DE AltName: Full=5DII; DE AltName: Full=DIOII; DE AltName: Full=Type 2 DI; DE AltName: Full=Type-II 5'-deiodinase; GN Name=Dio2; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Brain; RX PubMed=9927339; DOI=10.1210/en.140.2.1022; RA Davey J.C., Schneider M.J., Becker K.B., Galton V.A.; RT "Cloning of a 5.8 kb cDNA for a mouse type 2 deiodinase."; RL Endocrinology 140:1022-1025(1999). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE RP SPECIFICITY. RC STRAIN=C3H/HeN; TISSUE=Brain; RX PubMed=10715551; DOI=10.1016/S0303-7207(99)00249-X; RA Song S., Sorimachi K., Adachi K., Oka T.; RT "Biochemical and molecular biological evidence for the presence of RT type II iodothyronine deiodinase in mouse mammary gland."; RL Mol. Cell. Endocrinol. 160:173-181(2000). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Cochlea; RX PubMed=10655523; DOI=10.1073/pnas.97.3.1287; RA Campos-Barros A., Amma L.L., Faris J.S., Shailam R., Kelley M.W., RA Forrest D.; RT "Type 2 iodothyronine deiodinase expression in the cochlea before the RT onset of hearing."; RL Proc. Natl. Acad. Sci. U.S.A. 97:1287-1292(2000). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: Responsible for the deiodination of T4 (3,5,3',5'- CC tetraiodothyronine) into T3 (3,5,3'-triiodothyronine). Essential CC for providing the brain with appropriate levels of T3 during the CC critical period of development (By similarity). CC -!- CATALYTIC ACTIVITY: 3,5,3'-triiodo-L-thyronine + iodide + A + H(+) CC = L-thyroxine + AH(2). CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=1.1 nM for T4; CC -!- SUBUNIT: Interacts with USP20 and USP33. Interacts with MARCH6 (By CC similarity). CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein CC (Potential). CC -!- TISSUE SPECIFICITY: Expressed in mammary gland and in brain. CC -!- PTM: Ubiquitinated by MARCH6, leading to its degradation by the CC proteasome. Deubiquitinated by USP20 and USP33 (By similarity). CC -!- SIMILARITY: Belongs to the iodothyronine deiodinase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF096875; AAD11422.1; -; mRNA. DR EMBL; AF177196; AAD53113.1; -; mRNA. DR EMBL; AF093137; AAF00069.2; -; mRNA. DR EMBL; BC125383; AAI25384.1; -; mRNA. DR EMBL; BC125385; AAI25386.1; -; mRNA. DR RefSeq; NP_034180.1; NM_010050.2. DR UniGene; Mm.21389; -. DR UniGene; Mm.408815; -. DR ProteinModelPortal; Q9Z1Y9; -. DR PRIDE; Q9Z1Y9; -. DR Ensembl; ENSMUST00000082432; ENSMUSP00000081013; ENSMUSG00000007682. DR GeneID; 13371; -. DR KEGG; mmu:13371; -. DR UCSC; uc007okf.1; mouse. DR CTD; 1734; -. DR MGI; MGI:1338833; Dio2. DR eggNOG; NOG146259; -. DR GeneTree; ENSGT00730000110840; -. DR HOGENOM; HOG000007088; -. DR HOVERGEN; HBG000099; -. DR InParanoid; Q9Z1Y9; -. DR KO; K17904; -. DR OMA; AFERVCI; -. DR OrthoDB; EOG7XPZ7H; -. DR TreeFam; TF329721; -. DR BRENDA; 1.97.1.10; 3474. DR ChiTaRS; DIO2; mouse. DR NextBio; 283720; -. DR PRO; PR:Q9Z1Y9; -. DR ArrayExpress; Q9Z1Y9; -. DR Bgee; Q9Z1Y9; -. DR CleanEx; MM_DIO2; -. DR Genevestigator; Q9Z1Y9; -. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004800; F:thyroxine 5'-deiodinase activity; IDA:UniProtKB. DR GO; GO:0042446; P:hormone biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0042404; P:thyroid hormone catabolic process; IMP:MGI. DR GO; GO:0070460; P:thyroid-stimulating hormone secretion; TAS:UniProtKB. DR Gene3D; 3.40.30.10; -; 1. DR InterPro; IPR000643; Iodothyronine_deiodinase. DR InterPro; IPR008261; Iodothyronine_deiodinase_AS. DR InterPro; IPR012336; Thioredoxin-like_fold. DR PANTHER; PTHR11781; PTHR11781; 1. DR Pfam; PF00837; T4_deiodinase; 1. DR SUPFAM; SSF52833; SSF52833; 1. DR PROSITE; PS01205; T4_DEIODINASE; 1. PE 1: Evidence at protein level; KW Complete proteome; Membrane; Oxidoreductase; Reference proteome; KW Selenocysteine; Thyroid hormones biosynthesis; Transmembrane; KW Transmembrane helix; Ubl conjugation. FT CHAIN 1 266 Type II iodothyronine deiodinase. FT /FTId=PRO_0000154318. FT TRANSMEM 10 34 Helical; (Potential). FT ACT_SITE 130 130 FT NON_STD 130 130 Selenocysteine. FT NON_STD 263 263 Selenocysteine. SQ SEQUENCE 266 AA; 29929 MW; B2FD28E171DC5486 CRC64; MGLLSVDLLI TLQILPVFFS NCLFLALYDS VILLKHVALL LSRSKSTRGE WRRMLTSEGL RCVWNSFLLD AYKQVKLGED APNSSVVHVS NPESGNNYAS EKTADGAECH LLDFASAERP LVVNFGSATU PPFTRQLPAF RQLVEEFSSV ADFLLVYIDE AHPSDGWAVP GDSSLSFEVK KHRNQEDRCA AAHQLLERFS LPPQCQVVAD RMDNNANVAY GVAFERVCIV QRRKIAYLGG KGPFSYNLQE VRSWLEKNFS KRUILD // ID IOD3_MOUSE Reviewed; 278 AA. AC Q91ZI8; Q3UKD2; DT 11-JUL-2002, integrated into UniProtKB/Swiss-Prot. DT 26-FEB-2008, sequence version 3. DT 19-MAR-2014, entry version 111. DE RecName: Full=Type III iodothyronine deiodinase; DE EC=1.97.1.11; DE AltName: Full=5DIII; DE AltName: Full=DIOIII; DE AltName: Full=Type 3 DI; DE AltName: Full=Type-III 5'-deiodinase; GN Name=Dio3; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=129/SvJ; RX PubMed=9886816; DOI=10.1210/en.140.1.124; RA Hernandez A., Lyon G.J., Schneider M.J., St Germain D.L.; RT "Isolation and characterization of the mouse gene for the type 3 RT iodothyronine deiodinase."; RL Endocrinology 140:124-130(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Head, and Placenta; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: Responsible for the deiodination of T4 (3,5,3',5'- CC tetraiodothyronine) into RT3 (3,3',5'-triiodothyronine) and of T3 CC (3,5,3'-triiodothyronine) into T2 (3,3'-diiodothyronine). RT3 and CC T2 are inactive metabolites. May play a role in preventing CC premature exposure of developing fetal tissues to adult levels of CC thyroid hormones. Can regulate circulating fetal thyroid hormone CC concentrations throughout gestation. Essential role for regulation CC of thyroid hormone inactivation during embryological development CC (By similarity). CC -!- CATALYTIC ACTIVITY: 3,3',5'-triiodo-L-thyronine + iodide + A + CC H(+) = L-thyroxine + AH(2). CC -!- SUBUNIT: Homodimer. May undergo minor heretodimerization with DIO1 CC and DIO2 (By similarity). CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane CC protein (By similarity). Endosome membrane; Single-pass type II CC membrane protein (By similarity). CC -!- SIMILARITY: Belongs to the iodothyronine deiodinase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF426023; AAL23960.1; -; Genomic_DNA. DR EMBL; AK140797; BAE24483.1; -; mRNA. DR EMBL; AK146060; BAE26869.1; -; mRNA. DR EMBL; BC106847; AAI06848.1; -; mRNA. DR EMBL; BC106848; AAI06849.1; -; mRNA. DR RefSeq; NP_742117.2; NM_172119.2. DR UniGene; Mm.154427; -. DR ProteinModelPortal; Q91ZI8; -. DR SMR; Q91ZI8; 103-266. DR PRIDE; Q91ZI8; -. DR GeneID; 107585; -. DR KEGG; mmu:107585; -. DR CTD; 1735; -. DR MGI; MGI:1306782; Dio3. DR eggNOG; NOG297144; -. DR HOGENOM; HOG000007088; -. DR HOVERGEN; HBG000099; -. DR InParanoid; Q91ZI8; -. DR KO; K07754; -. DR NextBio; 359086; -. DR PRO; PR:Q91ZI8; -. DR Bgee; Q91ZI8; -. DR CleanEx; MM_DIO3; -. DR Genevestigator; Q91ZI8; -. DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0004800; F:thyroxine 5'-deiodinase activity; IMP:MGI. DR GO; GO:0033798; F:thyroxine 5-deiodinase activity; IDA:UniProtKB. DR GO; GO:0042446; P:hormone biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0040018; P:positive regulation of multicellular organism growth; IMP:MGI. DR GO; GO:0042404; P:thyroid hormone catabolic process; IMP:MGI. DR Gene3D; 3.40.30.10; -; 1. DR InterPro; IPR000643; Iodothyronine_deiodinase. DR InterPro; IPR008261; Iodothyronine_deiodinase_AS. DR InterPro; IPR027252; Iodothyronine_deiodinase_I/III. DR InterPro; IPR012336; Thioredoxin-like_fold. DR PANTHER; PTHR11781; PTHR11781; 1. DR Pfam; PF00837; T4_deiodinase; 1. DR PIRSF; PIRSF001330; IOD; 1. DR PIRSF; PIRSF500144; IODI_III; 1. DR SUPFAM; SSF52833; SSF52833; 1. DR PROSITE; PS01205; T4_DEIODINASE; 1. PE 2: Evidence at transcript level; KW Cell membrane; Complete proteome; Endosome; Membrane; Oxidoreductase; KW Reference proteome; Selenocysteine; Signal-anchor; KW Thyroid hormones biosynthesis; Transmembrane; Transmembrane helix. FT CHAIN 1 278 Type III iodothyronine deiodinase. FT /FTId=PRO_0000154324. FT TOPO_DOM 1 16 Cytoplasmic (Potential). FT TRANSMEM 17 36 Helical; Signal-anchor for type II FT membrane protein; (Potential). FT TOPO_DOM 37 278 Extracellular (Potential). FT ACT_SITE 144 144 FT NON_STD 144 144 Selenocysteine. SQ SEQUENCE 278 AA; 31665 MW; F93174A0EE3E7A6F CRC64; MLRSLLLHSL RLCAQTASCL VLFPRFLGTA FMLWLLDFLC IRKHFLRRRH PDHPEPEVEL NSEGEEMPPD DPPICVSDDN RLCTLASLKA VWHGQKLDFF KQAHEGGPAP NSEVVRPDGF QSQRILDYAQ GTRPLVLNFG SCTUPPFMAR MSAFQRLVTK YQRDVDFLII YIEEAHPSDG WVTTDSPYVI PQHRSLEDRV SAARVLQQGA PGCALVLDTM ANSSSSAYGA YFERLYVIQS GTIMYQGGRG PDGYQVSELR TWLERYDEQL HGTRPHRF // ID IVD_MOUSE Reviewed; 424 AA. AC Q9JHI5; Q9CYI3; Q9DBD7; DT 24-MAY-2005, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 19-MAR-2014, entry version 113. DE RecName: Full=Isovaleryl-CoA dehydrogenase, mitochondrial; DE Short=IVD; DE EC=1.3.8.4; DE Flags: Precursor; GN Name=Ivd; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. RC STRAIN=129/Ola; RX PubMed=11404023; DOI=10.1016/S0378-1119(01)00466-8; RA Willard J.M., Reinard T., Mohsen A.W., Vockley J.; RT "Cloning of genomic and cDNA for mouse isovaleryl-CoA dehydrogenase RT (IVD) and evolutionary comparison to other known IVDs."; RL Gene 270:253-257(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Liver; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Kidney, and Salivary gland; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP PROTEIN SEQUENCE OF 57-76; 154-178; 212-221; 231-239; 273-285; RP 339-346; 400-411 AND 418-424, AND MASS SPECTROMETRY. RC STRAIN=C57BL/6; TISSUE=Brain; RA Lubec G., Kang S.U.; RL Submitted (APR-2007) to UniProtKB. RN [5] RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-56; LYS-65; LYS-76; RP LYS-260 AND LYS-316, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE RP SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., RA Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). RN [6] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-56; LYS-65; LYS-76; LYS-239 RP AND LYS-260, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Liver; RX PubMed=23576753; DOI=10.1073/pnas.1302961110; RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., RA Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.; RT "Label-free quantitative proteomics of the lysine acetylome in RT mitochondria identifies substrates of SIRT3 in metabolic pathways."; RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013). CC -!- CATALYTIC ACTIVITY: Isovaleryl-CoA + electron-transfer CC flavoprotein = 3-methylcrotonyl-CoA + reduced electron-transfer CC flavoprotein. CC -!- COFACTOR: FAD. CC -!- PATHWAY: Amino-acid degradation; L-leucine degradation; (S)-3- CC hydroxy-3-methylglutaryl-CoA from 3-isovaleryl-CoA: step 1/3. CC -!- SUBUNIT: Homotetramer (By similarity). CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix. CC -!- PTM: Acetylation of Lys-76 is observed in liver mitochondria from CC fasted mice but not from fed mice. CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF225989; AAF35888.1; -; mRNA. DR EMBL; AF226043; AAF67667.1; -; Genomic_DNA. DR EMBL; AF226039; AAF67667.1; JOINED; Genomic_DNA. DR EMBL; AF226041; AAF67667.1; JOINED; Genomic_DNA. DR EMBL; AF226040; AAF67667.1; JOINED; Genomic_DNA. DR EMBL; AF226042; AAF67667.1; JOINED; Genomic_DNA. DR EMBL; AK005024; BAB23751.1; -; mRNA. DR EMBL; AK017660; BAB30859.1; -; mRNA. DR EMBL; BC018325; AAH18325.1; -; mRNA. DR EMBL; BC027198; AAH27198.1; -; mRNA. DR RefSeq; NP_062800.1; NM_019826.3. DR UniGene; Mm.6635; -. DR ProteinModelPortal; Q9JHI5; -. DR SMR; Q9JHI5; 36-422. DR IntAct; Q9JHI5; 3. DR MINT; MINT-1861781; -. DR PhosphoSite; Q9JHI5; -. DR REPRODUCTION-2DPAGE; IPI00471246; -. DR REPRODUCTION-2DPAGE; Q9JHI5; -. DR UCD-2DPAGE; Q9JHI5; -. DR PaxDb; Q9JHI5; -. DR PRIDE; Q9JHI5; -. DR Ensembl; ENSMUST00000028807; ENSMUSP00000028807; ENSMUSG00000027332. DR GeneID; 56357; -. DR KEGG; mmu:56357; -. DR UCSC; uc008lsv.1; mouse. DR CTD; 3712; -. DR MGI; MGI:1929242; Ivd. DR eggNOG; COG1960; -. DR GeneTree; ENSGT00740000114853; -. DR HOGENOM; HOG000131659; -. DR HOVERGEN; HBG000224; -. DR InParanoid; Q9JHI5; -. DR KO; K00253; -. DR OMA; ADMYTQM; -. DR OrthoDB; EOG74FF0S; -. DR TreeFam; TF105050; -. DR UniPathway; UPA00363; UER00860. DR ChiTaRS; IVD; mouse. DR NextBio; 312370; -. DR PRO; PR:Q9JHI5; -. DR Bgee; Q9JHI5; -. DR CleanEx; MM_IVD; -. DR Genevestigator; Q9JHI5; -. DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell. DR GO; GO:0031966; C:mitochondrial membrane; IEA:Ensembl. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. DR GO; GO:0008470; F:isovaleryl-CoA dehydrogenase activity; IEA:Ensembl. DR GO; GO:0006552; P:leucine catabolic process; IEA:UniProtKB-UniPathway. DR Gene3D; 1.10.540.10; -; 1. DR Gene3D; 2.40.110.10; -; 1. DR InterPro; IPR006089; Acyl-CoA_DH_CS. DR InterPro; IPR006091; Acyl-CoA_Oxase/DH_cen-dom. DR InterPro; IPR009075; AcylCo_DH/oxidase_C. DR InterPro; IPR013786; AcylCoA_DH/ox_N. DR InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom. DR Pfam; PF00441; Acyl-CoA_dh_1; 1. DR Pfam; PF02770; Acyl-CoA_dh_M; 1. DR Pfam; PF02771; Acyl-CoA_dh_N; 1. DR SUPFAM; SSF47203; SSF47203; 1. DR SUPFAM; SSF56645; SSF56645; 1. DR PROSITE; PS00072; ACYL_COA_DH_1; 1. DR PROSITE; PS00073; ACYL_COA_DH_2; 1. PE 1: Evidence at protein level; KW Acetylation; Complete proteome; Direct protein sequencing; FAD; KW Flavoprotein; Mitochondrion; Oxidoreductase; Reference proteome; KW Transit peptide. FT TRANSIT 1 30 Mitochondrion (By similarity). FT CHAIN 31 424 Isovaleryl-CoA dehydrogenase, FT mitochondrial. FT /FTId=PRO_0000000532. FT NP_BIND 163 172 FAD (By similarity). FT NP_BIND 196 198 FAD (By similarity). FT NP_BIND 378 382 FAD (By similarity). FT NP_BIND 407 409 FAD (By similarity). FT REGION 220 221 Substrate binding (By similarity). FT REGION 282 285 Substrate binding (By similarity). FT REGION 405 406 Substrate binding (By similarity). FT ACT_SITE 284 284 Proton acceptor (By similarity). FT BINDING 172 172 Substrate; via carbonyl oxygen (By FT similarity). FT BINDING 275 275 Substrate (By similarity). FT BINDING 310 310 FAD (By similarity). FT BINDING 321 321 FAD (By similarity). FT MOD_RES 56 56 N6-acetyllysine; alternate. FT MOD_RES 56 56 N6-succinyllysine; alternate. FT MOD_RES 65 65 N6-acetyllysine; alternate. FT MOD_RES 65 65 N6-succinyllysine; alternate. FT MOD_RES 76 76 N6-acetyllysine; alternate. FT MOD_RES 76 76 N6-succinyllysine; alternate. FT MOD_RES 239 239 N6-acetyllysine. FT MOD_RES 260 260 N6-acetyllysine; alternate. FT MOD_RES 260 260 N6-succinyllysine; alternate. FT MOD_RES 316 316 N6-succinyllysine. FT CONFLICT 29 29 R -> G (in Ref. 2; BAB23751). FT CONFLICT 41 41 N -> K (in Ref. 2; BAB30859). SQ SEQUENCE 424 AA; 46325 MW; 7B8A556A9E73B0B6 CRC64; MATAIRLLGR RVSSWRLRPS PSPLAVPRRA HSILPVDDDI NGLNEEQKQL RHTISKFLQE NLAPKAQEID QTNDFKNLRE FWKQLGSLGV LGITAPVQYG GSGLGYLEHV LVMEEISRAS GAVGLSYGAH SNLCVNQIVR NGNEAQKEKY LPKLISGEFI GALAMSEPNA GSDVVSMKLK AEKKGDHYVL NGNKFWITNG PDADILVVYA KTDLTAVPAS RGITAFIVEK GMPGFSTSKK LDKLGMRGSN TCELVFEDCK VPAANVLSQE SKGVYVLMSG LDLERLVLAG GPLGIMQAVL DHTIPYLHVR EAFGQKIGQF QLMQGKMADM YTRLMASRQY VYNVAKACDE GHIIPKDCAG VILYAAECAT QVALDGIQCL GGNGYINDFP MGRFLRDAKL YEIGAGTSEV RRLVIGRAFN ADFR // ID IYD1_MOUSE Reviewed; 285 AA. AC Q9DCX8; DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 19-FEB-2014, entry version 83. DE RecName: Full=Iodotyrosine dehalogenase 1; DE Short=IYD-1; DE EC=1.22.1.1; DE Flags: Precursor; GN Name=Iyd; Synonyms=Dehal1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Kidney; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Kidney; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 34-285 IN COMPLEXES WITH RP 3,5-DIIODOTYROSINE; 3-IODO-TYROSINE AND FMN, AND SUBUNIT. RX PubMed=19436071; DOI=10.1074/jbc.M109.013458; RA Thomas S.R., McTamney P.M., Adler J.M., Laronde-Leblanc N., RA Rokita S.E.; RT "Crystal structure of iodotyrosine deiodinase, a novel flavoprotein RT responsible for iodide salvage in thyroid glands."; RL J. Biol. Chem. 284:19659-19667(2009). CC -!- FUNCTION: Catalyzes the oxidative NADPH-dependent deiodination of CC monoiodotyrosine (L-MIT) or diiodotyrosine (L-DIT). Acts during CC the hydrolysis of thyroglobulin to liberate iodide, which can then CC reenter the hormone-producing pathways. Acts more efficiently on CC monoiodotyrosine than on diiodotyrosine (By similarity). CC -!- CATALYTIC ACTIVITY: L-tyrosine + 2 NADP(+) + 2 I(-) = 3,5-diiodo- CC L-tyrosine + 2 NADPH. CC -!- COFACTOR: FMN. CC -!- SUBUNIT: Homodimer (Probable). CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein (By CC similarity). CC -!- SIMILARITY: Belongs to the nitroreductase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK002363; BAB22041.1; -; mRNA. DR EMBL; BC023358; AAH23358.1; -; mRNA. DR RefSeq; NP_081667.1; NM_027391.3. DR UniGene; Mm.24153; -. DR PDB; 3GB5; X-ray; 2.00 A; A=34-285. DR PDB; 3GFD; X-ray; 2.45 A; A/B=34-285. DR PDB; 3GH8; X-ray; 2.61 A; A/B/C/D/E/F/G/H=34-285. DR PDB; 3TNZ; X-ray; 2.25 A; A/B=34-285. DR PDB; 3TO0; X-ray; 2.66 A; A/B=34-285. DR PDBsum; 3GB5; -. DR PDBsum; 3GFD; -. DR PDBsum; 3GH8; -. DR PDBsum; 3TNZ; -. DR PDBsum; 3TO0; -. DR ProteinModelPortal; Q9DCX8; -. DR SMR; Q9DCX8; 66-285. DR IntAct; Q9DCX8; 2. DR MINT; MINT-1857005; -. DR STRING; 10090.ENSMUSP00000019896; -. DR PhosphoSite; Q9DCX8; -. DR PaxDb; Q9DCX8; -. DR PRIDE; Q9DCX8; -. DR Ensembl; ENSMUST00000019896; ENSMUSP00000019896; ENSMUSG00000019762. DR GeneID; 70337; -. DR KEGG; mmu:70337; -. DR UCSC; uc007ehp.1; mouse. DR CTD; 389434; -. DR MGI; MGI:1917587; Iyd. DR eggNOG; COG0778; -. DR GeneTree; ENSGT00390000004348; -. DR HOGENOM; HOG000146731; -. DR HOVERGEN; HBG055004; -. DR InParanoid; Q9DCX8; -. DR KO; K17231; -. DR OMA; HQPWHFV; -. DR OrthoDB; EOG7HMS24; -. DR TreeFam; TF313415; -. DR EvolutionaryTrace; Q9DCX8; -. DR NextBio; 331404; -. DR PRO; PR:Q9DCX8; -. DR Bgee; Q9DCX8; -. DR CleanEx; MM_IYD; -. DR Genevestigator; Q9DCX8; -. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004447; F:iodide peroxidase activity; IDA:MGI. DR Gene3D; 3.40.109.10; -; 1. DR InterPro; IPR000415; Nitroreductase-like. DR Pfam; PF00881; Nitroreductase; 1. DR SUPFAM; SSF55469; SSF55469; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Flavoprotein; FMN; Membrane; NADP; KW Oxidoreductase; Reference proteome; Signal; Transmembrane; KW Transmembrane helix. FT SIGNAL 1 23 Potential. FT CHAIN 24 285 Iodotyrosine dehalogenase 1. FT /FTId=PRO_0000230279. FT TOPO_DOM 24 210 Extracellular (Potential). FT TRANSMEM 211 231 Helical; (Potential). FT TOPO_DOM 232 285 Cytoplasmic (Potential). FT NP_BIND 96 100 FMN. FT NP_BIND 123 125 FMN. FT NP_BIND 232 235 FMN. FT BINDING 100 100 Substrate. FT BINDING 157 157 Substrate. FT BINDING 178 178 Substrate. FT BINDING 275 275 FMN. FT STRAND 69 71 FT HELIX 79 94 FT HELIX 109 119 FT HELIX 125 127 FT STRAND 131 136 FT HELIX 139 151 FT TURN 159 161 FT HELIX 163 169 FT HELIX 170 172 FT HELIX 180 183 FT STRAND 184 193 FT STRAND 203 205 FT HELIX 209 226 FT HELIX 237 239 FT HELIX 240 246 FT STRAND 253 262 FT STRAND 269 271 FT HELIX 278 280 FT STRAND 282 284 SQ SEQUENCE 285 AA; 32814 MW; 7B7415D6C28B1A58 CRC64; MFLLTPVLVA VVCILVVWVF KNADRNLEKK KEEAQVQPWV DEDLKDSTED LQVEEDAEEW QEAEESVEHI PFSHTRYPEQ EMRMRSQEFY ELLNKRRSVR FISSEHVPME VIENVIKAAG TAPSGAHTEP WTFVVVKDPD MKHKIREIIE EEEEINYMKR MGKRWVTDLK KLRTNWIKEY LDTAPVLILI FKQVHGFAAN GKKKVHYYNE ISVSIACGLL LAALQNAGLV TVTTTPLNCG PRLRVLLGRP SHEKLLVLLP VGYPSRDATV PDLKRKALDQ IMVTV // ID JHD2C_MOUSE Reviewed; 2350 AA. AC Q69ZK6; E9QMM8; Q6NV48; Q8BUF5; Q8C4I5; Q8C5Q9; DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 3. DT 19-MAR-2014, entry version 80. DE RecName: Full=Probable JmjC domain-containing histone demethylation protein 2C; DE EC=1.14.11.-; DE AltName: Full=Jumonji domain-containing protein 1C; GN Name=Jmjd1c; Synonyms=Jhdm2c, Kiaa1380; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Embryonic intestine; RX PubMed=15368895; DOI=10.1093/dnares/11.3.205; RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H., RA Nagase T., Ohara O., Koga H.; RT "Prediction of the coding sequences of mouse homologues of KIAA gene: RT IV. The complete nucleotide sequences of 500 mouse KIAA-homologous RT cDNAs identified by screening of terminal sequences of cDNA clones RT randomly sampled from size-fractionated libraries."; RL DNA Res. 11:205-218(2004). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-141; 1112-1832 AND RP 1967-2350. RC STRAIN=C57BL/6J; TISSUE=Cerebellum, Head, and Kidney; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 968-2350. RC STRAIN=C57BL/6J; TISSUE=Embryonic germ cell; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP PROTEIN SEQUENCE OF 1032-1054, AND MASS SPECTROMETRY. RC STRAIN=OF1; TISSUE=Hippocampus; RA Lubec G., Sunyer B., Chen W.-Q.; RL Submitted (JAN-2009) to UniProtKB. RN [6] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006; RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M., RA Thibault P.; RT "The phagosomal proteome in interferon-gamma-activated macrophages."; RL Immunity 30:143-154(2009). CC -!- FUNCTION: Probable histone demethylase that specifically CC demethylates 'Lys-9' of histone H3, thereby playing a central role CC in histone code. Demethylation of Lys residue generates CC formaldehyde and succinate. May be involved in hormone-dependent CC transcriptional activation, by participating in recruitment to CC androgen-receptor target genes (By similarity). CC -!- COFACTOR: Binds 1 Fe(2+) ion per subunit (By similarity). CC -!- SUBCELLULAR LOCATION: Nucleus (By similarity). CC -!- DOMAIN: Leu-Xaa-Xaa-Leu-Leu (LXXLL) motifs are known to mediate CC the association with nuclear receptors (By similarity). CC -!- SIMILARITY: Belongs to the JHDM2 histone demethylase family. CC -!- SIMILARITY: Contains 1 JmjC domain. CC -!- SEQUENCE CAUTION: CC Sequence=AAH68318.1; Type=Frameshift; Positions=1075; CC Sequence=AAH68318.1; Type=Miscellaneous discrepancy; Note=Aberrant splicing; CC Sequence=BAC36783.1; Type=Erroneous termination; Positions=2326; Note=Translated as Leu; CC Sequence=BAC38410.1; Type=Erroneous initiation; Note=Translation N-terminally extended; CC Sequence=BAD32440.1; Type=Erroneous initiation; Note=Translation N-terminally shortened; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK173162; BAD32440.1; ALT_INIT; mRNA. DR EMBL; AC155712; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC156272; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AK077400; BAC36783.1; ALT_SEQ; mRNA. DR EMBL; AK082106; BAC38410.1; ALT_INIT; mRNA. DR EMBL; AK085500; BAC39458.1; -; mRNA. DR EMBL; BC068318; AAH68318.1; ALT_SEQ; mRNA. DR RefSeq; NP_001229325.1; NM_001242396.1. DR RefSeq; XP_006513104.1; XM_006513041.1. DR RefSeq; XP_006513105.1; XM_006513042.1. DR UniGene; Mm.23846; -. DR ProteinModelPortal; Q69ZK6; -. DR SMR; Q69ZK6; 1967-2307. DR BioGrid; 224438; 2. DR IntAct; Q69ZK6; 1. DR PhosphoSite; Q69ZK6; -. DR PaxDb; Q69ZK6; -. DR PRIDE; Q69ZK6; -. DR Ensembl; ENSMUST00000173689; ENSMUSP00000133700; ENSMUSG00000037876. DR GeneID; 108829; -. DR KEGG; mmu:108829; -. DR UCSC; uc007fls.2; mouse. DR CTD; 221037; -. DR MGI; MGI:1918614; Jmjd1c. DR eggNOG; NOG305537; -. DR GeneTree; ENSGT00530000063039; -. DR HOGENOM; HOG000113130; -. DR HOVERGEN; HBG079631; -. DR InParanoid; Q69ZK6; -. DR KO; K11449; -. DR TreeFam; TF324723; -. DR ChiTaRS; JMJD1C; mouse. DR NextBio; 361361; -. DR PRO; PR:Q69ZK6; -. DR ArrayExpress; Q69ZK6; -. DR Bgee; Q69ZK6; -. DR CleanEx; MM_JMJD1C; -. DR Genevestigator; Q69ZK6; -. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0016568; P:chromatin modification; IEA:UniProtKB-KW. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR InterPro; IPR003347; JmjC_dom. DR Pfam; PF02373; JmjC; 1. DR SMART; SM00558; JmjC; 1. DR PROSITE; PS51184; JMJC; 1. PE 1: Evidence at protein level; KW Chromatin regulator; Complete proteome; Dioxygenase; KW Direct protein sequencing; Iron; Metal-binding; Nucleus; KW Oxidoreductase; Phosphoprotein; Reference proteome; Transcription; KW Transcription regulation; Zinc; Zinc-finger. FT CHAIN 1 2350 Probable JmjC domain-containing histone FT demethylation protein 2C. FT /FTId=PRO_0000234375. FT DOMAIN 2084 2308 JmjC. FT ZN_FING 1657 1682 C6-type (Potential). FT MOTIF 1876 1880 LXXLL motif. FT METAL 2146 2146 Iron; catalytic (By similarity). FT METAL 2148 2148 Iron; catalytic (By similarity). FT METAL 2276 2276 Iron; catalytic (By similarity). FT MOD_RES 135 135 Phosphoserine (By similarity). FT MOD_RES 191 191 Phosphoserine (By similarity). FT MOD_RES 194 194 Phosphoserine (By similarity). FT MOD_RES 436 436 Phosphoserine (By similarity). FT MOD_RES 457 457 Phosphoserine (By similarity). FT MOD_RES 460 460 Phosphoserine (By similarity). FT MOD_RES 471 471 Phosphoserine (By similarity). FT MOD_RES 1800 1800 Phosphoserine (By similarity). FT CONFLICT 1506 1506 P -> S (in Ref. 4; AAH68318). FT CONFLICT 1715 1715 L -> P (in Ref. 1; BAD32440). FT CONFLICT 2189 2189 R -> I (in Ref. 1; BAD32440). SQ SEQUENCE 2350 AA; 260639 MW; B17F6FAEB48FBE73 CRC64; MQGPYSLNGY RVRVYRQDSA TQWFTGIITH HDLFTRTMIV MNDQVLEPQN VDPSMVQMTF LDDVVHSLLK GENIGITSRR RSRASQNIST VHGHYTRAQA NSPRPAMNSQ AAVPKQNTHQ QQQQRSIRPN KRKGSDSSIP DEEKMKEDKY DCVSRGENPK GKNKHVVTKR RKPEEAEKRL SMKRLRTDNA SDASESSDAE SSSKRVTETS SSEPMPEYEP KNKVTSKVNG EEGQSQAAEE AGEETLIDTR PPWDQMQEDK NHNEGEKPKS TDSHLQDKMT LRSSEQATVA DHNSNDSVLQ ECNVENQRTV ELLPKDRLVS RTPTPKCVTD IKNDTHSERA AQENLNTFGL QTPENMDPNV SDSKHSNAKY LETAKQDCDQ SWVSDVVKVD LTQSSVTNAP SGSDKRDTEK ERNHYVSYMS SLSAVSVTED QLHKRSPPPE TIKAKLTTSV DTQKAKSSSS PEVVKPKITH SPDSVKSKAA YGNSQAVGER RLANKIEHEL SRGSFHPVPT RGSALETTKS PLIIDKNEHF TVYRDPALIG SETGANHISP FLSQHPFSLH SSSHRTCLNP GTHHPALTPG PHLLAGSTSQ TPLPTINTHP LTSGPHHPVH HPHLLPTVLP GVPTASLLGG HPRLESAHAS SLSHLALAHQ QQQQLLQHQS PHLLGQAHPS ASYNQLGLYP IIWQYPNGTH AYSGLGLPSS KWVHPENAVN AEASLRRNSP SPWLHQPTPV TSADGIGLLS HIPVRPSSAE PHRPHKITVH SSPPLTKTLA DHHKEELERK AFMEPLRSNA STSVKGDLDL NRSQAGKDCH LHRHFVGPRP PQETGERLNK YKEEHRRILQ ESIDVAPFTT KIKGHEVERE NYSRVVPSSS SPKSHAIKQD KDVDRSVSEI YKMKHSVPQS LPQSNYFTTL SNSVVNEPPR SYPSKEVSNI YTEKQNNNLS ATANPQTHSF ISSLSKPPPL IKHQPESESL VGKIPDHLPH QSASHSVTTF RSDCRSPTHL TVSSTNALRS MPALHRAPVF HPPIHHSLER KESSYSSLSP PTLTPVMPVN AGGKVQESQK PPTLIPEPKD SQSNFKNSSD QSLTEMWRSN NNLNREKAEW PVEKSSGKSQ AAVASVIVRP PSSTKVDSVP SVPLASKDRV CERSSSGANK TDYLKPEAGE TGRIILPNVN LESAHVKSEK NFEAVSQGNV PVSVMSAVNV VSTTKADVFT SAATTTSVSS LSSAETSYSL SNTISASTPF ECTSSKSVVS QAVAQAKDCT VSTAVPGTLA CSKTGSAVQP GSGFSGTTDF IHLKKHKAAL AAAQFKNSSV SEAELNTVRN QTVAASLPLD STMTCTASNK AISVGNGPAA QSSQPNYHTK LKKAWLTRHS EEDKNTNKME NSGNSVSEII KPCSVNLIAS TSNDIENRAD GRVAVDKYGR DEKVSRRKAK RTYESGSESG DSDESESKSE QRTKRQPKPT YKKKQNDLQK RKGEVEEDSK PNGVLSRSAK DKSKLKLQNS NSAGVPRSVL KDWRKVKKLK QTGESFLQDD SCCEIGPNLQ KCRECRLIRS KKGEESTHSP VFCRFYYFRR LSFSKNGVVR IDGFSSPDQY DDEAMSLWTH ENYEDDEVDV ETSKYILDII GDKFCQLVTS EKTALSWVKK DAKIAWKRAV RGVREMCDAC EATLFNVHWV CRKCGFVACL DCYKAKERKS SRDKELYAWM KCVKGQPHDH KHLMLTQIIP GSVLTDLLDA MHILREKYGI KSHCHCTNRQ NLQGGNVPTM NGVSQVLQNV LHHSNKTSVS LPESQQQNSP QKSQTNGNSS PGSASTDSRL TPPESQSPLH WLADLAEQKS REEKQENKEF TLEREIKEDG DQDASDSPNG STSPPASQSN EQGSTLRDLL TTTAGKLRVG STDAGIAFAP VYSMGTSSGK GGRTMPNILD DIIASVVENK IPPNKTSKIN IKSEPNEEPK ESSLPATDES NKSYRDIPHS WICDQHILWL KDYKNSNNWK LFKECWKQGQ PAVVSGVHKK MNISLWKAES ISLDFGDHQA DLLNCKDSIV SNANVKEFWD GFEEVSKRQK NKGGETVVLK LKDCPSGEDF KAMMPTRYED FLRCLPLPEY CNPEGKFNLA SHLPGFFVRP DLGPRLCSAY GVAAAKDHDI GTTNLHIEAS DVVNVLVYVG IAKGNGVLSK AGILKKFEEE ELDDVLRKRL KDSSEIPGAL WHIYAGKDVD KIREFLQKIS KEQGLEVLPE HDPIRDQSWY VNRKLRQRLL EEYGVRACTL IQFLGDAIVL PAGTLHQVQN FHSCVQVTED FVSPEHLVQS FHLTQELRLL KEEINYDDKL QVKNILYHAV KEMVRALKMH EDEVEDMEDT // ID JMJD6_MOUSE Reviewed; 403 AA. AC Q9ERI5; A2AA26; A8Y5I2; Q80TX1; DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot. DT 04-DEC-2007, sequence version 2. DT 19-MAR-2014, entry version 101. DE RecName: Full=Bifunctional arginine demethylase and lysyl-hydroxylase JMJD6; DE EC=1.14.11.-; DE AltName: Full=Histone arginine demethylase JMJD6; DE AltName: Full=JmjC domain-containing protein 6; DE AltName: Full=Jumonji domain-containing protein 6; DE AltName: Full=Lysyl-hydroxylase JMJD6; DE AltName: Full=Peptide-lysine 5-dioxygenase JMJD6; DE AltName: Full=Phosphatidylserine receptor; DE Short=Protein PTDSR; GN Name=Jmjd6; Synonyms=Kiaa0585, Ptdsr; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC STRAIN=Swiss Webster; TISSUE=Brain; RX PubMed=10811223; DOI=10.1038/35011084; RA Fadok V.A., Bratton D.L., Rose D.M., Pearson A., Ezekewitz R.A., RA Henson P.M.; RT "A receptor for phosphatidylserine-specific clearance of apoptotic RT cells."; RL Nature 405:85-90(2000). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Brain; RX PubMed=12693553; DOI=10.1093/dnares/10.1.35; RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S., RA Nakajima D., Nagase T., Ohara O., Koga H.; RT "Prediction of the coding sequences of mouse homologues of KIAA gene: RT II. The complete nucleotide sequences of 400 mouse KIAA-homologous RT cDNAs identified by screening of terminal sequences of cDNA clones RT randomly sampled from size-fractionated libraries."; RL DNA Res. 10:35-48(2003). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC STRAIN=129; TISSUE=Mammary tumor; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE. RX PubMed=14645847; DOI=10.1126/science.1087621; RA Li M.O., Sarkisian M.R., Mehal W.Z., Rakic P., Flavell R.A.; RT "Phosphatidylserine receptor is required for clearance of apoptotic RT cells."; RL Science 302:1560-1563(2003). RN [6] RP DISRUPTION PHENOTYPE. RX PubMed=14715629; DOI=10.1182/blood-2003-09-3245; RA Kunisaki Y., Masuko S., Noda M., Inayoshi A., Sanui T., Harada M., RA Sasazuki T., Fukui Y.; RT "Defective fetal liver erythropoiesis and T lymphopoiesis in mice RT lacking the phosphatidylserine receptor."; RL Blood 103:3362-3364(2004). RN [7] RP SUBCELLULAR LOCATION. RX PubMed=14729065; DOI=10.1016/j.yexcr.2003.09.023; RA Cui P., Qin B., Liu N., Pan G., Pei D.; RT "Nuclear localization of the phosphatidylserine receptor protein via RT multiple nuclear localization signals."; RL Exp. Cell Res. 293:154-163(2004). RN [8] RP DISRUPTION PHENOTYPE, FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL RP STAGE. RX PubMed=15345036; DOI=10.1186/jbiol10; RA Boese J., Gruber A.D., Helming L., Schiebe S., Wegener I., Hafner M., RA Beales M., Koentgen F., Lengeling A.; RT "The phosphatidylserine receptor has essential functions during RT embryogenesis but not in apoptotic cell removal."; RL J. Biol. 3:15.1-15.18(2004). RN [9] RP REVIEW ON FUNCTION. RX PubMed=15453906; DOI=10.1186/jbiol14; RA Williamson P., Schlegel R.A.; RT "Hide and seek: the secret identity of the phosphatidylserine RT receptor."; RL J. Biol. 3:14.1-14.4(2004). RN [10] RP FUNCTION, AND INTERACTION WITH U2AF2. RX PubMed=21300889; DOI=10.1073/pnas.1008098108; RA Boeckel J.N., Guarani V., Koyanagi M., Roexe T., Lengeling A., RA Schermuly R.T., Gellert P., Braun T., Zeiher A., Dimmeler S.; RT "Jumonji domain-containing protein 6 (Jmjd6) is required for RT angiogenic sprouting and regulates splicing of VEGF-receptor 1."; RL Proc. Natl. Acad. Sci. U.S.A. 108:3276-3281(2011). CC -!- FUNCTION: Dioxygenase that can both act as a histone arginine CC demethylase and a lysyl-hydroxylase. Acts as a lysyl-hydroxylase CC that catalyzes 5-hydroxylation on specific lysine residues of CC target proteins such as U2AF2/U2AF65 and LUC7L2. Acts as a CC regulator of RNA splicing by mediating 5-hydroxylation of CC U2AF2/U2AF65, affecting the pre-mRNA splicing activity of CC U2AF2/U2AF65. In addition to peptidyl-lysine 5-dioxygenase CC activity, may act as an RNA hydroxylase, as suggested by its CC ability to bind single strand RNA. Also acts as an arginine CC demethylase which demethylates histone H3 at 'Arg-2' (H3R2me) and CC histone H4 at 'Arg-3' (H4R3me), thereby playing a role in histone CC code. However, histone arginine demethylation may not constitute CC the primary activity in vivo. Has no histone lysine demethylase CC activity. Required for differentiation of multiple organs during CC embryogenesis. Acts as a key regulator of hematopoietic CC differentiation: required for angiogenic sprouting by regulating CC the pre-mRNA splicing activity of U2AF2/U2AF65. Seems to be CC necessary for the regulation of macrophage cytokine responses (By CC similarity). CC -!- COFACTOR: Binds 1 Fe(2+) ion per subunit (By similarity). CC -!- SUBUNIT: Interacts with LUC7L2 and LUC7L3. Interacts with BRD4 (By CC similarity). Interacts with U2AF2/U2AF65. CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm. Nucleus, nucleolus (By CC similarity). Note=Mainly found throughout the nucleoplasm outside CC of regions containing heterochromatic DNA, with some localization CC in nucleolus. During mitosis, excluded from the nucleus and CC reappears in the telophase of the cell cycle (By similarity). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9ERI5-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9ERI5-2; Sequence=VSP_014024, VSP_014025; CC Note=No experimental confirmation available; CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed in brain, eye, CC spinal chord, thymus, lung, liver, kidney and intestine. CC -!- DEVELOPMENTAL STAGE: Expressed early in development. Expressed CC from embryonic stem cells and throughout embryogenesis. CC -!- DOMAIN: The nuclear localization signal motifs are necessary and CC sufficient to target it into the nucleus (By similarity). CC -!- DISRUPTION PHENOTYPE: Mice display perinatal lethality, growth CC retardation, severe anemia and a delay in terminal differentiation CC of the kidney, intestine, liver and lungs during embryogenesis. CC Moreover, eye development can be severely disturbed, ranging from CC defects in retinal differentiation to complete unilateral or CC bilateral absence of eyes. According to PubMed:14645847, mice are CC defective in removing apoptotic cells, especially in the lung and CC brain, in which dead cells accumulate, causing abnormal CC development and leading to neonatal lethality. According to CC PubMed:14715629, mice lacking Jmjd6 display a reduced number of CC macrophages and apoptotic cells in fetal liver. In contrast, CC according to PubMed:15345036, mice show a normal engulfment of CC apoptotic cells. The contradictory results concerning apoptosis CC and macrophage function may be explained by the fact that the CC protein plays a key role in hematopoietic differentiation. CC -!- SIMILARITY: Belongs to the JMJD6 family. CC -!- SIMILARITY: Contains 1 JmjC domain. CC -!- CAUTION: Was initially thought to constitute the CC phosphatidylserine receptor, a receptor that mediates recognition CC of phosphatidylserine, a specific marker only present at the CC surface of apoptotic cells. Phosphatidylserine receptor probably CC participates in apoptotic cell phagocytosis. This protein was CC identified using phage display expressing mAb 217, an antibody CC that specifically recognizes phosphatidylserine receptor. However, CC its nuclear localization and the fact that mAb 217 antibody still CC recognizes the phosphatidylserine receptor in mice lacking Jmjd6, CC strongly suggest that it does not constitute the receptor for CC phosphatidylserine and is not involved in apoptotic cell removal. CC -!- SEQUENCE CAUTION: CC Sequence=BAC65599.1; Type=Erroneous initiation; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF304118; AAG27719.1; -; mRNA. DR EMBL; AK122317; BAC65599.1; ALT_INIT; mRNA. DR EMBL; AL645542; CAP19369.1; -; Genomic_DNA. DR EMBL; BC056629; AAH56629.1; -; mRNA. DR RefSeq; NP_203971.2; NM_033398.2. DR UniGene; Mm.481684; -. DR ProteinModelPortal; Q9ERI5; -. DR SMR; Q9ERI5; 1-335. DR PhosphoSite; Q9ERI5; -. DR PRIDE; Q9ERI5; -. DR Ensembl; ENSMUST00000047616; ENSMUSP00000047570; ENSMUSG00000056962. [Q9ERI5-1] DR GeneID; 107817; -. DR KEGG; mmu:107817; -. DR UCSC; uc007mmi.1; mouse. [Q9ERI5-1] DR UCSC; uc007mmj.1; mouse. [Q9ERI5-2] DR CTD; 23210; -. DR MGI; MGI:1858910; Jmjd6. DR eggNOG; NOG124833; -. DR GeneTree; ENSGT00530000063579; -. DR HOGENOM; HOG000265824; -. DR HOVERGEN; HBG054774; -. DR InParanoid; Q9ERI5; -. DR KO; K11323; -. DR OrthoDB; EOG7R56SG; -. DR TreeFam; TF314988; -. DR ChiTaRS; JMJD6; mouse. DR NextBio; 359521; -. DR PRO; PR:Q9ERI5; -. DR ArrayExpress; Q9ERI5; -. DR Bgee; Q9ERI5; -. DR CleanEx; MM_JMJD6; -. DR Genevestigator; Q9ERI5; -. DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB. DR GO; GO:0005886; C:plasma membrane; IDA:MGI. DR GO; GO:0033746; F:histone demethylase activity (H3-R2 specific); ISS:UniProtKB. DR GO; GO:0033749; F:histone demethylase activity (H4-R3 specific); ISS:UniProtKB. DR GO; GO:0005506; F:iron ion binding; IEA:Ensembl. DR GO; GO:0070815; F:peptidyl-lysine 5-dioxygenase activity; ISS:UniProtKB. DR GO; GO:0004872; F:receptor activity; IDA:MGI. DR GO; GO:0003727; F:single-stranded RNA binding; ISS:UniProtKB. DR GO; GO:0007166; P:cell surface receptor signaling pathway; IDA:MGI. DR GO; GO:0048821; P:erythrocyte development; IMP:MGI. DR GO; GO:0007507; P:heart development; IMP:MGI. DR GO; GO:0001822; P:kidney development; IMP:MGI. DR GO; GO:0030324; P:lung development; IMP:MGI. DR GO; GO:0042116; P:macrophage activation; IMP:MGI. DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW. DR GO; GO:0018395; P:peptidyl-lysine hydroxylation to 5-hydroxy-L-lysine; ISS:UniProtKB. DR GO; GO:0043654; P:recognition of apoptotic cell; IDA:MGI. DR GO; GO:0048024; P:regulation of mRNA splicing, via spliceosome; IMP:UniProtKB. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW. DR GO; GO:0060041; P:retina development in camera-type eye; IMP:MGI. DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW. DR GO; GO:0002040; P:sprouting angiogenesis; IMP:UniProtKB. DR GO; GO:0033077; P:T cell differentiation in thymus; IMP:MGI. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR InterPro; IPR003347; JmjC_dom. DR Pfam; PF02373; JmjC; 1. DR SMART; SM00558; JmjC; 1. DR PROSITE; PS51184; JMJC; 1. PE 1: Evidence at protein level; KW Alternative splicing; Chromatin regulator; Complete proteome; KW Developmental protein; Differentiation; Dioxygenase; Iron; KW Metal-binding; mRNA processing; mRNA splicing; Nucleus; KW Oxidoreductase; Reference proteome; RNA-binding; Transcription; KW Transcription regulation. FT CHAIN 1 403 Bifunctional arginine demethylase and FT lysyl-hydroxylase JMJD6. FT /FTId=PRO_0000129370. FT DOMAIN 141 305 JmjC. FT MOTIF 6 10 Nuclear localization signal 1 (By FT similarity). FT MOTIF 91 95 Nuclear localization signal 2 (By FT similarity). FT MOTIF 141 145 Nuclear localization signal 3 (By FT similarity). FT MOTIF 167 170 Nuclear localization signal 4 (By FT similarity). FT MOTIF 373 378 Nuclear localization signal 5 (By FT similarity). FT COMPBIAS 340 365 Ser-rich. FT METAL 187 187 Iron; catalytic (By similarity). FT METAL 189 189 Iron; catalytic (By similarity). FT METAL 273 273 Iron; catalytic (By similarity). FT BINDING 184 184 Substrate (By similarity). FT BINDING 197 197 2-oxoglutarate (By similarity). FT BINDING 204 204 Substrate (By similarity). FT BINDING 285 285 2-oxoglutarate (By similarity). FT VAR_SEQ 270 298 GWWHVVLNLDTTIAITQNFASSTNFPVVW -> IDELEETI FT PVRPSSDWSGLVLYCHFGVES (in isoform 2). FT /FTId=VSP_014024. FT VAR_SEQ 299 403 Missing (in isoform 2). FT /FTId=VSP_014025. FT CONFLICT 43 43 P -> S (in Ref. 1; AAG27719 and 4; FT AAH56629). SQ SEQUENCE 403 AA; 46567 MW; D440E880B2F1BB37 CRC64; MNHKSKKRIR EAKRSARPEL KDSLDWTRHN YYESYPLNPA AVPDNVERAD ALQLSVKEFV ERYERPYKPV VLLNAQEGWS AQEKWTLERL KRKYRNQKFK CGEDNDGYSV KMKMKYYIEY MESTRDDSPL YIFDSSYGEH PKRRKLLEDY KVPKFFTDDL FQYAGEKRRP PYRWFVMGPP RSGTGIHIDP LGTSAWNALV QGHKRWCLFP TNTPRELIKV TREEGGNQQD EAITWFNVIY PRTQLPTWPP EFKPLEILQK PGETVFVPGG WWHVVLNLDT TIAITQNFAS STNFPVVWHK TVRGRPKLSR KWYRILKQEH PELAVLADAV DLQESTGIAS DSSSDSSSSS SSSSSDSDSE CESGSEGDGT THRRKKRRTC SMVGNGDTTS QDDCVSKERS SSR // ID KDM1B_MOUSE Reviewed; 826 AA. AC Q8CIG3; Q8C5C4; Q8CEC1; DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 19-MAR-2014, entry version 87. DE RecName: Full=Lysine-specific histone demethylase 1B; DE EC=1.-.-.-; DE AltName: Full=Flavin-containing amine oxidase domain-containing protein 1; DE AltName: Full=Lysine-specific histone demethylase 2; GN Name=Kdm1b; Synonyms=Aof1, Lsd2; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE RP SEQUENCE [LARGE SCALE MRNA] OF 285-826 (ISOFORM 2). RC STRAIN=C57BL/6J; TISSUE=Cecum, and Skin; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC STRAIN=FVB/N; TISSUE=Mammary tumor; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, AND ENZYME RP REGULATION. RX PubMed=19407342; DOI=10.1074/jbc.M109.003087; RA Karytinos A., Forneris F., Profumo A., Ciossani G., Battaglioli E., RA Binda C., Mattevi A.; RT "A novel mammalian flavin-dependent histone demethylase."; RL J. Biol. Chem. 284:17775-17782(2009). RN [4] RP FUNCTION, MUTAGENESIS OF LYS-667, SUBCELLULAR LOCATION, TISSUE RP SPECIFICITY, AND DISRUPTION PHENOTYPE. RX PubMed=19727073; DOI=10.1038/nature08315; RA Ciccone D.N., Su H., Hevi S., Gay F., Lei H., Bajko J., Xu G., Li E., RA Chen T.; RT "KDM1B is a histone H3K4 demethylase required to establish maternal RT genomic imprints."; RL Nature 461:415-418(2009). CC -!- FUNCTION: Histone demethylase that demethylates 'Lys-4' of histone CC H3, a specific tag for epigenetic transcriptional activation, CC thereby acting as a corepressor. Required for de novo DNA CC methylation of a subset of imprinted genes during oogenesis. Acts CC by oxidizing the substrate by FAD to generate the corresponding CC imine that is subsequently hydrolyzed. Demethylates both mono- and CC di-methylated 'Lys-4' of histone H3. Has no effect on tri- CC methylated 'Lys-4', mono-, di- or tri-methylated 'Lys-9', mono-, CC di- or tri-methylated 'Lys-27', mono-, di- or tri-methylated 'Lys- CC 36' of histone H3, or on mono-, di- or tri-methylated 'Lys-20' of CC histone H4. CC -!- COFACTOR: FAD. CC -!- ENZYME REGULATION: Inhibited by tranylcypromine, but not by CC pargyline, deprenyl or rasagiline. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=9.2 uM for mono-methylated 'Lys-4' histone H3 N-terminal CC peptide; CC KM=11.3 uM for di-methylated 'Lys-4' histone H3 N-terminal CC peptide; CC KM=9.0 uM for mono-methylated 'Lys-4', mono-methylated 'Lys-9' CC histone H3 N-terminal peptide; CC KM=6.6 uM for di-methylated 'Lys-4', di-methylated 'Lys-9' CC histone H3 N-terminal peptide; CC KM=70.5 uM for mono-methylated 'Lys-4', acetylated 'Lys-9' CC histone H3 N-terminal peptide; CC KM=8.1 uM for mono-methylated 'Lys-4', mono-methylated 'Arg-17' CC histone H3 N-terminal peptide; CC pH dependence: CC Optimum pH is 8.5; CC -!- SUBUNIT: Does not form a complex with RCOR1/CoREST. CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q8CIG3-1; Sequence=Displayed; CC Name=2; CC IsoId=Q8CIG3-2; Sequence=VSP_019969; CC Note=No experimental confirmation available; CC Name=3; CC IsoId=Q8CIG3-3; Sequence=VSP_019968; CC Note=No experimental confirmation available; CC -!- TISSUE SPECIFICITY: Expressed in growing oocytes and in intestinal CC gland. CC -!- DOMAIN: The SWIRM domain may act as an anchor site for a histone CC tail (By similarity). CC -!- DISRUPTION PHENOTYPE: No effect on mouse development and CC oogenesis, but embryos derived from oocytes from Kdm1b-deficient CC females die before mid-gestation. CC -!- MISCELLANEOUS: Acetylation of 'Lys-9' decreases the binding of the CC substrate, while hyperacetylation of 'Lys-9', 'Lys-14' and 'Lys- CC 18', phosphorylation of 'Thr3' or 'Ser-10', and methylation of CC 'Arg-2' or 'Arg-8' abolishes its binding. Methylation of 'Lys-9' CC and 'Arg-17' are the only two epigenetic modifications that have CC no significant effect on catalysis. CC -!- SIMILARITY: Belongs to the flavin monoamine oxidase family. CC -!- SIMILARITY: Contains 1 CW-type zinc finger. CC -!- SIMILARITY: Contains 1 SWIRM domain. CC -!- SEQUENCE CAUTION: CC Sequence=BAC26005.1; Type=Erroneous initiation; Note=Translation N-terminally extended; CC Sequence=BAC37460.1; Type=Frameshift; Positions=825; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK028553; BAC26005.1; ALT_INIT; mRNA. DR EMBL; AK078920; BAC37460.1; ALT_FRAME; mRNA. DR EMBL; BC023917; AAH23917.1; -; mRNA. DR RefSeq; NP_758466.1; NM_172262.3. DR UniGene; Mm.31259; -. DR ProteinModelPortal; Q8CIG3; -. DR SMR; Q8CIG3; 49-826. DR BioGrid; 230002; 1. DR DIP; DIP-59111N; -. DR PhosphoSite; Q8CIG3; -. DR PRIDE; Q8CIG3; -. DR Ensembl; ENSMUST00000037025; ENSMUSP00000038373; ENSMUSG00000038080. [Q8CIG3-1] DR GeneID; 218214; -. DR KEGG; mmu:218214; -. DR UCSC; uc007qht.2; mouse. [Q8CIG3-1] DR UCSC; uc007qhu.2; mouse. [Q8CIG3-2] DR UCSC; uc011yyy.1; mouse. [Q8CIG3-3] DR CTD; 221656; -. DR MGI; MGI:2145261; Kdm1b. DR eggNOG; COG1231; -. DR GeneTree; ENSGT00530000062888; -. DR HOGENOM; HOG000230870; -. DR InParanoid; Q8CIG3; -. DR OMA; KALCVRP; -. DR OrthoDB; EOG7X9G66; -. DR TreeFam; TF352593; -. DR ChiTaRS; KDM1B; mouse. DR NextBio; 376196; -. DR PRO; PR:Q8CIG3; -. DR ArrayExpress; Q8CIG3; -. DR Bgee; Q8CIG3; -. DR CleanEx; MM_AOF1; -. DR Genevestigator; Q8CIG3; -. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IDA:UniProtKB. DR GO; GO:0034648; F:histone demethylase activity (H3-dimethyl-K4 specific); IDA:UniProtKB. DR GO; GO:0034649; F:histone demethylase activity (H3-monomethyl-K4 specific); IDA:UniProtKB. DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW. DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB. DR GO; GO:0043046; P:DNA methylation involved in gamete generation; IMP:MGI. DR GO; GO:0007275; P:multicellular organismal development; IEA:UniProtKB-KW. DR GO; GO:0044030; P:regulation of DNA methylation; IMP:UniProtKB. DR GO; GO:0006349; P:regulation of gene expression by genetic imprinting; IMP:UniProtKB. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.10.10; -; 1. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR002937; Amino_oxidase. DR InterPro; IPR009057; Homeodomain-like. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR007526; SWIRM. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR InterPro; IPR011124; Znf_CW. DR Pfam; PF01593; Amino_oxidase; 1. DR Pfam; PF07496; zf-CW; 1. DR SUPFAM; SSF46689; SSF46689; 1. DR PROSITE; PS50934; SWIRM; 1. DR PROSITE; PS51050; ZF_CW; 1. PE 1: Evidence at protein level; KW Alternative splicing; Chromatin regulator; Complete proteome; KW Developmental protein; FAD; Flavoprotein; Metal-binding; Nucleus; KW Oxidoreductase; Phosphoprotein; Reference proteome; Repressor; KW Transcription; Transcription regulation; Zinc; Zinc-finger. FT CHAIN 1 826 Lysine-specific histone demethylase 1B. FT /FTId=PRO_0000247337. FT DOMAIN 281 379 SWIRM. FT ZN_FING 133 193 CW-type. FT NP_BIND 389 445 FAD (Potential). FT MOD_RES 17 17 Phosphoserine (By similarity). FT MOD_RES 253 253 Phosphoserine (By similarity). FT VAR_SEQ 1 621 Missing (in isoform 3). FT /FTId=VSP_019968. FT VAR_SEQ 459 558 Missing (in isoform 2). FT /FTId=VSP_019969. FT MUTAGEN 667 667 K->A: Loss of activity. SQ SEQUENCE 826 AA; 92633 MW; 02FD6FE991B1C030 CRC64; MAASRGRSKK RSNLELSPDN LPLRSSGRQA KKKAVEIPDE DEDGSSEKKY RKCEKAGCTA AYPVCFASAS ERCAKNGYTS RWYHLSCGEH FCNECFDHYY RSHKDGYDKY SAWKRVWTSN GKTEPSPKAF MADQQLPYWV QCTKPECGKW RQLTKEIQLT PHMARTYRCG MKPNTITKPD TPDHCSFPED LRVLEVSNHW WYPMLIQPPL LKDSVAAPLL SAYYPDCVGM SPSCTSTHRA TVTAATTTTG SASPGEMEPS KAAPSSLVLG MNRYFQPFYQ PNECGKALCV RPDVMELDEL YEFPEYSRDP TMYLALRNLI LALWYTNCKE ALTPQKCIPH IIVRGLVRIR CVQEVERILY FMTRKGLINT GVLTVAAGQH LLPKHYHNKS VLVVGAGPAG LAAARQLHNF GMKVTVLEAK DRIGGRVWDD KSFKGVVVGR GPQIVNGCIN NPVALMCEQL GISMRKLGER CDLIQEGGRI TDPTVDKRMD FHFNALLDVV SEWRKDKTLL QDVPLGEKIE EIYRAFVKES GIQFSELEGQ VLQFHLSNLE YACGSSLHQV SARSWDHNEF FAQFAGDHTL LTPGYSTIIE KLAEGLDIRL KSPVQSIDYT GDEVQVTTTD GMGHSAQKVL VTVPLAILQR GAIQFNPPLS EKKMKAINSL GAGIIEKIAL QFPYRFWDSK VQGADFFGHV PPSASQRGLF AVFYDMDSQQ SVLMSVITGE AVASLRTMDD KQVLQQCMGI LRELFKEQEI PEPTKYFVTR WSTEPWIQMA YSFVKTFGSG EAYDIIAEEI QGTVFFAGEA TNRHFPQTVT GAYLSGVREA SKIAAF // ID KDM3B_MOUSE Reviewed; 1562 AA. AC Q6ZPY7; Q2VPQ5; Q5U5V7; Q6P9K3; Q8CCE2; Q8K2A5; Q9CU57; DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 16-MAY-2006, sequence version 2. DT 19-MAR-2014, entry version 72. DE RecName: Full=Lysine-specific demethylase 3B; DE EC=1.14.11.-; DE AltName: Full=JmjC domain-containing histone demethylation protein 2B; DE AltName: Full=Jumonji domain-containing protein 1B; GN Name=Kdm3b; Synonyms=Jhdm2b, Jmjd1b, Kiaa1082; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Embryonic tail; RX PubMed=14621295; DOI=10.1093/dnares/10.4.167; RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., RA Saga Y., Nagase T., Ohara O., Koga H.; RT "Prediction of the coding sequences of mouse homologues of KIAA gene: RT III. The complete nucleotide sequences of 500 mouse KIAA-homologous RT cDNAs identified by screening of terminal sequences of cDNA clones RT randomly sampled from size-fractionated libraries."; RL DNA Res. 10:167-180(2003). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 574-1562 (ISOFORM 1). RC STRAIN=C57BL/6, and Czech II; TISSUE=Brain, Eye, and Mammary tumor; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1119-1562. RC STRAIN=C57BL/6J; TISSUE=Testis, and Thymus; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). CC -!- FUNCTION: Histone demethylase that specifically demethylates 'Lys- CC 9' of histone H3, thereby playing a central role in histone code. CC Demethylation of Lys residue generates formaldehyde and succinate CC May have tumor suppressor activity (By similarity). CC -!- COFACTOR: Binds 1 Fe(2+) ion per subunit (By similarity). CC -!- SUBCELLULAR LOCATION: Nucleus (By similarity). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q6ZPY7-1; Sequence=Displayed; CC Name=2; CC IsoId=Q6ZPY7-2; Sequence=VSP_018301, VSP_018302; CC Note=No experimental confirmation available; CC -!- DOMAIN: Leu-Xaa-Xaa-Leu-Leu (LXXLL) motifs are known to mediate CC the association with nuclear receptors (By similarity). CC -!- SIMILARITY: Belongs to the JHDM2 histone demethylase family. CC -!- SIMILARITY: Contains 1 JmjC domain. CC -!- SEQUENCE CAUTION: CC Sequence=AAH38376.1; Type=Frameshift; Positions=1555; CC Sequence=BAC98091.1; Type=Erroneous initiation; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK129281; BAC98091.1; ALT_INIT; mRNA. DR EMBL; BC031981; AAH31981.1; -; mRNA. DR EMBL; BC038376; AAH38376.1; ALT_FRAME; mRNA. DR EMBL; BC060727; AAH60727.1; -; mRNA. DR EMBL; BC108415; AAI08416.1; -; mRNA. DR EMBL; AK018027; BAB31043.1; -; mRNA. DR EMBL; AK033343; BAC28239.1; -; mRNA. DR RefSeq; XP_006526040.1; XM_006525977.1. DR UniGene; Mm.277906; -. DR ProteinModelPortal; Q6ZPY7; -. DR SMR; Q6ZPY7; 832-859, 1181-1521. DR PhosphoSite; Q6ZPY7; -. DR PaxDb; Q6ZPY7; -. DR PRIDE; Q6ZPY7; -. DR GeneID; 277250; -. DR MGI; MGI:1923356; Kdm3b. DR eggNOG; NOG305537; -. DR PRO; PR:Q6ZPY7; -. DR CleanEx; MM_JMJD1B; -. DR Genevestigator; Q6ZPY7; -. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0016568; P:chromatin modification; IEA:UniProtKB-KW. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR InterPro; IPR003347; JmjC_dom. DR Pfam; PF02373; JmjC; 1. DR SMART; SM00558; JmjC; 1. DR PROSITE; PS51184; JMJC; 1. PE 2: Evidence at transcript level; KW Acetylation; Alternative splicing; Chromatin regulator; KW Complete proteome; Dioxygenase; Iron; Metal-binding; Nucleus; KW Oxidoreductase; Phosphoprotein; Reference proteome; Transcription; KW Transcription regulation; Zinc; Zinc-finger. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 1562 Lysine-specific demethylase 3B. FT /FTId=PRO_0000234374. FT DOMAIN 1299 1522 JmjC. FT ZN_FING 832 857 C6-type (Potential). FT MOTIF 1094 1098 LXXLL motif. FT COMPBIAS 255 545 Ser-rich. FT METAL 1361 1361 Iron; catalytic (By similarity). FT METAL 1363 1363 Iron; catalytic (By similarity). FT METAL 1490 1490 Iron; catalytic (By similarity). FT MOD_RES 2 2 N-acetylalanine (By similarity). FT MOD_RES 574 574 Phosphoserine (By similarity). FT MOD_RES 599 599 Phosphoserine (By similarity). FT VAR_SEQ 1070 1124 LTPKLFNSLLLGPTASNSKTEGSSLRDLLHSGPGKLPQTPL FT DTGIPFPPVFSSSS -> HVTSDLAHPRRWGCSPSRTLHEH FT RSLQDPGRAHCFSQEAPGLGNVYLVKNRFVVK (in FT isoform 2). FT /FTId=VSP_018301. FT VAR_SEQ 1125 1562 Missing (in isoform 2). FT /FTId=VSP_018302. FT CONFLICT 1126 1126 V -> G (in Ref. 2; AAH31981). FT CONFLICT 1369 1370 NV -> SL (in Ref. 3; BAB31043). FT CONFLICT 1545 1545 V -> G (in Ref. 3; BAB31043). SQ SEQUENCE 1562 AA; 170875 MW; 4F2D7818104B50BE CRC64; MADAAASPVG KRLLLLFADP TASASASAPT AAAVVSGDPG PALRTRAWRA GTVRAMSGAV PQDLAIFVEF DGCNWKQHSW VKVHAEDVLA LLLEGSLVWA PRKDPVLLQG TRVPVAQWPA LTFTPLVDKL GLGSVVPVEY LVDRELRFLS DANGMHLFQM GTDVQNQILL EHAALRETVN ALISDQKLQE IFSRGPYSVQ GHRVKVYQPE GEEVWLCGVV SRQDSVTRLM EVSITETGEV KSVDPRLTHV MLMDSSTPQS ENSRNSSLAS SGFGVSLSSL SQPLTFGSGR SQSNGVLATD NKPLGFSFSC SSASESQKDS DLSKNLFFQC MSQNVPSTNY LSRVSESVAD DSSSRDSFTQ SLESLTSGLC KGRSVLGADT QPGPKAGSSV DRKVPAESMP TLTPAFPRSL LNTRTPENHE NLFLQPPKLS REEPSNPFLA FVEKVEHSPF SSFVSQASGS SSSATSVTSK ATASWPESHS SAESAPLAKK KPLFITTDSS KLVSGVLGSA LSTGSPSLSA VGNGRSSSPT NSLTQPIEMP TLSSSPTEER PTVGPGQQDN PLLKTFSTVF GRHSGSFLSA PAEFAQENKA PFEAVKRFSL DERSLACRQD SDSSTNSDLS DLSDSEEQLQ AKSGLKGIPE HLMGKLGPNG ERSAELLLGK GKGKQAPKGR PRTAPLKVGQ SVLKDVSKVR KLKQSGEPFL QDGSCINVAP HLHKCRECRL ERYRKFKEQE QDDSTVACRF FHFRRLVFTR KGVLRVEGFL SPQQSDPDAM NLWIPSSSLA EGIDLETSKY ILANVGDQFC QLVMSEKEAM MMVEPHQKVA WKRAVRGVRE MCDVCETTLF NIHWVCRKCG FGVCLDCYRL RKSRPRSETE EMGDEEVFSW LKCAKGQSHE PENLMPTQII PGTALYNIGD MVHAARGKWG IKANCPCISR QSKSVLRPAV TNGISQLPSV TPSASSGNET TFSSGGGAAA VTNPEPDQVP KGAGTDGRSE EPLKAEGSAS NSNSELKAIR PPCPDTAPPS SALHWLADLA TQKAKEETKD AGSLRSVLNK ESHSPFGLDS FNSTAKVSPL TPKLFNSLLL GPTASNSKTE GSSLRDLLHS GPGKLPQTPL DTGIPFPPVF SSSSAVAKSK ASLPDFLDHI IASVVENKKT SDPSKRSCNL TDTQKEVKEM AMGLNVLDPH TSHSWLCDGR LLCLHDPSNK NNWKIFRECW KQGQPVLVSG VHKKLKSELW KPEAFSQEFG DQDVDLVNCR NCAIISDVKV RDFWDGFEII CKRLRSEDGQ PMVLKLKDWP PGEDFRDMMP TRFEDLMENL PLPEYTKRDG RLNLASRLPS YFVRPDLGPK MYNAYGLITA EDRRVGTTNL HLDVSDAVNV MVYVGIPVGE GAHDEEVLKT IDEGDADEVT KQRIHDGKEK PGALWHIYAA KDAEKIRELL RKVGEEQGQE NPPDHDPIHD QSWYLDQILR KRLFEEYGVQ GWAIVQFLGD AVFIPAGAPH QVHNLYSCIK VAEDFVSPEH VKHCFRLTQE FRHLSNTHTN HEDKLQVKNI IYHAVKDAVG TLKAHESKLA RS // ID KDM4B_MOUSE Reviewed; 1086 AA. AC Q91VY5; Q3UR22; Q6ZQ30; Q99K42; DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 19-MAR-2014, entry version 97. DE RecName: Full=Lysine-specific demethylase 4B; DE EC=1.14.11.-; DE AltName: Full=JmjC domain-containing histone demethylation protein 3B; DE AltName: Full=Jumonji domain-containing protein 2B; GN Name=Kdm4b; Synonyms=Jhdm3b, Jmjd2b; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC STRAIN=C57BL/6J; TISSUE=Embryonic tail, and Spinal ganglion; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Mammary tumor; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: Histone demethylase that specifically demethylates 'Lys- CC 9' of histone H3, thereby playing a role in histone code. Does not CC demethylate histone H3 'Lys-4', H3 'Lys-27', H3 'Lys-36' nor H4 CC 'Lys-20'. Only able to demethylate trimethylated H3 'Lys-9', with CC a weaker activity than KDM4A, KDM4C and KDM4D. Demethylation of CC Lys residue generates formaldehyde and succinate (By similarity). CC -!- COFACTOR: Binds 1 Fe(2+) ion per subunit (By similarity). CC -!- SUBCELLULAR LOCATION: Nucleus (By similarity). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q91VY5-1; Sequence=Displayed; CC Name=2; CC IsoId=Q91VY5-2; Sequence=VSP_018309, VSP_018310; CC Note=No experimental confirmation available; CC -!- DOMAIN: The 2 Tudor domains recognize and bind methylated CC histones. Double Tudor domain has an interdigitated structure and CC the unusual fold is required for its ability to bind methylated CC histone tails (By similarity). CC -!- SIMILARITY: Belongs to the JHDM3 histone demethylase family. CC -!- SIMILARITY: Contains 1 JmjC domain. CC -!- SIMILARITY: Contains 1 JmjN domain. CC -!- SIMILARITY: Contains 2 PHD-type zinc fingers. CC -!- SIMILARITY: Contains 2 Tudor domains. CC -!- SEQUENCE CAUTION: CC Sequence=BAC98043.1; Type=Erroneous initiation; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK129233; BAC98043.1; ALT_INIT; mRNA. DR EMBL; AK141879; BAE24866.1; -; mRNA. DR EMBL; BC005480; AAH05480.1; -; mRNA. DR EMBL; BC007145; AAH07145.1; -; mRNA. DR RefSeq; NP_742144.1; NM_172132.2. DR RefSeq; XP_006523956.1; XM_006523893.1. DR UniGene; Mm.45047; -. DR ProteinModelPortal; Q91VY5; -. DR SMR; Q91VY5; 10-346, 831-879, 905-1022. DR BioGrid; 228758; 6. DR PhosphoSite; Q91VY5; -. DR PRIDE; Q91VY5; -. DR Ensembl; ENSMUST00000025036; ENSMUSP00000025036; ENSMUSG00000024201. [Q91VY5-1] DR GeneID; 193796; -. DR KEGG; mmu:193796; -. DR UCSC; uc008dbu.2; mouse. [Q91VY5-2] DR UCSC; uc008dbv.2; mouse. [Q91VY5-1] DR CTD; 23030; -. DR MGI; MGI:2442355; Kdm4b. DR eggNOG; COG5141; -. DR GeneTree; ENSGT00530000063342; -. DR HOGENOM; HOG000231125; -. DR InParanoid; Q91VY5; -. DR KO; K06709; -. DR OMA; VSQWNIG; -. DR OrthoDB; EOG7TQV03; -. DR TreeFam; TF106449; -. DR ChiTaRS; KDM4B; mouse. DR NextBio; 371516; -. DR PRO; PR:Q91VY5; -. DR ArrayExpress; Q91VY5; -. DR Bgee; Q91VY5; -. DR CleanEx; MM_JMJD2B; -. DR Genevestigator; Q91VY5; -. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0016568; P:chromatin modification; IEA:UniProtKB-KW. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 3.30.40.10; -; 1. DR InterPro; IPR003347; JmjC_dom. DR InterPro; IPR003349; TF_JmjN. DR InterPro; IPR002999; Tudor. DR InterPro; IPR011011; Znf_FYVE_PHD. DR InterPro; IPR001965; Znf_PHD. DR InterPro; IPR013083; Znf_RING/FYVE/PHD. DR Pfam; PF02373; JmjC; 1. DR Pfam; PF02375; JmjN; 1. DR SMART; SM00558; JmjC; 1. DR SMART; SM00545; JmjN; 1. DR SMART; SM00249; PHD; 2. DR SMART; SM00333; TUDOR; 2. DR SUPFAM; SSF57903; SSF57903; 1. DR PROSITE; PS51184; JMJC; 1. DR PROSITE; PS51183; JMJN; 1. PE 2: Evidence at transcript level; KW Acetylation; Alternative splicing; Chromatin regulator; KW Complete proteome; Dioxygenase; Iron; Metal-binding; Nucleus; KW Oxidoreductase; Reference proteome; Repeat; Transcription; KW Transcription regulation; Zinc; Zinc-finger. FT CHAIN 1 1086 Lysine-specific demethylase 4B. FT /FTId=PRO_0000183176. FT DOMAIN 15 57 JmjN. FT DOMAIN 146 309 JmjC. FT DOMAIN 905 962 Tudor 1. FT DOMAIN 963 1019 Tudor 2. FT ZN_FING 719 777 PHD-type 1. FT ZN_FING 839 895 PHD-type 2. FT METAL 189 189 Iron; catalytic (By similarity). FT METAL 191 191 Iron; catalytic (By similarity). FT METAL 235 235 Zinc (By similarity). FT METAL 241 241 Zinc (By similarity). FT METAL 277 277 Iron; catalytic (By similarity). FT METAL 307 307 Zinc (By similarity). FT METAL 309 309 Zinc (By similarity). FT BINDING 133 133 Alpha-ketoglutarate (By similarity). FT BINDING 199 199 Alpha-ketoglutarate (By similarity). FT BINDING 207 207 Alpha-ketoglutarate (By similarity). FT MOD_RES 599 599 N6-acetyllysine (By similarity). FT VAR_SEQ 593 599 Missing (in isoform 2). FT /FTId=VSP_018309. FT VAR_SEQ 940 997 Missing (in isoform 2). FT /FTId=VSP_018310. FT CONFLICT 40 40 A -> T (in Ref. 1; BAE24866). FT CONFLICT 576 576 M -> L (in Ref. 2; AAH05480). SQ SEQUENCE 1086 AA; 121604 MW; 5418B6CBF5E14DAA CRC64; MGSEDHSAQN PSCKIMTFRP TMDEFRDFNR YVAYIESQGA HRAGLAKIIP PKEWKPRQTY DDIDDVVIPA PIQQVVTGQS GLFTQYNIQK KAMTVGEYRR LANSEKYCTP RHQDFDDLER KYWKNLTFVS PIYGADISGS LYDDDVAQWN IGNLRTILDM VERECGTIIE GVNTPYLYFG MWKTTFAWHT EDMDLYSINY LHFGEPKSWY AIPPEHGKRL ERLAIGFFPG SSQGCDAFLR HKMTLISPII LKKYGIPFSR ITQEAGEFMI TFPYGYHAGF NHGFNCAEST NFATLRWIDY GKVATQCTCR KDMVKISMDV FVRILQPERY EQWKQGRDLT VLDHTRPTAL SSPELSSWSA SRTSIKAKLL RRQISVKESR PWRKAEEERR REPTRRPGPA SHRRRSQPKK SKPEESRSPG EATAGVSTLD EARGCSRGEA MPEDEEEEEL LPSQGHEAEG VEEDGRGKPR PTKARNKKKT PSPSSPPLLS APPALFPTEE VLRPPPQPKS PGPAMGPMAA EGGPPPTPLN VVPPGAPVEE AEVRPRPIIP MLYVLPRTSS TDGDREHSAH AQLAPMELGP EEENQAQAGD SQGTTPFSKL KVEIKKSRRH PLGRPPTRSP LSVVKQEASS DEEAFLFSGE DDVTDPEALR SLLSLQWKNK AASFQAERKF NAAAALSEPY CAICTLFYPY SQSVQTERDS AVQPPSKSGQ RTRPLIPEMC FTSSGENTEP LPANSYVGED GTSPLISCAH CCLQVHASCY GVRPELAKEG WTCSRCAAHA WTAECCLCNL RGGALQRTTE HRWIHVICAI AVPEVRFLNV IERNPVDVSA IPEQRWKLKC IYCRKRMKRV SGACIQCSYE HCSTSFHVTC AHAAGVLMEP DDWPYVVSIT CLKHRASGAG GQLLRTVSLG QIVITKNRNG LYYRCRVIGT TAQTFYEVNF DDGSYSDNLY PESITSRDCL RLGPPPEGEL VELRWTDGNL YRARFISMAT SLIYQVEFED GSQLTVKRGD IFTLEEELPK RVRSRLSLST GTPQEPSFSG DDVKAAKRPR VASVLATTTE DTGRSPEYLS FMESLLQAQG RPGAPF // ID KDM4A_MOUSE Reviewed; 1064 AA. AC Q8BW72; A2A8L8; Q3UKM5; Q3UM81; Q3UWV2; Q6ZQ72; Q8K137; DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 3. DT 19-MAR-2014, entry version 101. DE RecName: Full=Lysine-specific demethylase 4A; DE EC=1.14.11.-; DE AltName: Full=JmjC domain-containing histone demethylation protein 3A; DE AltName: Full=Jumonji domain-containing protein 2A; GN Name=Kdm4a; Synonyms=Jhdm3a, Jmjd2, Jmjd2a, Kiaa0677; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Embryonic tail; RX PubMed=14621295; DOI=10.1093/dnares/10.4.167; RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., RA Saga Y., Nagase T., Ohara O., Koga H.; RT "Prediction of the coding sequences of mouse homologues of KIAA gene: RT III. The complete nucleotide sequences of 500 mouse KIAA-homologous RT cDNAs identified by screening of terminal sequences of cDNA clones RT randomly sampled from size-fractionated libraries."; RL DNA Res. 10:167-180(2003). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC STRAIN=C57BL/6J; TISSUE=Embryo, Mammary gland, Oviduct, and Placenta; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC STRAIN=FVB/N; TISSUE=Colon; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP PROTEIN SEQUENCE OF 499-505, AND MASS SPECTROMETRY. RC STRAIN=OF1; TISSUE=Hippocampus; RA Lubec G., Sunyer B., Chen W.-Q.; RL Submitted (JAN-2009) to UniProtKB. RN [6] RP TISSUE SPECIFICITY. RX PubMed=16024779; DOI=10.1128/MCB.25.15.6404-6414.2005; RA Zhang D., Yoon H.-G., Wong J.; RT "JMJD2A is a novel N-CoR-interacting protein and is involved in RT repression of the human transcription factor achaete scute-like RT homologue 2 (ASCL2/Hash2)."; RL Mol. Cell. Biol. 25:6404-6414(2005). CC -!- FUNCTION: Histone demethylase that specifically demethylates 'Lys- CC 9' and 'Lys-36' residues of histone H3, thereby playing a central CC role in histone code. Does not demethylate histone H3 'Lys-4', H3 CC 'Lys-27' nor H4 'Lys-20'. Demethylates trimethylated H3 'Lys-9' CC and H3 'Lys-36' residue, while it has no activity on mono- and CC dimethylated residues. Demethylation of Lys residue generates CC formaldehyde and succinate. Participates in transcriptional CC repression of ASCL2 and E2F-responsive promoters via the CC recruitment of histone deacetylases and NCOR1, respectively (By CC similarity). CC -!- COFACTOR: Binds 1 Fe(2+) ion per subunit (By similarity). CC -!- SUBUNIT: Interacts with histone deacetylase proteins HDAC1, HDAC2 CC and HDAC3. Interacts with RB and NCOR1 (By similarity). CC -!- SUBCELLULAR LOCATION: Nucleus (By similarity). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q8BW72-1; Sequence=Displayed; CC Name=2; CC IsoId=Q8BW72-2; Sequence=VSP_016144, VSP_016145; CC Note=No experimental confirmation available; CC -!- TISSUE SPECIFICITY: Widely expressed. CC -!- DOMAIN: The 2 Tudor domains recognize and bind methylated histone CC H3 'Lys-4' residue (H3K4me). Double Tudor domain has an CC interdigitated structure and the unusual fold is required for its CC ability to bind methylated histone tails. Trimethylated H3 'Lys-4' CC (H3K4me3) is bound in a cage of 3 aromatic residues, 2 of which CC are from the Tudor domain 2, while the binding specificity is CC determined by side-chain interactions involving residues from the CC Tudor domain 1. The Tudor domains are also able to bind CC trimethylated histone H3 'Lys-9' (H3K9me3), di- and trimethylated CC H4 'Lys-20' (H4K20me2 and H4K20me3). Has high affinity for CC H4K20me2, blocking recruitment of proteins such as TP53BP1 (By CC similarity). CC -!- PTM: Ubiquitinated by RNF8 and RNF168 following DNA damage, CC leading to its degradation. Degradation promotes accessibility of CC H4K20me2 mark for DNA repair protein TP53BP1, which is then CC recruited (By similarity). CC -!- SIMILARITY: Belongs to the JHDM3 histone demethylase family. CC -!- SIMILARITY: Contains 1 JmjC domain. CC -!- SIMILARITY: Contains 1 JmjN domain. CC -!- SIMILARITY: Contains 2 PHD-type zinc fingers. CC -!- SIMILARITY: Contains 2 Tudor domains. CC -!- SEQUENCE CAUTION: CC Sequence=BAC97997.1; Type=Erroneous initiation; Note=Translation N-terminally shortened; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK129187; BAC97997.1; ALT_INIT; mRNA. DR EMBL; AK054095; BAC35653.1; -; mRNA. DR EMBL; AK136085; BAE22812.1; -; mRNA. DR EMBL; AK145066; BAE26217.1; -; mRNA. DR EMBL; AK145947; BAE26776.1; -; mRNA. DR EMBL; AL626764; CAM27385.1; -; Genomic_DNA. DR EMBL; BC028866; AAH28866.1; -; mRNA. DR RefSeq; NP_001155295.1; NM_001161823.1. DR RefSeq; NP_759014.2; NM_172382.2. DR RefSeq; XP_006503073.1; XM_006503010.1. DR UniGene; Mm.234234; -. DR ProteinModelPortal; Q8BW72; -. DR SMR; Q8BW72; 3-355, 730-770, 821-869, 898-1011. DR BioGrid; 230999; 4. DR PhosphoSite; Q8BW72; -. DR PaxDb; Q8BW72; -. DR PRIDE; Q8BW72; -. DR Ensembl; ENSMUST00000097911; ENSMUSP00000095524; ENSMUSG00000033326. [Q8BW72-1] DR Ensembl; ENSMUST00000106403; ENSMUSP00000102011; ENSMUSG00000033326. [Q8BW72-1] DR Ensembl; ENSMUST00000106406; ENSMUSP00000102014; ENSMUSG00000033326. [Q8BW72-1] DR GeneID; 230674; -. DR KEGG; mmu:230674; -. DR UCSC; uc008ujn.2; mouse. [Q8BW72-1] DR CTD; 9682; -. DR MGI; MGI:2446210; Kdm4a. DR eggNOG; COG5141; -. DR GeneTree; ENSGT00530000063342; -. DR HOVERGEN; HBG080483; -. DR InParanoid; A2A8L8; -. DR KO; K06709; -. DR OMA; RKRTAGC; -. DR OrthoDB; EOG7TQV03; -. DR TreeFam; TF106449; -. DR ChiTaRS; Kdm4A; mouse. DR NextBio; 380043; -. DR PRO; PR:Q8BW72; -. DR ArrayExpress; Q8BW72; -. DR Bgee; Q8BW72; -. DR CleanEx; MM_JMJD2A; -. DR Genevestigator; Q8BW72; -. DR GO; GO:0005813; C:centrosome; IEA:Ensembl. DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl. DR GO; GO:0005730; C:nucleolus; IEA:Ensembl. DR GO; GO:0051864; F:histone demethylase activity (H3-K36 specific); IEA:Ensembl. DR GO; GO:0035064; F:methylated histone residue binding; ISS:UniProtKB. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0014898; P:cardiac muscle hypertrophy in response to stress; IMP:MGI. DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IEA:Ensembl. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 3.30.40.10; -; 1. DR InterPro; IPR003347; JmjC_dom. DR InterPro; IPR003349; TF_JmjN. DR InterPro; IPR002999; Tudor. DR InterPro; IPR011011; Znf_FYVE_PHD. DR InterPro; IPR001965; Znf_PHD. DR InterPro; IPR013083; Znf_RING/FYVE/PHD. DR Pfam; PF02373; JmjC; 1. DR Pfam; PF02375; JmjN; 1. DR SMART; SM00558; JmjC; 1. DR SMART; SM00545; JmjN; 1. DR SMART; SM00249; PHD; 2. DR SMART; SM00333; TUDOR; 2. DR SUPFAM; SSF57903; SSF57903; 1. DR PROSITE; PS51184; JMJC; 1. DR PROSITE; PS51183; JMJN; 1. PE 1: Evidence at protein level; KW Acetylation; Alternative splicing; Chromatin regulator; KW Complete proteome; Dioxygenase; Direct protein sequencing; Iron; KW Metal-binding; Nucleus; Oxidoreductase; Reference proteome; Repeat; KW Transcription; Transcription regulation; Ubl conjugation; Zinc; KW Zinc-finger. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 1064 Lysine-specific demethylase 4A. FT /FTId=PRO_0000183173. FT DOMAIN 14 56 JmjN. FT DOMAIN 142 308 JmjC. FT DOMAIN 897 954 Tudor 1. FT DOMAIN 955 1011 Tudor 2. FT ZN_FING 709 767 PHD-type 1. FT ZN_FING 829 885 PHD-type 2. FT REGION 597 638 Interaction with NCOR1 (By similarity). FT METAL 188 188 Iron; catalytic (By similarity). FT METAL 190 190 Iron; catalytic (By similarity). FT METAL 234 234 Zinc (By similarity). FT METAL 240 240 Zinc (By similarity). FT METAL 276 276 Iron; catalytic (By similarity). FT METAL 306 306 Zinc (By similarity). FT METAL 308 308 Zinc (By similarity). FT BINDING 132 132 Alpha-ketoglutarate (By similarity). FT BINDING 198 198 Alpha-ketoglutarate (By similarity). FT BINDING 206 206 Alpha-ketoglutarate (By similarity). FT BINDING 945 945 Histone H3K4me3 (By similarity). FT BINDING 967 967 Histone H3K4me3 (By similarity). FT BINDING 973 973 Histone H3K4me3 (By similarity). FT MOD_RES 2 2 N-acetylalanine (By similarity). FT VAR_SEQ 948 1033 SQDCLQLGPPAEGEVVQVRWTDGQVYGAKFVASHPIQMYQV FT EFEDGSQLVVKRDDVYTLDEELPKRVKSRLSVASDMRFNEI FT FTEK -> MSESGFWQHFGSSGTSSCYCRLDDCGLFACPWS FT VSKQKEPLFPGSLSRKSGHAGALSFPEEFRGVSVPCSPLKY FT AYISDQIISNSI (in isoform 2). FT /FTId=VSP_016144. FT VAR_SEQ 1034 1064 Missing (in isoform 2). FT /FTId=VSP_016145. FT CONFLICT 339 339 M -> T (in Ref. 1; BAC97997, 2; BAE26217 FT and 4; AAH28866). FT CONFLICT 1007 1007 D -> G (in Ref. 2; BAE26776). SQ SEQUENCE 1064 AA; 120334 MW; 92FB3E363FDF9E7D CRC64; MASESETLNP SARIMTFYPT MEEFRNFSRY IAYIESQGAH RAGLAKVVPP KEWKPRTSYD DIDDLVIPAP IQQLVTGQSG LFTQYNIQKK AMTVREFRKI ANSDKYCTPR YSEFEELERK YWKNLTFNPP IYGADVNGTL YEQHVDEWNI GRLKTILDLV EKESGITIEG VNTPYLYFGM WKTSFAWHTE DMDLYSINYL HFGEPKSWYS VPPEHGKRLE RLAKGFFPGS AQSCEAFLRH KMTLISPLML KKYGIPFDKV TQEAGEFMIT FPYGYHAGFN HGFNCAESTN FATRRWIEYG KQAVLCSCRK DMVKISMDVF VRRFQPERYK LWKAGKDSMV IDHTLPTPEA AEFLKDSGGL TPRAGSEECP EEDVEAADQG EEGDVKRSLA KHRIGTKRHR VCLEIPQEVS QSELFPKEEL SSGQYEMTEC PATLAPVRPT HSSVRQVEDS LPFPDYSDPT EVKFEELKNV KLEEEDEEDE PEAAALDLSV NPASVGGRLV FSGSKKKSSS SLGSTSSQDS VSSDSETAES VSCQGQEKTG VLTVHSYARG DGKAATGEPS VKKKRSAPRS ISEQELAEVA DEYMLSLEEN KKTKGRRQPL SKLPRHHPLV LQECGSDDET SEQLTPEEEA EETEAWAKPL SQLWQNRPPN FEAEKEFNEI MAQQAPHCAV CMIFQTYHQV EFGAFSQSCG DASEPAAQTQ RTKPLIPEMC FTTTGCSTDI NLSTPYLEED GTSMLVSCKK CSVRVHASCY GVPPAKASEE WMCSRCSANA LEEDCCLCSL RGGALQRAND DRWVHVSCAV AILEARFVNI AERSPVDVSK IPLPRFKLKC VFCKKRRKRN AGCCVQCSHG RCPTAFHVSC AQAAGVMMQP DDWPFVVFIT CFRHKIPNLE RAKGALLSIT AGQKVISKHK NGRFYQCEVV RLTTETFYEV NFDDGSFSDN LYPEDIVSQD CLQLGPPAEG EVVQVRWTDG QVYGAKFVAS HPIQMYQVEF EDGSQLVVKR DDVYTLDEEL PKRVKSRLSV ASDMRFNEIF TEKEVKQEKK RQRVINSRYR EDYIEPALYR AIME // ID KDM4C_MOUSE Reviewed; 1054 AA. AC Q8VCD7; Q3UNP7; Q69ZZ5; Q8BUY6; Q8BWA1; DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2002, sequence version 1. DT 19-MAR-2014, entry version 100. DE RecName: Full=Lysine-specific demethylase 4C; DE EC=1.14.11.-; DE AltName: Full=JmjC domain-containing histone demethylation protein 3C; DE AltName: Full=Jumonji domain-containing protein 2C; GN Name=Kdm4c; Synonyms=Jhdm3c, Jmjd2c, Kiaa0780; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Pancreatic islet; RX PubMed=15368895; DOI=10.1093/dnares/11.3.205; RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H., RA Nagase T., Ohara O., Koga H.; RT "Prediction of the coding sequences of mouse homologues of KIAA gene: RT IV. The complete nucleotide sequences of 500 mouse KIAA-homologous RT cDNAs identified by screening of terminal sequences of cDNA clones RT randomly sampled from size-fractionated libraries."; RL DNA Res. 11:205-218(2004). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C3H, and C57BL/6J; TISSUE=Brain, and Head; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Eye, and Salivary gland; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP PROTEIN SEQUENCE OF 815-829, AND MASS SPECTROMETRY. RC STRAIN=OF1; TISSUE=Hippocampus; RA Lubec G., Sunyer B., Chen W.-Q.; RL Submitted (JAN-2009) to UniProtKB. CC -!- FUNCTION: Histone demethylase that specifically demethylates 'Lys- CC 9' and 'Lys-36' residues of histone H3, thereby playing a central CC role in histone code. Does not demethylate histone H3 'Lys-4', H3 CC 'Lys-27' nor H4 'Lys-20'. Demethylates trimethylated H3 'Lys-9' CC and H3 'Lys-36' residue, while it has no activity on mono- and CC dimethylated residues. Demethylation of Lys residue generates CC formaldehyde and succinate (By similarity). CC -!- COFACTOR: Binds 1 Fe(2+) ion per subunit (By similarity). CC -!- SUBCELLULAR LOCATION: Nucleus (By similarity). CC -!- DOMAIN: The 2 Tudor domains recognize and bind methylated CC histones. Double Tudor domain has an interdigitated structure and CC the unusual fold is required for its ability to bind methylated CC histone tails (By similarity). CC -!- SIMILARITY: Belongs to the JHDM3 histone demethylase family. CC -!- SIMILARITY: Contains 1 JmjC domain. CC -!- SIMILARITY: Contains 1 JmjN domain. CC -!- SIMILARITY: Contains 2 PHD-type zinc fingers. CC -!- SIMILARITY: Contains 2 Tudor domains. CC -!- SEQUENCE CAUTION: CC Sequence=BAD32301.1; Type=Erroneous initiation; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK173023; BAD32301.1; ALT_INIT; mRNA. DR EMBL; AK053104; BAC35267.1; -; mRNA. DR EMBL; AK081769; BAC38327.1; -; mRNA. DR EMBL; AK144103; BAE25700.1; -; mRNA. DR EMBL; BC020180; AAH20180.1; -; mRNA. DR EMBL; BC042424; AAH42424.1; -; mRNA. DR RefSeq; NP_001165566.1; NM_001172095.1. DR RefSeq; NP_659036.1; NM_144787.2. DR RefSeq; XP_006538415.1; XM_006538352.1. DR RefSeq; XP_006538416.1; XM_006538353.1. DR UniGene; Mm.209059; -. DR ProteinModelPortal; Q8VCD7; -. DR SMR; Q8VCD7; 10-347, 874-992. DR BioGrid; 218326; 8. DR STRING; 10090.ENSMUSP00000077017; -. DR PhosphoSite; Q8VCD7; -. DR PRIDE; Q8VCD7; -. DR Ensembl; ENSMUST00000030102; ENSMUSP00000030102; ENSMUSG00000028397. DR Ensembl; ENSMUST00000077851; ENSMUSP00000077017; ENSMUSG00000028397. DR GeneID; 76804; -. DR KEGG; mmu:76804; -. DR UCSC; uc008tjj.2; mouse. DR CTD; 23081; -. DR MGI; MGI:1924054; Kdm4c. DR eggNOG; COG5141; -. DR GeneTree; ENSGT00530000063342; -. DR HOGENOM; HOG000231125; -. DR InParanoid; Q8VCD7; -. DR KO; K06709; -. DR OMA; DIIQGER; -. DR OrthoDB; EOG7TQV03; -. DR TreeFam; TF106449; -. DR NextBio; 345851; -. DR PRO; PR:Q8VCD7; -. DR ArrayExpress; Q8VCD7; -. DR Bgee; Q8VCD7; -. DR CleanEx; MM_JMJD2C; -. DR Genevestigator; Q8VCD7; -. DR GO; GO:0000790; C:nuclear chromatin; IEA:Ensembl. DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW. DR GO; GO:0032454; F:histone demethylase activity (H3-K9 specific); ISS:UniProtKB. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0008284; P:positive regulation of cell proliferation; IEA:Ensembl. DR GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; IEA:Ensembl. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 3.30.40.10; -; 1. DR InterPro; IPR003347; JmjC_dom. DR InterPro; IPR003349; TF_JmjN. DR InterPro; IPR002999; Tudor. DR InterPro; IPR011011; Znf_FYVE_PHD. DR InterPro; IPR001965; Znf_PHD. DR InterPro; IPR013083; Znf_RING/FYVE/PHD. DR Pfam; PF02373; JmjC; 1. DR Pfam; PF02375; JmjN; 1. DR SMART; SM00558; JmjC; 1. DR SMART; SM00545; JmjN; 1. DR SMART; SM00249; PHD; 2. DR SMART; SM00333; TUDOR; 2. DR SUPFAM; SSF57903; SSF57903; 1. DR PROSITE; PS51184; JMJC; 1. DR PROSITE; PS51183; JMJN; 1. PE 1: Evidence at protein level; KW Chromatin regulator; Complete proteome; Dioxygenase; KW Direct protein sequencing; Iron; Metal-binding; Nucleus; KW Oxidoreductase; Reference proteome; Repeat; Transcription; KW Transcription regulation; Zinc; Zinc-finger. FT CHAIN 1 1054 Lysine-specific demethylase 4C. FT /FTId=PRO_0000183178. FT DOMAIN 16 58 JmjN. FT DOMAIN 144 310 JmjC. FT DOMAIN 875 932 Tudor 1. FT DOMAIN 933 989 Tudor 2. FT ZN_FING 687 745 PHD-type 1. FT ZN_FING 807 863 PHD-type 2. FT METAL 190 190 Iron; catalytic (By similarity). FT METAL 192 192 Iron; catalytic (By similarity). FT METAL 236 236 Zinc (By similarity). FT METAL 242 242 Zinc (By similarity). FT METAL 278 278 Iron; catalytic (By similarity). FT METAL 308 308 Zinc (By similarity). FT METAL 310 310 Zinc (By similarity). FT BINDING 134 134 Alpha-ketoglutarate (By similarity). FT BINDING 200 200 Alpha-ketoglutarate (By similarity). FT BINDING 208 208 Alpha-ketoglutarate (By similarity). FT CONFLICT 300 300 D -> V (in Ref. 2; BAC35267). FT CONFLICT 687 687 M -> V (in Ref. 2; BAE25700). SQ SEQUENCE 1054 AA; 119966 MW; 86F275FC428B8EDA CRC64; MEVVEVESPL NPSCKIMTFR PSMEEFREFN KYLAYMESKG AHRAGLAKVI PPKEWKPRQC YDDIDNLLIP APIQQMVTGQ SGLFTQYNIQ KKAMTVKEFR QLANSSKYCT PRYLDYEDLE RKYWKNLTFV APIYGADING SIYDEGVDEW NIARLNTVLD VVEEECGISI EGVNTPYLYF GMWKTTFAWH TEDMDLYSIN YLHFGEPKSW YAIPPEHGKR LERLAQGFFP SSSQGCDAFL RHKMTLISPS VLKKYGIPFD KITQEAGEFM ITFPYGYHAG FNHGFNCAES TNFATVRWID YGKVAKLCTC RNDMVKISMD IFVKKFQPDR YQIWKQGKDI YTIDHTKPTP ESTPEVKTWL QRKKKLRKPP KSLQGNKPLC KRPKPEEDEE FAEFSGEEGA NPAMGPRHLK VTEKPEKALK LGKLEESSAK EALDTRIQVD QSLLNDTKLS GKGCISSSVT AEIPPEDNRA SAVISPSQLK EGADCIPLSH GHQAGKESHL LKILKLESPK IPSPLPESNK VLTEGEENDE EGHGSNLEPG EIPEALSEER NGLNIPKIIE GQPKTTKSWR HPLGKPPARS PMTLVKQQVA SDEELPEVLS IDEEVEETES WAKPLIHLWQ TKSPNFMAEQ EYNATVAKME PNCAICTLLM PYYKPDSSKE ENDSRWETAV NEVVQSGRKT KPIIPEMCFI YSEENVDYSP PNAFLEEDGT SLLISCAKCF VRVHASCYGV PSHEVCDGWL CARCKRNAWT AECCLCNLRG GALKQTKNNQ WAHVICAVAV PEVRFTNVPE RTQIDVDRIP LQRLKLKCIF CRHRVKKVSG ACIQCSYGRC PASFHVTCAH AAGVLMEPDD WPYVVNITCF RHRVNSNAKS KTCEKAISVG QTVITKHRNT RYYSCRVIDV TSQTFYEVMF DDGSFSRDTF PEDIVSRNCV KLGPPAEGEV IQVKWPDGKL YGAKYLGSNV AYMYQVEFED GSQIAMKRED IYTLDEELPK RVKARFSTAS DMRFEDTFYG ADVIQGERKR QRVLSSRLKN EYVDDPVYRT FLKSSFQKKC QKRQ // ID KDM4D_MOUSE Reviewed; 510 AA. AC Q3U2K5; A2CGB5; B8JK34; Q2M1G7; Q8BI19; DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 16-MAY-2006, sequence version 2. DT 19-MAR-2014, entry version 65. DE RecName: Full=Lysine-specific demethylase 4D; DE EC=1.14.11.-; DE AltName: Full=JmjC domain-containing histone demethylation protein 3D; DE AltName: Full=Jumonji domain-containing protein 2D; GN Name=Kdm4d; Synonyms=Jhdm3d, Jmjd2d; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J, and NOD; TISSUE=Testis; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 106-510. RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: Histone demethylase that specifically demethylates 'Lys- CC 9' of histone H3, thereby playing a central role in histone code. CC Does not demethylate histone H3 'Lys-4', H3 'Lys-27', H3 'Lys-36' CC nor H4 'Lys-20'. Demethylates both di- and trimethylated H3 'Lys- CC 9' residue, while it has no activity on monomethylated residues. CC Demethylation of Lys residue generates formaldehyde and succinate CC (By similarity). CC -!- COFACTOR: Binds 1 Fe(2+) ion per subunit (By similarity). CC -!- SUBCELLULAR LOCATION: Nucleus (By similarity). CC -!- SIMILARITY: Belongs to the JHDM3 histone demethylase family. CC -!- SIMILARITY: Contains 1 JmjC domain. CC -!- SIMILARITY: Contains 1 JmjN domain. CC -!- SEQUENCE CAUTION: CC Sequence=BAC26740.1; Type=Erroneous initiation; Note=Translation N-terminally extended; CC Sequence=BAC26740.1; Type=Erroneous termination; Positions=209; Note=Translated as Trp; CC Sequence=BAE33135.1; Type=Frameshift; Positions=419; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK030020; BAC26740.1; ALT_SEQ; mRNA. DR EMBL; AK155227; BAE33135.1; ALT_FRAME; mRNA. DR EMBL; CT485607; CAM15687.1; -; Genomic_DNA. DR EMBL; CT485607; CAX15698.1; -; Genomic_DNA. DR EMBL; BC112372; AAI12373.1; -; mRNA. DR RefSeq; NP_775609.2; NM_173433.2. DR RefSeq; XP_006510333.1; XM_006510270.1. DR RefSeq; XP_006510334.1; XM_006510271.1. DR UniGene; Mm.240457; -. DR ProteinModelPortal; Q3U2K5; -. DR SMR; Q3U2K5; 8-338. DR PhosphoSite; Q3U2K5; -. DR PRIDE; Q3U2K5; -. DR DNASU; 244694; -. DR Ensembl; ENSMUST00000058796; ENSMUSP00000061632; ENSMUSG00000053914. DR GeneID; 244694; -. DR KEGG; mmu:244694; -. DR UCSC; uc009oen.1; mouse. DR CTD; 55693; -. DR MGI; MGI:3606484; Kdm4d. DR eggNOG; NOG317950; -. DR GeneTree; ENSGT00530000063342; -. DR HOGENOM; HOG000231125; -. DR InParanoid; A2CGB5; -. DR KO; K06709; -. DR OMA; TMKSKAN; -. DR OrthoDB; EOG7TQV03; -. DR TreeFam; TF106449; -. DR NextBio; 386391; -. DR PRO; PR:Q3U2K5; -. DR Bgee; Q3U2K5; -. DR CleanEx; MM_JMJD2D; -. DR Genevestigator; Q3U2K5; -. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0033169; P:histone H3-K9 demethylation; IMP:MGI. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR InterPro; IPR003347; JmjC_dom. DR InterPro; IPR003349; TF_JmjN. DR Pfam; PF02373; JmjC; 1. DR Pfam; PF02375; JmjN; 1. DR SMART; SM00558; JmjC; 1. DR PROSITE; PS51184; JMJC; 1. DR PROSITE; PS51183; JMJN; 1. PE 2: Evidence at transcript level; KW ADP-ribosylation; Chromatin regulator; Complete proteome; Dioxygenase; KW Iron; Metal-binding; Nucleus; Oxidoreductase; Reference proteome; KW Transcription; Transcription regulation; Zinc. FT CHAIN 1 510 Lysine-specific demethylase 4D. FT /FTId=PRO_0000234377. FT DOMAIN 15 57 JmjN. FT DOMAIN 143 309 JmjC. FT COMPBIAS 88 91 Poly-Lys. FT METAL 189 189 Iron; catalytic (By similarity). FT METAL 191 191 Iron; catalytic (By similarity). FT METAL 235 235 Zinc (By similarity). FT METAL 241 241 Zinc (By similarity). FT METAL 277 277 Iron; catalytic (By similarity). FT METAL 307 307 Zinc (By similarity). FT METAL 309 309 Zinc (By similarity). FT BINDING 133 133 Alpha-ketoglutarate (By similarity). FT BINDING 199 199 Alpha-ketoglutarate (By similarity). FT BINDING 207 207 Alpha-ketoglutarate (By similarity). FT MOD_RES 23 23 PolyADP-ribosyl glutamic acid (By FT similarity). FT MOD_RES 24 24 PolyADP-ribosyl glutamic acid (By FT similarity). FT CONFLICT 374 374 R -> L (in Ref. 1; BAC26740). SQ SEQUENCE 510 AA; 57212 MW; 6B57A0300BAD94C9 CRC64; MKTKSTCAQN PNCSIMIFRP TKEEFNDFDK YIAYMESQGA HRAGLAKVIP PKEWRARQSY DNISNILIAT PLQQVVSGQA GVFTQYHKKK KGMTVGEYRE LANSKKYQTP PHLDFEDLER KYWKNRLYES PIYGADVSGS LFDGKTQQWN VGHLGTIQDL LEQECGIVIE GVNTPYLYFG MWKTTFAWHT EDMDLYSINY LHFGQPKTWY AVPPEHGRRL ERLARELFPG SSQGCQAFLR HKVALISPTV LKENGIPFGR ITQEAGEFMV TFPYGYHAGF NHGFNCAEAI NFATPRWIDY GKVASQCSCG EARVSFSMDA FVRILQPERY ELWKRGQDQA VVDHTETMVS TSQELTTRRV TKAPRKTWGL KRLRLRQVSR SLLPIATVSN VPCNMQVCHT SRQPSDVKGD DVQKSDSARA SPHPLSLPSS GHMSTRRCSL GRRPCELGAQ ESSNGAPVKR QLPAGRDDTS PSPELQPQAV SGDLIVDSGL VNPGPQHLMT ASEGGLTSDP // ID KDM2A_MOUSE Reviewed; 1161 AA. AC P59997; Q3U1M5; Q3UR56; Q3V3Q1; Q69ZT4; DT 07-NOV-2003, integrated into UniProtKB/Swiss-Prot. DT 07-MAR-2006, sequence version 2. DT 19-MAR-2014, entry version 100. DE RecName: Full=Lysine-specific demethylase 2A; DE EC=1.14.11.27; DE AltName: Full=F-box and leucine-rich repeat protein 11; DE AltName: Full=F-box/LRR-repeat protein 11; DE AltName: Full=JmjC domain-containing histone demethylation protein 1A; DE AltName: Full=[Histone-H3]-lysine-36 demethylase 1A; GN Name=Kdm2a; Synonyms=Fbxl11, Jhdm1a, Kiaa1004; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), AND RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 646-1161. RC STRAIN=C57BL/6J; TISSUE=Skin; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC STRAIN=C57BL/6; TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 453-1161. RC TISSUE=Thymus; RX PubMed=15368895; DOI=10.1093/dnares/11.3.205; RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H., RA Nagase T., Ohara O., Koga H.; RT "Prediction of the coding sequences of mouse homologues of KIAA gene: RT IV. The complete nucleotide sequences of 500 mouse KIAA-homologous RT cDNAs identified by screening of terminal sequences of cDNA clones RT randomly sampled from size-fractionated libraries."; RL DNA Res. 11:205-218(2004). RN [4] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-550, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=17242355; DOI=10.1073/pnas.0609836104; RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; RT "Large-scale phosphorylation analysis of mouse liver."; RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). RN [5] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-632, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic fibroblast; RX PubMed=17525332; DOI=10.1126/science.1140321; RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, RA Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., RA Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.; RT "ATM and ATR substrate analysis reveals extensive protein networks RT responsive to DNA damage."; RL Science 316:1160-1166(2007). CC -!- FUNCTION: Histone demethylase that specifically demethylates 'Lys- CC 36' of histone H3, thereby playing a central role in histone code. CC Preferentially demethylates dimethylated H3 'Lys-36' residue while CC it has weak or no activity for mono- and tri-methylated H3 'Lys- CC 36'. May also recognize and bind to some phosphorylated proteins CC and promote their ubiquitination and degradation. Required to CC maintain the heterochromatic state. Associates with centromeres CC and represses transcription of small non-coding RNAs that are CC encoded by the clusters of satellite repeats at the centromere. CC Required to sustain centromeric integrity and genomic stability, CC particularly during mitosis (By similarity). CC -!- CATALYTIC ACTIVITY: Protein N(6),N(6)-dimethyl-L-lysine + 2- CC oxoglutarate + O(2) = protein N(6)-methyl-L-lysine + succinate + CC formaldehyde + CO(2). CC -!- CATALYTIC ACTIVITY: Protein N(6)-methyl-L-lysine + 2-oxoglutarate CC + O(2) = protein L-lysine + succinate + formaldehyde + CO(2). CC -!- COFACTOR: Binds 1 Fe(2+) ion per subunit (By similarity). CC -!- SUBUNIT: Part of a SCF (SKP1-cullin-F-box) protein ligase complex. CC Interacts with CBX5/HP1A; the interaction promotes CBX5 CC localization to chromatin (By similarity). CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm (By similarity). CC Note=Punctate expression throughout the nucleoplasm and enriched CC in the perinucleolar region. Specifically nucleates at CpG islands CC where it's presence results in chromatin depleted in H3K36me2 (By CC similarity). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=P59997-1; Sequence=Displayed; CC Name=2; CC IsoId=P59997-2; Sequence=VSP_017473, VSP_017474; CC Note=No experimental confirmation available; CC Name=3; CC IsoId=P59997-3; Sequence=VSP_017471, VSP_017472; CC Note=No experimental confirmation available; CC -!- DOMAIN: The JmjC domain mediates demethylation activity and is CC required for satellite silencing (By similarity). CC -!- DOMAIN: The CXXC zinc finger preferentially recognizes CC nonmethylated CpG DNA, and binding is blocked when the CpG DNA is CC methylated (By similarity). CC -!- SIMILARITY: Belongs to the JHDM1 histone demethylase family. CC -!- SIMILARITY: Contains 1 CXXC-type zinc finger. CC -!- SIMILARITY: Contains 1 F-box domain. CC -!- SIMILARITY: Contains 1 JmjC domain. CC -!- SIMILARITY: Contains 6 LRR (leucine-rich) repeats. CC -!- SIMILARITY: Contains 1 PHD-type zinc finger. CC -!- SEQUENCE CAUTION: CC Sequence=BC076576; Type=Frameshift; Positions=834; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK037157; BAE20506.1; -; mRNA. DR EMBL; AK141779; BAE24832.1; -; mRNA. DR EMBL; AK155866; BAE33470.1; -; mRNA. DR EMBL; BC057051; AAH57051.1; -; mRNA. DR EMBL; BC076576; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; AK173084; BAD32362.1; -; mRNA. DR RefSeq; NP_001001984.2; NM_001001984.2. DR UniGene; Mm.31941; -. DR ProteinModelPortal; P59997; -. DR SMR; P59997; 34-517, 567-676, 890-1139. DR DIP; DIP-46352N; -. DR PhosphoSite; P59997; -. DR PaxDb; P59997; -. DR PRIDE; P59997; -. DR GeneID; 225876; -. DR KEGG; mmu:225876; -. DR UCSC; uc008fzy.1; mouse. [P59997-3] DR CTD; 22992; -. DR MGI; MGI:1354736; Kdm2a. DR eggNOG; NOG290496; -. DR HOGENOM; HOG000007396; -. DR KO; K10276; -. DR ChiTaRS; KDM2A; mouse. DR NextBio; 377841; -. DR PRO; PR:P59997; -. DR CleanEx; MM_FBXL11; -. DR Genevestigator; P59997; -. DR GO; GO:0000790; C:nuclear chromatin; IDA:MGI. DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0051864; F:histone demethylase activity (H3-K36 specific); IEA:UniProtKB-EC. DR GO; GO:0045322; F:unmethylated CpG binding; IDA:MGI. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0070544; P:histone H3-K36 demethylation; IEA:GOC. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 3.30.40.10; -; 1. DR InterPro; IPR001810; F-box_dom. DR InterPro; IPR003347; JmjC_dom. DR InterPro; IPR019786; Zinc_finger_PHD-type_CS. DR InterPro; IPR002857; Znf_CXXC. DR InterPro; IPR011011; Znf_FYVE_PHD. DR InterPro; IPR001965; Znf_PHD. DR InterPro; IPR019787; Znf_PHD-finger. DR InterPro; IPR013083; Znf_RING/FYVE/PHD. DR Pfam; PF00646; F-box; 1. DR Pfam; PF02373; JmjC; 1. DR Pfam; PF02008; zf-CXXC; 1. DR SMART; SM00256; FBOX; 1. DR SMART; SM00558; JmjC; 1. DR SMART; SM00249; PHD; 1. DR SUPFAM; SSF57903; SSF57903; 1. DR PROSITE; PS51184; JMJC; 1. DR PROSITE; PS51058; ZF_CXXC; 1. DR PROSITE; PS01359; ZF_PHD_1; 1. DR PROSITE; PS50016; ZF_PHD_2; 1. PE 1: Evidence at protein level; KW Alternative splicing; Chromatin regulator; Complete proteome; KW Dioxygenase; DNA-binding; Iron; Leucine-rich repeat; Metal-binding; KW Nucleus; Oxidoreductase; Phosphoprotein; Reference proteome; Repeat; KW Repressor; Transcription; Transcription regulation; KW Ubl conjugation pathway; Zinc; Zinc-finger. FT CHAIN 1 1161 Lysine-specific demethylase 2A. FT /FTId=PRO_0000119856. FT DOMAIN 148 316 JmjC. FT DOMAIN 888 935 F-box. FT REPEAT 960 981 LRR 1. FT REPEAT 983 1009 LRR 2. FT REPEAT 1047 1072 LRR 3. FT REPEAT 1073 1102 LRR 4. FT REPEAT 1103 1127 LRR 5. FT REPEAT 1128 1155 LRR 6. FT ZN_FING 564 610 CXXC-type. FT ZN_FING 617 678 PHD-type. FT METAL 212 212 Iron; catalytic (By similarity). FT METAL 214 214 Iron; catalytic (By similarity). FT METAL 284 284 Iron; catalytic (By similarity). FT BINDING 209 209 Substrate (By similarity). FT BINDING 229 229 Substrate (By similarity). FT MOD_RES 28 28 Phosphoserine (By similarity). FT MOD_RES 390 390 Phosphoserine (By similarity). FT MOD_RES 394 394 Phosphoserine (By similarity). FT MOD_RES 550 550 Phosphothreonine. FT MOD_RES 558 558 Phosphoserine (By similarity). FT MOD_RES 632 632 Phosphothreonine. FT MOD_RES 692 692 Phosphoserine (By similarity). FT MOD_RES 713 713 Phosphothreonine (By similarity). FT MOD_RES 731 731 Phosphoserine (By similarity). FT MOD_RES 868 868 Phosphoserine (By similarity). FT MOD_RES 882 882 Phosphoserine (By similarity). FT VAR_SEQ 321 338 PNKFRYPFYYEMCWYVLE -> SNVTIICVDVSPFKADVR FT (in isoform 3). FT /FTId=VSP_017471. FT VAR_SEQ 339 1161 Missing (in isoform 3). FT /FTId=VSP_017472. FT VAR_SEQ 494 494 I -> S (in isoform 2). FT /FTId=VSP_017473. FT VAR_SEQ 495 1161 Missing (in isoform 2). FT /FTId=VSP_017474. FT CONFLICT 159 159 W -> R (in Ref. 1; BAE20506 and 2; FT BC076576). FT CONFLICT 202 202 I -> M (in Ref. 1; BAE20506 and 2; FT BC076576). FT CONFLICT 913 913 M -> I (in Ref. 2; AAH57051). SQ SEQUENCE 1161 AA; 132680 MW; 210BD9F65BED0AE4 CRC64; MEPEEERIRY SQRLRGTMRR RYEDDGISDD EIEGKRTFDL EEKLQTNKYN ANFVTFMEGK DFNVEYIQRG GLRDPLIFKN SDGLGIKMPD PDFTVNDVKM CVGSRRMVDV MDVNTQKGIE MTMAQWTRYY ETPEEEREKL YNVISLEFSH TRLENMVQWP STVDFIDWVD NMWPRHLKES QTESTNAILE MQYPKVQKYC LISVRGCYTD FHVDFGGTSV WYHIHQGGKV FWLIPPTAHN LELYENWLLS GKQGDIFLGD RVSDCQRIEL KQGYTFVIPS GWIHAVYTPT DTLVFGGNFL HSFNIPMQLK IYSIEDRTRV PNKFRYPFYY EMCWYVLERY VYCITNRSHL TKDFQKESLS MDMELNELES GNGDEEGVDR EARRMNNKRS VLTSPVANGV NLDYDGLGKA CRSLPSLKKT LSGDSSSDST RGSHNGQVWD PQCSPKKDRQ VHLTHFELEG LRCLVDKLES LPLHKKCVPT GIEDEDALIA DVKILLEELA SSDPKLALTG VPIVQWPKRD KLKFPTRPKV RVPTIPITKP HTMKPAPRLT PVRPAAASPI VSGARRRRVR CRKCKACVQG ECGVCHYCRD MKKFGGPGRM KQSCVLRQCL APRLPHSVTC SLCGEVDQNE ETQDFEKKLM ECCICNEIVH PGCLQMDGEG LLNEELPNCW ECPKCYQEDS SDKAQKRKIE ESDEEAVQAK VLRPLRSCEE PLTPPPHSPT SMLQLIHDPV SPRGMVTRSS PGAGPSDHHS ASRDERFKRR QLLRLQATER TMVREKENNP SGKKELSEVE KAKIRGSYLT VTLQRPTKEL HGTSIVPKLQ AITASSANLR PNPRVLMQHC PARNPQHGDE EGLGGEEEEE EEEEEDDSAE EGGAARLNGR GSWAQDGDES WMQREVWMSV FRYLSRKELC ECMRVCKTWY KWCCDKRLWT KIDLSRCKAI VPQALSGIIK RQPVSLDLSW TNISKKQLTW LVNRLPGLKD LLLAGCSWSA VSALSTSSCP LLRTLDLRWA VGIKDPQIRD LLTPPTDKPG QDNRSKLRNM TDFRLAGLDI TDATLRLIIR HMPLLSRLDL SHCSHLTDQS SNLLTAVGSS TRYSLTELNM AGCNKLTDQT LFFLRRIANV TLIDLRGCKQ ITRKACEHFI SDLSINSLYC LSDEKLIQKI S // ID KDM2B_MOUSE Reviewed; 1309 AA. AC Q6P1G2; Q3V396; Q6PFD0; Q6ZPE8; Q9CSF7; Q9QZN6; DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 19-MAR-2014, entry version 108. DE RecName: Full=Lysine-specific demethylase 2B; DE EC=1.14.11.27; DE AltName: Full=F-box and leucine-rich repeat protein 10; DE AltName: Full=F-box protein FBL10; DE AltName: Full=F-box/LRR-repeat protein 10; DE AltName: Full=JmjC domain-containing histone demethylation protein 1B; DE AltName: Full=[Histone-H3]-lysine-36 demethylase 1B; GN Name=Kdm2b; Synonyms=Fbl10, Fbxl10, Jhdm1b, Kiaa3014; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4). RC STRAIN=C57BL/6J; TISSUE=Cerebellum, and Embryo; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC STRAIN=C57BL/6; TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 6-1309 (ISOFORM 1). RC TISSUE=Brain; RX PubMed=14621295; DOI=10.1093/dnares/10.4.167; RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., RA Saga Y., Nagase T., Ohara O., Koga H.; RT "Prediction of the coding sequences of mouse homologues of KIAA gene: RT III. The complete nucleotide sequences of 500 mouse KIAA-homologous RT cDNAs identified by screening of terminal sequences of cDNA clones RT randomly sampled from size-fractionated libraries."; RL DNA Res. 10:167-180(2003). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1011-1309 (ISOFORMS 1/2). RX PubMed=10531037; DOI=10.1016/S0960-9822(00)80021-4; RA Winston J.T., Koepp D.M., Zhu C., Elledge S.J., Harper J.W.; RT "A family of mammalian F-box proteins."; RL Curr. Biol. 9:1180-1182(1999). CC -!- FUNCTION: Histone demethylase that demethylates 'Lys-4' and 'Lys- CC 36' of histone H3, thereby playing a central role in histone code. CC Preferentially demethylates trimethylated H3 'Lys-4' and CC dimethylated H3 'Lys-36' residue while it has weak or no activity CC for mono- and tri-methylated H3 'Lys-36'. Preferentially binds the CC transcribed region of ribosomal RNA and represses the CC transcription of ribosomal RNA genes which inhibits cell growth CC and proliferation. May also serve as a substrate-recognition CC component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin CC ligase complex (By similarity). CC -!- CATALYTIC ACTIVITY: Protein N(6),N(6)-dimethyl-L-lysine + 2- CC oxoglutarate + O(2) = protein N(6)-methyl-L-lysine + succinate + CC formaldehyde + CO(2). CC -!- CATALYTIC ACTIVITY: Protein N(6)-methyl-L-lysine + 2-oxoglutarate CC + O(2) = protein L-lysine + succinate + formaldehyde + CO(2). CC -!- COFACTOR: Binds 1 Fe(2+) ion per subunit (By similarity). CC -!- SUBUNIT: Directly interacts with SKP1 and CUL1 (By similarity). CC -!- INTERACTION: CC Q9CQJ4:Rnf2; NbExp=4; IntAct=EBI-1216214, EBI-927321; CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus (By similarity). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; CC IsoId=Q6P1G2-1; Sequence=Displayed; CC Name=2; CC IsoId=Q6P1G2-2; Sequence=VSP_011342, VSP_011343; CC Name=3; CC IsoId=Q6P1G2-3; Sequence=VSP_017477, VSP_017478; CC Note=No experimental confirmation available; CC Name=4; CC IsoId=Q6P1G2-4; Sequence=VSP_019003; CC Note=No experimental confirmation available; CC -!- DOMAIN: The JmjC domain mediates demethylation activity. It is CC also required for repression of ribosomal RNA genes (By CC similarity). CC -!- SIMILARITY: Belongs to the JHDM1 histone demethylase family. CC -!- SIMILARITY: Contains 1 CXXC-type zinc finger. CC -!- SIMILARITY: Contains 1 F-box domain. CC -!- SIMILARITY: Contains 1 JmjC domain. CC -!- SIMILARITY: Contains 6 LRR (leucine-rich) repeats. CC -!- SIMILARITY: Contains 1 PHD-type zinc finger. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK012952; BAB28568.2; -; mRNA. DR EMBL; AK043352; BAE20639.1; -; mRNA. DR EMBL; BC057622; AAH57622.1; -; mRNA. DR EMBL; BC065090; AAH65090.1; -; mRNA. DR EMBL; AK129479; BAC98289.1; -; mRNA. DR EMBL; AF176524; AAF09133.1; -; mRNA. DR RefSeq; NP_001003953.1; NM_001003953.1. DR RefSeq; NP_001005866.1; NM_001005866.1. DR RefSeq; NP_038938.1; NM_013910.2. DR UniGene; Mm.86406; -. DR ProteinModelPortal; Q6P1G2; -. DR SMR; Q6P1G2; 33-546, 582-695, 1037-1306. DR BioGrid; 205978; 19. DR DIP; DIP-46351N; -. DR IntAct; Q6P1G2; 11. DR PhosphoSite; Q6P1G2; -. DR PRIDE; Q6P1G2; -. DR Ensembl; ENSMUST00000031435; ENSMUSP00000031435; ENSMUSG00000029475. [Q6P1G2-2] DR Ensembl; ENSMUST00000046073; ENSMUSP00000038229; ENSMUSG00000029475. [Q6P1G2-1] DR GeneID; 30841; -. DR KEGG; mmu:30841; -. DR UCSC; uc008zmq.2; mouse. [Q6P1G2-2] DR UCSC; uc008zms.2; mouse. [Q6P1G2-1] DR UCSC; uc008zmu.1; mouse. [Q6P1G2-3] DR CTD; 84678; -. DR MGI; MGI:1354737; Kdm2b. DR eggNOG; NOG290496; -. DR GeneTree; ENSGT00550000074396; -. DR HOGENOM; HOG000007396; -. DR InParanoid; Q6P1G2; -. DR KO; K10276; -. DR OMA; NAEDRMA; -. DR OrthoDB; EOG78SQH0; -. DR TreeFam; TF106480; -. DR NextBio; 307252; -. DR PRO; PR:Q6P1G2; -. DR ArrayExpress; Q6P1G2; -. DR Bgee; Q6P1G2; -. DR CleanEx; MM_FBXL10; -. DR Genevestigator; Q6P1G2; -. DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell. DR GO; GO:0031519; C:PcG protein complex; IEA:Ensembl. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0032452; F:histone demethylase activity; TAS:BHF-UCL. DR GO; GO:0051864; F:histone demethylase activity (H3-K36 specific); IEA:UniProtKB-EC. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0048596; P:embryonic camera-type eye morphogenesis; IMP:BHF-UCL. DR GO; GO:0021592; P:fourth ventricle development; IMP:BHF-UCL. DR GO; GO:0035518; P:histone H2A monoubiquitination; IEA:Ensembl. DR GO; GO:0070544; P:histone H3-K36 demethylation; IEA:GOC. DR GO; GO:0021993; P:initiation of neural tube closure; IMP:BHF-UCL. DR GO; GO:0021670; P:lateral ventricle development; IMP:BHF-UCL. DR GO; GO:0030901; P:midbrain development; IMP:BHF-UCL. DR GO; GO:0021555; P:midbrain-hindbrain boundary morphogenesis; IMP:BHF-UCL. DR GO; GO:2000178; P:negative regulation of neural precursor cell proliferation; IMP:BHF-UCL. DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IMP:BHF-UCL. DR GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IMP:BHF-UCL. DR GO; GO:0007283; P:spermatogenesis; IMP:BHF-UCL. DR GO; GO:0021678; P:third ventricle development; IMP:BHF-UCL. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 3.30.40.10; -; 1. DR InterPro; IPR001810; F-box_dom. DR InterPro; IPR003347; JmjC_dom. DR InterPro; IPR002857; Znf_CXXC. DR InterPro; IPR011011; Znf_FYVE_PHD. DR InterPro; IPR001965; Znf_PHD. DR InterPro; IPR019787; Znf_PHD-finger. DR InterPro; IPR013083; Znf_RING/FYVE/PHD. DR Pfam; PF00646; F-box; 1. DR Pfam; PF02008; zf-CXXC; 1. DR SMART; SM00256; FBOX; 1. DR SMART; SM00558; JmjC; 1. DR SMART; SM00249; PHD; 1. DR SUPFAM; SSF57903; SSF57903; 1. DR PROSITE; PS51184; JMJC; 1. DR PROSITE; PS51058; ZF_CXXC; 1. DR PROSITE; PS50016; ZF_PHD_2; 1. PE 1: Evidence at protein level; KW Alternative splicing; Chromatin regulator; Coiled coil; KW Complete proteome; Dioxygenase; Iron; Leucine-rich repeat; KW Metal-binding; Nucleus; Oxidoreductase; Phosphoprotein; KW Reference proteome; Repeat; Repressor; RNA-binding; rRNA-binding; KW Transcription; Transcription regulation; Ubl conjugation pathway; KW Zinc; Zinc-finger. FT CHAIN 1 1309 Lysine-specific demethylase 2B. FT /FTId=PRO_0000119854. FT DOMAIN 147 315 JmjC. FT DOMAIN 1032 1078 F-box. FT REPEAT 1106 1127 LRR 1. FT REPEAT 1129 1155 LRR 2. FT REPEAT 1195 1220 LRR 3. FT REPEAT 1221 1250 LRR 4. FT REPEAT 1251 1275 LRR 5. FT REPEAT 1276 1309 LRR 6. FT ZN_FING 579 625 CXXC-type. FT ZN_FING 632 698 PHD-type. FT COILED 916 944 Potential. FT COMPBIAS 378 403 Glu-rich. FT METAL 211 211 Iron; catalytic (By similarity). FT METAL 213 213 Iron; catalytic (By similarity). FT METAL 283 283 Iron; catalytic (By similarity). FT BINDING 208 208 Substrate (By similarity). FT BINDING 228 228 Substrate (By similarity). FT MOD_RES 447 447 Phosphoserine (By similarity). FT MOD_RES 450 450 Phosphoserine (By similarity). FT MOD_RES 466 466 Phosphothreonine (By similarity). FT MOD_RES 470 470 Phosphoserine (By similarity). FT MOD_RES 948 948 Phosphoserine (By similarity). FT MOD_RES 952 952 Phosphoserine (By similarity). FT VAR_SEQ 1 533 Missing (in isoform 2). FT /FTId=VSP_011342. FT VAR_SEQ 2 1196 Missing (in isoform 4). FT /FTId=VSP_019003. FT VAR_SEQ 534 551 TLAITGVPVVSWPKKTAK -> MAMSVSAEDDDYESEPDQ FT (in isoform 2). FT /FTId=VSP_011343. FT VAR_SEQ 627 656 PVLPHTAVCLVCGEAGKEDTVEEEEGKFNL -> VSAQKAQ FT AGLMQGLPAICPALGLLCGMGEV (in isoform 3). FT /FTId=VSP_017477. FT VAR_SEQ 657 1309 Missing (in isoform 3). FT /FTId=VSP_017478. FT CONFLICT 461 461 T -> M (in Ref. 3; BAC98289). SQ SEQUENCE 1309 AA; 149733 MW; 5BD203C3535C4D88 CRC64; MEAEKDSGRR LRAIDRQRYD ENEDLSDVEE IVSVRGFSLE EKLRSQLYQG DFVHAMEGKD FNYEYVQREA LRVPLVFRDK DGLGIKMPDP DFTVRDVKLL VGSRRLVDVM DVNTQKGTEM SMSQFVRYYE TPEAQRDKLY NVISLEFSHT KLEHLVKRPT VVDLVDWVDN MWPQHLKEKQ TEATNALAEM KYPKVKKYCL MSVKGCFTDF HIDFGGTSVW YHVFRGGKIF WLIPPTLHNL ALYEEWVLSG KQSDIFLGDR VERCQRIELK QGYTFFIPSG WIHAVYTPVD SLVFGGNILH SFNVPMQLRI YEIEDRTRVQ PKFRYPFYYE MCWYVLERYV YCVTQRSYLT QEYQRELMLI DAPRKTSVDG FSSDSWLDME EESCEQQPQE EEEEEEDKEE EGDGADKTPK PPTDDPTSPT STPPEDQDST GKKPKAPAIR FLKRTLSNES EESVKSTSMP TDDPKTPTGS PATEVSTKWT HLTEFELKGL KALVEKLESL PENKKCVPEG IEDPQALLEG VKNVLKEHVD DDPTLAITGV PVVSWPKKTA KNRVVGRPKG KLGPASAVKL AANRTTAGAR RRRTRCRKCE ACLRTECGEC HFCKDMKKFG GPGRMKQSCI MRQCIAPVLP HTAVCLVCGE AGKEDTVEEE EGKFNLMLME CSICNEIIHP GCLKIKESEG VVNDELPNCW ECPKCNHAGK TGKQKRGPGF KYASNLPGSL LKEQKMNRDN KEGQEPAKRR SECEEAPRRR SDEHPKKVPA DGILRRKSDD VHLRRKRKYE KPQELSGRKR ASSLQTSPGS SSHLSPRPPL GSSLSPWWRS SLTYFQQQLK PGKEDKLFRK KRRSWKNAED RLSLANKPLR RFKQEPEDDL PEAPPKTRES DQSRSSSPTA GPSTEGAEGP EEKKKVKMRR KRRLVNKELS KELSKELNHE IQKTESTLAH ESQQPIKSEP ESENDEPKRP LSHCERPHRF SKGLNGTPRE LRHSLGPGLR SPPRVMSRPP PSASPPKCIQ MERHVIRPPP ISPPPDSLPL DDGAAHVMHR EVWMAVFSYL SHRDLCVCMR VCRTWNRWCC DKRLWTRIDL NRCKSITPLM LSGIIRRQPV SLDLSWTNIS KKQLSWLINR LPGLRDLVLS GCSWIAVSAL CSSSCPLLRT LDVQWVEGLK DAQMRDLLSP PTDNRPGQMD NRSKLRNIVE LRLAGLDITD VSLRLIIRHM PLLSKLQLSY CNHINDQSIN LLTAVGTTTR DSLTEVNLSD CNKVTDLCLS FFKRCGNICH IDLRYCKQVT KEGCEQFIAE MSVSVQFGQV EEKLLQKLS // ID KDM5B_MOUSE Reviewed; 1544 AA. AC Q80Y84; Q5DTR9; Q8BLU1; Q8JZL8; DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2003, sequence version 1. DT 19-MAR-2014, entry version 92. DE RecName: Full=Lysine-specific demethylase 5B; DE EC=1.14.11.-; DE AltName: Full=Histone demethylase JARID1B; DE AltName: Full=Jumonji/ARID domain-containing protein 1B; DE AltName: Full=PLU-1; GN Name=Kdm5b; Synonyms=Jarid1b, Kiaa4034, Plu1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND RP DEVELOPMENTAL STAGE. RC STRAIN=BALB/c; TISSUE=Testis; RX PubMed=14516692; DOI=10.1016/S0925-4773(03)00123-0; RA Madsen B., Spencer-Dene B., Poulsom R., Hall D., Lu P.J., Scott K., RA Shaw A.T., Burchell J.M., Freemont P., Taylor-Papadimitriou J.; RT "Characterisation and developmental expression of mouse Plu-1, a RT homologue of a human nuclear protein (PLU-1) which is specifically up- RT regulated in breast cancer."; RL Mech. Dev. 119:S239-S246(2002). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Brain; RA Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O., RA Koga H.; RT "Prediction of the coding sequences of mouse homologues of KIAA gene. RT The complete nucleotide sequences of mouse KIAA-homologous cDNAs RT identified by screening of terminal sequences of cDNA clones randomly RT sampled from size-fractionated libraries."; RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC STRAIN=C57BL/6; TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1433. RC STRAIN=C57BL/6J; TISSUE=Aorta; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [5] RP TISSUE SPECIFICITY. RX PubMed=12237901; DOI=10.1002/ijc.10644; RA Barrett A., Madsen B., Copier J., Lu P.J., Cooper L., Scibetta A.G., RA Burchell J., Taylor-Papadimitriou J.; RT "PLU-1 nuclear protein, which is upregulated in breast cancer, shows RT restricted expression in normal human adult tissues: a new RT cancer/testis antigen?"; RL Int. J. Cancer 101:581-588(2002). RN [6] RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION. RX PubMed=14579128; DOI=10.1007/s00412-003-0252-6; RA Madsen B., Tarsounas M., Burchell J.M., Hall D., Poulsom R., RA Taylor-Papadimitriou J.; RT "PLU-1, a transcriptional repressor and putative testis-cancer RT antigen, has a specific expression and localisation pattern during RT meiosis."; RL Chromosoma 112:124-132(2003). RN [7] RP FUNCTION. RX PubMed=17320160; DOI=10.1016/j.cell.2007.02.017; RA Iwase S., Lan F., Bayliss P., de la Torre-Ubieta L., Huarte M., RA Qi H.H., Whetstine J.R., Bonni A., Roberts T.M., Shi Y.; RT "The X-linked mental retardation gene SMCX/JARID1C defines a family of RT histone H3 lysine 4 demethylases."; RL Cell 128:1077-1088(2007). RN [8] RP FUNCTION, AND MUTAGENESIS OF HIS-499. RX PubMed=17310255; DOI=10.1038/nsmb1200; RA Seward D.J., Cubberley G., Kim S., Schonewald M., Zhang L., Tripet B., RA Bentley D.L.; RT "Demethylation of trimethylated histone H3 Lys4 in vivo by JARID1 JmjC RT proteins."; RL Nat. Struct. Mol. Biol. 14:240-242(2007). RN [9] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-832, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic fibroblast; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., RA Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). CC -!- FUNCTION: Histone demethylase that demethylates 'Lys-4' of histone CC H3, thereby playing a central role in histone code. Does not CC demethylate histone H3 'Lys-9' or H3 'Lys-27'. Demethylates CC trimethylated, dimethylated and monomethylated H3 'Lys-4'. Acts as CC a transcriptional corepressor for FOXG1B and PAX9. CC -!- COFACTOR: Binds 1 Fe(2+) ion per subunit (By similarity). CC -!- SUBUNIT: Interacts with FOXG1B, PAX9, MYC, MYCN and RB1. Interacts CC with HDAC1, HDAC4, HDAC5 and HDAC7 (By similarity). CC -!- INTERACTION: CC P60762:Morf4l1; NbExp=4; IntAct=EBI-1249551, EBI-2943018; CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q80Y84-1; Sequence=Displayed; CC Name=2; CC IsoId=Q80Y84-2; Sequence=VSP_026409; CC Note=No experimental confirmation available; CC -!- TISSUE SPECIFICITY: Present at highest levels in testis, where it CC is enriched in spermatogonia and pachytene cells (at protein CC level). CC -!- DEVELOPMENTAL STAGE: Expressed in developing brain, mammary bud, CC thymus, teeth, whisker follicle, intervertebral disks, olfactory CC epithelium, eye, stomach and limbs. CC -!- DOMAIN: Both the JmjC domain and the JmjN domain are required for CC enzymatic activity. CC -!- DOMAIN: The 2 first PHD-type zinc finger domains are required for CC transcription repression activity (By similarity). CC -!- SIMILARITY: Belongs to the JARID1 histone demethylase family. CC -!- SIMILARITY: Contains 1 ARID domain. CC -!- SIMILARITY: Contains 1 JmjC domain. CC -!- SIMILARITY: Contains 1 JmjN domain. CC -!- SIMILARITY: Contains 3 PHD-type zinc fingers. CC -!- SEQUENCE CAUTION: CC Sequence=BAD90482.1; Type=Erroneous initiation; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AY082429; AAL92848.1; -; mRNA. DR EMBL; AY082430; AAL92849.1; -; mRNA. DR EMBL; AK220451; BAD90482.1; ALT_INIT; mRNA. DR EMBL; BC048180; AAH48180.1; -; mRNA. DR EMBL; BC057318; AAH57318.1; -; mRNA. DR EMBL; AK041304; BAC30898.1; -; mRNA. DR RefSeq; NP_690855.2; NM_152895.2. DR UniGene; Mm.28995; -. DR UniGene; Mm.391994; -. DR PDB; 2EQY; NMR; -; A=94-208. DR PDBsum; 2EQY; -. DR DisProt; DP00711; -. DR ProteinModelPortal; Q80Y84; -. DR SMR; Q80Y84; 31-208, 304-637, 1180-1222, 1486-1544. DR BioGrid; 217610; 3. DR IntAct; Q80Y84; 4. DR PhosphoSite; Q80Y84; -. DR PaxDb; Q80Y84; -. DR PRIDE; Q80Y84; -. DR Ensembl; ENSMUST00000047714; ENSMUSP00000038138; ENSMUSG00000042207. [Q80Y84-1] DR Ensembl; ENSMUST00000112198; ENSMUSP00000107817; ENSMUSG00000042207. [Q80Y84-2] DR GeneID; 75605; -. DR KEGG; mmu:75605; -. DR UCSC; uc007csg.2; mouse. [Q80Y84-2] DR UCSC; uc011wsg.1; mouse. [Q80Y84-1] DR CTD; 10765; -. DR MGI; MGI:1922855; Kdm5b. DR eggNOG; NOG327026; -. DR GeneTree; ENSGT00530000063118; -. DR HOGENOM; HOG000290719; -. DR InParanoid; Q80Y84; -. DR KO; K11446; -. DR OMA; EDYICIS; -. DR OrthoDB; EOG7D85VK; -. DR TreeFam; TF106476; -. DR EvolutionaryTrace; Q80Y84; -. DR NextBio; 343484; -. DR PRO; PR:Q80Y84; -. DR ArrayExpress; Q80Y84; -. DR Bgee; Q80Y84; -. DR Genevestigator; Q80Y84; -. DR GO; GO:0005730; C:nucleolus; IEA:Ensembl. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0034648; F:histone demethylase activity (H3-dimethyl-K4 specific); ISS:UniProtKB. DR GO; GO:0034647; F:histone demethylase activity (H3-trimethyl-K4 specific); ISS:UniProtKB. DR GO; GO:0016706; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors; IEA:InterPro. DR GO; GO:0003714; F:transcription corepressor activity; IEA:Ensembl. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IEA:Ensembl. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.150.60; -; 1. DR Gene3D; 3.30.40.10; -; 3. DR InterPro; IPR001606; ARID/BRIGHT_DNA-bd. DR InterPro; IPR003347; JmjC_dom. DR InterPro; IPR013637; Lys_sp_deMease_like_dom. DR InterPro; IPR003349; TF_JmjN. DR InterPro; IPR019786; Zinc_finger_PHD-type_CS. DR InterPro; IPR004198; Znf_C5HC2. DR InterPro; IPR011011; Znf_FYVE_PHD. DR InterPro; IPR001965; Znf_PHD. DR InterPro; IPR019787; Znf_PHD-finger. DR InterPro; IPR013083; Znf_RING/FYVE/PHD. DR Pfam; PF01388; ARID; 1. DR Pfam; PF02373; JmjC; 1. DR Pfam; PF02375; JmjN; 1. DR Pfam; PF00628; PHD; 3. DR Pfam; PF08429; PLU-1; 1. DR Pfam; PF02928; zf-C5HC2; 1. DR SMART; SM00501; BRIGHT; 1. DR SMART; SM00558; JmjC; 1. DR SMART; SM00545; JmjN; 1. DR SMART; SM00249; PHD; 3. DR SUPFAM; SSF46774; SSF46774; 1. DR SUPFAM; SSF57903; SSF57903; 3. DR PROSITE; PS51011; ARID; 1. DR PROSITE; PS51184; JMJC; 1. DR PROSITE; PS51183; JMJN; 1. DR PROSITE; PS01359; ZF_PHD_1; 2. DR PROSITE; PS50016; ZF_PHD_2; 3. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Chromatin regulator; KW Complete proteome; Dioxygenase; Iron; Metal-binding; Nucleus; KW Oxidoreductase; Reference proteome; Repeat; Transcription; KW Transcription regulation; Zinc; Zinc-finger. FT CHAIN 1 1544 Lysine-specific demethylase 5B. FT /FTId=PRO_0000292413. FT DOMAIN 32 73 JmjN. FT DOMAIN 97 187 ARID. FT DOMAIN 453 619 JmjC. FT ZN_FING 309 359 PHD-type 1. FT ZN_FING 1176 1224 PHD-type 2. FT ZN_FING 1484 1538 PHD-type 3. FT METAL 499 499 Iron; catalytic (By similarity). FT METAL 502 502 Iron; catalytic (By similarity). FT METAL 587 587 Iron; catalytic (By similarity). FT MOD_RES 832 832 N6-acetyllysine. FT VAR_SEQ 1501 1544 DWVQCDGSCNQWFHQVCVGVSPEMAEKEDYICVRCTGKDAP FT SRK -> SEVWAIEDALSPNSETL (in isoform 2). FT /FTId=VSP_026409. FT MUTAGEN 499 499 H->A: Abolishes enzymatic activity. FT CONFLICT 28 28 P -> S (in Ref. 2; BAD90482). FT CONFLICT 139 139 E -> Q (in Ref. 4; BAC30898). FT CONFLICT 761 761 N -> Y (in Ref. 1; AAL92848/AAL92849). FT CONFLICT 1428 1428 K -> R (in Ref. 1; AAL92848/AAL92849). FT HELIX 97 114 FT STRAND 122 127 FT HELIX 130 140 FT HELIX 143 148 FT TURN 149 151 FT HELIX 152 158 FT STRAND 163 165 FT HELIX 166 177 FT HELIX 179 187 SQ SEQUENCE 1544 AA; 175555 MW; D83E2691C65DCB31 CRC64; MEPATTLPPG PRPALPLGGP GPLGEFLPPP ECPVFEPSWE EFADPFAFIH KIRPIAEQTG ICKVRPPPDW QPPFACDVDK LHFTPRIQRL NELEAQTRVK LNFLDQIAKY WELQGSTLKI PHVERKILDL FQLNKLVAEE GGFAVVCKDR KWTKIATKMG FAPGKAVGSH IRGHYERILN PYNLFLSGDS LRCLQKPNLT SDTKDKEYKP HDIPQRQSVQ PAETCPPARR AKRMRAEAMN IKIEPEEATE ARTHNLRRRM GCTTPKWENE KEMKSTIKQE PTEKKDCELE SEKEKPKSRA KKTATAVDLY VCLLCGSGND EDRLLLCDGC DDSYHTFCLV PPLHDVPKGD WRCPKCLAQE CNKPQEAFGF EQAARDYTLR TFGEMADAFK SDYFNMPVHM VPTELVEKEF WRLVSTIEED VTVEYGADIA SKEFGSGFPV RDGKIKISPE EEEYLDSGWN LNNMPVMEQS VLAHITADIC GMKLPWLYVG MCFSSFCWHI EDHWSYSINY LHWGEPKTWY GVPGYAAEQL ENVMKKLAPE LFVSQPDLLH QLVTIMNPNT LMTHEVPVYR TNQCAGEFVI TFPRAYHSGF NQGFNFAEAV NFCTVDWLPL GRQCVEHYRL LHRYCVFSHD EMICKMASKA DVLDVVVAST VQKDMAIMIE DEKALRETVR KLGVIDSERM DFELLPDDER QCIKCKTTCF MSAISCSCKP GLLVCLHHVK ELCSCPPYKY NLRYRYTLDD LYPMMNALKL RAESYNEWAL NVNEALEAKI NKKKSLVSFK ALIEESEMKK FPDNDLLRHL RLVTQDAEKC ASVAQQLLNG KRQTRYRSGG GKSQNQLTVN ELRQFVTQLY ALPCVLSQTP LLKDLLNRVE DFQQQSQKLL SEEMPSAAEL QELLDVSFEF DVELPQLTEM RIRLEQARWL EEVQQACLDS SSLSLDDMRR LIDLGVGLAP YSAVEKAMAR LQELLTVSEH WDDKAKSLLR ARPRHSLSSL ATAVKEMEEI PAYLPNGTVL KDSVQRARDW VQDVDALQAG GRVPVLETLI ELVARGRSIP VHLNSLPRLE MLVAEVHAWK ECAAKTFLPE NSTYSLLEVL CPRCDIGLLG LKRKQRKLKE PLPSGKKRST KLESLSDLER ALMESKETAA AMATLGEARL REMEALQSLR FANEEKLLSP VQDLEMKVCL CQKTPATPMI QCELCRDAFH TSCVAAPSIS QSSRIWLCPH CRRSEKPPLE KILPLLASLQ RIRVRLPEGD ALRYMIERTV NWQHRAQQLL SSGNLKLVQD QVGSGLLSSR WPASAGQASA TDKVSQPPGT TSFSLPDDWD NRTSYLHSPF STGQSCLPLH GLSPEVNELL MEAQLLQVSL PEIQELYQTL LTKPSSVQQA DRSSPVRSSS EKNDCLRGKR DAINSPERKL KRRPEREGLP SERWDRVKHM RTPQKKKIKL SHPKDMDSFK LERERSYDLV RNAETHSLPS DTSYSEQEDS EDEDAICPAV SCLQPEGDEV DWVQCDGSCN QWFHQVCVGV SPEMAEKEDY ICVRCTGKDA PSRK // ID KDM5C_MOUSE Reviewed; 1554 AA. AC P41230; O54995; Q3TYU8; Q3U1X6; Q3U282; Q6ZQF8; Q80XQ9; Q9CVI4; AC Q9D0C3; Q9QVR8; Q9R039; DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot. DT 26-JUN-2007, sequence version 4. DT 19-MAR-2014, entry version 123. DE RecName: Full=Lysine-specific demethylase 5C; DE EC=1.14.11.-; DE AltName: Full=Histone demethylase JARID1C; DE AltName: Full=Jumonji/ARID domain-containing protein 1C; DE AltName: Full=Protein SmcX; DE AltName: Full=Protein Xe169; GN Name=Kdm5c; Synonyms=Jarid1c, Kiaa0234, Smcx, Xe169; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RC STRAIN=129/SvJ; RX PubMed=10441747; DOI=10.1007/s003359901116; RA Agulnik A.I., Longepied G., Ty M.T., Bishop C.E., Mitchell M.J.; RT "Mouse H-Y encoding Smcy gene and its X chromosomal homolog Smcx."; RL Mamm. Genome 10:926-929(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC STRAIN=C57BL/6J, and NOD; RC TISSUE=Dendritic cell, Embryo, Inner ear, and Small intestine; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). RC STRAIN=C57BL/6; TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] OF 36-1068. RC STRAIN=BALB/c; TISSUE=Testis; RX PubMed=7951230; DOI=10.1093/hmg/3.6.879; RA Agulnik A.I., Mitchell M.J., Mattei M.-G., Borsani G., Avner P.A., RA Lerner J.L., Bishop C.E.; RT "A novel X gene with a widely transcribed Y-linked homologue escapes RT X-inactivation in mouse and human."; RL Hum. Mol. Genet. 3:879-884(1994). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 165-1554 (ISOFORM 1). RC TISSUE=Embryonic tail; RX PubMed=14621295; DOI=10.1093/dnares/10.4.167; RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., RA Saga Y., Nagase T., Ohara O., Koga H.; RT "Prediction of the coding sequences of mouse homologues of KIAA gene: RT III. The complete nucleotide sequences of 500 mouse KIAA-homologous RT cDNAs identified by screening of terminal sequences of cDNA clones RT randomly sampled from size-fractionated libraries."; RL DNA Res. 10:167-180(2003). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1206-1385 (ISOFORM 1). RX PubMed=7951318; DOI=10.1038/ng0894-491; RA Wu J., Salido E., Yen P., Mohandas T., Shapiro L.J.; RT "The murine Xe169 gene escapes X-inactivation like its human RT homologue."; RL Nat. Genet. 7:491-496(1994). RN [7] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-39. RX PubMed=9723615; DOI=10.1038/29522; RA Jegalian K.G., Page D.C.; RT "A proposed path by which genes common to mammalian X and Y RT chromosomes evolve to become X inactivated."; RL Nature 394:776-780(1998). RN [8] RP FUNCTION. RC STRAIN=C3H; RX PubMed=7544442; DOI=10.1038/376695a0; RA Scott D.M., Ehrmann I.E., Ellis P.S., Bishop C.E., Agulnik A.I., RA Simpson E., Mitchell M.J.; RT "Identification of a mouse male-specific transplantation antigen, H- RT Y."; RL Nature 376:695-698(1995). CC -!- FUNCTION: Histone demethylase that specifically demethylates 'Lys- CC 4' of histone H3, thereby playing a central role in histone code. CC Does not demethylate histone H3 'Lys-9', H3 'Lys-27', H3 'Lys-36', CC H3 'Lys-79' or H4 'Lys-20'. Demethylates trimethylated and CC dimethylated but not monomethylated H3 'Lys-4'. Participates in CC transcriptional repression of neuronal genes by recruiting histone CC deacetylases and REST at neuron-restrictive silencer elements (By CC similarity). CC -!- COFACTOR: Alpha-ketoglutarate (By similarity). CC -!- COFACTOR: Binds 1 Fe(2+) ion per subunit (By similarity). CC -!- SUBUNIT: Part of two distinct complexes, one containing E2F6, and CC the other containing REST (By similarity). CC -!- SUBCELLULAR LOCATION: Nucleus (By similarity). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=P41230-1; Sequence=Displayed; CC Name=2; CC IsoId=P41230-2; Sequence=VSP_000316; CC Name=3; CC IsoId=P41230-3; Sequence=VSP_026411, VSP_000316; CC -!- DOMAIN: The first PHD-type zinc finger domain recognizes and binds CC H3-K9Me3 (By similarity). CC -!- DOMAIN: Both the JmjC domain and the JmjN domain are required for CC enzymatic activity (By similarity). CC -!- MISCELLANEOUS: Escapes X-inactivation. CC -!- SIMILARITY: Belongs to the JARID1 histone demethylase family. CC -!- SIMILARITY: Contains 1 ARID domain. CC -!- SIMILARITY: Contains 1 JmjC domain. CC -!- SIMILARITY: Contains 1 JmjN domain. CC -!- SIMILARITY: Contains 2 PHD-type zinc fingers. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF127245; AAD53049.1; -; mRNA. DR EMBL; AK008105; BAB25462.1; -; mRNA. DR EMBL; AK155279; BAE33161.1; -; mRNA. DR EMBL; AK155427; BAE33260.1; -; mRNA. DR EMBL; AK155651; BAE33367.1; -; mRNA. DR EMBL; AK158340; BAE34464.1; -; mRNA. DR EMBL; AK011577; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; BC043096; AAH43096.1; -; mRNA. DR EMBL; BC054550; AAH54550.1; -; mRNA. DR EMBL; Z29651; CAA82759.1; -; mRNA. DR EMBL; AK129096; BAC97906.1; -; mRNA. DR EMBL; L29563; AAA62384.1; -; mRNA. DR EMBL; AF039894; AAB96762.1; -; mRNA. DR PIR; I48775; I48775. DR PIR; I84689; I84689. DR RefSeq; NP_038696.2; NM_013668.3. DR RefSeq; XP_006528832.1; XM_006528769.1. DR RefSeq; XP_006528835.1; XM_006528772.1. DR UniGene; Mm.142655; -. DR ProteinModelPortal; P41230; -. DR SMR; P41230; 13-188, 261-652, 1185-1248. DR BioGrid; 203341; 2. DR PhosphoSite; P41230; -. DR PaxDb; P41230; -. DR PRIDE; P41230; -. DR Ensembl; ENSMUST00000082177; ENSMUSP00000080814; ENSMUSG00000025332. [P41230-3] DR Ensembl; ENSMUST00000112584; ENSMUSP00000108203; ENSMUSG00000025332. [P41230-1] DR Ensembl; ENSMUST00000112588; ENSMUSP00000108207; ENSMUSG00000025332. [P41230-2] DR GeneID; 20591; -. DR KEGG; mmu:20591; -. DR UCSC; uc009uqc.2; mouse. [P41230-2] DR UCSC; uc009uqd.2; mouse. [P41230-3] DR UCSC; uc009uqe.2; mouse. [P41230-1] DR CTD; 8242; -. DR MGI; MGI:99781; Kdm5c. DR eggNOG; NOG327026; -. DR GeneTree; ENSGT00530000063118; -. DR InParanoid; P41230; -. DR KO; K11446; -. DR OMA; TTSICVC; -. DR OrthoDB; EOG7D85VK; -. DR TreeFam; TF106476; -. DR ChiTaRS; KDM5C; mouse. DR NextBio; 298901; -. DR PRO; PR:P41230; -. DR ArrayExpress; P41230; -. DR Bgee; P41230; -. DR Genevestigator; P41230; -. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0032453; F:histone demethylase activity (H3-K4 specific); IEA:Ensembl. DR GO; GO:0016706; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.150.60; -; 1. DR Gene3D; 3.30.40.10; -; 2. DR InterPro; IPR001606; ARID/BRIGHT_DNA-bd. DR InterPro; IPR003347; JmjC_dom. DR InterPro; IPR013637; Lys_sp_deMease_like_dom. DR InterPro; IPR003349; TF_JmjN. DR InterPro; IPR019786; Zinc_finger_PHD-type_CS. DR InterPro; IPR004198; Znf_C5HC2. DR InterPro; IPR011011; Znf_FYVE_PHD. DR InterPro; IPR001965; Znf_PHD. DR InterPro; IPR019787; Znf_PHD-finger. DR InterPro; IPR013083; Znf_RING/FYVE/PHD. DR Pfam; PF01388; ARID; 1. DR Pfam; PF02373; JmjC; 1. DR Pfam; PF02375; JmjN; 1. DR Pfam; PF00628; PHD; 1. DR Pfam; PF08429; PLU-1; 1. DR Pfam; PF02928; zf-C5HC2; 1. DR SMART; SM00501; BRIGHT; 1. DR SMART; SM00558; JmjC; 1. DR SMART; SM00545; JmjN; 1. DR SMART; SM00249; PHD; 2. DR SUPFAM; SSF46774; SSF46774; 1. DR SUPFAM; SSF57903; SSF57903; 2. DR PROSITE; PS51011; ARID; 1. DR PROSITE; PS51184; JMJC; 1. DR PROSITE; PS51183; JMJN; 1. DR PROSITE; PS01359; ZF_PHD_1; 2. DR PROSITE; PS50016; ZF_PHD_2; 1. PE 2: Evidence at transcript level; KW Alternative splicing; Chromatin regulator; Complete proteome; KW Dioxygenase; Iron; Metal-binding; Nucleus; Oxidoreductase; KW Phosphoprotein; Reference proteome; Repeat; Transcription; KW Transcription regulation; Zinc; Zinc-finger. FT CHAIN 1 1554 Lysine-specific demethylase 5C. FT /FTId=PRO_0000200587. FT DOMAIN 14 55 JmjN. FT DOMAIN 79 169 ARID. FT DOMAIN 468 634 JmjC. FT ZN_FING 326 372 PHD-type 1. FT ZN_FING 1187 1248 PHD-type 2. FT METAL 514 514 Iron; catalytic (By similarity). FT METAL 517 517 Iron; catalytic (By similarity). FT METAL 602 602 Iron; catalytic (By similarity). FT MOD_RES 317 317 Phosphoserine (By similarity). FT MOD_RES 1353 1353 Phosphoserine (By similarity). FT VAR_SEQ 77 117 Missing (in isoform 3). FT /FTId=VSP_026411. FT VAR_SEQ 1364 1366 Missing (in isoform 2 and isoform 3). FT /FTId=VSP_000316. FT CONFLICT 3 3 L -> M (in Ref. 7; AAB96762). FT CONFLICT 26 26 D -> G (in Ref. 7; AAB96762). FT CONFLICT 123 123 G -> S (in Ref. 2; BAE33161/BAE33260). FT CONFLICT 249 249 G -> D (in Ref. 2; BAE34464). FT CONFLICT 726 726 D -> N (in Ref. 5; BAC97906). FT CONFLICT 865 865 C -> L (in Ref. 1; AAD53049 and 4; FT CAA82759). FT CONFLICT 1068 1068 L -> P (in Ref. 4; CAA82759). FT CONFLICT 1126 1126 Y -> C (in Ref. 2; BAE33367). SQ SEQUENCE 1554 AA; 175313 MW; 585EA9F890B0D9A0 CRC64; MELGSDDFLP PPECPVFEPS WAEFRDPLGY IAKIRPIAEK SGICKIRPPA DWQPPFAVEV DNFRFTPRIQ RLNELEAQTR VKLNYLDQIA KFWEIQGSSL KIPNVERRIL DLYSLSKIVV EEGGYETICK DRRWARVAQR LNYPPGKNIG SLLRSHYERI VYPYEMYQSG ANLVQCNTRP FDNEEKDKEY KPHSIPLRQS VQPSKFNSYG RRAKRLQPDP EPTEEDIEKN PELKKLQIYG AGPKMMGLGL MAKDKTLRKK DKEGPECPPT VVVKEELGGD VKMESTSPKT FLEGKEELSH SPEPCTKMTM RLRRNHSNAQ FIESYVCRMC SRGDEDDKLL LCDGCDDNYH IFCLLPPLPE IPKGVWRCPK CVMAECKRPP EAFGFEQATR EYTLQSFGEM ADSFKADYFN MPVHMVPTEL VEKEFWRLVN SIEEDVTVEY GADIHSKEFG SGFPVSDSKR HLTPEEEEYA TSGWNLNVMP VLEQSVLCHI NADISGMKVP WLYVGMVFSA FCWHIEDHWS YSINYLHWGE PKTWYGVPSL AAEHLEEVMK KLTPELFDSQ PDLLHQLVTL MNPNTLMSHG VPVVRTNQCA GEFVITFPRA YHSGFNQGYN FAEAVNFCTA DWLPAGRQCI EHYRRLRRYC VFSHEELICK MAACPEKLDL NLAAAVHKEM FIMVQEERRL RKALLEKGIT EAEREAFELL PDDERQCIKC KTTCFLSALA CYDCPDGLVC LSHINDLCKC SSSRQYLRYR YTLDELPAML HKLKVRAESF DTWANKVRVA LEVEDGRKRS LEELRALESE ARERRFPNSE LLQRLKNCLS EAEACVSRAL GLVSGQEAGP DRVAGLQMTL AELRDFLGQM NNLPCAMHQI GDVKGILEQV EAYQTEAREA LVSQPSSPGL LQSLLERGQQ LGVEVPEAQQ LQRQVEQARW LDEVKRTLAP SARRGTLAIM RGLLVAGASV APSPAVDKAQ AELQELLTIA ERWEEKAHLC LEARQKHPPA TLEAIIHEAE NIPVHLPNIQ SLKEALAKAR AWIADVDEIQ NGDHYPCLDD LEGLVAVGRD LPVGLEELRQ LELQVLTAHS WREKASKTFL KKNSCYTLLE VLCPCADAGS DSTKRSRWME KELGLYKSDT ELLGLSAQDL RDPGSVIVAF KEGEQKEKEG ILQLRRTNSA KPSPLALLTT ASSTASICVC GQVPAGVGAL QCDLCQDWFH GRCVTVPRLL SSQRSSLPSS PLLAWWEWDT KFLCPLCMRS RRPRLETILA LLVALQRLPV RLPEGEALQC LTERAISWQG RARQVLASEE VTALLGRLAE LRQRLQAESK PEESLAYPSD GGEGTGNMPK VQGLLENGDS VTSPEKVATE EGSGKRDLEL LSSILPQLSG PVLELPEATR APLEELMMEG DLLEVTLDEN HSIWQLLQAG QPPDLKRVQT LLELEKAERH GSRTRGRALE RRRRRKVDRG GEPDDPAREE LEPKRVRSSG PEAEEVQEEE ELEEETGGEV PPVPFPNSGS PSIQEDQDGL EPVLEAGSDT SAPFSTLTSR LLMSCPQQPS LQQL // ID KDM5A_MOUSE Reviewed; 1690 AA. AC Q3UXZ9; Q3TM94; Q3UMI5; Q66JZ3; DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot. DT 26-JUN-2007, sequence version 2. DT 19-MAR-2014, entry version 79. DE RecName: Full=Lysine-specific demethylase 5A; DE EC=1.14.11.-; DE AltName: Full=Histone demethylase JARID1A; DE AltName: Full=Jumonji/ARID domain-containing protein 1A; DE AltName: Full=Retinoblastoma-binding protein 2; DE Short=RBBP-2; GN Name=Kdm5a; Synonyms=Jarid1a, Rbp2; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1552. RC STRAIN=C57BL/6J; TISSUE=Lung, and Olfactory bulb; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1099. RC STRAIN=C57BL/6J; TISSUE=Germ cell; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP PROTEIN SEQUENCE OF 1538-1546, AND MASS SPECTROMETRY. RC STRAIN=OF1; TISSUE=Hippocampus; RA Lubec G., Sunyer B., Chen W.-Q.; RL Submitted (JAN-2009) to UniProtKB. RN [5] RP FUNCTION, AND DISRUPTION PHENOTYPE. RX PubMed=17320163; DOI=10.1016/j.cell.2007.02.013; RA Klose R.J., Yan Q., Tothova Z., Yamane K., Erdjument-Bromage H., RA Tempst P., Gilliland D.G., Zhang Y., Kaelin W.G. Jr.; RT "The retinoblastoma binding protein RBP2 is an H3K4 demethylase."; RL Cell 128:889-900(2007). RN [6] RP FUNCTION. RX PubMed=17320161; DOI=10.1016/j.cell.2007.02.003; RA Christensen J., Agger K., Cloos P.A.C., Pasini D., Rose S., RA Sennels L., Rappsilber J., Hansen K.H., Salcini A.E., Helin K.; RT "RBP2 belongs to a family of demethylases, specific for tri-and RT dimethylated lysine 4 on histone 3."; RL Cell 128:1063-1076(2007). RN [7] RP SUBCELLULAR LOCATION, DOMAIN GSGFP MOTIF, AND INTERACTION WITH SUZ12. RX PubMed=20064375; DOI=10.1016/j.cell.2009.12.002; RA Peng J.C., Valouev A., Swigut T., Zhang J., Zhao Y., Sidow A., RA Wysocka J.; RT "Jarid2/Jumonji coordinates control of PRC2 enzymatic activity and RT target gene occupancy in pluripotent cells."; RL Cell 139:1290-1302(2009). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1111, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006; RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M., RA Thibault P.; RT "The phagosomal proteome in interferon-gamma-activated macrophages."; RL Immunity 30:143-154(2009). CC -!- FUNCTION: Histone demethylase that specifically demethylates 'Lys- CC 4' of histone H3, thereby playing a central role in histone code. CC Does not demethylate histone H3 'Lys-9', H3 'Lys-27', H3 'Lys-36', CC H3 'Lys-79' or H4 'Lys-20'. Demethylates trimethylated and CC dimethylated but not monomethylated H3 'Lys-4'. May stimulate CC transcription mediated by nuclear receptors. Involved in CC transcriptional regulation of Hox proteins during cell CC differentiation. May participate in transcriptional repression of CC cytokines such as CXCL12. CC -!- COFACTOR: Binds 1 Fe(2+) ion per subunit (By similarity). CC -!- SUBUNIT: Interacts with RB1, ESR1, MYC, MYCN and LMO2 (By CC similarity). Interacts with SUZ12; the interaction is direct. CC -!- INTERACTION: CC Q80U70:Suz12; NbExp=2; IntAct=EBI-2531441, EBI-2526494; CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus (By similarity). Nucleus. CC Note=Occupies promoters of genes involved in RNA metabolism and CC mitochondrial function. CC -!- DOMAIN: The GSGFP motif is required for the interaction with CC SUZ12. CC -!- DISRUPTION PHENOTYPE: Mice are grossly normal, except that they CC exhibit behavioral abnormalities when held upside down by the CC tail, and slight hematological defects. CC -!- SIMILARITY: Belongs to the JARID1 histone demethylase family. CC -!- SIMILARITY: Contains 1 ARID domain. CC -!- SIMILARITY: Contains 1 JmjC domain. CC -!- SIMILARITY: Contains 1 JmjN domain. CC -!- SIMILARITY: Contains 3 PHD-type zinc fingers. CC -!- SEQUENCE CAUTION: CC Sequence=BAE22414.1; Type=Erroneous initiation; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AC155720; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC078896; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AK135085; BAE22414.1; ALT_INIT; mRNA. DR EMBL; AK144877; BAE26113.1; -; mRNA. DR EMBL; AK166055; BAE38548.1; -; mRNA. DR EMBL; BC080691; AAH80691.1; ALT_TERM; mRNA. DR RefSeq; NP_666109.2; NM_145997.2. DR UniGene; Mm.404761; -. DR UniGene; Mm.463658; -. DR ProteinModelPortal; Q3UXZ9; -. DR SMR; Q3UXZ9; 18-177, 260-620, 1159-1219, 1608-1659. DR BioGrid; 229572; 1. DR IntAct; Q3UXZ9; 1. DR PhosphoSite; Q3UXZ9; -. DR PaxDb; Q3UXZ9; -. DR PRIDE; Q3UXZ9; -. DR Ensembl; ENSMUST00000100996; ENSMUSP00000098558; ENSMUSG00000030180. DR GeneID; 214899; -. DR KEGG; mmu:214899; -. DR UCSC; uc009dne.2; mouse. DR CTD; 5927; -. DR MGI; MGI:2136980; Kdm5a. DR eggNOG; NOG327026; -. DR GeneTree; ENSGT00530000063118; -. DR HOGENOM; HOG000290719; -. DR InParanoid; Q3UXZ9; -. DR KO; K11446; -. DR OMA; CVAHYRR; -. DR TreeFam; TF106476; -. DR ChiTaRS; KDM5A; mouse. DR NextBio; 374501; -. DR PRO; PR:Q3UXZ9; -. DR ArrayExpress; Q3UXZ9; -. DR Bgee; Q3UXZ9; -. DR CleanEx; MM_RBP2; -. DR Genevestigator; Q3UXZ9; -. DR GO; GO:0019907; C:cyclin-dependent protein kinase activating kinase holoenzyme complex; IEA:Ensembl. DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl. DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell. DR GO; GO:0003682; F:chromatin binding; IDA:UniProtKB. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0016706; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0016568; P:chromatin modification; IEA:UniProtKB-KW. DR GO; GO:0007275; P:multicellular organismal development; IEA:UniProtKB-KW. DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IEA:Ensembl. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.150.60; -; 1. DR Gene3D; 3.30.40.10; -; 3. DR InterPro; IPR001606; ARID/BRIGHT_DNA-bd. DR InterPro; IPR003347; JmjC_dom. DR InterPro; IPR013637; Lys_sp_deMease_like_dom. DR InterPro; IPR003349; TF_JmjN. DR InterPro; IPR019786; Zinc_finger_PHD-type_CS. DR InterPro; IPR004198; Znf_C5HC2. DR InterPro; IPR011011; Znf_FYVE_PHD. DR InterPro; IPR001965; Znf_PHD. DR InterPro; IPR019787; Znf_PHD-finger. DR InterPro; IPR013083; Znf_RING/FYVE/PHD. DR Pfam; PF01388; ARID; 1. DR Pfam; PF02373; JmjC; 1. DR Pfam; PF02375; JmjN; 1. DR Pfam; PF00628; PHD; 2. DR Pfam; PF08429; PLU-1; 1. DR Pfam; PF02928; zf-C5HC2; 1. DR SMART; SM00501; BRIGHT; 1. DR SMART; SM00558; JmjC; 1. DR SMART; SM00545; JmjN; 1. DR SMART; SM00249; PHD; 3. DR SUPFAM; SSF46774; SSF46774; 1. DR SUPFAM; SSF57903; SSF57903; 3. DR PROSITE; PS51011; ARID; 1. DR PROSITE; PS51184; JMJC; 1. DR PROSITE; PS51183; JMJN; 1. DR PROSITE; PS01359; ZF_PHD_1; 2. DR PROSITE; PS50016; ZF_PHD_2; 3. PE 1: Evidence at protein level; KW Chromatin regulator; Complete proteome; Developmental protein; KW Dioxygenase; Direct protein sequencing; Iron; Metal-binding; Nucleus; KW Oxidoreductase; Phosphoprotein; Reference proteome; Repeat; KW Transcription; Transcription regulation; Zinc; Zinc-finger. FT CHAIN 1 1690 Lysine-specific demethylase 5A. FT /FTId=PRO_0000292411. FT DOMAIN 19 60 JmjN. FT DOMAIN 84 174 ARID. FT DOMAIN 437 603 JmjC. FT ZN_FING 293 343 PHD-type 1. FT ZN_FING 1153 1210 PHD-type 2. FT ZN_FING 1599 1653 PHD-type 3. FT REGION 1622 1690 Interaction with LMO2 (By similarity). FT MOTIF 419 423 GSGFP motif. FT COMPBIAS 1484 1579 Lys-rich. FT METAL 483 483 Iron; catalytic (By similarity). FT METAL 486 486 Iron; catalytic (By similarity). FT METAL 571 571 Iron; catalytic (By similarity). FT MOD_RES 1111 1111 Phosphoserine. FT MOD_RES 1331 1331 Phosphoserine (By similarity). FT MOD_RES 1598 1598 Phosphoserine (By similarity). FT MOD_RES 1603 1603 Phosphoserine (By similarity). FT MOD_RES 1666 1666 Phosphoserine (By similarity). FT CONFLICT 10 10 A -> S (in Ref. 2; BAE38548). FT CONFLICT 14 14 V -> R (in Ref. 2; BAE38548). FT CONFLICT 17 17 P -> A (in Ref. 2; BAE38548). FT CONFLICT 24 24 P -> A (in Ref. 2; BAE38548). FT CONFLICT 544 544 V -> A (in Ref. 2; BAE38548). FT CONFLICT 1272 1272 A -> P (in Ref. 2; BAE22414). SQ SEQUENCE 1690 AA; 192216 MW; EFCF56AAAA51F0FC CRC64; MASVGPGGYA AEFVPPPECP VFEPSWEEFT DPLSFIGRIR PFAEKTGICK IRPPKDWQPP FACEVKTFRF TPRVQRLNEL EAMTRVRLDF LDQLAKFWEL QGSTLKIPVV ERKILDLYAL SKIVASKGGF EIVTKEKKWS KVGSRLGYLP GKGTGSLLKS HYERILYPYE LFQSGVSLMG VQMPDLDLKE KVEAEVLSTD IQPSPERGTR MNIPPKRTRR VKSQSDSGEV NRNTELKKLQ IFGAGPKVVG LAVGAKDKED EVTRRRKVTN RSDAFNMQMR QRKGTLSVNF VDLYVCMFCG RGNNEDKLLL CDGCDDSYHT FCLLPPLPDV PKGDWRCPKC VAEECNKPRE AFGFEQAVRE YTLQSFGEMA DNFKSDYFNM PVHMVPTELV EKEFWRLVSS IEEDVIVEYG ADISSKDFGS GFPKKDGQRK MLPEEEEYAL SGWNLNNMPV LEQSVLAHIN VDISGMKVPW LYVGMCFSSF CWHIEDHWSY SINYLHWGEP KTWYGVPSHA AEQLEEVMRE LAPELFESQP DLLHQLVTIM NPNVLMEHGV PVYRTNQCAG EFVVTFPRAY HSGFNQGYNF AEAVNFCTAD WLPIGRQCVN HYRRLRRHCV FSHEELIFKM AADPECLDVG LAAMVCKELT LMTEEETRLR ESVVQMGVVM SEEEVFELVP DDERQCSACR TTCFLSALTC SCNPERLVCL YHPTDLCSCP MQNKCLRYRY PLEDLPSLLY GVKVRAQSYD TWVNRVTEAL SASFNHKKDL IELRVMLEDA EDRKYPENDL FRKLRDAVKE AETCGSVAQL LLSKKQKHRQ SSDSGKTRTK LTVEELKAFV QQLVSLPCVI SQTRQVKNLL DDVEEFHERA QEAMMDETPD SSKLQMLIDM GSSLYVELPE LPRLKQELQQ ARWLDEVRLT LSDPQQVTLD VMKKLIDSGV GLAPHHAVEK AMAELQELLT VSERWEEKAK VCLQARPRHS MANLENIVNE AKNIPAFLPN VLSLKEALQK AREWTAKVEA IQSGNNYAYL EQLESLSAKG RPIPVRLDAL PQVESQVAAA RAWRERTGRT FLKKNSSHTL LQVLSPRTDI GVYGSGKNRR KKVKEIIEKE KEKDLDLEPL SDLEEGLEES RDTAMVVAVF KEREQKEIEA MHSLRAANLA KMTIVERIEE VKFCICRKTA SGFMLQCELC KDWFHNSCVP LPKSSSQKKG SSWQAKDVKF LCPLCMRSRR PRLETILSLL VSLQKLPVRL PEGEALQCLT ERAMSWQDKA RQALATDELS SALAKLSVLS QRMVEQAARE KTEKIISAEL QKAAANPDLQ GHLPSFQQSA FNRVVSSVSS SPHQTMDYDD EETDSDEDIR ETYGYDMKDT ASVKSSSSLE PNLFCDEEIP IKSEEVVTHM WTAPSFCAEH AYSSASKSCS QGSSTPRKQP RKSPLVPRSL EPPVLELSPG AKAQLEELMM VGDLLEVSLD ETQHIWRILQ ATHPPSEDRF LHIMEDDSIE EKPLKMKGKD SSEKKRKRKL EKVEQLFGEG KQKTKELKKI DKPKKKKLKL NVDKSKELNK LAKKLAKEEE RKKKKEKAAA AKVELVKEST EKKRERKVLD IPSKYDWSGA EESDDENAVC AAQNCQRPCK DKVDWVQCDG GCDEWFHQVC VGVSAEMAEN EDYICINCAK KQGPDSPGQA PPPPFLMSYK LPMEDLKETS // ID KDM3A_MOUSE Reviewed; 1323 AA. AC Q6PCM1; Q2MJQ6; Q3TKW8; Q3UML3; Q6ZQ57; Q8K2J6; Q8K2K4; Q8R350; DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 19-MAR-2014, entry version 86. DE RecName: Full=Lysine-specific demethylase 3A; DE EC=1.14.11.-; DE AltName: Full=JmjC domain-containing histone demethylation protein 2A; DE AltName: Full=Jumonji domain-containing protein 1A; GN Name=Kdm3a; Synonyms=Jhdm2a, Jmjd1a, Kiaa0742; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Embryonic tail; RX PubMed=14621295; DOI=10.1093/dnares/10.4.167; RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., RA Saga Y., Nagase T., Ohara O., Koga H.; RT "Prediction of the coding sequences of mouse homologues of KIAA gene: RT III. The complete nucleotide sequences of 500 mouse KIAA-homologous RT cDNAs identified by screening of terminal sequences of cDNA clones RT randomly sampled from size-fractionated libraries."; RL DNA Res. 10:167-180(2003). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE RP SEQUENCE [LARGE SCALE MRNA] OF 1-1034 (ISOFORM 2). RC STRAIN=C57BL/6, Czech II, and FVB/N; TISSUE=Brain, and Mammary tumor; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-834. RC TISSUE=Lung; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] OF 115-1323. RC STRAIN=BALB/c; TISSUE=Testis; RA Knebel J., De Haro L., Janknecht R.; RT "Characterization of murine Jmjd1a/TSGA."; RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL RP STAGE. RX PubMed=17943087; DOI=10.1038/nature06236; RA Okada Y., Scott G., Ray M.K., Mishina Y., Zhang Y.; RT "Histone demethylase JHDM2A is critical for Tnp1 and Prm1 RT transcription and spermatogenesis."; RL Nature 450:119-123(2007). RN [6] RP FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE. RX PubMed=19194461; DOI=10.1038/nature07777; RA Tateishi K., Okada Y., Kallin E.M., Zhang Y.; RT "Role of Jhdm2a in regulating metabolic gene expression and obesity RT resistance."; RL Nature 458:757-761(2009). CC -!- FUNCTION: Histone demethylase that specifically demethylates 'Lys- CC 9' of histone H3, thereby playing a central role in histone code. CC Preferentially demethylates mono- and dimethylated H3 'Lys-9' CC residue, with a preference for dimethylated residue, while it has CC weak or no activity on trimethylated H3 'Lys-9'. Demethylation of CC Lys residue generates formaldehyde and succinate. Involved in CC hormone-dependent transcriptional activation, by participating in CC recruitment to androgen-receptor target genes, resulting in H3 CC 'Lys-9' demethylation and transcriptional activation (By CC similarity). Involved in spermatogenesis by regulating expression CC of target genes such as PRM1 and TMP1 which are required for CC packaging and condensation of sperm chromatin. Involved in obesity CC resistance through regulation of metabolic genes such as PPARA and CC UCP1. CC -!- COFACTOR: Binds 1 Fe(2+) ion per subunit (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Nuclear in round CC spermatids. When spermatids start to elongate, localizes to the CC cytoplasm where it forms distinct foci which disappear in mature CC spermatozoa. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q6PCM1-1; Sequence=Displayed; CC Name=2; CC IsoId=Q6PCM1-2; Sequence=VSP_018296, VSP_018297; CC Note=No experimental confirmation available; CC -!- TISSUE SPECIFICITY: Highly expressed in testis (at protein level). CC Also expressed at high levels in tissues responsive to sympathetic CC nerve activity such as brown adipose tissue and skeletal muscle. CC -!- DEVELOPMENTAL STAGE: Expression increases significantly during CC spermatogenesis with a 70-fold increase from day 7 testis to day CC 30 testis. First detected in the late pachytene stage, increases CC in diplotene and secondary spermatocytes and reaches its highest CC levels in round spermatids. CC -!- INDUCTION: By beta-adrenergic stimulation (at protein level). CC -!- DOMAIN: The JmjC domain and the C6-type zinc-finger are required CC for the demethylation activity (By similarity). CC -!- DOMAIN: Leu-Xaa-Xaa-Leu-Leu (LXXLL) motifs are known to mediate CC the association with nuclear receptors (By similarity). CC -!- DISRUPTION PHENOTYPE: Spermatogenesis defects and adult obesity. CC -!- SIMILARITY: Belongs to the JHDM2 histone demethylase family. CC -!- SIMILARITY: Contains 1 JmjC domain. CC -!- SEQUENCE CAUTION: CC Sequence=BAC98014.1; Type=Erroneous initiation; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK129204; BAC98014.1; ALT_INIT; mRNA. DR EMBL; BC026605; AAH26605.1; -; mRNA. DR EMBL; BC031158; AAH31158.1; -; mRNA. DR EMBL; BC031200; AAH31200.1; -; mRNA. DR EMBL; BC059264; AAH59264.1; -; mRNA. DR EMBL; AK144825; BAE26085.1; -; mRNA. DR EMBL; AK166797; BAE39025.1; -; mRNA. DR EMBL; DQ323991; ABC54567.1; -; mRNA. DR RefSeq; NP_001033784.2; NM_001038695.3. DR RefSeq; NP_766589.1; NM_173001.3. DR RefSeq; XP_006505327.1; XM_006505264.1. DR RefSeq; XP_006505330.1; XM_006505267.1. DR UniGene; Mm.260479; -. DR ProteinModelPortal; Q6PCM1; -. DR SMR; Q6PCM1; 644-689, 941-1282. DR BioGrid; 222501; 1. DR IntAct; Q6PCM1; 1. DR PhosphoSite; Q6PCM1; -. DR PaxDb; Q6PCM1; -. DR PRIDE; Q6PCM1; -. DR Ensembl; ENSMUST00000065509; ENSMUSP00000065716; ENSMUSG00000053470. [Q6PCM1-1] DR Ensembl; ENSMUST00000167220; ENSMUSP00000128789; ENSMUSG00000053470. [Q6PCM1-1] DR GeneID; 104263; -. DR KEGG; mmu:104263; -. DR UCSC; uc009cgy.2; mouse. [Q6PCM1-1] DR CTD; 55818; -. DR MGI; MGI:98847; Kdm3a. DR eggNOG; NOG305537; -. DR GeneTree; ENSGT00530000063039; -. DR InParanoid; Q6PCM1; -. DR KO; K15601; -. DR OMA; RRLQFNK; -. DR OrthoDB; EOG7B5WVG; -. DR TreeFam; TF324723; -. DR NextBio; 356834; -. DR PRO; PR:Q6PCM1; -. DR ArrayExpress; Q6PCM1; -. DR Bgee; Q6PCM1; -. DR CleanEx; MM_JMJD1A; -. DR Genevestigator; Q6PCM1; -. DR GO; GO:0005737; C:cytoplasm; IDA:MGI. DR GO; GO:0005634; C:nucleus; IDA:MGI. DR GO; GO:0001047; F:core promoter binding; IDA:MGI. DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW. DR GO; GO:0005506; F:iron ion binding; IEA:Ensembl. DR GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; IDA:MGI. DR GO; GO:0000976; F:transcription regulatory region sequence-specific DNA binding; IDA:MGI. DR GO; GO:0030521; P:androgen receptor signaling pathway; IEA:Ensembl. DR GO; GO:0046293; P:formaldehyde biosynthetic process; IEA:Ensembl. DR GO; GO:0033169; P:histone H3-K9 demethylation; IEA:Ensembl. DR GO; GO:0036123; P:histone H3-K9 dimethylation; IDA:MGI. DR GO; GO:0009755; P:hormone-mediated signaling pathway; IEA:Ensembl. DR GO; GO:0051573; P:negative regulation of histone H3-K9 methylation; IMP:MGI. DR GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:MGI. DR GO; GO:0007290; P:spermatid nucleus elongation; IMP:MGI. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR InterPro; IPR003347; JmjC_dom. DR Pfam; PF02373; JmjC; 1. DR SMART; SM00558; JmjC; 1. DR PROSITE; PS51184; JMJC; 1. PE 1: Evidence at protein level; KW Acetylation; Activator; Alternative splicing; Chromatin regulator; KW Complete proteome; Cytoplasm; Differentiation; Dioxygenase; Iron; KW Metal-binding; Nucleus; Oxidoreductase; Phosphoprotein; KW Reference proteome; Spermatogenesis; Transcription; KW Transcription regulation; Zinc; Zinc-finger. FT CHAIN 1 1323 Lysine-specific demethylase 3A. FT /FTId=PRO_0000084286. FT DOMAIN 1060 1283 JmjC. FT ZN_FING 662 687 C6-type (Potential). FT MOTIF 885 889 LXXLL motif. FT METAL 1122 1122 Iron; catalytic (By similarity). FT METAL 1124 1124 Iron; catalytic (By similarity). FT METAL 1251 1251 Iron; catalytic (By similarity). FT MOD_RES 264 264 Phosphoserine (By similarity). FT MOD_RES 446 446 Phosphoserine (By similarity). FT MOD_RES 895 895 N6-acetyllysine (By similarity). FT VAR_SEQ 1 492 Missing (in isoform 2). FT /FTId=VSP_018296. FT VAR_SEQ 493 507 NESCCTRSSNKTQTP -> MFWGDWKNIMEGAPA (in FT isoform 2). FT /FTId=VSP_018297. FT CONFLICT 144 144 K -> Q (in Ref. 4; ABC54567). FT CONFLICT 229 229 P -> L (in Ref. 4; ABC54567). FT CONFLICT 618 618 A -> T (in Ref. 4; ABC54567). FT CONFLICT 832 832 V -> F (in Ref. 2; AAH31200). SQ SEQUENCE 1323 AA; 147847 MW; 6D9C4A7779076AED CRC64; MVLTLGESWP VLVGKRFLSL SAAEGNEGGQ DNWDLERVAE WPWLSGTIRA VSHTDVTKKD LKVCVEFDGE SWRKRRWIDV YSLQRKAFLV EHNLVLAERK SPEVPEQVIQ WPAIMYKSLL DKAGLGAITS VRFLGDQQSV FVSKDLLKPI QDVNSLRLSL TDNQTVSKEF QALIVKHLDE SHLLQGDKNL VGSEVKIYSL DPSTQWFSAT VVHGNPSSKT LQVNCEEIPA LKIVDPALIH VEVVHDNFVT CGNSTRTGAV KRKSSENNGS SVSKQAKSCS EASPSMCPVQ SVPTTVFKEI LLGCTAATPS SKDPRQQNTP QAANSPPNIG AKLPQGCHKQ NLPEELSSCL NTKPEVPRTK PDVCKEGLLS SKSSQVGAGD LKILSEPKGS CIQPKTNTDQ ESRLESAPQP VTGLPKECLP AKTSSKAELD IATTPELQKH LEHAASTSDD LSDKPEVKAG VTSLNSCAEK KVEPSHLGSQ SQNLKETSVK VDNESCCTRS SNKTQTPPAR KSVLTDPDKV RKLQQSGEAF VQDDSCVNIV AQLPKCRECR LDSLRKDKDQ QKDSPVFCRF FHFRRLQFNK HGVLRVEGFL TPNKYDSEAI GLWLPLTKNV VGTDLDTAKY ILANIGDHFC QMVISEKEAM STIEPHRQVA WKRAVKGVRE MCDVCDTTIF NLHWVCPRCG FGVCVDCYRM KRKNCQQGAA YKTFSWIRCV KSQIHEPENL MPTQIIPGKA LYDVGDIVHS VRAKWGIKAN CPCSNRQFKL FSKPALKEDL KQTSLSGEKP TLGTMVQQSS PVLEPVAVCG EAASKPASSV KPTCPTSTSP LNWLADLTSG NVNKENKEKQ LTMPILKNEI KCLPPLPPLN KPSTVLHTFN STILTPVSNN NSGFLRNLLN SSTAKTENGL KNTPKILDDI FASLVQNKTS SDSSKRPQGL TIKPSILGFD TPHYWLCDNR LLCLQDPNNK SNWNVFRECW KQGQPVMVSG VHHKLNTELW KPESFRKEFG EQEVDLVNCR TNEIITGATV GDFWDGFEDV PNRLKNDKEK EPMVLKLKDW PPGEDFRDMM PSRFDDLMAN IPLPEYTRRD GKLNLASRLP NYFVRPDLGP KMYNAYGLIT PEDRKYGTTN LHLDVSDAAN VMVYVGIPKG QCEQEEEVLR TIQDGDSDEL TIKRFIEGKE KPGALWHIYA AKDTEKIREF LKKVSEEQGQ DNPADHDPIH DQSWYLDRSL RKRLYQEYGV QGWAIVQFLG DVVFIPAGAP HQVHNLYSCI KVAEDFVSPE HVKHCFWLTQ EFRYLSQTHT NHEDKLQVKN VIYHAVKDAV AMLKASESSL GKP // ID KDM1A_MOUSE Reviewed; 853 AA. AC Q6ZQ88; A3KG94; Q6PB53; Q8VEA1; DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot. DT 16-AUG-2004, sequence version 2. DT 19-MAR-2014, entry version 104. DE RecName: Full=Lysine-specific histone demethylase 1A; DE EC=1.-.-.-; DE AltName: Full=BRAF35-HDAC complex protein BHC110; DE AltName: Full=Flavin-containing amine oxidase domain-containing protein 2; GN Name=Kdm1a; Synonyms=Aof2, Kiaa0601, Lsd1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; RX PubMed=14621295; DOI=10.1093/dnares/10.4.167; RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., RA Saga Y., Nagase T., Ohara O., Koga H.; RT "Prediction of the coding sequences of mouse homologues of KIAA gene: RT III. The complete nucleotide sequences of 500 mouse KIAA-homologous RT cDNAs identified by screening of terminal sequences of cDNA clones RT randomly sampled from size-fractionated libraries."; RL DNA Res. 10:167-180(2003). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6; TISSUE=Brain, and Mammary gland; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP TISSUE SPECIFICITY. RX PubMed=16079795; DOI=10.1038/nature04020; RA Metzger E., Wissmann M., Yin N., Mueller J.M., Schneider R., RA Peters A.H.F.M., Guenther T., Buettner R., Schuele R.; RT "LSD1 demethylates repressive histone marks to promote androgen- RT receptor-dependent transcription."; RL Nature 437:436-439(2005). RN [5] RP IDENTIFICATION BY MASS SPECTROMETRY AS A COMPONENT OF A RP GFI-RCOR-KDM1A-HDAC COMPLEX, INTERACTION WITH GFI1 AND GFI1B, AND RP FUNCTION. RX PubMed=17707228; DOI=10.1016/j.molcel.2007.06.039; RA Saleque S., Kim J., Rooke H.M., Orkin S.H.; RT "Epigenetic regulation of hematopoietic differentiation by Gfi-1 and RT Gfi-1b is mediated by the cofactors CoREST and LSD1."; RL Mol. Cell 27:562-572(2007). RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-167, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006; RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M., RA Thibault P.; RT "The phagosomal proteome in interferon-gamma-activated macrophages."; RL Immunity 30:143-154(2009). RN [7] RP FUNCTION, AND DEVELOPMENTAL STAGE. RX PubMed=19098913; DOI=10.1038/ng.268; RA Wang J., Hevi S., Kurash J.K., Lei H., Gay F., Bajko J., Su H., RA Sun W., Chang H., Xu G., Gaudet F., Li E., Chen T.; RT "The lysine demethylase LSD1 (KDM1) is required for maintenance of RT global DNA methylation."; RL Nat. Genet. 41:125-129(2009). RN [8] RP INTERACTION WITH INSM1. RX PubMed=24227653; DOI=10.1242/dev.097642; RA Welcker J.E., Hernandez-Miranda L.R., Paul F.E., Jia S., Ivanov A., RA Selbach M., Birchmeier C.; RT "Insm1 controls development of pituitary endocrine cells and requires RT a SNAG domain for function and for recruitment of histone-modifying RT factors."; RL Development 140:4947-4958(2013). CC -!- FUNCTION: Histone demethylase that demethylates both 'Lys-4' CC (H3K4me) and 'Lys-9' (H3K9me) of histone H3, thereby acting as a CC coactivator or a corepressor, depending on the context. Acts by CC oxidizing the substrate by FAD to generate the corresponding imine CC that is subsequently hydrolyzed. Acts as a corepressor by CC mediating demethylation of H3K4me, a specific tag for epigenetic CC transcriptional activation. Demethylates both mono- (H3K4me1) and CC di-methylated (H3K4me2) H3K4me. May play a role in the repression CC of neuronal genes. Alone, it is unable to demethylate H3K4me on CC nucleosomes and requires the presence of RCOR1/CoREST to achieve CC such activity. Also acts as a coactivator of androgen receptor CC (ANDR)-dependent transcription, by being recruited to ANDR target CC genes and mediating demethylation of H3K9me, a specific tag for CC epigenetic transcriptional repression. The presence of PRKCB in CC ANDR-containing complexes, which mediates phosphorylation of 'Thr- CC 6' of histone H3 (H3T6ph), a specific tag that prevents CC demethylation H3K4me, prevents H3K4me demethylase activity of CC KDM1A. Demethylates di-methylated 'Lys-370' of p53/TP53 which CC prevents interaction of p53/TP53 with TP53BP1 and represses CC p53/TP53-mediated transcriptional activation (By similarity). CC Demethylates and stabilizes the DNA methylase DNMT1. Required for CC gastrulation during embryogenesis. Component of a CC RCOR/GFI/KDM1A/HDAC complex that suppresses, via histone CC deacetylase (HDAC) recruitment, a number of genes implicated in CC multilineage blood cell development. Effector of SNAI1-mediated CC transcription repression of E-cadherin/CDH1, CDN7 and KRT8. CC Required for the maintenance of the silenced state of the SNAI1 CC target genes E-cadherin/CDH1 and CDN7. CC -!- COFACTOR: FAD (By similarity). CC -!- SUBUNIT: Component of a BHC histone deacetylase complex that CC contains HDAC1, HDAC2, HMG20B, KDM1A, RCOR1 and PHF21A. The BHC CC complex may also contain ZMYM2, ZNF217, ZMYM3, GSE1 and GTF2I. In CC the complex, RCOR1 strongly enhances the demethylase activity and CC protects it from the proteasome while PHF21A inhibits the CC demethylase activity. Interacts with the androgen receptor (AR) CC (By similarity). Component of a RCOR/GFI/KDM1A/HDAC complex. CC Interacts directly with GFI1 and GFI1B. Interacts with ASXL1. CC Interacts with SNAI1 (via SNAG domain) (By similarity). Interacts CC with INSM1. CC -!- INTERACTION: CC Q9CQJ4:Rnf2; NbExp=3; IntAct=EBI-1216284, EBI-927321; CC -!- SUBCELLULAR LOCATION: Nucleus (By similarity). CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. CC -!- DEVELOPMENTAL STAGE: Zygotic expression first appears at the CC morula stage. In blastocysts, expressed in the inner cell mass and CC trophectodermal cells. In postimplantation embryos, expression CC becomes ubiquitous. CC -!- DOMAIN: The SWIRM domain may act as an anchor site for a histone CC tail (By similarity). CC -!- SIMILARITY: Belongs to the flavin monoamine oxidase family. CC -!- SIMILARITY: Contains 1 SWIRM domain. CC -!- SEQUENCE CAUTION: CC Sequence=AAH59885.1; Type=Erroneous initiation; Note=Translation N-terminally extended; CC Sequence=BAC97980.1; Type=Erroneous initiation; Note=Translation N-terminally shortened; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK129170; BAC97980.1; ALT_INIT; mRNA. DR EMBL; AL671173; CAM46211.1; -; Genomic_DNA. DR EMBL; BC019417; AAH19417.1; -; mRNA. DR EMBL; BC059885; AAH59885.1; ALT_INIT; mRNA. DR RefSeq; NP_598633.2; NM_133872.2. DR UniGene; Mm.28540; -. DR ProteinModelPortal; Q6ZQ88; -. DR SMR; Q6ZQ88; 172-837. DR BioGrid; 221360; 13. DR DIP; DIP-38599N; -. DR IntAct; Q6ZQ88; 7. DR MINT; MINT-4100561; -. DR PhosphoSite; Q6ZQ88; -. DR PaxDb; Q6ZQ88; -. DR PRIDE; Q6ZQ88; -. DR Ensembl; ENSMUST00000116273; ENSMUSP00000111977; ENSMUSG00000036940. DR GeneID; 99982; -. DR KEGG; mmu:99982; -. DR UCSC; uc008vig.2; mouse. DR CTD; 23028; -. DR MGI; MGI:1196256; Kdm1a. DR eggNOG; COG1231; -. DR GeneTree; ENSGT00530000062888; -. DR HOGENOM; HOG000246945; -. DR KO; K11450; -. DR OrthoDB; EOG7X9G66; -. DR TreeFam; TF312972; -. DR ChiTaRS; KDM1A; mouse. DR NextBio; 354201; -. DR PRO; PR:Q6ZQ88; -. DR ArrayExpress; Q6ZQ88; -. DR Bgee; Q6ZQ88; -. DR CleanEx; MM_AOF2; -. DR Genevestigator; Q6ZQ88; -. DR GO; GO:0000790; C:nuclear chromatin; IDA:BHF-UCL. DR GO; GO:0005667; C:transcription factor complex; IDA:MGI. DR GO; GO:0050681; F:androgen receptor binding; ISS:UniProtKB. DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; ISS:UniProtKB. DR GO; GO:0034648; F:histone demethylase activity (H3-dimethyl-K4 specific); ISS:UniProtKB. DR GO; GO:0032454; F:histone demethylase activity (H3-K9 specific); ISS:UniProtKB. DR GO; GO:0030374; F:ligand-dependent nuclear receptor transcription coactivator activity; ISS:UniProtKB. DR GO; GO:0016491; F:oxidoreductase activity; ISS:UniProtKB. DR GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; IDA:MGI. DR GO; GO:0044212; F:transcription regulatory region DNA binding; IDA:BHF-UCL. DR GO; GO:0008283; P:cell proliferation; IMP:MGI. DR GO; GO:0030851; P:granulocyte differentiation; IMP:UniProtKB. DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI. DR GO; GO:0055001; P:muscle cell development; IMP:BHF-UCL. DR GO; GO:0043518; P:negative regulation of DNA damage response, signal transduction by p53 class mediator; IEA:Ensembl. DR GO; GO:0051572; P:negative regulation of histone H3-K4 methylation; IMP:BHF-UCL. DR GO; GO:0051573; P:negative regulation of histone H3-K9 methylation; IMP:BHF-UCL. DR GO; GO:1902166; P:negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; IEA:Ensembl. DR GO; GO:0032091; P:negative regulation of protein binding; IEA:Ensembl. DR GO; GO:0043433; P:negative regulation of sequence-specific DNA binding transcription factor activity; ISS:BHF-UCL. DR GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:BHF-UCL. DR GO; GO:0021983; P:pituitary gland development; IMP:MGI. DR GO; GO:0045648; P:positive regulation of erythrocyte differentiation; IMP:UniProtKB. DR GO; GO:0046886; P:positive regulation of hormone biosynthetic process; IMP:MGI. DR GO; GO:0045654; P:positive regulation of megakaryocyte differentiation; IMP:UniProtKB. DR GO; GO:2000179; P:positive regulation of neural precursor cell proliferation; IMP:BHF-UCL. DR GO; GO:0051091; P:positive regulation of sequence-specific DNA binding transcription factor activity; IEA:Ensembl. DR GO; GO:2000648; P:positive regulation of stem cell proliferation; IMP:BHF-UCL. DR GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IMP:MGI. DR GO; GO:0010725; P:regulation of primitive erythrocyte differentiation; IMP:UniProtKB. DR GO; GO:0034401; P:regulation of transcription by chromatin organization; IC:BHF-UCL. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.10.10; -; 1. DR InterPro; IPR002937; Amino_oxidase. DR InterPro; IPR017366; Hist_Lys-spec_deMease. DR InterPro; IPR009057; Homeodomain-like. DR InterPro; IPR007526; SWIRM. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF01593; Amino_oxidase; 1. DR Pfam; PF04433; SWIRM; 1. DR PIRSF; PIRSF038051; Histone_Lys-demethylase; 1. DR SUPFAM; SSF46689; SSF46689; 1. DR PROSITE; PS50934; SWIRM; 1. PE 1: Evidence at protein level; KW Chromatin regulator; Coiled coil; Complete proteome; KW Developmental protein; FAD; Flavoprotein; Nucleus; Oxidoreductase; KW Phosphoprotein; Reference proteome; Repressor; Transcription; KW Transcription regulation. FT CHAIN 1 853 Lysine-specific histone demethylase 1A. FT /FTId=PRO_0000099882. FT DOMAIN 175 274 SWIRM. FT NP_BIND 282 310 FAD (Potential). FT REGION 301 853 Demethylase activity (By similarity). FT COILED 111 152 Potential. FT COILED 429 515 Potential. FT COMPBIAS 7 56 Ala-rich. FT COMPBIAS 153 157 Poly-Pro. FT BINDING 290 290 FAD (By similarity). FT BINDING 309 309 FAD (By similarity). FT BINDING 311 311 FAD (By similarity). FT BINDING 317 317 FAD (By similarity). FT BINDING 802 802 FAD (By similarity). FT MOD_RES 105 105 Phosphothreonine (By similarity). FT MOD_RES 127 127 Phosphoserine (By similarity). FT MOD_RES 132 132 Phosphoserine (By similarity). FT MOD_RES 138 138 Phosphoserine (By similarity). FT MOD_RES 167 167 Phosphoserine. FT MOD_RES 850 850 Phosphoserine (By similarity). FT CONFLICT 226 226 P -> S (in Ref. 3; AAH59885). SQ SEQUENCE 853 AA; 92851 MW; 43CD401FA0452B2F CRC64; MLSGKKAAAA AAAAAAAAAA GTEAGSGAAG GAENGSEVAA PPAGLTGPTD MATGAAGERT PRKKEPPRAS PPGGLAEPPG SAGPQAGPTA GPGSATPMET GIAETPEGRR TSRRKRAKVE YREMDESLAN LSEDEYYSEE ERNAKAEKEK KLPPPPPQAP PEEENESEPE EPSGVEGAAF QSRLPHDRMT SQEAACFPDI ISGPQQTQKV FLFIRNRTLQ LWLDNPKIQL TFEATLQQLE APYNSDTVLV HRVHSYLERH GLINFGIYKR IKPLPIKKTG KVIIIGSGVS GLAAARQLQS FGMDVTLLEA RDRVGGRVAT FRKGNYVADL GAMVVTGLGG NPMAVVSKQV NMELAKIKQK CPLYEANGQA VPKEKDEMVE QEFNRLLEAT SYLSHQLDFN VLNNKPVSLG QALEVVIQLQ EKHVKDEQIE HWKKIVKTQE ELKELLNKMV NLKEKIKELH QQYKEASEVK PPRDITAEFL VKSKHRDLTA LCKEYDELAE TQGKLEEKLQ ELEANPPSDV YLSSRDRQIL DWHFANLEFA NATPLSTLSL KHWDQDDDFE FTGSHLTVRN GYSCVPVALA EGLDIKLNTA VRQVRYTASG CEVIAVNTRS TSQTFIYKCD AVLCTLPLGV LKQQPPAVQF VPPLPEWKTS AVQRMGFGNL NKVVLCFDRV FWDPSVNLFG HVGSTTASRG ELFLFWNLYK APILLALVAG EAAGIMENIS DDVIVGRCLA ILKGIFGSSA VPQPKETVVS RWRADPWARG SYSYVAAGSS GNDYDLMAQP ITPGPSIPGA PQPIPRLFFA GEHTIRNYPA TVHGALLSGL REAGRIADQF LGAMYTLPRQ ATPGVPAQQS PSM // ID KDM6B_MOUSE Reviewed; 1641 AA. AC Q5NCY0; Q3UWY9; Q4VC26; Q6ZQD3; DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-2005, sequence version 1. DT 19-MAR-2014, entry version 73. DE RecName: Full=Lysine-specific demethylase 6B; DE EC=1.14.11.-; DE AltName: Full=JmjC domain-containing protein 3; DE AltName: Full=Jumonji domain-containing protein 3; GN Name=Kdm6b; Synonyms=Jmjd3, Kiaa0346; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6; TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 935-1641. RC TISSUE=Embryonic tail; RX PubMed=14621295; DOI=10.1093/dnares/10.4.167; RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., RA Saga Y., Nagase T., Ohara O., Koga H.; RT "Prediction of the coding sequences of mouse homologues of KIAA gene: RT III. The complete nucleotide sequences of 500 mouse KIAA-homologous RT cDNAs identified by screening of terminal sequences of cDNA clones RT randomly sampled from size-fractionated libraries."; RL DNA Res. 10:167-180(2003). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1138-1641. RC STRAIN=C57BL/6J; TISSUE=Egg; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [5] RP FUNCTION, AND INDUCTION. RX PubMed=17825402; DOI=10.1016/j.cell.2007.08.019; RA De Santa F., Totaro M.G., Prosperini E., Notarbartolo S., Testa G., RA Natoli G.; RT "The histone H3 lysine-27 demethylase Jmjd3 links inflammation to RT inhibition of polycomb-mediated gene silencing."; RL Cell 130:1083-1094(2007). CC -!- FUNCTION: Histone demethylase that specifically demethylates 'Lys- CC 27' of histone H3, thereby playing a central role in histone code. CC Demethylates trimethylated and dimethylated H3 'Lys-27'. Plays a CC central role in regulation of posterior development, by regulating CC HOX gene expression. Involved in inflammatory response by CC participating in macrophage differentiation in case of CC inflammation by regulating gene expression and macrophage CC differentiation. CC -!- COFACTOR: Ascorbate (By similarity). CC -!- COFACTOR: Fe(2+) (By similarity). CC -!- SUBUNIT: Interacts with TLE1 (By similarity). Component of the CC MLL4 complex, at least composed of KMT2B/MLL4, ASH2L, RBBP5, WDR5, CC and KDM6B (By similarity). CC -!- SUBCELLULAR LOCATION: Nucleus (By similarity). CC -!- INDUCTION: By inflammatory stimuli; mediated by NF-kappa-B. CC -!- SIMILARITY: Belongs to the UTX family. CC -!- SIMILARITY: Contains 1 JmjC domain. CC -!- SEQUENCE CAUTION: CC Sequence=BAE22775.1; Type=Erroneous initiation; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AL596125; CAI35996.1; -; Genomic_DNA. DR EMBL; BC075632; AAH75632.1; -; mRNA. DR EMBL; AK129121; BAC97931.1; -; mRNA. DR EMBL; AK136019; BAE22775.1; ALT_INIT; mRNA. DR RefSeq; NP_001017426.1; NM_001017426.1. DR RefSeq; XP_006532961.1; XM_006532898.1. DR UniGene; Mm.261201; -. DR UniGene; Mm.472522; -. DR PDB; 4EYU; X-ray; 2.30 A; A/B=1155-1641. DR PDB; 4EZ4; X-ray; 2.99 A; A/B=1155-1641. DR PDB; 4EZH; X-ray; 2.52 A; A/B=1155-1641. DR PDBsum; 4EYU; -. DR PDBsum; 4EZ4; -. DR PDBsum; 4EZH; -. DR ProteinModelPortal; Q5NCY0; -. DR SMR; Q5NCY0; 1155-1636. DR BioGrid; 229803; 5. DR DIP; DIP-39160N; -. DR IntAct; Q5NCY0; 3. DR STRING; 10090.ENSMUSP00000091620; -. DR PhosphoSite; Q5NCY0; -. DR PaxDb; Q5NCY0; -. DR PRIDE; Q5NCY0; -. DR Ensembl; ENSMUST00000094077; ENSMUSP00000091620; ENSMUSG00000018476. DR GeneID; 216850; -. DR KEGG; mmu:216850; -. DR UCSC; uc007jqd.1; mouse. DR CTD; 23135; -. DR MGI; MGI:2448492; Kdm6b. DR eggNOG; NOG246325; -. DR GeneTree; ENSGT00410000025758; -. DR HOGENOM; HOG000113217; -. DR InParanoid; Q5NCY0; -. DR KO; K11448; -. DR OMA; MDPLPRP; -. DR OrthoDB; EOG7CG6Z5; -. DR TreeFam; TF317405; -. DR ChiTaRS; KDM6B; mouse. DR NextBio; 375392; -. DR PRO; PR:Q5NCY0; -. DR ArrayExpress; Q5NCY0; -. DR Bgee; Q5NCY0; -. DR CleanEx; MM_JMJD3; -. DR Genevestigator; Q5NCY0; -. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI. DR GO; GO:0070301; P:cellular response to hydrogen peroxide; IDA:MGI. DR GO; GO:0016577; P:histone demethylation; IMP:MGI. DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW. DR GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:MGI. DR Gene3D; 1.25.40.10; -; 1. DR InterPro; IPR003347; JmjC_dom. DR InterPro; IPR011990; TPR-like_helical. DR Pfam; PF02373; JmjC; 1. DR SMART; SM00558; JmjC; 1. DR PROSITE; PS51184; JMJC; 1. PE 1: Evidence at protein level; KW 3D-structure; Chromatin regulator; Complete proteome; Dioxygenase; KW Inflammatory response; Iron; Metal-binding; Nucleus; Oxidoreductase; KW Reference proteome. FT CHAIN 1 1641 Lysine-specific demethylase 6B. FT /FTId=PRO_0000292008. FT DOMAIN 1337 1500 JmjC. FT COMPBIAS 32 85 Pro-rich. FT COMPBIAS 195 908 Pro-rich. FT COMPBIAS 370 408 Ser-rich. FT COMPBIAS 743 766 Thr-rich. FT COMPBIAS 1045 1080 Pro-rich. FT METAL 1388 1388 Iron (By similarity). FT METAL 1390 1390 Iron (By similarity). FT CONFLICT 172 172 P -> S (in Ref. 2; AAH75632). FT CONFLICT 965 965 A -> T (in Ref. 3; BAC97931). FT CONFLICT 1290 1290 L -> LQ (in Ref. 3; BAC97931). FT HELIX 1160 1162 FT STRAND 1170 1172 FT HELIX 1176 1179 FT STRAND 1185 1187 FT HELIX 1191 1195 FT HELIX 1197 1203 FT STRAND 1209 1214 FT HELIX 1216 1220 FT HELIX 1224 1227 FT HELIX 1229 1236 FT STRAND 1240 1247 FT STRAND 1260 1262 FT STRAND 1269 1274 FT HELIX 1275 1293 FT STRAND 1323 1331 FT TURN 1335 1338 FT HELIX 1339 1344 FT HELIX 1345 1347 FT HELIX 1350 1352 FT STRAND 1353 1355 FT HELIX 1360 1363 FT STRAND 1364 1366 FT TURN 1369 1371 FT STRAND 1375 1379 FT STRAND 1384 1388 FT HELIX 1391 1393 FT STRAND 1395 1404 FT STRAND 1406 1411 FT HELIX 1413 1415 FT HELIX 1416 1425 FT TURN 1430 1432 FT HELIX 1439 1444 FT STRAND 1450 1454 FT STRAND 1459 1462 FT STRAND 1467 1483 FT HELIX 1488 1503 FT HELIX 1512 1522 FT HELIX 1528 1553 FT TURN 1554 1556 FT STRAND 1559 1561 FT TURN 1574 1576 FT STRAND 1582 1588 FT STRAND 1596 1599 FT HELIX 1601 1607 FT STRAND 1615 1620 FT HELIX 1622 1631 SQ SEQUENCE 1641 AA; 176355 MW; 6CBE3620998427EA CRC64; MHRAVDPPGA RSAREAFALG GLSCAGAWSS CPPHPPPRSS WLPGGRCSAS VGQPPLSAPL PPSHGSSSGH PNKPYYAPGT PTPRPLHGKL ESLHGCVQAL LREPAQPGLW EQLGQLYESE HDSEEAVCCY HRALRYGGSF AELGPRIGRL QQAQLWNFHA GSCQHRAKVL PPLEQVWNLL HLEHKRNYGA KRGGPPVKRS AEPPVVQPMP PAALSGPSGE EGLSPGGKRR RGCSSEQAGL PPGLPLPPPP PPPPPPPPPP PPPPPPLPGL AISPPFQLTK PGLWNTLHGD AWGPERKGSA PPERQEQRHS MPHSYPYPAP AYSAHPPSHR LVPNTPLGPG PRPPGAESHG CLPATRPPGS DLRESRVQRS RMDSSVSPAA STACVPYAPS RPPGLPGTSS SSSSSSSSNN TGLRGVEPSP GIPGADHYQN PALEISPHQA RLGPSAHSSR KPFLTAPAAT PHLSLPPGTP SSPPPPCPRL LRPPPPPAWM KGSACRAARE DGEILGELFF GAEGPPRPPP PPLPHRDGFL GPPNPRFSVG TQDSHNPPIP PTTTSSSSSS NSHSSSPTGP VPFPPPSYLA RSIDPLPRPS SPTLSPQDPP LPPLTLALPP APPSSCHQNT SGSFRRSESP RPRVSFPKTP EVGQGPPPGP VSKAPQPVPP GVGELPARGP RLFDFPPTPL EDQFEEPAEF KILPDGLANI MKMLDESIRK EEEQQQQQEA GVAPPPPLKE PFASLQPPFP SDTAPATTTA APTTATTTTT TTTTTTQEEE KKPPPALPPP PPLAKFPPPP QPQPPPPPPA SPASLLKSLA SVLEGQKYCY RGTGAAVSTR PGSVPATQYS PSPASGATAP PPTSVAPSAQ GSPKPSVSSS SQFSTSGGPW AREHRAGEEP APGPVTPAQL PPPLPLPPAR SESEVLEEIS RACETLVERV GRSAINPVDT ADPVDSGTEP QPPPAQAKEE SGGVAVAAAG PGSGKRRQKE HRRHRRACRD SVGRRPREGR AKAKAKAPKE KSRRVLGNLD LQSEEIQGRE KARPDVGGVS KVKTPTAPAP PPAPAPAAQP TPPSAPVPGK KTREEAPGPP GVSRADMLKL RSLSEGPPKE LKIRLIKVES GDKETFIASE VEERRLRMAD LTISHCAADV MRASKNAKVK GKFRESYLSP AQSVKPKINT EEKLPREKLN PPTPSIYLES KRDAFSPVLL QFCTDPRNPI TVIRGLAGSL RLNLGLFSTK TLVEASGEHT VEVRTQVQQP SDENWDLTGT RQIWPCESSR SHTTIAKYAQ YQASSFQESL QEERESEDEE SEEPDSTTGT SPSSAPDPKN HHIIKFGTNI DLSDAKRWKP QLQELLKLPA FMRVTSTGNM LSHVGHTILG MNTVQLYMKV PGSRTPGHQE NNNFCSVNIN IGPGDCEWFA VHEHYWETIS AFCDRHGVDY LTGSWWPILD DLYASNIPVY RFVQRPGDLV WINAGTVHWV QATGWCNNIA WNVGPLTAYQ YQLALERYEW NEVKNVKSIV PMIHVSWNVA RTVKISDPDL FKMIKFCLLQ SMKHCQVQRE SLVRAGKKIA YQGRVKDEPA YYCNECDVEV FNILFVTSEN GSRNTYLVHC EGCARRRSAG LQGVVVLEQY RTEELAQAYD AFTLAPASTS R // ID KDM7A_MOUSE Reviewed; 940 AA. AC Q3UWM4; A6H6E5; Q3UWN8; Q6ZPJ5; Q8C969; Q8C9E0; Q91VX8; DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot. DT 07-MAR-2006, sequence version 2. DT 19-MAR-2014, entry version 77. DE RecName: Full=Lysine-specific demethylase 7A; DE EC=1.14.11.-; DE AltName: Full=JmjC domain-containing histone demethylation protein 1D; DE AltName: Full=Lysine-specific demethylase 7; GN Name=Kdm7a; Synonyms=Jhdm1d, Kdm7, Kiaa1718; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Cerebellum, Egg, and Thymus; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain, and Mammary tumor; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 508-940. RC TISSUE=Embryonic tail; RX PubMed=14621295; DOI=10.1093/dnares/10.4.167; RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., RA Saga Y., Nagase T., Ohara O., Koga H.; RT "Prediction of the coding sequences of mouse homologues of KIAA gene: RT III. The complete nucleotide sequences of 500 mouse KIAA-homologous RT cDNAs identified by screening of terminal sequences of cDNA clones RT randomly sampled from size-fractionated libraries."; RL DNA Res. 10:167-180(2003). RN [4] RP FUNCTION. RX PubMed=20194436; DOI=10.1101/gad.1864410; RA Tsukada Y., Ishitani T., Nakayama K.I.; RT "KDM7 is a dual demethylase for histone H3 Lys 9 and Lys 27 and RT functions in brain development."; RL Genes Dev. 24:432-437(2010). CC -!- FUNCTION: Histone demethylase required for brain development. CC Specifically demethylates dimethylated 'Lys-9' and 'Lys-27' CC (H3K9me2 and H3K27me2, respectively) of histone H3 and CC monomethylated histone H4 'Lys-20' residue (H4K20Me1), thereby CC playing a central role in histone code. Specifically binds CC trimethylated 'Lys-4' of histone H3 (H3K4me3), affecting histone CC demethylase specificity: in presence of H3K4me3, it has no CC demethylase activity toward H3K9me2, while it has high activity CC toward H3K27me2. Demethylates H3K9me2 in absence of H3K4me3. Has CC activity toward H4K20Me1 only when nucleosome is used as a CC substrate and when not histone octamer is used as substrate (By CC similarity). CC -!- COFACTOR: Binds 1 Fe(2+) ion per subunit (By similarity). CC -!- SUBCELLULAR LOCATION: Nucleus (By similarity). CC -!- DOMAIN: The PHD-type zinc finger mediates the binding to H3K4me3. CC Binding to H3K4me3 prevents its access to H3K9me2 (By similarity). CC -!- DOMAIN: The linker region is a critical determinant of demethylase CC specificity. It prevents the active site of JmjC to reach the CC target H3K9me2 when the PHD-type zinc finger binds to H3K4me3, CC while it favors selectivity toward H3K27me2 (By similarity). CC -!- SIMILARITY: Belongs to the JHDM1 histone demethylase family. CC JHDM1D subfamily. CC -!- SIMILARITY: Contains 1 JmjC domain. CC -!- SIMILARITY: Contains 1 PHD-type zinc finger. CC -!- SEQUENCE CAUTION: CC Sequence=AAI45849.1; Type=Erroneous initiation; Note=Translation N-terminally extended; CC Sequence=BAE22876.1; Type=Erroneous initiation; Note=Translation N-terminally extended; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK042327; BAC31226.2; -; mRNA. DR EMBL; AK042834; BAC31377.1; -; mRNA. DR EMBL; AK136209; BAE22876.1; ALT_INIT; mRNA. DR EMBL; AK136238; BAE22890.1; -; mRNA. DR EMBL; BC007161; AAH07161.1; -; mRNA. DR EMBL; BC145848; AAI45849.1; ALT_INIT; mRNA. DR EMBL; AK129429; BAC98239.1; -; mRNA. DR RefSeq; NP_001028602.2; NM_001033430.4. DR UniGene; Mm.293175; -. DR ProteinModelPortal; Q3UWM4; -. DR SMR; Q3UWM4; 3-479. DR STRING; 10090.ENSMUSP00000002305; -. DR PhosphoSite; Q3UWM4; -. DR PaxDb; Q3UWM4; -. DR PRIDE; Q3UWM4; -. DR Ensembl; ENSMUST00000002305; ENSMUSP00000002305; ENSMUSG00000042599. DR GeneID; 338523; -. DR KEGG; mmu:338523; -. DR UCSC; uc009bli.2; mouse. DR CTD; 80853; -. DR MGI; MGI:2443388; Kdm7a. DR eggNOG; NOG290496; -. DR GeneTree; ENSGT00550000074396; -. DR HOVERGEN; HBG045631; -. DR InParanoid; A6H6E5; -. DR KO; K11445; -. DR OMA; LWMKKEL; -. DR OrthoDB; EOG73JKV9; -. DR TreeFam; TF106480; -. DR NextBio; 400221; -. DR PRO; PR:Q3UWM4; -. DR Bgee; Q3UWM4; -. DR Genevestigator; Q3UWM4; -. DR GO; GO:0005730; C:nucleolus; IEA:Ensembl. DR GO; GO:0071558; F:histone demethylase activity (H3-K27 specific); IMP:UniProtKB. DR GO; GO:0051864; F:histone demethylase activity (H3-K36 specific); ISS:UniProtKB. DR GO; GO:0032454; F:histone demethylase activity (H3-K9 specific); IMP:UniProtKB. DR GO; GO:0035575; F:histone demethylase activity (H4-K20 specific); ISS:UniProtKB. DR GO; GO:0005506; F:iron ion binding; ISS:UniProtKB. DR GO; GO:0035064; F:methylated histone residue binding; ISS:UniProtKB. DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB. DR GO; GO:0030901; P:midbrain development; ISS:UniProtKB. DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:UniProtKB. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 3.30.40.10; -; 1. DR InterPro; IPR003347; JmjC_dom. DR InterPro; IPR019786; Zinc_finger_PHD-type_CS. DR InterPro; IPR011011; Znf_FYVE_PHD. DR InterPro; IPR001965; Znf_PHD. DR InterPro; IPR019787; Znf_PHD-finger. DR InterPro; IPR013083; Znf_RING/FYVE/PHD. DR Pfam; PF02373; JmjC; 1. DR Pfam; PF00628; PHD; 1. DR SMART; SM00558; JmjC; 1. DR SMART; SM00249; PHD; 1. DR SUPFAM; SSF57903; SSF57903; 1. DR PROSITE; PS51184; JMJC; 1. DR PROSITE; PS01359; ZF_PHD_1; 1. DR PROSITE; PS50016; ZF_PHD_2; 1. PE 2: Evidence at transcript level; KW Chromatin regulator; Complete proteome; Dioxygenase; Iron; KW Metal-binding; Neurogenesis; Nucleus; Oxidoreductase; KW Reference proteome; Transcription; Transcription regulation; Zinc; KW Zinc-finger. FT CHAIN 1 940 Lysine-specific demethylase 7A. FT /FTId=PRO_0000226772. FT DOMAIN 230 386 JmjC. FT ZN_FING 37 88 PHD-type. FT REGION 97 114 Linker (By similarity). FT COMPBIAS 2 31 Ala-rich. FT METAL 282 282 Iron; catalytic (By similarity). FT METAL 284 284 Iron; catalytic (By similarity). FT METAL 354 354 Iron; catalytic (By similarity). FT BINDING 279 279 Substrate (By similarity). FT BINDING 299 299 Substrate (By similarity). FT CONFLICT 372 372 N -> D (in Ref. 1; BAE22890). SQ SEQUENCE 940 AA; 106075 MW; B14FC1F85C7A5AFE CRC64; MAGAAAAVAA GAAAGAAAAA GSVSAPGRAS APPPPPPVYC VCRQPYDVNR FMIECDVCKD WFHGSCVGVE EHHAVDIDLY HCPDCAALHG SSLMKKRRNW HRHDYTEVDD GSKPVQAGTR AFVKELRSRV FPSADEIIVK MHGSQLTQRY LEKHGFDVPI MVPKLDDLGL RLPSPAFSVM DVERYVGGDK VIDVIDVARQ ADSKMTLHNY VKYFMNPDRP KVLNVISLEF SDTKMSELVE VPDIARKLSW VENYWPDDSV FPKPFVQKYC LMGVQDSYTD FHIDFGGTSV WYHVLWGEKI FYLIKPTNEN LALYESWSSS VTQSEVFFGD KVDKCYKCVV KQGHTLFVPT GWIHAVLTSQ DCMAFGGNFL HNLNIGMQLR CYEMEKRLKT PDLFKFPFFE AICWFVAKSL LETLKELKED GFQPQSYLVQ GVKALHTALK LWMKKELVSE HAFEIPDNVR PGHLIKELSK VIRAIEEENG KPVKSQGIPS VCPVSRPSNE ASPPYHSRRK MRKLRDHNVR TPSNLDILEL HTREVLKRLE MCPWEEDLLS SKLNGKFNKH LQPSSTVPEW RAKDNDLRLL LTNGRIIKDE RQLFADRSLY TADSENEEDK KPTQNANMKT EQSSGREEAE SQGSPKPLNR IFTSVRSELR SRPSEYSDGS DSEDSGPDCT ALKINFATED SESSGDEKKH EITSHFKEES DIVRNLLQKS QKPSRQEIPV KRECPTSTST EEEAIQGMLS MAGLHYSSCL QRQIQSTDCS GEKNSLQDPS SCHGSNPEFR QLYRCNKPVE FGYHAKTEDQ DLMTSSWNKQ FDRTSRFNAQ DLSRSQKHIK KESSSEINQK AQSRHCVDSN SSSIQNGKYT LNPSLVSCQI SNGSLSPERP IGETSFSMPL HPTKRPASNP PPISNQATKG KRPKKGMATA KQRLGKILKL NRNGHARFFV // ID KDM5D_MOUSE Reviewed; 1548 AA. AC Q62240; Q3US03; Q6PCX3; Q9QVR9; Q9R040; DT 24-OCT-2001, integrated into UniProtKB/Swiss-Prot. DT 24-OCT-2001, sequence version 2. DT 19-MAR-2014, entry version 114. DE RecName: Full=Lysine-specific demethylase 5D; DE EC=1.14.11.-; DE AltName: Full=Histocompatibility Y antigen; DE Short=H-Y; DE AltName: Full=Histone demethylase JARID1D; DE AltName: Full=Jumonji/ARID domain-containing protein 1D; DE AltName: Full=Protein SmcY; GN Name=Kdm5d; Synonyms=Hya, Jarid1d, Smcy; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC STRAIN=129/SvJ; RX PubMed=10441747; DOI=10.1007/s003359901116; RA Agulnik A.I., Longepied G., Ty M.T., Bishop C.E., Mitchell M.J.; RT "Mouse H-Y encoding Smcy gene and its X chromosomal homolog Smcx."; RL Mamm. Genome 10:926-929(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4). RC STRAIN=C57BL/6J; TISSUE=Head; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC STRAIN=C57BL/6; TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] OF 23-1548 (ISOFORM 3). RC STRAIN=BALB/c; TISSUE=Testis; RX PubMed=7524912; DOI=10.1093/hmg/3.6.873; RA Agulnik A.I., Mitchell M.J., Lerner J.L., Woods D.R., Bishop C.E.; RT "A mouse Y chromosome gene encoded by a region essential for RT spermatogenesis and expression of male-specific minor RT histocompatibility antigens."; RL Hum. Mol. Genet. 3:873-878(1994). RN [5] RP FUNCTION. RX PubMed=7544442; DOI=10.1038/376695a0; RA Scott D.M., Ehrmann I.E., Ellis P.S., Bishop C.E., Agulnik A.I., RA Simpson E., Mitchell M.J.; RT "Identification of a mouse male-specific transplantation antigen, H- RT Y."; RL Nature 376:695-698(1995). RN [6] RP FUNCTION. RX PubMed=3951555; DOI=10.1038/320170a0; RA Burgoyne P.S., Levy E.R., McLaren A.; RT "Spermatogenic failure in male mice lacking H-Y antigen."; RL Nature 320:170-172(1986). CC -!- FUNCTION: Histone demethylase that specifically demethylates 'Lys- CC 4' of histone H3, thereby playing a central role in histone code. CC Does not demethylate histone H3 'Lys-9', H3 'Lys-27', H3 'Lys-36', CC H3 'Lys-79' or H4 'Lys-20'. Demethylates trimethylated and CC dimethylated but not monomethylated H3 'Lys-4'. May play a role in CC spermatogenesis (By similarity). CC -!- COFACTOR: Ascorbate (By similarity). CC -!- COFACTOR: Binds 1 Fe(2+) ion per subunit (By similarity). CC -!- SUBUNIT: Interacts with PCGF6 and MSH5 (By similarity). CC -!- SUBCELLULAR LOCATION: Nucleus (By similarity). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; CC IsoId=Q62240-1; Sequence=Displayed; CC Name=2; CC IsoId=Q62240-2; Sequence=VSP_026412; CC Note=No experimental confirmation available; CC Name=3; CC IsoId=Q62240-3; Sequence=VSP_026413, VSP_026414; CC Note=May be due to an intron retention. No experimental CC confirmation available; CC Name=4; CC IsoId=Q62240-4; Sequence=VSP_026415, VSP_026416; CC Note=No experimental confirmation available. May be produced at CC very low levels due to a premature stop codon in the mRNA, CC leading to nonsense-mediated mRNA decay; CC -!- DOMAIN: The JmjC domain is required for enzymatic activity (By CC similarity). CC -!- MISCELLANEOUS: KDM5D encodes an H-Y epitope that is defined by the CC octamer peptide TENSGKDI; since no similar peptide was found in CC KDM5C, it is presumably the genetic basis for the antigenic CC difference between males and females that contributes toward a CC tissue transplant rejection response. CC -!- SIMILARITY: Belongs to the JARID1 histone demethylase family. CC -!- SIMILARITY: Contains 1 ARID domain. CC -!- SIMILARITY: Contains 1 JmjC domain. CC -!- SIMILARITY: Contains 1 JmjN domain. CC -!- SIMILARITY: Contains 2 PHD-type zinc fingers. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF127244; AAD53048.1; -; mRNA. DR EMBL; AK140971; BAE24534.1; -; mRNA. DR EMBL; BC059077; AAH59077.1; -; mRNA. DR EMBL; Z29652; CAA82760.1; -; mRNA. DR PIR; I48776; I48776. DR RefSeq; NP_035549.1; NM_011419.3. DR UniGene; Mm.262676; -. DR ProteinModelPortal; Q62240; -. DR SMR; Q62240; 13-171, 319-659, 1180-1245. DR BioGrid; 203342; 3. DR STRING; 10090.ENSMUSP00000061095; -. DR PhosphoSite; Q62240; -. DR PaxDb; Q62240; -. DR PRIDE; Q62240; -. DR Ensembl; ENSMUST00000055032; ENSMUSP00000061095; ENSMUSG00000056673. [Q62240-1] DR GeneID; 20592; -. DR KEGG; mmu:20592; -. DR UCSC; uc009uyz.1; mouse. [Q62240-3] DR UCSC; uc009uzb.1; mouse. [Q62240-1] DR CTD; 8284; -. DR MGI; MGI:99780; Kdm5d. DR eggNOG; NOG327026; -. DR GeneTree; ENSGT00530000063118; -. DR HOGENOM; HOG000290719; -. DR InParanoid; Q62240; -. DR KO; K11446; -. DR OMA; ILMNANV; -. DR OrthoDB; EOG7D85VK; -. DR TreeFam; TF106476; -. DR NextBio; 298905; -. DR PRO; PR:Q62240; -. DR Bgee; Q62240; -. DR Genevestigator; Q62240; -. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0032453; F:histone demethylase activity (H3-K4 specific); IEA:Ensembl. DR GO; GO:0016706; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR Gene3D; 1.10.150.60; -; 1. DR Gene3D; 3.30.40.10; -; 2. DR InterPro; IPR001606; ARID/BRIGHT_DNA-bd. DR InterPro; IPR003347; JmjC_dom. DR InterPro; IPR013637; Lys_sp_deMease_like_dom. DR InterPro; IPR003349; TF_JmjN. DR InterPro; IPR019786; Zinc_finger_PHD-type_CS. DR InterPro; IPR004198; Znf_C5HC2. DR InterPro; IPR011011; Znf_FYVE_PHD. DR InterPro; IPR001965; Znf_PHD. DR InterPro; IPR019787; Znf_PHD-finger. DR InterPro; IPR013083; Znf_RING/FYVE/PHD. DR Pfam; PF01388; ARID; 1. DR Pfam; PF02373; JmjC; 1. DR Pfam; PF02375; JmjN; 1. DR Pfam; PF00628; PHD; 1. DR Pfam; PF08429; PLU-1; 1. DR Pfam; PF02928; zf-C5HC2; 1. DR SMART; SM00501; BRIGHT; 1. DR SMART; SM00558; JmjC; 1. DR SMART; SM00545; JmjN; 1. DR SMART; SM00249; PHD; 2. DR SUPFAM; SSF46774; SSF46774; 1. DR SUPFAM; SSF57903; SSF57903; 2. DR PROSITE; PS51011; ARID; 1. DR PROSITE; PS51184; JMJC; 1. DR PROSITE; PS51183; JMJN; 1. DR PROSITE; PS01359; ZF_PHD_1; 2. DR PROSITE; PS50016; ZF_PHD_2; 1. PE 2: Evidence at transcript level; KW Alternative splicing; Chromatin regulator; Complete proteome; KW Dioxygenase; Iron; Metal-binding; Nucleus; Oxidoreductase; KW Reference proteome; Repeat; Zinc; Zinc-finger. FT CHAIN 1 1548 Lysine-specific demethylase 5D. FT /FTId=PRO_0000200589. FT DOMAIN 14 55 JmjN. FT DOMAIN 79 169 ARID. FT DOMAIN 467 633 JmjC. FT ZN_FING 325 371 PHD-type 1. FT ZN_FING 1182 1243 PHD-type 2. FT METAL 513 513 Iron; catalytic (By similarity). FT METAL 516 516 Iron; catalytic (By similarity). FT METAL 601 601 Iron; catalytic (By similarity). FT VAR_SEQ 1 398 Missing (in isoform 2). FT /FTId=VSP_026412. FT VAR_SEQ 583 586 VRTN -> SIWK (in isoform 3). FT /FTId=VSP_026413. FT VAR_SEQ 587 1548 Missing (in isoform 3). FT /FTId=VSP_026414. FT VAR_SEQ 687 691 GITEA -> LSLQA (in isoform 4). FT /FTId=VSP_026415. FT VAR_SEQ 692 1548 Missing (in isoform 4). FT /FTId=VSP_026416. FT CONFLICT 160 162 IIY -> SFT (in Ref. 4; CAA82760). FT CONFLICT 167 167 F -> S (in Ref. 4; CAA82760). FT CONFLICT 215 215 R -> K (in Ref. 4; CAA82760). SQ SEQUENCE 1548 AA; 177018 MW; 44AAB94708EA4A02 CRC64; MKPGSDDFLP PPECPVFEPS WAEFRDPLGY IAKIRPIAEK SGICKIRPPA DWQPPFAVEV DNFRFTPRIQ RLNELEAQTR VKLNYLDQIA KFWEIQGSSL KIPNVERKIL DLYSLNKIVM EEGGYEAICK DRRWARVAQR LNYPSGKNIG SLLRSHYERI IYPYEIFQSG ANLVQCNTDP FDSEERDKEY KPHSIPLRQS VQPSKFSCYS RRGKRLQPEP EPTEEDIEKN PELKKLQIYG AGPKMIGLGL KAKEKTLRKK DSKQPDKEEV TCPATIVVKG EASEFGKVTS AFSDKNLNHS FEPCMKMTMQ LRNNHSSTQF MNSYVCRICS RGDEVDKFLL CDGCSDNYHI FCLLPPLSEV PKGVWRCPKC ILAECKSPPE AFGFEQATQE YTLQSFGEMA DSFKADYFNM PVHMVPTEVV EKEFWRLVSS IEEDVTVEYG ADIHSKEFGS GFPVNNSKWD LSPEEKEYAA CGWNLNVMPV LDQSVLCHIN ADISGMKVPW LYVGMVFSAF CWHIEDHWSY SINYLHWGEP KTWYGVPSLA AEHLEDVMKR LTPELFDSQP DLLHQLVTLM NPNTLMSHGV PVVRTNQCAG EFVITFPRAY HSGFNQGYNF AEAVNFCTAD WLPVGRQCIE HYRRLRRYCV FSHEELICKM AAFPEKLDLN LAVAVHKEMF IMVQEERRLR KTLLEKGITE AEREAFELLP DDERQCIKCK TTCFLSALAC YDCPDSLVCL SHINDLCKCS RNRQYLRYRY TLDELPAMLQ KLKIRAESFD NWANKVQAAL EVEDGRKRSF EELRALESEA RDRRFPNSEL LQRLKKCLTE AEACISQVLG LISNSEDRLQ TPQITLTELQ LLLKQMGTLP CTMHQIDEVK DVLQQVESYQ IETREALTSL PYSLEILQSL MEKGQQLRVE VPEAHQLEEL LEQAQWLDQV KQALAPSGQR HSLVIMKKLL VMGTKVASSP SVNKARAELQ ELLTIAECWE EKAHFCLKAS QKHSPATLEV IIREAENIPV YLPNIQSLKE ALTKAQAWIA DVNEIQNGDH YPCLDDLEGL VAVGRDLPVE LEELRQLENQ VLTAHSWKEK ASKTFLKKNS CYTLLEVLCP CADAGSVSTK RSRWIEKEMG LYKYDTELLG LSAQDLRDPG SVIMAFKEGE EKEKEGILHL RHINSAKPSP MSSSMNASAT SICICGQVCA GVESLQCDLC HDWFHGQCVT VPHLLSSVRA SHTSSQLLAW WEWDTKFLCP LCMRSRRPRL ETILSLLVGL QRLSVRLPEG EALQCLTERA IGWQGRARQA LASEDVTALL KQLEKSRQQL QDELRHKKPP TLPSGFAFDC LTENSGKDIL KEEEELVLNE ERIKSSEKIV PKESSCKGDK ELLPSLLSQL TGPVLELPEA TRAPLEELMM EGDLLEVTLD ENYSIWQLLQ AGQNPNLERI HTLLELEKPE NPGNWSEEQT PERRRQRRQK VVLSRKGEDF TQKELESKRV KSSRIKPKEE KFQKPILGDN VLYTHHTEHT NILKEHINSV QGKDPSPSSS FPSLTPLLHL SYFHQQKL // ID KDM8_MOUSE Reviewed; 414 AA. AC Q9CXT6; DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 19-FEB-2014, entry version 80. DE RecName: Full=Lysine-specific demethylase 8; DE EC=1.14.11.27; DE AltName: Full=JmjC domain-containing protein 5; DE AltName: Full=Jumonji domain-containing protein 5; GN Name=Kdm8; Synonyms=Jmjd5; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Head; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Mammary tumor; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: Histone demethylase required for G2/M phase cell cycle CC progression. Specifically demethylates dimethylated 'Lys-36' CC (H3K36me2) of histone H3, an epigenetic repressive mark, thereby CC acting as a transcription activator. Regulates expression of CCNA1 CC (cyclin-A1) (By similarity). CC -!- CATALYTIC ACTIVITY: Protein N(6),N(6)-dimethyl-L-lysine + 2- CC oxoglutarate + O(2) = protein N(6)-methyl-L-lysine + succinate + CC formaldehyde + CO(2). CC -!- CATALYTIC ACTIVITY: Protein N(6)-methyl-L-lysine + 2-oxoglutarate CC + O(2) = protein L-lysine + succinate + formaldehyde + CO(2). CC -!- COFACTOR: Binds 1 Fe(2+) ion per subunit (By similarity). CC -!- SUBCELLULAR LOCATION: Nucleus (By similarity). CC -!- SIMILARITY: Contains 1 JmjC domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK014006; BAB29111.1; -; mRNA. DR EMBL; BC024807; AAH24807.1; -; mRNA. DR RefSeq; NP_084118.1; NM_029842.5. DR UniGene; Mm.307239; -. DR ProteinModelPortal; Q9CXT6; -. DR SMR; Q9CXT6; 177-414. DR STRING; 10090.ENSMUSP00000033010; -. DR PhosphoSite; Q9CXT6; -. DR PRIDE; Q9CXT6; -. DR Ensembl; ENSMUST00000033010; ENSMUSP00000033010; ENSMUSG00000030752. DR GeneID; 77035; -. DR KEGG; mmu:77035; -. DR UCSC; uc009jpz.2; mouse. DR CTD; 79831; -. DR MGI; MGI:1924285; Kdm8. DR eggNOG; NOG71927; -. DR GeneTree; ENSGT00530000062914; -. DR HOVERGEN; HBG105493; -. DR InParanoid; Q9CXT6; -. DR OMA; DYCCLGE; -. DR OrthoDB; EOG7KWSJQ; -. DR TreeFam; TF315056; -. DR NextBio; 346338; -. DR PRO; PR:Q9CXT6; -. DR ArrayExpress; Q9CXT6; -. DR Bgee; Q9CXT6; -. DR CleanEx; MM_JMJD5; -. DR Genevestigator; Q9CXT6; -. DR GO; GO:0005634; C:nucleus; ISS:UniProtKB. DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB. DR GO; GO:0051864; F:histone demethylase activity (H3-K36 specific); ISS:UniProtKB. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; ISS:UniProtKB. DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR InterPro; IPR003347; JmjC_dom. DR SMART; SM00558; JmjC; 1. DR PROSITE; PS51184; JMJC; 1. PE 2: Evidence at transcript level; KW Cell cycle; Chromatin regulator; Complete proteome; Dioxygenase; Iron; KW Metal-binding; Nucleus; Oxidoreductase; Reference proteome; KW Transcription; Transcription regulation. FT CHAIN 1 414 Lysine-specific demethylase 8. FT /FTId=PRO_0000292011. FT DOMAIN 269 414 JmjC. FT METAL 319 319 Iron; catalytic (By similarity). FT METAL 321 321 Iron; catalytic (By similarity). FT METAL 398 398 Iron; catalytic (By similarity). SQ SEQUENCE 414 AA; 47145 MW; 4C794D0F5E9EC996 CRC64; MSEDTTEPLV GSSTLWKELR TLLPDKEEEL KLDLGEKVDR SVAALLRQAV GLFYAGHWQG CLQASEAVLD YSWEKLNTGP WRDVDKEWRR VYSFGCLLKA LCLCQAPQKA TTVVEALRVC DMGLLMGAAI LEDILLKVVA VLQTHQLPGK QPARGPHQDQ PATKKAKCDA SPAPDVMLER MVPRLRCPPL QYFKQHFLVP GRPVILEGVA DHWPCMKKWS LQYIQEIAGC RTVPVEVGSR YTDEDWSQTL MTVDEFIQKF ILSEAKDVGY LAQHQLFDQI PELKRDISIP DYCCLGNGEE EEITINAWFG PQGTISPLHQ DPQQNFLVQV LGRKYIRLYS PQESEAVYPH ETHILHNTSQ VDVENPDLEK FPKFTEAPFL SCILSPGDTL FIPAKYWHYV RSLDLSFSVS FWWS // ID KDM6A_MOUSE Reviewed; 1401 AA. AC O70546; A2AID2; Q6DI80; Q7TSG4; DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot. DT 09-JAN-2007, sequence version 2. DT 19-MAR-2014, entry version 111. DE RecName: Full=Lysine-specific demethylase 6A; DE EC=1.14.11.-; DE AltName: Full=Histone demethylase UTX; DE AltName: Full=Ubiquitously transcribed TPR protein on the X chromosome; DE AltName: Full=Ubiquitously transcribed X chromosome tetratricopeptide repeat protein; GN Name=Kdm6a; Synonyms=Utx; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE RP SEQUENCE [LARGE SCALE MRNA] OF 255-1401 (ISOFORM 1). RC STRAIN=C57BL/6J; TISSUE=Embryonic germ cell, and Limb; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] OF 69-1401 (ISOFORM 1). RC STRAIN=C57BL/6; TISSUE=Embryo; RX PubMed=9499428; DOI=10.1093/hmg/7.4.737; RA Greenfield A., Carrel L., Pennisi D., Phillippe C., Quaderi N., RA Siggers P., Steiner K., Tam P.P.L., Monaco A.P., Willard H.F., RA Koopman P.; RT "The UTX gene escapes X inactivation in mice and humans."; RL Hum. Mol. Genet. 7:737-742(1998). RN [4] RP INTERACTION WITH TLE1. RX PubMed=9854018; DOI=10.1042/0264-6021:3370013; RA Grbavec D., Lo R., Liu Y., Greenfield A., Stifani S.; RT "Groucho/transducin-like enhancer of split (TLE) family members RT interact with the yeast transcriptional co-repressor SSN6 and RT mammalian SSN6-related proteins: implications for evolutionary RT conservation of transcription repression mechanisms."; RL Biochem. J. 337:13-17(1999). RN [5] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic brain; RX PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200; RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.; RT "Phosphoproteomic analysis of the developing mouse brain."; RL Mol. Cell. Proteomics 3:1093-1101(2004). RN [6] RP INTERACTION WITH SUPT6H. RX PubMed=23503590; DOI=10.1038/emboj.2013.54; RA Wang A.H., Zare H., Mousavi K., Wang C., Moravec C.E., Sirotkin H.I., RA Ge K., Gutierrez-Cruz G., Sartorelli V.; RT "The histone chaperone Spt6 coordinates histone H3K27 demethylation RT and myogenesis."; RL EMBO J. 32:1075-1086(2013). CC -!- FUNCTION: Histone demethylase that specifically demethylates 'Lys- CC 27' of histone H3, thereby playing a central role in histone code. CC Demethylates trimethylated and dimethylated but not monomethylated CC H3 'Lys-27'. Plays a central role in regulation of posterior CC development, by regulating HOX gene expression. Demethylation of CC 'Lys-27' of histone H3 is concomitant with methylation of 'Lys-4' CC of histone H3, and regulates the recruitment of the PRC1 complex CC and monoubiquitination of histone H2A (By similarity). CC -!- COFACTOR: Ascorbate (By similarity). CC -!- COFACTOR: Fe(2+) (By similarity). CC -!- SUBUNIT: Component of the MLL2/3 complex (also named ASCOM CC complex), at least composed of KMT2D/MLL2 or KMT2C/MLL3, ASH2L, CC RBBP5, WDR5, NCOA6, DPY30, KDM6A (or KDM6B), PAXIP1/PTIP, PAGR1 CC and alpha- and beta-tubulin (By similarity). Interacts with TLE1. CC Interacts with SUPT6H. CC -!- INTERACTION: CC Q61321:Six4; NbExp=2; IntAct=EBI-1573712, EBI-986524; CC -!- SUBCELLULAR LOCATION: Nucleus (Potential). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=O70546-1; Sequence=Displayed; CC Name=2; CC IsoId=O70546-2; Sequence=VSP_022196; CC -!- TISSUE SPECIFICITY: Expressed in brain, heart and spleen. CC -!- DEVELOPMENTAL STAGE: Widely expressed at E13.5. CC -!- MISCELLANEOUS: Escapes X chromosome inactivation. CC -!- SIMILARITY: Belongs to the UTX family. CC -!- SIMILARITY: Contains 1 JmjC domain. CC -!- SIMILARITY: Contains 8 TPR repeats. CC -!- SEQUENCE CAUTION: CC Sequence=AAH75703.1; Type=Miscellaneous discrepancy; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AL732451; CAM27157.1; -; Genomic_DNA. DR EMBL; AL773547; CAM27157.1; JOINED; Genomic_DNA. DR EMBL; AL773547; CAM18408.1; -; Genomic_DNA. DR EMBL; AL732451; CAM18408.1; JOINED; Genomic_DNA. DR EMBL; BC053433; AAH53433.1; -; mRNA. DR EMBL; BC075703; AAH75703.1; ALT_INIT; mRNA. DR EMBL; AJ002730; CAA05692.1; -; mRNA. DR RefSeq; NP_033509.1; NM_009483.1. DR RefSeq; XP_006527661.1; XM_006527598.1. DR UniGene; Mm.257498; -. DR UniGene; Mm.417709; -. DR ProteinModelPortal; O70546; -. DR SMR; O70546; 110-380, 886-1395. DR BioGrid; 204471; 2. DR IntAct; O70546; 4. DR MINT; MINT-4584348; -. DR PhosphoSite; O70546; -. DR PaxDb; O70546; -. DR PRIDE; O70546; -. DR Ensembl; ENSMUST00000044484; ENSMUSP00000045862; ENSMUSG00000037369. [O70546-1] DR Ensembl; ENSMUST00000052368; ENSMUSP00000061539; ENSMUSG00000037369. [O70546-2] DR GeneID; 22289; -. DR KEGG; mmu:22289; -. DR UCSC; uc009ssk.1; mouse. [O70546-1] DR CTD; 7403; -. DR MGI; MGI:1095419; Kdm6a. DR eggNOG; COG0457; -. DR GeneTree; ENSGT00410000025758; -. DR HOGENOM; HOG000220834; -. DR KO; K11447; -. DR OMA; HHTVDQL; -. DR OrthoDB; EOG7CG6Z5; -. DR TreeFam; TF317405; -. DR NextBio; 302431; -. DR PRO; PR:O70546; -. DR ArrayExpress; O70546; -. DR Bgee; O70546; -. DR Genevestigator; O70546; -. DR GO; GO:0035097; C:histone methyltransferase complex; ISO:MGI. DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW. DR GO; GO:0071558; F:histone demethylase activity (H3-K27 specific); IDA:MGI. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0000978; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding; IDA:MGI. DR GO; GO:0060070; P:canonical Wnt signaling pathway; IMP:MGI. DR GO; GO:0007507; P:heart development; IMP:MGI. DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI. DR GO; GO:0048333; P:mesodermal cell differentiation; IMP:MGI. DR GO; GO:0001843; P:neural tube closure; IMP:MGI. DR GO; GO:0048570; P:notochord morphogenesis; IMP:MGI. DR GO; GO:0003016; P:respiratory system process; IMP:MGI. DR GO; GO:0032525; P:somite rostral/caudal axis specification; IMP:MGI. DR Gene3D; 1.25.40.10; -; 1. DR InterPro; IPR003347; JmjC_dom. DR InterPro; IPR013026; TPR-contain_dom. DR InterPro; IPR011990; TPR-like_helical. DR InterPro; IPR001440; TPR_1. DR InterPro; IPR019734; TPR_repeat. DR Pfam; PF02373; JmjC; 1. DR Pfam; PF00515; TPR_1; 3. DR Pfam; PF13181; TPR_8; 1. DR SMART; SM00558; JmjC; 1. DR SMART; SM00028; TPR; 6. DR PROSITE; PS51184; JMJC; 1. DR PROSITE; PS50005; TPR; 7. DR PROSITE; PS50293; TPR_REGION; 1. PE 1: Evidence at protein level; KW Alternative splicing; Chromatin regulator; Complete proteome; KW Dioxygenase; Iron; Metal-binding; Nucleus; Oxidoreductase; KW Phosphoprotein; Reference proteome; Repeat; TPR repeat; Zinc. FT CHAIN 1 1401 Lysine-specific demethylase 6A. FT /FTId=PRO_0000106410. FT REPEAT 95 128 TPR 1. FT REPEAT 132 165 TPR 2. FT REPEAT 169 203 TPR 3. FT REPEAT 207 240 TPR 4. FT REPEAT 245 285 TPR 5. FT REPEAT 286 319 TPR 6. FT REPEAT 321 353 TPR 7. FT REPEAT 355 387 TPR 8. FT DOMAIN 1095 1258 JmjC. FT REGION 1 1095 Interaction with SUPT6H. FT COMPBIAS 9 19 Poly-Ala. FT COMPBIAS 919 941 Pro-rich. FT METAL 1146 1146 Iron (By similarity). FT METAL 1148 1148 Iron (By similarity). FT METAL 1226 1226 Iron (By similarity). FT METAL 1331 1331 Zinc (By similarity). FT METAL 1334 1334 Zinc (By similarity). FT METAL 1358 1358 Zinc (By similarity). FT METAL 1361 1361 Zinc (By similarity). FT MOD_RES 769 769 Phosphoserine (By similarity). FT MOD_RES 829 829 Phosphoserine (By similarity). FT VAR_SEQ 1393 1401 APPLPSASS -> VSEINMLLHYHPPHLDIVPWTLNMRPFL FT LFRK (in isoform 2). FT /FTId=VSP_022196. FT CONFLICT 321 321 D -> G (in Ref. 2; AAH75703). FT CONFLICT 1198 1198 E -> G (in Ref. 2; AAH75703). SQ SEQUENCE 1401 AA; 154355 MW; 293DA417F49EECFF CRC64; MKSCGVSLAT AAAAAAAAAF GDEEKKMAAG KASGESEEAS PSLTAEEREA LGGLDSRLFG FVRFHEDGAR MKALLGKAVR CYESLILKAE GKVESDFFCQ LGHFNLLLED YPKALSAYQR YYSLQSDYWK NAAFLYGLGL VYFHYNAFQW AIKAFQEVLY VDPSFCRAKE IHLRLGLMFK VNTDYESSLK HFQLALVDCN PCTLSNAEIQ FHIAHLYETQ RKYHSAKEAY EQLLQTENLS AQVKATILQQ LGWMHHTVDL LGDKATKESY AIQYLQKSLE ADPNSGQSWY FLGRCYSSIG KVQDAFISYR QSIDKSEASA DTWCSIGVLY QQQNQPMDAL QAYICAVQLD HGHAAAWMDL GTLYESCNQP QDAIKCYLNA TRSKNCSNTS GLAARIKYLQ AQLCNLPQGS LQNKTKLLPS IEEAWSLPIP AELTSRQGAM NTAQQNTSDN WSGGNAPPPV EQQTHSWCLT PQKLQHLEQL RANRNNLNPA QKLMLEQLES QFVLMQQHQM RQTGVAQVRP TGILNGPTVD SSLPTNSVSG QQPQLPLTRM PSVSQPGVHT ACPRQTLANG PFSAGHVPCS TSRTLGSTDT VLIGNNHVTG SGSNGNVPYL QRNAPTLPHN RTNLTSSTEE PWKNQLSNST QGLHKGPSSH LAGPNGERPL SSTGPSQHLQ AAGSGIQNQN GHPTLPSNSV TQGAALNHLS SHTATSGGQQ GITLTKESKP SGNTLTVPET SRQTGETPNS TASVEGLPNH VHQVMADAVC SPSHGDSKSP GLLSSDNPQL SALLMGKANN NVGPGTCDKV NNIHPTVHTK TDNSVASSPS SAISTATPSP KSTEQTTTNS VTSLNSPHSG LHTINGEGME ESQSPIKTDL LLVSHRPSPQ IIPSMSVSIY PSSAEVLKAC RNLGKNGLSN SSILLDKCPP PRPPSSPYPP LPKDKLNPPT PSIYLENKRD AFFPPLHQFC TNPNNPVTVI RGLAGALKLD LGLFSTKTLV EANNEHMVEV RTQLLQPADE NWDPTGTKKI WHCESNRSHT TIAKYAQYQA SSFQESLREE NEKRSHHKDH SDSESTSSDN SGKRRKGPFK TIKFGTNIDL SDDKKWKLQL HELTKLPAFV RVVSAGNLLS HVGHTILGMN TVQLYMKVPG SRTPGHQENN NFCSVNINIG PGDCEWFVVP EGYWGVLNDF CEKNNLNFLM GSWWPNLEDL YEANVPVYRF IQRPGDLVWI NAGTVHWVQA IGWCNNIAWN VGPLTACQYK LAVERYEWNK LQNVKSIVPM VHLSWNMARN IKVSDPKLFE MIKYCLLRTL KQCQTLREAL IAAGKEIIWH GRTKEEPAHY CSICEVEVFD LLFVTNESNS RKTYIVHCQD CARKTSGNLE NFVVLEQYKM EDLMQVYDQF TLAPPLPSAS S // ID KDSR_MOUSE Reviewed; 332 AA. AC Q6GV12; DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 19-JUL-2004, sequence version 1. DT 19-FEB-2014, entry version 99. DE RecName: Full=3-ketodihydrosphingosine reductase; DE Short=KDS reductase; DE EC=1.1.1.102; DE AltName: Full=3-dehydrosphinganine reductase; DE AltName: Full=Follicular variant translocation protein 1 homolog; DE Short=FVT-1; DE Flags: Precursor; GN Name=Kdsr; Synonyms=Fvt1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION. RX PubMed=15328338; DOI=10.1074/jbc.M405915200; RA Kihara A., Igarashi Y.; RT "FVT-1 is a mammalian 3-ketodihydrosphingosine reductase with an RT active site that faces the cytosolic side of the endoplasmic reticulum RT membrane."; RL J. Biol. Chem. 279:49243-49250(2004). CC -!- FUNCTION: Catalyzes the reduction of 3-ketodihydrosphingosine CC (KDS) to dihydrosphingosine (DHS). CC -!- CATALYTIC ACTIVITY: Sphinganine + NADP(+) = 3-dehydrosphinganine + CC NADPH. CC -!- PATHWAY: Lipid metabolism; sphingolipid metabolism. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass CC membrane protein. CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases CC (SDR) family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AY634684; AAT57900.1; -; mRNA. DR RefSeq; NP_081810.1; NM_027534.2. DR UniGene; Mm.458911; -. DR ProteinModelPortal; Q6GV12; -. DR SMR; Q6GV12; 35-255. DR BioGrid; 214234; 1. DR STRING; 10090.ENSMUSP00000010049; -. DR PhosphoSite; Q6GV12; -. DR PaxDb; Q6GV12; -. DR PRIDE; Q6GV12; -. DR Ensembl; ENSMUST00000010049; ENSMUSP00000010049; ENSMUSG00000009905. DR GeneID; 70750; -. DR KEGG; mmu:70750; -. DR UCSC; uc007cgy.2; mouse. DR CTD; 2531; -. DR MGI; MGI:1918000; Kdsr. DR eggNOG; COG1028; -. DR HOVERGEN; HBG005757; -. DR InParanoid; Q6GV12; -. DR KO; K04708; -. DR OMA; DAVQGNF; -. DR OrthoDB; EOG744T98; -. DR TreeFam; TF105430; -. DR BRENDA; 1.1.1.102; 3474. DR UniPathway; UPA00222; -. DR ChiTaRS; KDSR; mouse. DR NextBio; 332193; -. DR PRO; PR:Q6GV12; -. DR ArrayExpress; Q6GV12; -. DR Bgee; Q6GV12; -. DR CleanEx; MM_KDSR; -. DR Genevestigator; Q6GV12; -. DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0047560; F:3-dehydrosphinganine reductase activity; ISO:MGI. DR GO; GO:0006666; P:3-keto-sphinganine metabolic process; ISO:MGI. DR GO; GO:0030148; P:sphingolipid biosynthetic process; IGI:MGI. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR002198; DH_sc/Rdtase_SDR. DR InterPro; IPR002347; Glc/ribitol_DH. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR020904; Sc_DH/Rdtase_CS. DR Pfam; PF00106; adh_short; 1. DR PIRSF; PIRSF000126; 11-beta-HSD1; 1. DR PRINTS; PR00081; GDHRDH. DR PRINTS; PR00080; SDRFAMILY. DR PROSITE; PS00061; ADH_SHORT; 1. PE 2: Evidence at transcript level; KW Complete proteome; Endoplasmic reticulum; Lipid metabolism; Membrane; KW NADP; Oxidoreductase; Proto-oncogene; Reference proteome; Signal; KW Sphingolipid metabolism; Transmembrane; Transmembrane helix. FT SIGNAL 1 25 Potential. FT CHAIN 26 332 3-ketodihydrosphingosine reductase. FT /FTId=PRO_0000031983. FT TOPO_DOM 26 270 Cytoplasmic (Potential). FT TRANSMEM 271 291 Helical; (Potential). FT TOPO_DOM 292 293 Lumenal (Potential). FT TRANSMEM 294 314 Helical; (Potential). FT TOPO_DOM 315 332 Cytoplasmic (Potential). FT NP_BIND 36 60 NADP (Probable). FT ACT_SITE 186 186 Proton acceptor (By similarity). FT ACT_SITE 190 190 Probable. FT BINDING 173 173 Substrate (By similarity). SQ SEQUENCE 332 AA; 35956 MW; FBB23BD1C3A3906D CRC64; MLLLAAAGLV AFVLLLYMVS PLISPKPLAL PGAHVVVTGG SSGIGKCIAI ECYKQGAFIT LVARNEDKLL QAKKDIEKHS INDKQVVLCI SVDVSQDYNQ VENVIKQAQE KLGPVDMLVN CAGTSMSGKF EELEVSSFEK LMSINYLGSV YPSRAVITTM KERRVGRIVF VSSQAGQLGL FGFTAYSSSK FAIRGLAEAL QMEVKPYNVY VTVAYPPDTD TPGLAEENKT KPLETRLISE TTAICKPEQV AKQIVKDAIQ GNFNSSIGSD GYMLSSLTCG MAPVTSITEG LQQVVTMGLF RTIALFYLGS FDNIVRRCMV QKAKPEVVDK TA // ID KMO_MOUSE Reviewed; 479 AA. AC Q91WN4; DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 19-MAR-2014, entry version 95. DE RecName: Full=Kynurenine 3-monooxygenase; DE EC=1.14.13.9; DE AltName: Full=Kynurenine 3-hydroxylase; GN Name=Kmo; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC STRAIN=FVB/N; TISSUE=Liver; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: Catalyzes the hydroxylation of L-kynurenine (L-Kyn) to CC form 3-hydroxy-L-kynurenine (L-3OHKyn). Required for synthesis of CC quinolinic acid, a neurotoxic NMDA receptor antagonist and CC potential endogenous inhibitor of NMDA receptor signaling in CC axonal targeting, synaptogenesis and apoptosis during brain CC development. Quinolinic acid may also affect NMDA receptor CC signaling in pancreatic beta cells, osteoblasts, myocardial cells, CC and the gastrointestinal tract (By similarity). CC -!- CATALYTIC ACTIVITY: L-kynurenine + NADPH + O(2) = 3-hydroxy-L- CC kynurenine + NADP(+) + H(2)O. CC -!- COFACTOR: FAD (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate CC from L-kynurenine: step 1/3. CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane; Multi-pass CC membrane protein (By similarity). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q91WN4-1; Sequence=Displayed; CC Name=2; CC IsoId=Q91WN4-2; Sequence=VSP_051974; CC Note=No experimental confirmation available; CC -!- SIMILARITY: Belongs to the aromatic-ring hydroxylase family. KMO CC subfamily. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK129011; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; BC014683; AAH14683.1; -; mRNA. DR RefSeq; NP_598570.1; NM_133809.1. DR UniGene; Mm.27217; -. DR ProteinModelPortal; Q91WN4; -. DR SMR; Q91WN4; 7-367. DR PhosphoSite; Q91WN4; -. DR PaxDb; Q91WN4; -. DR PRIDE; Q91WN4; -. DR Ensembl; ENSMUST00000040250; ENSMUSP00000038914; ENSMUSG00000039783. [Q91WN4-1] DR Ensembl; ENSMUST00000097458; ENSMUSP00000095067; ENSMUSG00000039783. [Q91WN4-2] DR GeneID; 98256; -. DR KEGG; mmu:98256; -. DR UCSC; uc007dto.1; mouse. [Q91WN4-1] DR UCSC; uc011wxd.1; mouse. [Q91WN4-2] DR CTD; 8564; -. DR MGI; MGI:2138151; Kmo. DR eggNOG; COG0654; -. DR GeneTree; ENSGT00390000000747; -. DR HOGENOM; HOG000251788; -. DR HOVERGEN; HBG057213; -. DR InParanoid; Q91WN4; -. DR KO; K00486; -. DR OMA; QPMISVK; -. DR TreeFam; TF312990; -. DR UniPathway; UPA00253; UER00328. DR NextBio; 353386; -. DR PRO; PR:Q91WN4; -. DR ArrayExpress; Q91WN4; -. DR Bgee; Q91WN4; -. DR Genevestigator; Q91WN4; -. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:MGI. DR GO; GO:0005741; C:mitochondrial outer membrane; ISS:UniProtKB. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:Ensembl. DR GO; GO:0004502; F:kynurenine 3-monooxygenase activity; ISS:UniProtKB. DR GO; GO:0016174; F:NAD(P)H oxidase activity; IEA:Ensembl. DR GO; GO:0009435; P:NAD biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0019674; P:NAD metabolic process; ISS:UniProtKB. DR GO; GO:0019805; P:quinolinate biosynthetic process; IEA:InterPro. DR GO; GO:0009651; P:response to salt stress; IEA:Ensembl. DR GO; GO:0019441; P:tryptophan catabolic process to kynurenine; IEA:Ensembl. DR HAMAP; MF_01971; Kynurenine_monooxygenase; 1. DR InterPro; IPR027545; Kynurenine_monooxygenase. DR InterPro; IPR002938; mOase_FAD-bd. DR InterPro; IPR003042; Rng_hydrolase-like. DR Pfam; PF01494; FAD_binding_3; 1. DR PRINTS; PR00420; RNGMNOXGNASE. PE 2: Evidence at transcript level; KW Alternative splicing; Complete proteome; FAD; Flavoprotein; Membrane; KW Mitochondrion; Mitochondrion outer membrane; Monooxygenase; NADP; KW Oxidoreductase; Pyridine nucleotide biosynthesis; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 479 Kynurenine 3-monooxygenase. FT /FTId=PRO_0000229743. FT TRANSMEM 385 404 Helical; (Potential). FT TRANSMEM 425 445 Helical; (Potential). FT VAR_SEQ 367 400 Missing (in isoform 2). FT /FTId=VSP_051974. SQ SEQUENCE 479 AA; 54532 MW; E880997DBC9C8163 CRC64; MASSDTQGKR VAVIGGGLVG ALNACFLAKR NFQVDVYEAR EDIRVAKSAR GRSINLALSY RGRQALKAIG LEDQIVSKGV PMKARMIHSL SGKKSAIPYG NKSQYILSIS RENLNKDLLT AVESYANAKV HFGHKLSKCI PEEGVLTVLG PDKVPRDVTC DLVVGCDGAY STVRAHLMKK PRFDYTQQYI PHGYMELTIP PKNGEYAMEP NCLHIWPRNA YMMIALPNMD KSFTCTLFMP FEEFERLPTR SDVLDFFQKN FPDAIPLMGE QALMRDFFLL PAQPMISVKC SPFHLKSHCV LMGDAAHAIV PFFGQGMNAG FEDCLVFDEL MDKFNNNLSM CLPEFSRFRI PDDHAISDLS MYNYIEMRAH VNSRWFLFQK LLDKFLHAIM PSTFIPLYTM VAFTRIRYHE AVLRWHWQKK VINRGLFVLG SLIAIGGTYL LVHHLSLRPL EFLRRPAWMG TTGYWTRSTD ISLQVPWSY // ID L2HDH_MOUSE Reviewed; 464 AA. AC Q91YP0; Q3TH61; Q3U7Z0; Q3ULY6; DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 19-MAR-2014, entry version 92. DE RecName: Full=L-2-hydroxyglutarate dehydrogenase, mitochondrial; DE EC=1.1.99.2; DE AltName: Full=Duranin; DE Flags: Precursor; GN Name=L2hgdh; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Amnion, Bone marrow, and Mammary gland; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Mammary tumor; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-105 AND LYS-174, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23576753; DOI=10.1073/pnas.1302961110; RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., RA Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.; RT "Label-free quantitative proteomics of the lysine acetylome in RT mitochondria identifies substrates of SIRT3 in metabolic pathways."; RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013). CC -!- CATALYTIC ACTIVITY: (S)-2-hydroxyglutarate + acceptor = 2- CC oxoglutarate + reduced acceptor. CC -!- COFACTOR: FAD (By similarity). CC -!- SUBCELLULAR LOCATION: Mitochondrion (By similarity). CC -!- SIMILARITY: Belongs to the L2HGDH family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK145228; BAE26312.1; -; mRNA. DR EMBL; AK152450; BAE31229.1; -; mRNA. DR EMBL; AK168429; BAE40337.1; -; mRNA. DR EMBL; BC016226; AAH16226.1; -; mRNA. DR RefSeq; NP_663418.1; NM_145443.2. DR UniGene; Mm.103362; -. DR ProteinModelPortal; Q91YP0; -. DR SMR; Q91YP0; 48-459. DR PhosphoSite; Q91YP0; -. DR PaxDb; Q91YP0; -. DR PRIDE; Q91YP0; -. DR Ensembl; ENSMUST00000021370; ENSMUSP00000021370; ENSMUSG00000020988. DR GeneID; 217666; -. DR KEGG; mmu:217666; -. DR UCSC; uc011ynb.1; mouse. DR CTD; 79944; -. DR MGI; MGI:2384968; L2hgdh. DR eggNOG; COG0579; -. DR GeneTree; ENSGT00490000043421; -. DR HOGENOM; HOG000245180; -. DR HOVERGEN; HBG081883; -. DR InParanoid; Q91YP0; -. DR KO; K00109; -. DR OMA; GVHFTRM; -. DR OrthoDB; EOG7MPRDR; -. DR TreeFam; TF105922; -. DR NextBio; 375942; -. DR PRO; PR:Q91YP0; -. DR Bgee; Q91YP0; -. DR CleanEx; MM_L2HGDH; -. DR Genevestigator; Q91YP0; -. DR GO; GO:0016021; C:integral component of membrane; ISS:HGNC. DR GO; GO:0005739; C:mitochondrion; ISS:HGNC. DR GO; GO:0047545; F:2-hydroxyglutarate dehydrogenase activity; ISS:HGNC. DR GO; GO:0044267; P:cellular protein metabolic process; ISS:HGNC. DR InterPro; IPR006076; FAD-dep_OxRdtase. DR Pfam; PF01266; DAO; 1. PE 1: Evidence at protein level; KW Acetylation; Complete proteome; FAD; Flavoprotein; Mitochondrion; KW Oxidoreductase; Reference proteome; Transit peptide. FT TRANSIT 1 52 Mitochondrion (Potential). FT CHAIN 53 464 L-2-hydroxyglutarate dehydrogenase, FT mitochondrial. FT /FTId=PRO_0000228130. FT MOD_RES 105 105 N6-acetyllysine. FT MOD_RES 174 174 N6-acetyllysine. FT CONFLICT 184 184 M -> I (in Ref. 1; BAE31229). FT CONFLICT 216 216 R -> K (in Ref. 1; BAE26312). FT CONFLICT 225 225 I -> V (in Ref. 1; BAE26312). FT CONFLICT 228 228 E -> G (in Ref. 1; BAE31229). FT CONFLICT 416 416 L -> P (in Ref. 1; BAE40337). SQ SEQUENCE 464 AA; 50899 MW; 27270B28FCCC3762 CRC64; MWPTLRYVGG VCGLARYCVA GGFLRASGPA SGVPGLLCGG GRRSSSTSSF DIVIVGGGIV GLASARTLIL KHPGLSIGVV EKEKDLALHQ TGHNSGVIHS GIYYKPESLK AKLCVEGAAL IYEYCNLKGI PYRQCGKLIV AVEQEEIPRL QALYERGLQN GVEGLRLIQQ EDIKKKEPYC RGLMAIDCPY TGIVNYQQVA LSFAQDFQEA GGSILRDFEV KGIEIAKENS SRSKDGMNYP IAVKNSKGKE IRCRYVVTCA GLYSDRISEL SGCNPDPQIV PFRGDYLVLK PEKGYLVKGN IYPVPDSRFP FLGVHFTPRL DGTIWLGPNA VLAFKREGYR PFDFDARDVM EVILKSGFIN LVFQHFSYGV NEMYKACFLS ETVKHLQKFI PEITISDVLR GPAGVRAQAL DRDGNLVEDF VFDGGTGEIA DRVLHVRNAP SPAATSSLAI SRMIAEEAQQ RFKL // ID LDHA_MOUSE Reviewed; 332 AA. AC P06151; DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 19-MAR-2014, entry version 144. DE RecName: Full=L-lactate dehydrogenase A chain; DE Short=LDH-A; DE EC=1.1.1.27; DE AltName: Full=LDH muscle subunit; DE Short=LDH-M; GN Name=Ldha; Synonyms=Ldh-1, Ldh1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=C57BL/10; TISSUE=Liver; RX PubMed=3036647; RA Fukasawa K.M., Li S.S.-L.; RT "Complete nucleotide sequence of the mouse lactate dehydrogenase-A RT functional gene: comparison of the exon-intron organization of RT dehydrogenase genes."; RL Genetics 116:99-105(1987). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=3996406; DOI=10.1111/j.1432-1033.1985.tb08914.x; RA Li S.S.-L., Tiano H.F., Fukasawa K.M., Yagi K., Shimizu M., RA Sharief F.S., Nakashima Y., Pan Y.E.; RT "Protein structure and gene organization of mouse lactate RT dehydrogenase-A isozyme."; RL Eur. J. Biochem. 149:215-225(1985). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=DBA/2J; RA Hiraoka Y., Li S.S.-L.; RT "Lactate dehydrogenase-A mRNAs in mouse testis and somatic tissues RT containing different 5' noncoding sequences."; RL J. Genet. Mol. Biol. 1:1-6(1990). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-42. RX PubMed=3017306; RA Fukasawa K.M., Li S.S.-L.; RT "Nucleotide sequence of the putative regulatory region of mouse RT lactate dehydrogenase-A gene."; RL Biochem. J. 235:435-439(1986). RN [5] RP PROTEIN SEQUENCE OF 6-14; 23-73; 82-99; 107-126; 133-149; 158-169; RP 172-177; 213-228; 233-243; 246-265; 269-315 AND 319-328, AND MASS RP SPECTROMETRY. RC STRAIN=C57BL/6, and OF1; TISSUE=Brain, and Hippocampus; RA Lubec G., Kang S.U., Klug S., Yang J.W., Zigmond M., Sunyer B., RA Chen W.-Q.; RL Submitted (JAN-2009) to UniProtKB. RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] OF 202-332. RX PubMed=2993055; DOI=10.1016/0020-711X(85)90298-8; RA Akai K., Yagi K., Tiano H.F., Pan Y.-C.E., Shimizu M., Fong K., RA Jungmann R.A., Li S.S.-L.; RT "Isolation and characterization of a cDNA and a pseudogene for mouse RT lactate dehydrogenase-A isozyme."; RL Int. J. Biochem. 17:645-648(1985). RN [7] RP ISGYLATION. RX PubMed=16139798; DOI=10.1016/j.bbrc.2005.08.132; RA Giannakopoulos N.V., Luo J.K., Papov V., Zou W., Lenschow D.J., RA Jacobs B.S., Borden E.C., Li J., Virgin H.W., Zhang D.E.; RT "Proteomic identification of proteins conjugated to ISG15 in mouse and RT human cells."; RL Biochem. Biophys. Res. Commun. 336:496-506(2005). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-239, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Mast cell; RX PubMed=17947660; RA Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., RA Kawakami T., Salomon A.R.; RT "Quantitative time-resolved phosphoproteomic analysis of mast cell RT signaling."; RL J. Immunol. 179:5864-5876(2007). RN [9] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2; LYS-5; LYS-81; LYS-118; RP LYS-126; LYS-224; LYS-232; LYS-243 AND LYS-318, SUCCINYLATION [LARGE RP SCALE ANALYSIS] AT LYS-5; LYS-118 AND LYS-318, IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS], AND CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic fibroblast, and Liver; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., RA Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). CC -!- CATALYTIC ACTIVITY: (S)-lactate + NAD(+) = pyruvate + NADH. CC -!- PATHWAY: Fermentation; pyruvate fermentation to lactate; (S)- CC lactate from pyruvate: step 1/1. CC -!- SUBUNIT: Homotetramer. CC -!- INTERACTION: CC Q60668:Hnrnpd; NbExp=2; IntAct=EBI-444940, EBI-299932; CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- PTM: ISGylated. CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily. LDH family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; Y00309; CAA68410.1; -; Genomic_DNA. DR EMBL; X02520; CAA26360.1; -; Genomic_DNA. DR EMBL; X02521; CAA26360.1; JOINED; Genomic_DNA. DR EMBL; X02522; CAA26360.1; JOINED; Genomic_DNA. DR EMBL; X02523; CAA26360.1; JOINED; Genomic_DNA. DR EMBL; X02524; CAA26360.1; JOINED; Genomic_DNA. DR EMBL; X02525; CAA26360.1; JOINED; Genomic_DNA. DR EMBL; X02526; CAA26360.1; JOINED; Genomic_DNA. DR EMBL; U13687; AAA21466.1; -; mRNA. DR EMBL; X03753; CAA27387.1; -; Genomic_DNA. DR EMBL; M17516; AAA39424.1; -; mRNA. DR PIR; A25205; DEMSLM. DR PIR; I48240; I48240. DR RefSeq; NP_034829.1; NM_010699.2. DR UniGene; Mm.29324; -. DR ProteinModelPortal; P06151; -. DR SMR; P06151; 4-332. DR BioGrid; 201127; 5. DR IntAct; P06151; 13. DR MINT; MINT-1612559; -. DR PhosphoSite; P06151; -. DR REPRODUCTION-2DPAGE; P06151; -. DR SWISS-2DPAGE; P06151; -. DR UCD-2DPAGE; P06151; -. DR PaxDb; P06151; -. DR PRIDE; P06151; -. DR Ensembl; ENSMUST00000048209; ENSMUSP00000036386; ENSMUSG00000063229. DR GeneID; 16828; -. DR KEGG; mmu:16828; -. DR UCSC; uc009gzm.2; mouse. DR CTD; 3939; -. DR MGI; MGI:96759; Ldha. DR eggNOG; COG0039; -. DR HOGENOM; HOG000213793; -. DR HOVERGEN; HBG000462; -. DR InParanoid; P06151; -. DR KO; K00016; -. DR UniPathway; UPA00554; UER00611. DR ChiTaRS; LDHA; mouse. DR NextBio; 290734; -. DR PRO; PR:P06151; -. DR ArrayExpress; P06151; -. DR Bgee; P06151; -. DR CleanEx; MM_LDHA; -. DR Genevestigator; P06151; -. DR GO; GO:0005829; C:cytosol; IDA:MGI. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR GO; GO:0035686; C:sperm fibrous sheath; IDA:MGI. DR GO; GO:0004459; F:L-lactate dehydrogenase activity; IDA:MGI. DR GO; GO:0044262; P:cellular carbohydrate metabolic process; IEA:InterPro. DR GO; GO:0031668; P:cellular response to extracellular stimulus; IDA:MGI. DR GO; GO:0006096; P:glycolysis; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.720; -; 1. DR Gene3D; 3.90.110.10; -; 1. DR HAMAP; MF_00488; Lactate_dehydrog; 1. DR InterPro; IPR001557; L-lactate/malate_DH. DR InterPro; IPR011304; L-lactate_DH. DR InterPro; IPR018177; L-lactate_DH_AS. DR InterPro; IPR022383; Lactate/malate_DH_C. DR InterPro; IPR001236; Lactate/malate_DH_N. DR InterPro; IPR015955; Lactate_DH/Glyco_Ohase_4_C. DR InterPro; IPR016040; NAD(P)-bd_dom. DR PANTHER; PTHR11540; PTHR11540; 1. DR Pfam; PF02866; Ldh_1_C; 1. DR Pfam; PF00056; Ldh_1_N; 1. DR PIRSF; PIRSF000102; Lac_mal_DH; 1. DR PRINTS; PR00086; LLDHDRGNASE. DR SUPFAM; SSF56327; SSF56327; 1. DR TIGRFAMs; TIGR01771; L-LDH-NAD; 1. DR PROSITE; PS00064; L_LDH; 1. PE 1: Evidence at protein level; KW Acetylation; Complete proteome; Cytoplasm; Direct protein sequencing; KW Glycolysis; NAD; Oxidoreductase; Phosphoprotein; Reference proteome; KW Ubl conjugation. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 332 L-lactate dehydrogenase A chain. FT /FTId=PRO_0000168414. FT NP_BIND 29 57 NAD (By similarity). FT ACT_SITE 193 193 Proton acceptor (By similarity). FT BINDING 99 99 NAD (By similarity). FT BINDING 106 106 Substrate (By similarity). FT BINDING 138 138 NAD or substrate (By similarity). FT BINDING 169 169 Substrate (By similarity). FT BINDING 248 248 Substrate (By similarity). FT MOD_RES 2 2 N-acetylalanine. FT MOD_RES 5 5 N6-acetyllysine; alternate. FT MOD_RES 5 5 N6-succinyllysine; alternate. FT MOD_RES 14 14 N6-acetyllysine (By similarity). FT MOD_RES 57 57 N6-acetyllysine (By similarity). FT MOD_RES 81 81 N6-acetyllysine. FT MOD_RES 118 118 N6-acetyllysine; alternate. FT MOD_RES 118 118 N6-succinyllysine; alternate. FT MOD_RES 126 126 N6-acetyllysine. FT MOD_RES 224 224 N6-acetyllysine. FT MOD_RES 232 232 N6-acetyllysine. FT MOD_RES 239 239 Phosphotyrosine. FT MOD_RES 243 243 N6-acetyllysine. FT MOD_RES 318 318 N6-acetyllysine; alternate. FT MOD_RES 318 318 N6-succinyllysine; alternate. FT CONFLICT 11 11 N -> I (in Ref. 2). SQ SEQUENCE 332 AA; 36499 MW; 5AEB41E1E0B95100 CRC64; MATLKDQLIV NLLKEEQAPQ NKITVVGVGA VGMACAISIL MKDLADELAL VDVMEDKLKG EMMDLQHGSL FLKTPKIVSS KDYCVTANSK LVIITAGARQ QEGESRLNLV QRNVNIFKFI IPNIVKYSPH CKLLIVSNPV DILTYVAWKI SGFPKNRVIG SGCNLDSARF RYLMGERLGV HALSCHGWVL GEHGDSSVPV WSGVNVAGVS LKSLNPELGT DADKEQWKEV HKQVVDSAYE VIKLKGYTSW AIGLSVADLA ESIMKNLRRV HPISTMIKGL YGINEDVFLS VPCILGQNGI SDVVKVTLTP EEEARLKKSA DTLWGIQKEL QF // ID LDHB_MOUSE Reviewed; 334 AA. AC P16125; Q545Y4; DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 19-MAR-2014, entry version 131. DE RecName: Full=L-lactate dehydrogenase B chain; DE Short=LDH-B; DE EC=1.1.1.27; DE AltName: Full=LDH heart subunit; DE Short=LDH-H; GN Name=Ldhb; Synonyms=Ldh-2, Ldh2; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=2338075; DOI=10.1111/j.1432-1033.1990.tb15479.x; RA Hiraoka B.Y., Sharief F.S., Yang Y.W., Li W.H., Li S.S.-L.; RT "The cDNA and protein sequences of mouse lactate dehydrogenase B. RT Molecular evolution of vertebrate lactate dehydrogenase genes A RT (muscle), B (heart) and C (testis)."; RL Eur. J. Biochem. 189:215-220(1990). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Cerebellum, Head, and Kidney; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6; TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP PROTEIN SEQUENCE OF 24-77; 120-127; 159-170 AND 271-299, AND MASS RP SPECTROMETRY. RC STRAIN=C57BL/6; TISSUE=Brain, and Hippocampus; RA Lubec G., Klug S., Kang S.U.; RL Submitted (APR-2007) to UniProtKB. RN [5] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-240, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain; RX PubMed=18034455; DOI=10.1021/pr0701254; RA Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.; RT "Large-scale identification and evolution indexing of tyrosine RT phosphorylation sites from murine brain."; RL J. Proteome Res. 7:311-318(2008). CC -!- CATALYTIC ACTIVITY: (S)-lactate + NAD(+) = pyruvate + NADH. CC -!- PATHWAY: Fermentation; pyruvate fermentation to lactate; (S)- CC lactate from pyruvate: step 1/1. CC -!- SUBUNIT: Homotetramer. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily. LDH family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X51905; CAA36185.1; -; mRNA. DR EMBL; AK002257; BAB21970.1; -; mRNA. DR EMBL; AK019391; BAB31697.1; -; mRNA. DR EMBL; AK131637; BAE20732.1; -; mRNA. DR EMBL; BC046755; AAH46755.1; -; mRNA. DR PIR; S09954; S09954. DR RefSeq; NP_032518.1; NM_008492.2. DR UniGene; Mm.9745; -. DR ProteinModelPortal; P16125; -. DR SMR; P16125; 2-333. DR BioGrid; 201130; 2. DR IntAct; P16125; 6. DR MINT; MINT-4100306; -. DR PhosphoSite; P16125; -. DR REPRODUCTION-2DPAGE; P16125; -. DR REPRODUCTION-2DPAGE; Q545Y4; -. DR UCD-2DPAGE; P16125; -. DR PaxDb; P16125; -. DR PRIDE; P16125; -. DR Ensembl; ENSMUST00000032373; ENSMUSP00000032373; ENSMUSG00000030246. DR GeneID; 16832; -. DR KEGG; mmu:16832; -. DR UCSC; uc009epj.1; mouse. DR CTD; 3945; -. DR MGI; MGI:96763; Ldhb. DR eggNOG; COG0039; -. DR GeneTree; ENSGT00550000074541; -. DR HOGENOM; HOG000213793; -. DR HOVERGEN; HBG000462; -. DR InParanoid; P16125; -. DR KO; K00016; -. DR OMA; SFNGWIL; -. DR OrthoDB; EOG7X0VH3; -. DR TreeFam; TF314963; -. DR UniPathway; UPA00554; UER00611. DR NextBio; 290742; -. DR PRO; PR:P16125; -. DR ArrayExpress; P16125; -. DR Bgee; P16125; -. DR CleanEx; MM_LDHB; -. DR Genevestigator; P16125; -. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR GO; GO:0004459; F:L-lactate dehydrogenase activity; IDA:MGI. DR GO; GO:0051287; F:NAD binding; IEA:Ensembl. DR GO; GO:0044262; P:cellular carbohydrate metabolic process; IEA:InterPro. DR GO; GO:0006096; P:glycolysis; IEA:UniProtKB-KW. DR GO; GO:0006089; P:lactate metabolic process; IEA:Ensembl. DR GO; GO:0019674; P:NAD metabolic process; IEA:Ensembl. DR Gene3D; 3.40.50.720; -; 1. DR Gene3D; 3.90.110.10; -; 1. DR HAMAP; MF_00488; Lactate_dehydrog; 1. DR InterPro; IPR001557; L-lactate/malate_DH. DR InterPro; IPR011304; L-lactate_DH. DR InterPro; IPR018177; L-lactate_DH_AS. DR InterPro; IPR022383; Lactate/malate_DH_C. DR InterPro; IPR001236; Lactate/malate_DH_N. DR InterPro; IPR015955; Lactate_DH/Glyco_Ohase_4_C. DR InterPro; IPR016040; NAD(P)-bd_dom. DR PANTHER; PTHR11540; PTHR11540; 1. DR Pfam; PF02866; Ldh_1_C; 1. DR Pfam; PF00056; Ldh_1_N; 1. DR PIRSF; PIRSF000102; Lac_mal_DH; 1. DR PRINTS; PR00086; LLDHDRGNASE. DR SUPFAM; SSF56327; SSF56327; 1. DR TIGRFAMs; TIGR01771; L-LDH-NAD; 1. DR PROSITE; PS00064; L_LDH; 1. PE 1: Evidence at protein level; KW Acetylation; Complete proteome; Cytoplasm; Direct protein sequencing; KW Glycolysis; NAD; Oxidoreductase; Phosphoprotein; Reference proteome. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 334 L-lactate dehydrogenase B chain. FT /FTId=PRO_0000168461. FT NP_BIND 30 58 NAD (By similarity). FT ACT_SITE 194 194 Proton acceptor (By similarity). FT BINDING 100 100 NAD (By similarity). FT BINDING 107 107 Substrate (By similarity). FT BINDING 139 139 NAD or substrate (By similarity). FT BINDING 170 170 Substrate (By similarity). FT BINDING 249 249 Substrate (By similarity). FT MOD_RES 2 2 N-acetylalanine (By similarity). FT MOD_RES 7 7 N6-acetyllysine (By similarity). FT MOD_RES 44 44 Phosphoserine (By similarity). FT MOD_RES 58 58 N6-acetyllysine (By similarity). FT MOD_RES 119 119 N6-acetyllysine (By similarity). FT MOD_RES 240 240 Phosphotyrosine. FT MOD_RES 329 329 N6-acetyllysine (By similarity). SQ SEQUENCE 334 AA; 36572 MW; 86E6CDCDD251285D CRC64; MATLKEKLIA SVADDEAAVP NNKITVVGVG QVGMACAISI LGKSLADELA LVDVLEDKLK GEMMDLQHGS LFLQTPKIVA DKDYSVTANS KIVVVTAGVR QQEGESRLNL VQRNVNVFKF IIPQIVKYSP DCTIIVVSNP VDILTYVTWK LSGLPKHRVI GSGCNLDSAR FRYLMAEKLG IHPSSCHGWI LGEHGDSSVA VWSGVNVAGV SLQELNPEMG TDNDSENWKE VHKMVVDSAY EVIKLKGYTN WAIGLSVADL IESMLKNLSR IHPVSTMVKG MYGIENEVFL SLPCILNARG LTSVINQKLK DDEVAQLRKS ADTLWDIQKD LKDL // ID LDHC_MOUSE Reviewed; 332 AA. AC P00342; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 19-MAR-2014, entry version 140. DE RecName: Full=L-lactate dehydrogenase C chain; DE Short=LDH-C; DE EC=1.1.1.27; DE AltName: Full=LDH testis subunit; DE AltName: Full=LDH-X; GN Name=Ldhc; Synonyms=Ldh-3, Ldh3; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=DBA/2J; TISSUE=Testis; RX PubMed=2439071; RA Sakai I., Sharief F.S., Li S.S.-L.; RT "Molecular cloning and nucleotide sequence of the cDNA for sperm- RT specific lactate dehydrogenase-C from mouse."; RL Biochem. J. 242:619-622(1987). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=3619944; DOI=10.1016/0006-291X(87)90741-8; RA Wu K.C., Chan K., Lee C.-Y.G., Lau Y.-F.C.; RT "Molecular isolation and sequence determination of the cDNA for the RT mouse sperm-specific lactate dehydrogenase-X gene."; RL Biochem. Biophys. Res. Commun. 146:964-970(1987). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Testis; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP PRELIMINARY PROTEIN SEQUENCE OF 2-332. RX PubMed=468774; RA Musick W.D., Rossmann M.G.; RT "The tentative amino acid sequencing of lactate dehydrogenase C4 by X- RT ray diffraction analysis."; RL J. Biol. Chem. 254:7621-7623(1979). RN [5] RP PRELIMINARY PROTEIN SEQUENCE OF 2-332. RX PubMed=7429427; RA Pan Y.-C.E., Huang S., Marciniszyn J.P. Jr., Lee C.-Y., Li S.S.-L.; RT "The preliminary amino acid sequence of mouse testicular lactate RT dehydrogenase."; RL Hoppe-Seyler's Z. Physiol. Chem. 361:795-799(1980). RN [6] RP PROTEIN SEQUENCE OF 2-332. RX PubMed=6343385; RA Pan Y.-C.E., Sharief F.S., Okabe M., Huang S., Li S.S.-L.; RT "Amino acid sequence studies on lactate dehydrogenase C4 isozymes from RT mouse and rat testes."; RL J. Biol. Chem. 258:7005-7016(1983). RN [7] RP NUCLEOTIDE SEQUENCE [MRNA] OF 194-332. RX PubMed=3754749; DOI=10.1016/0006-291X(86)90504-8; RA Tanaka S., Fujimoto H.; RT "A postmeiotically expressed clone encodes lactate dehydrogenase RT isozyme X."; RL Biochem. Biophys. Res. Commun. 136:760-766(1986). RN [8] RP INTERACTION WITH RABL2, AND TISSUE SPECIFICITY. RX PubMed=23055941; DOI=10.1371/journal.pgen.1002969; RA Lo J.C., Jamsai D., O'Connor A.E., Borg C., Clark B.J., RA Whisstock J.C., Field M.C., Adams V., Ishikawa T., Aitken R.J., RA Whittle B., Goodnow C.C., Ormandy C.J., O'Bryan M.K.; RT "RAB-like 2 has an essential role in male fertility, sperm intra- RT flagellar transport, and tail assembly."; RL PLoS Genet. 8:E1002969-E1002969(2012). RN [9] RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS). RX PubMed=468772; RA Musick W.D.L., Rossmann M.G.; RT "The structure of mouse testicular lactate dehydrogenase isoenzyme C4 RT at 2.9-A resolution."; RL J. Biol. Chem. 254:7611-7620(1979). CC -!- FUNCTION: Possible role in sperm motility (By similarity). CC -!- CATALYTIC ACTIVITY: (S)-lactate + NAD(+) = pyruvate + NADH. CC -!- PATHWAY: Fermentation; pyruvate fermentation to lactate; (S)- CC lactate from pyruvate: step 1/1. CC -!- SUBUNIT: Homotetramer. Interacts with RABL2/RABL2A; binds CC preferentially to GTP-bound RABL2. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- TISSUE SPECIFICITY: Expressed within the midpiece of sperm tail CC (at protein level). CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily. LDH family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X04752; CAA28449.1; -; mRNA. DR EMBL; M17587; AAA39425.1; -; mRNA. DR EMBL; BC049602; AAH49602.1; -; mRNA. DR EMBL; M12781; AAA88315.1; -; mRNA. DR PIR; A26824; DEMSLC. DR RefSeq; NP_038608.1; NM_013580.4. DR RefSeq; XP_006540742.1; XM_006540679.1. DR RefSeq; XP_006540743.1; XM_006540680.1. DR RefSeq; XP_006540744.1; XM_006540681.1. DR UniGene; Mm.16563; -. DR PDB; 2LDX; X-ray; 2.96 A; A/B/C/D=2-328. DR PDBsum; 2LDX; -. DR ProteinModelPortal; P00342; -. DR SMR; P00342; 2-332. DR IntAct; P00342; 2. DR MINT; MINT-6611882; -. DR PhosphoSite; P00342; -. DR REPRODUCTION-2DPAGE; P00342; -. DR PaxDb; P00342; -. DR PRIDE; P00342; -. DR Ensembl; ENSMUST00000014545; ENSMUSP00000014545; ENSMUSG00000030851. DR GeneID; 16833; -. DR KEGG; mmu:16833; -. DR UCSC; uc009gzp.1; mouse. DR CTD; 3948; -. DR MGI; MGI:96764; Ldhc. DR eggNOG; COG0039; -. DR HOGENOM; HOG000213793; -. DR HOVERGEN; HBG000462; -. DR InParanoid; P00342; -. DR KO; K00016; -. DR OMA; NVGSHIA; -. DR OrthoDB; EOG7X0VH3; -. DR TreeFam; TF314963; -. DR UniPathway; UPA00554; UER00611. DR ChiTaRS; LDHC; mouse. DR EvolutionaryTrace; P00342; -. DR NextBio; 290746; -. DR PRO; PR:P00342; -. DR ArrayExpress; P00342; -. DR Bgee; P00342; -. DR CleanEx; MM_LDHC; -. DR Genevestigator; P00342; -. DR GO; GO:0005737; C:cytoplasm; IDA:MGI. DR GO; GO:0031514; C:motile cilium; IDA:MGI. DR GO; GO:0004459; F:L-lactate dehydrogenase activity; IMP:MGI. DR GO; GO:0006754; P:ATP biosynthetic process; IMP:MGI. DR GO; GO:0044262; P:cellular carbohydrate metabolic process; IEA:InterPro. DR GO; GO:0006096; P:glycolysis; IEA:UniProtKB-KW. DR GO; GO:0019244; P:lactate biosynthetic process from pyruvate; IDA:MGI. DR GO; GO:0019516; P:lactate oxidation; IDA:MGI. DR GO; GO:0030317; P:sperm motility; IMP:MGI. DR Gene3D; 3.40.50.720; -; 1. DR Gene3D; 3.90.110.10; -; 1. DR HAMAP; MF_00488; Lactate_dehydrog; 1. DR InterPro; IPR001557; L-lactate/malate_DH. DR InterPro; IPR011304; L-lactate_DH. DR InterPro; IPR018177; L-lactate_DH_AS. DR InterPro; IPR022383; Lactate/malate_DH_C. DR InterPro; IPR001236; Lactate/malate_DH_N. DR InterPro; IPR015955; Lactate_DH/Glyco_Ohase_4_C. DR InterPro; IPR016040; NAD(P)-bd_dom. DR PANTHER; PTHR11540; PTHR11540; 1. DR Pfam; PF02866; Ldh_1_C; 1. DR Pfam; PF00056; Ldh_1_N; 1. DR PIRSF; PIRSF000102; Lac_mal_DH; 1. DR PRINTS; PR00086; LLDHDRGNASE. DR SUPFAM; SSF56327; SSF56327; 1. DR TIGRFAMs; TIGR01771; L-LDH-NAD; 1. DR PROSITE; PS00064; L_LDH; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Cytoplasm; Direct protein sequencing; KW Glycolysis; NAD; Oxidoreductase; Reference proteome. FT INIT_MET 1 1 Removed. FT CHAIN 2 332 L-lactate dehydrogenase C chain. FT /FTId=PRO_0000168480. FT NP_BIND 29 57 NAD (By similarity). FT ACT_SITE 193 193 Proton acceptor (By similarity). FT BINDING 99 99 NAD (By similarity). FT BINDING 106 106 Substrate (By similarity). FT BINDING 138 138 NAD or substrate (By similarity). FT BINDING 169 169 Substrate (By similarity). FT BINDING 248 248 Substrate (By similarity). FT MOD_RES 2 2 Blocked amino end (Ser). FT CONFLICT 7 7 Q -> E (in Ref. 6; AA sequence). FT CONFLICT 15 15 Missing (in Ref. 6; AA sequence). FT CONFLICT 30 30 N -> D (in Ref. 6; AA sequence). FT CONFLICT 56 56 N -> D (in Ref. 6; AA sequence). FT CONFLICT 104 104 E -> Q (in Ref. 6; AA sequence). FT CONFLICT 124 125 IV -> VI (in Ref. 6; AA sequence). FT CONFLICT 135 135 I -> V (in Ref. 6; AA sequence). FT CONFLICT 223 225 DKE -> NKQ (in Ref. 6; AA sequence). FT CONFLICT 243 243 N -> D (in Ref. 6; AA sequence). FT CONFLICT 297 297 Q -> E (in Ref. 6; AA sequence). FT CONFLICT 329 331 DLQ -> NLE (in Ref. 6; AA sequence). FT HELIX 4 8 FT STRAND 9 11 FT STRAND 22 26 FT HELIX 30 40 FT TURN 41 43 FT STRAND 46 51 FT HELIX 55 67 FT TURN 68 71 FT STRAND 76 82 FT HELIX 83 86 FT STRAND 89 94 FT TURN 102 104 FT HELIX 111 120 FT TURN 121 123 FT HELIX 124 127 FT STRAND 132 135 FT STRAND 137 139 FT HELIX 140 151 FT TURN 155 157 FT STRAND 158 160 FT HELIX 164 178 FT STRAND 189 191 FT STRAND 193 195 FT STRAND 197 199 FT HELIX 201 203 FT STRAND 205 207 FT STRAND 209 214 FT TURN 215 217 FT STRAND 221 226 FT HELIX 228 245 FT HELIX 250 264 FT STRAND 269 276 FT STRAND 288 296 FT STRAND 299 304 FT HELIX 310 326 SQ SEQUENCE 332 AA; 35912 MW; 367A7EA8B2A6D86A CRC64; MSTVKEQLIQ NLVPEDKLSR CKITVVGVGN VGMACAISIL LKGLADELAL VDADTNKLRG EALDLLHGSL FLSTPKIVFG KDYNVSANSK LVIITAGARM VSGETRLDLL QRNVAIMKAI VPGIVQNSPD CKIIIVTNPV DILTYVVWKI SGFPVGRVIG SGCNLDSARF RYLIGEKLGV NPTSCHGWVL GEHGDSSVPI WSGVNVAGVT LKSLNPAIGT DSDKEHWKNV HKQVVEGGYE VLNMKGYTSW AIGLSVTDLA RSILKNLKRV HPVTTLVKGF HGIKEEVFLS IPCVLGQSGI TDFVKVNMTA EEEGLLKKSA DTLWNMQKDL QL // ID LDHD_MOUSE Reviewed; 484 AA. AC Q7TNG8; Q8BYU7; Q8CIV4; DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2003, sequence version 1. DT 19-MAR-2014, entry version 82. DE RecName: Full=Probable D-lactate dehydrogenase, mitochondrial; DE Short=DLD; DE Short=Lactate dehydrogenase D; DE EC=1.1.2.4; DE Flags: Precursor; GN Name=Ldhd; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH CSRP3, SUBCELLULAR RP LOCATION, AND TISSUE SPECIFICITY. RC STRAIN=129/Sv; RX PubMed=12127981; DOI=10.1016/S0006-291X(02)00768-4; RA Flick M.J., Konieczny S.F.; RT "Identification of putative mammalian D-lactate dehydrogenase RT enzymes."; RL Biochem. Biophys. Res. Commun. 295:910-916(2002). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Kidney; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 286-430. RC STRAIN=C57BL/6J; TISSUE=Thymus; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [4] RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-335, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., RA Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). RN [5] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-36; LYS-292; LYS-335; RP LYS-422 AND LYS-449, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE RP SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23576753; DOI=10.1073/pnas.1302961110; RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., RA Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.; RT "Label-free quantitative proteomics of the lysine acetylome in RT mitochondria identifies substrates of SIRT3 in metabolic pathways."; RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013). CC -!- CATALYTIC ACTIVITY: (R)-lactate + 2 ferricytochrome c = pyruvate + CC 2 ferrocytochrome c + 2 H(+). CC -!- COFACTOR: FAD (By similarity). CC -!- SUBUNIT: Interacts with CSRP3. CC -!- SUBCELLULAR LOCATION: Mitochondrion. CC -!- TISSUE SPECIFICITY: Readily detected in liver and kidney, with a CC weaker signal observed in heart, skeletal muscle, stomach, brain, CC and lung. CC -!- SIMILARITY: Belongs to the FAD-binding oxidoreductase/transferase CC type 4 family. CC -!- SIMILARITY: Contains 1 FAD-binding PCMH-type domain. CC -!- SEQUENCE CAUTION: CC Sequence=AAM50323.1; Type=Frameshift; Positions=459, 474; CC Sequence=BAC29917.1; Type=Frameshift; Positions=141, 229, 315; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AY092768; AAM50323.1; ALT_FRAME; mRNA. DR EMBL; BC039155; AAH39155.1; -; mRNA. DR EMBL; BC055443; AAH55443.1; -; mRNA. DR EMBL; AK037996; BAC29917.1; ALT_FRAME; mRNA. DR RefSeq; NP_081846.3; NM_027570.3. DR UniGene; Mm.271578; -. DR UniGene; Mm.27589; -. DR ProteinModelPortal; Q7TNG8; -. DR SMR; Q7TNG8; 27-484. DR IntAct; Q7TNG8; 2. DR MINT; MINT-4116468; -. DR PhosphoSite; Q7TNG8; -. DR PaxDb; Q7TNG8; -. DR PRIDE; Q7TNG8; -. DR Ensembl; ENSMUST00000070004; ENSMUSP00000068086; ENSMUSG00000031958. DR GeneID; 52815; -. DR KEGG; mmu:52815; -. DR UCSC; uc009nmn.1; mouse. DR CTD; 197257; -. DR MGI; MGI:106428; Ldhd. DR eggNOG; COG0277; -. DR GeneTree; ENSGT00530000063515; -. DR HOGENOM; HOG000230995; -. DR HOVERGEN; HBG066407; -. DR InParanoid; Q7TNG8; -. DR KO; K00102; -. DR OMA; PDKFNED; -. DR OrthoDB; EOG7QNVKV; -. DR TreeFam; TF314122; -. DR NextBio; 309579; -. DR PRO; PR:Q7TNG8; -. DR Bgee; Q7TNG8; -. DR CleanEx; MM_LDHD; -. DR Genevestigator; Q7TNG8; -. DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:Ensembl. DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB. DR GO; GO:0004458; F:D-lactate dehydrogenase (cytochrome) activity; IEA:UniProtKB-EC. DR GO; GO:0008720; F:D-lactate dehydrogenase activity; NAS:UniProtKB. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. DR GO; GO:0008762; F:UDP-N-acetylmuramate dehydrogenase activity; IEA:InterPro. DR GO; GO:0006754; P:ATP biosynthetic process; NAS:UniProtKB. DR Gene3D; 1.10.45.10; -; 1. DR Gene3D; 3.30.43.10; -; 1. DR Gene3D; 3.30.465.10; -; 1. DR InterPro; IPR016169; CO_DH_flavot_FAD-bd_sub2. DR InterPro; IPR016166; FAD-bd_2. DR InterPro; IPR016167; FAD-bd_2_sub1. DR InterPro; IPR016164; FAD-linked_Oxase-like_C. DR InterPro; IPR004113; FAD-linked_oxidase_C. DR InterPro; IPR006094; Oxid_FAD_bind_N. DR InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2. DR Pfam; PF02913; FAD-oxidase_C; 1. DR Pfam; PF01565; FAD_binding_4; 1. DR SUPFAM; SSF55103; SSF55103; 1. DR SUPFAM; SSF56176; SSF56176; 1. DR PROSITE; PS51387; FAD_PCMH; 1. PE 1: Evidence at protein level; KW Acetylation; Complete proteome; FAD; Flavoprotein; Mitochondrion; KW Oxidoreductase; Reference proteome; Transit peptide. FT TRANSIT 1 ? Mitochondrion (Potential). FT CHAIN ? 484 Probable D-lactate dehydrogenase, FT mitochondrial. FT /FTId=PRO_0000262953. FT DOMAIN 62 242 FAD-binding PCMH-type. FT MOD_RES 36 36 N6-acetyllysine. FT MOD_RES 292 292 N6-acetyllysine. FT MOD_RES 335 335 N6-acetyllysine; alternate. FT MOD_RES 335 335 N6-succinyllysine; alternate. FT MOD_RES 422 422 N6-acetyllysine. FT MOD_RES 449 449 N6-acetyllysine. FT CONFLICT 413 413 D -> H (in Ref. 2; BAC29917). SQ SEQUENCE 484 AA; 51848 MW; 78BDF31A861B9A82 CRC64; MAMLLRVATQ RLSPWRSFCS RGSQGGLSQD FVEALKAVVG SPHVSTASAV REQHGHDESM HRCQPPDAVV WPQNVDQVSR VASLCYNQGV PIIPFGTGTG VEGGVCAVQG GVCINLTHMD QITELNTEDF SVVVEPGVTR KALNTHLRDS GLWFPVDPGA DASLCGMAAT GASGTNAVRY GTMRDNVINL EVVLPDGRLL HTAGRGRHYR KSAAGYNLTG LFVGSEGTLG IITSTTLRLH PAPEATVAAT CAFPSVQAAV DSTVQILQAA VPVARIEFLD DVMMDACNRH SKLNCPVAPT LFLEFHGSQQ TLAEQLQRTE AITQDNGGSH FSWAKEAEKR NELWAARHNA WYAALALSPG SKAYSTDVCV PISRLPEILV ETKEEIKASK LTGAIVGHVG DGNFHCILLV DPDDAEEQRR VKAFAENLGR RALALGGTCT GEHGIGLGKR QLLQEEVGPV GVETMRQLKN TLDPRGLMNP GKVL // ID LOX12_MOUSE Reviewed; 663 AA. AC P39655; Q8BHG4; DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot. DT 11-SEP-2007, sequence version 4. DT 19-FEB-2014, entry version 121. DE RecName: Full=Arachidonate 12-lipoxygenase, 12S-type; DE Short=12S-LOX; DE Short=12S-lipoxygenase; DE EC=1.13.11.31; DE AltName: Full=Lipoxin synthase 12-LO; DE EC=3.3.2.-; DE AltName: Full=Platelet-type lipoxygenase 12; DE Short=P-12LO; GN Name=Alox12; Synonyms=Alox12p; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, MUTAGENESIS OF RP ILE-663, AND TISSUE SPECIFICITY. RC STRAIN=C57BL/6, and ICR; TISSUE=Spleen; RX PubMed=8188678; RA Chen X.-S., Kurre U., Jenkins N.A., Copeland N.G., Funk C.D.; RT "cDNA cloning, expression, mutagenesis of C-terminal isoleucine, RT genomic structure, and chromosomal localizations of murine 12- RT lipoxygenases."; RL J. Biol. Chem. 269:13979-13987(1994). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=7576099; DOI=10.1002/mc.2940140208; RA Krieg P., Kinzig A., Ress-Loschke M., Vogel S., Vanlandingham B., RA Stephan M., Lehmann W.D., Marks F., Furstenberger G.; RT "12-lipoxygenase isoenzymes in mouse skin tumor development."; RL Mol. Carcinog. 14:118-129(1995). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Ovary, and Vagina; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 126-218. RC TISSUE=Lung; RX PubMed=7792391; DOI=10.1016/0090-6980(94)00005-H; RA Hagmann W., Gao X., Zacharek A., Wojciechowski L.A., Honn K.V.; RT "12-lipoxygenase in Lewis lung carcinoma cells: molecular identity, RT intracellular distribution of activity and protein, and Ca(2+)- RT dependent translocation from cytosol to membranes."; RL Prostaglandins 49:49-62(1995). RN [6] RP SUBCELLULAR LOCATION. RX PubMed=7868854; RA Nakamura M., Ueda N., Kishimoto K., Yoshimoto T., Yamamoto S., RA Ishimura K.; RT "Immunocytochemical localization of platelet-type arachidonate 12- RT lipoxygenase in mouse blood cells."; RL J. Histochem. Cytochem. 43:237-244(1995). RN [7] RP FUNCTION IN PLATELET ACTIVATION, DISRUPTION PHENOTYPE, AND TISSUE RP SPECIFICITY. RX PubMed=9501222; DOI=10.1073/pnas.95.6.3100; RA Johnson E.N., Brass L.F., Funk C.D.; RT "Increased platelet sensitivity to ADP in mice lacking platelet-type RT 12-lipoxygenase."; RL Proc. Natl. Acad. Sci. U.S.A. 95:3100-3105(1998). RN [8] RP DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY. RX PubMed=10383730; DOI=10.1046/j.1523-1747.1999.00595.x; RA Johnson E.N., Nanney L.B., Virmani J., Lawson J.A., Funk C.D.; RT "Basal transepidermal water loss is increased in platelet-type 12- RT lipoxygenase deficient mice."; RL J. Invest. Dermatol. 112:861-865(1999). CC -!- FUNCTION: Non-heme iron-containing dioxygenase that catalyzes the CC stereo-specific peroxidation of free and esterified CC polyunsaturated fatty acids generating a spectrum of bioactive CC lipid mediators. Mainly converts arachidonic acid to (12S)- CC hydroperoxyeicosatetraenoic acid/(12S)-HPETE but can also CC metabolize linoleic acid. Has a dual activity since it also CC converts leukotriene A4/LTA4 into both the bioactive lipoxin CC A4/LXA4 and lipoxin B4/LXB4. Through the production of specific CC bioactive lipids like (12S)-HPETE it regulates different CC biological processes including platelet activation. It also CC probably positively regulates angiogenesis through regulation of CC the expression of the vascular endothelial growth factor. Plays a CC role in apoptotic process, promoting the survival of vascular CC smooth muscle cells for instance. May also play a role in the CC control of cell migration and proliferation. CC -!- CATALYTIC ACTIVITY: Arachidonate + O(2) = (5Z,8Z,10E,14Z)-(12S)- CC 12-hydroperoxyicosa-5,8,10,14-tetraenoate. CC -!- CATALYTIC ACTIVITY: (7E,9E,11Z,14Z)-(5S,6S)-5,6-epoxyicosa- CC 7,9,11,14-tetraenoate + H(2)O = (5S,6R,15S)-trihydroxy- CC (7E,9E,11Z,13E)-eicosatetraenoate. CC -!- CATALYTIC ACTIVITY: (7E,9E,11Z,14Z)-(5S,6S)-5,6-epoxyicosa- CC 7,9,11,14-tetraenoate + H(2)O = (5S,14R,15S)-trihydroxy- CC (6E,8Z,10E,12E)-eicosatetraenoate. CC -!- COFACTOR: Binds 1 iron ion per subunit. CC -!- ENZYME REGULATION: Activated by EGF (By similarity). CC -!- PATHWAY: Lipid metabolism; hydroperoxy eicosatetraenoic acid CC biosynthesis. CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol. Membrane (By CC similarity). Note=Membrane association is stimulated by EGF (By CC similarity). CC -!- TISSUE SPECIFICITY: Found primarily in platelets and in microsomal CC and cytosolic fractions of the epidermis (at protein level). CC -!- DISRUPTION PHENOTYPE: Mice are fertile and appear to exhibit no CC gross abnormalities. However, they display increased aggregation CC of platelets in response to ADP. They also display a mild basal CC transepidermal water loss. CC -!- SIMILARITY: Belongs to the lipoxygenase family. CC -!- SIMILARITY: Contains 1 lipoxygenase domain. CC -!- SIMILARITY: Contains 1 PLAT domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U04334; AAA20659.1; -; mRNA. DR EMBL; S80446; AAB36013.1; -; mRNA. DR EMBL; AK036898; BAC29629.1; -; mRNA. DR EMBL; AK087724; BAC39981.1; -; mRNA. DR EMBL; AL669869; CAI35235.1; -; Genomic_DNA. DR EMBL; S77511; AAB34667.1; -; mRNA. DR PIR; A54075; A54075. DR RefSeq; NP_031466.2; NM_007440.4. DR UniGene; Mm.12286; -. DR ProteinModelPortal; P39655; -. DR SMR; P39655; 2-663. DR BindingDB; P39655; -. DR ChEMBL; CHEMBL3225; -. DR PhosphoSite; P39655; -. DR PaxDb; P39655; -. DR PRIDE; P39655; -. DR DNASU; 11684; -. DR Ensembl; ENSMUST00000000329; ENSMUSP00000000329; ENSMUSG00000000320. DR GeneID; 11684; -. DR KEGG; mmu:11684; -. DR UCSC; uc007juj.1; mouse. DR CTD; 239; -. DR MGI; MGI:87998; Alox12. DR eggNOG; NOG69653; -. DR GeneTree; ENSGT00550000074415; -. DR HOGENOM; HOG000234358; -. DR HOVERGEN; HBG005150; -. DR InParanoid; P39655; -. DR KO; K00458; -. DR OMA; QNQLCHF; -. DR OrthoDB; EOG7B05CG; -. DR TreeFam; TF105320; -. DR UniPathway; UPA00881; -. DR NextBio; 279319; -. DR PRO; PR:P39655; -. DR ArrayExpress; P39655; -. DR Bgee; P39655; -. DR CleanEx; MM_ALOX12; -. DR Genevestigator; P39655; -. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell. DR GO; GO:0042383; C:sarcolemma; ISS:UniProtKB. DR GO; GO:0004052; F:arachidonate 12-lipoxygenase activity; IDA:UniProtKB. DR GO; GO:0047977; F:hepoxilin-epoxide hydrolase activity; ISS:UniProtKB. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0016165; F:linoleate 13S-lipoxygenase activity; IEA:Ensembl. DR GO; GO:0007568; P:aging; IEA:Ensembl. DR GO; GO:0019369; P:arachidonic acid metabolic process; IDA:UniProtKB. DR GO; GO:0006928; P:cellular component movement; ISS:UniProtKB. DR GO; GO:0071396; P:cellular response to lipid; IEA:Ensembl. DR GO; GO:0061436; P:establishment of skin barrier; IMP:UniProtKB. DR GO; GO:0019395; P:fatty acid oxidation; ISS:UniProtKB. DR GO; GO:0051122; P:hepoxilin biosynthetic process; ISS:UniProtKB. DR GO; GO:1901751; P:leukotriene A4 metabolic process; ISS:UniProtKB. DR GO; GO:0043651; P:linoleic acid metabolic process; ISS:UniProtKB. DR GO; GO:2001303; P:lipoxin A4 biosynthetic process; ISS:UniProtKB. DR GO; GO:2001306; P:lipoxin B4 biosynthetic process; ISS:UniProtKB. DR GO; GO:0019372; P:lipoxygenase pathway; IDA:UniProtKB. DR GO; GO:0010656; P:negative regulation of muscle cell apoptotic process; ISS:UniProtKB. DR GO; GO:0090331; P:negative regulation of platelet aggregation; IMP:UniProtKB. DR GO; GO:0045766; P:positive regulation of angiogenesis; ISS:UniProtKB. DR GO; GO:0043065; P:positive regulation of apoptotic process; ISS:UniProtKB. DR GO; GO:0045785; P:positive regulation of cell adhesion; ISS:UniProtKB. DR GO; GO:0030307; P:positive regulation of cell growth; ISS:UniProtKB. DR GO; GO:0030335; P:positive regulation of cell migration; ISS:UniProtKB. DR GO; GO:0008284; P:positive regulation of cell proliferation; IMP:UniProtKB. DR GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; IEA:Ensembl. DR GO; GO:0045603; P:positive regulation of endothelial cell differentiation; IEA:Ensembl. DR GO; GO:0010595; P:positive regulation of endothelial cell migration; IEA:Ensembl. DR GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl. DR GO; GO:0051901; P:positive regulation of mitochondrial depolarization; IEA:Ensembl. DR GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; IEA:Ensembl. DR GO; GO:0045909; P:positive regulation of vasodilation; IEA:Ensembl. DR Gene3D; 2.60.60.20; -; 1. DR InterPro; IPR008976; Lipase_LipOase. DR InterPro; IPR000907; LipOase. DR InterPro; IPR013819; LipOase_C. DR InterPro; IPR020834; LipOase_CS. DR InterPro; IPR020833; LipOase_Fe_BS. DR InterPro; IPR001885; LipOase_mml. DR InterPro; IPR001024; PLAT/LH2_dom. DR PANTHER; PTHR11771; PTHR11771; 1. DR Pfam; PF00305; Lipoxygenase; 1. DR Pfam; PF01477; PLAT; 1. DR PRINTS; PR00087; LIPOXYGENASE. DR PRINTS; PR00467; MAMLPOXGNASE. DR SMART; SM00308; LH2; 1. DR SUPFAM; SSF48484; SSF48484; 1. DR SUPFAM; SSF49723; SSF49723; 1. DR PROSITE; PS00711; LIPOXYGENASE_1; 1. DR PROSITE; PS00081; LIPOXYGENASE_2; 1. DR PROSITE; PS51393; LIPOXYGENASE_3; 1. DR PROSITE; PS50095; PLAT; 1. PE 1: Evidence at protein level; KW Complete proteome; Cytoplasm; Dioxygenase; Fatty acid metabolism; KW Hydrolase; Iron; Lipid metabolism; Membrane; Metal-binding; KW Oxidoreductase; Reference proteome. FT CHAIN 1 663 Arachidonate 12-lipoxygenase, 12S-type. FT /FTId=PRO_0000220683. FT DOMAIN 2 114 PLAT. FT DOMAIN 115 663 Lipoxygenase. FT METAL 360 360 Iron; catalytic (By similarity). FT METAL 365 365 Iron; catalytic (By similarity). FT METAL 540 540 Iron; catalytic (By similarity). FT METAL 544 544 Iron; catalytic (By similarity). FT METAL 663 663 Iron; via carboxylate; catalytic (By FT similarity). FT MUTAGEN 663 663 I->D,R,K,G: Loss of activity. FT MUTAGEN 663 663 I->S,N: Little activity (8-15%). FT MUTAGEN 663 663 I->V: Nearly full activity. FT CONFLICT 3 3 R -> A (in Ref. 1; AAA20659). FT CONFLICT 112 112 T -> Q (in Ref. 1; AAA20659 and 2; FT AAB36013). FT CONFLICT 403 403 S -> T (in Ref. 1; AAA20659 and 2; FT AAB36013). SQ SEQUENCE 663 AA; 75390 MW; 205BE32BE2CF3E87 CRC64; MGRYRVRVVT GAWLFSGSLN LVRLWLVGEH REAKLELQLR PARGKEEEFD FDVPEDLGPL QFVKLHKQHT VVDDAWFCNL ITVQGPGTSA EAVFPCYRWV QGEGILSLPE GTARLAGDNA LDVFQKYREK ELKERQQTYC WATWKEGLPQ TIAADCKDDL PPNMRFHEEK RLDFEWTLKA GVLEMGLKRV YTLLRSWNHL EDFDQIFWGQ KSALAEKVHQ CWQEDELFGY QFLNGANPML LRRSTSLPSR LVLPSGMEEL QAQLEKELKN GSLFEADFIL LDGIPANVIR GEPQYLAAPL VMLRMDPGGK LLPMAIQIQP PNPSSPAPTL FLPSDPPLAW LLAKIWVRNS DFQLQELQFH LLNTHLVAEV IAVATMRCLP GLHPIFKLLV PHIRYTMEIN TRSRTQLISD GGIFDQVVST GGGGHVQLLT RAVAQLTYHS LCPPDDLANR GLLRIPSALY ARDALQLWEV TARYVKGMVH LFYQSDDIVR GDPELQAWCR EITEVGLCHA QDRGFPVSFQ SRAQLCHFLT MCVFTCTAQH AAINQGQLDW YGWVPNAPCT MRMPPPTSKD DVTMETVMGS LPDVQKACLQ MTITWHLGRL QPDMVPLGHH TEKYFSDPRT KAVLSQFQAD LDNLEKEITA RNEQLDLPYE YLKPSRIENS ITI // ID LOX5_MOUSE Reviewed; 674 AA. AC P48999; Q3TB75; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 3. DT 19-FEB-2014, entry version 116. DE RecName: Full=Arachidonate 5-lipoxygenase; DE Short=5-LO; DE Short=5-lipoxygenase; DE EC=1.13.11.34; GN Name=Alox5; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND RP MUTAGENESIS OF VAL-672. RC STRAIN=C57BL/6 X 129/Sv; TISSUE=Peritoneal cavity; RX PubMed=7629107; DOI=10.1074/jbc.270.30.17993; RA Chen X.-S., Naumann T.A., Kurre U., Jenkins N.A., Copeland N.G., RA Funk C.D.; RT "cDNA cloning, expression, mutagenesis, intracellular localization, RT and gene chromosomal assignment of mouse 5-lipoxygenase."; RL J. Biol. Chem. 270:17993-17999(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Bone; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Testis; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: Catalyzes the first step in leukotriene biosynthesis, CC and thereby plays a role in inflammatory processes. CC -!- CATALYTIC ACTIVITY: Arachidonate + O(2) = leukotriene A(4) + CC H(2)O. CC -!- COFACTOR: Binds 1 iron ion per subunit (By similarity). CC -!- COFACTOR: Binds 2 calcium ions per subunit (By similarity). CC -!- PATHWAY: Lipid metabolism; leukotriene A4 biosynthesis. CC -!- SUBUNIT: Interacts with ALOX5AP and LTC4S. Interacts with COTL1, CC the interaction is required for stability and efficient catalytic CC activity (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus matrix. Nucleus membrane; CC Peripheral membrane protein (By similarity). Note=Shuttles between CC cytoplasm and nucleus. Found exclusively in the nucleus, when CC phosphorylated on Ser-272. Calcium binding promotes translocation CC from the cytosol and the nuclear matrix to the nuclear envelope CC and membrane association (By similarity). CC -!- PTM: Serine phosphorylation by MAPKAPK2 is stimulated by CC arachidonic acid. Phosphorylation on Ser-524 by PKA has an CC inhibitory effect. Phosphorylation on Ser-272 prevents export from CC the nucleus (By similarity). CC -!- SIMILARITY: Belongs to the lipoxygenase family. CC -!- SIMILARITY: Contains 1 lipoxygenase domain. CC -!- SIMILARITY: Contains 1 PLAT domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42198; AAC37673.1; -; mRNA. DR EMBL; AK137481; BAE23373.1; -; mRNA. DR EMBL; AK171413; BAE42439.1; -; mRNA. DR EMBL; BC139102; AAI39103.1; -; mRNA. DR EMBL; BC141213; AAI41214.1; -; mRNA. DR PIR; I49479; I49479. DR RefSeq; NP_033792.1; NM_009662.2. DR UniGene; Mm.41072; -. DR ProteinModelPortal; P48999; -. DR SMR; P48999; 2-674. DR BioGrid; 198076; 1. DR BindingDB; P48999; -. DR ChEMBL; CHEMBL5211; -. DR PhosphoSite; P48999; -. DR PaxDb; P48999; -. DR PRIDE; P48999; -. DR Ensembl; ENSMUST00000026795; ENSMUSP00000026795; ENSMUSG00000025701. DR GeneID; 11689; -. DR KEGG; mmu:11689; -. DR UCSC; uc009dkd.1; mouse. DR CTD; 240; -. DR MGI; MGI:87999; Alox5. DR eggNOG; NOG69653; -. DR GeneTree; ENSGT00550000074415; -. DR HOGENOM; HOG000234358; -. DR HOVERGEN; HBG005150; -. DR InParanoid; Q3TB75; -. DR KO; K00461; -. DR OMA; GIDANKT; -. DR OrthoDB; EOG7B05CG; -. DR TreeFam; TF105320; -. DR UniPathway; UPA00877; -. DR NextBio; 279339; -. DR PRO; PR:P48999; -. DR ArrayExpress; P48999; -. DR Bgee; P48999; -. DR CleanEx; MM_ALOX5; -. DR Genevestigator; P48999; -. DR GO; GO:0005829; C:cytosol; ISS:UniProtKB. DR GO; GO:0005641; C:nuclear envelope lumen; ISS:UniProtKB. DR GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell. DR GO; GO:0031965; C:nuclear membrane; ISS:UniProtKB. DR GO; GO:0004051; F:arachidonate 5-lipoxygenase activity; IEA:UniProtKB-EC. DR GO; GO:0005506; F:iron ion binding; ISS:UniProtKB. DR GO; GO:0019370; P:leukotriene biosynthetic process; IDA:MGI. DR GO; GO:0002540; P:leukotriene production involved in inflammatory response; IMP:MGI. DR Gene3D; 2.60.60.20; -; 1. DR InterPro; IPR008976; Lipase_LipOase. DR InterPro; IPR000907; LipOase. DR InterPro; IPR013819; LipOase_C. DR InterPro; IPR020834; LipOase_CS. DR InterPro; IPR020833; LipOase_Fe_BS. DR InterPro; IPR001885; LipOase_mml. DR InterPro; IPR001024; PLAT/LH2_dom. DR PANTHER; PTHR11771; PTHR11771; 1. DR Pfam; PF00305; Lipoxygenase; 2. DR Pfam; PF01477; PLAT; 1. DR PRINTS; PR00087; LIPOXYGENASE. DR PRINTS; PR00467; MAMLPOXGNASE. DR SMART; SM00308; LH2; 1. DR SUPFAM; SSF48484; SSF48484; 1. DR SUPFAM; SSF49723; SSF49723; 1. DR PROSITE; PS00711; LIPOXYGENASE_1; 1. DR PROSITE; PS00081; LIPOXYGENASE_2; 1. DR PROSITE; PS51393; LIPOXYGENASE_3; 1. DR PROSITE; PS50095; PLAT; 1. PE 1: Evidence at protein level; KW Calcium; Complete proteome; Cytoplasm; Dioxygenase; Iron; KW Leukotriene biosynthesis; Membrane; Metal-binding; Nucleus; KW Oxidoreductase; Phosphoprotein; Reference proteome. FT CHAIN 1 674 Arachidonate 5-lipoxygenase. FT /FTId=PRO_0000220695. FT DOMAIN 2 118 PLAT. FT DOMAIN 119 674 Lipoxygenase. FT METAL 17 17 Calcium 1; via carbonyl oxygen; FT structural (By similarity). FT METAL 18 18 Calcium 2; via carbonyl oxygen; FT structural (By similarity). FT METAL 19 19 Calcium 2; structural (By similarity). FT METAL 44 44 Calcium 2; structural (By similarity). FT METAL 45 45 Calcium 2; via carbonyl oxygen; FT structural (By similarity). FT METAL 47 47 Calcium 2; structural (By similarity). FT METAL 79 79 Calcium 1; via carbonyl oxygen; FT structural (By similarity). FT METAL 80 80 Calcium 1; via carbonyl oxygen; FT structural (By similarity). FT METAL 368 368 Iron; catalytic (By similarity). FT METAL 373 373 Iron; catalytic (By similarity). FT METAL 551 551 Iron; catalytic (By similarity). FT METAL 555 555 Iron; catalytic (By similarity). FT METAL 674 674 Iron; via carboxylate; catalytic (By FT similarity). FT SITE 103 103 Essential for stabilizing binding to FT COTL1 (By similarity). FT MOD_RES 272 272 Phosphoserine (By similarity). FT MOD_RES 524 524 Phosphoserine (By similarity). FT MUTAGEN 672 672 V->M: Loss of activity. FT CONFLICT 466 466 I -> M (in Ref. 1; AAC37673). FT CONFLICT 646 646 V -> I (in Ref. 1; AAC37673). SQ SEQUENCE 674 AA; 77967 MW; 130F27F9A77A3D88 CRC64; MPSYTVTVAT GSQWFAGTDD YIYLSLIGSA GCSEKHLLDK AFYNDFERGA VDSYDVTVDE ELGEIYLVKI EKRKYWLHDD WYLKYITLKT PHGDYIEFPC YRWITGEGEI VLRDGRAKLA RDDQIHILKQ HRRKELEARQ KQYRWMEWNP GFPLSIDAKC HKDLPRDIQF DSEKGVDFVL NYSKAMENLF INRFMHMFQS SWHDFADFEK IFVKISNTIS ERVKNHWQED LMFGYQFLNG CNPVLIKRCT ALPPKLPVTT EMVECSLERQ LSLEQEVQEG NIFIVDYELL DGIDANKTDP CTHQFLAAPI CLLYKNLANK IVPIAIQLNQ TPGESNPIFL PTDSKYDWLL AKIWVRSSDF HVHQTITHLL RTHLVSEVFG IAMYRQLPAV HPLFKLLVAH VRFTIAINTK AREQLICEYG LFDKANATGG GGHVQMVQRA VQDLTYSSLC FPEAIKARGM DSTEDIPFYF YRDDGLLVWE AIQSFTMEVV SIYYENDQVV EEDQELQDFV KDVYVYGMRG KKASGFPKSI KSREKLSEYL TVVIFTASAQ HAAVNFGQYD WCSWIPNAPP TMRAPPPTAK GVVTIEQIVD TLPDRGRSCW HLGAVWALSQ FQENELFLGM YPEEHFIEKP VKEAMIRFRK NLEAIVSVIA ERNKNKKLPY YYLSPDRIPN SVAI // ID LOXL1_MOUSE Reviewed; 607 AA. AC P97873; Q91ZY4; Q99KX3; DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot. DT 19-SEP-2003, sequence version 3. DT 19-FEB-2014, entry version 101. DE RecName: Full=Lysyl oxidase homolog 1; DE EC=1.4.3.-; DE AltName: Full=Lysyl oxidase 2; DE AltName: Full=Lysyl oxidase-like protein 1; DE Flags: Precursor; GN Name=Loxl1; Synonyms=Lox2, Loxl; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Seve S., Borel A., Gleyzal C., Farjanel J., Eichenberger D., Font B., RA Sommer P.; RT "Identification of the recombinant and natural forms of mature lysyl RT oxidase-like 1."; RL Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Mammary gland; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] OF 498-607. RX PubMed=9250877; DOI=10.1007/s003359900520; RA Tchernev V.T., Yang T.P., Kingsmore S.F.; RT "Genetic mapping of lysyl oxidase-2 (Loxl) on mouse chromosome 9."; RL Mamm. Genome 8:621-622(1997). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 526-540. RC STRAIN=C57BL/6J; RX PubMed=9119402; DOI=10.1006/geno.1996.4574; RA Wydner K.S., Kim Y., Csiszar K., Boyd C.D., Passmore H.C.; RT "An intron capture strategy used to identify and map a lysyl oxidase- RT like gene on chromosome 9 in the mouse."; RL Genomics 40:342-345(1997). CC -!- FUNCTION: Active on elastin and collagen substrates (By CC similarity). CC -!- COFACTOR: Copper (By similarity). CC -!- COFACTOR: Contains 1 lysine tyrosylquinone (By similarity). CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space (Potential). CC -!- PTM: The lysine tyrosylquinone cross-link (LTQ) is generated by CC condensation of the epsilon-amino group of a lysine with a CC topaquinone produced by oxidation of tyrosine. CC -!- SIMILARITY: Belongs to the lysyl oxidase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF357006; AAK97375.1; -; mRNA. DR EMBL; BC003973; AAH03973.1; -; mRNA. DR EMBL; BC037999; AAH37999.1; -; mRNA. DR EMBL; AH006767; AAC53067.1; -; Genomic_DNA. DR EMBL; U79144; AAB86802.1; -; mRNA. DR RefSeq; NP_034859.2; NM_010729.3. DR UniGene; Mm.250492; -. DR BioGrid; 201192; 1. DR IntAct; P97873; 2. DR MINT; MINT-6743519; -. DR PhosphoSite; P97873; -. DR PaxDb; P97873; -. DR PRIDE; P97873; -. DR Ensembl; ENSMUST00000061799; ENSMUSP00000057406; ENSMUSG00000032334. DR GeneID; 16949; -. DR KEGG; mmu:16949; -. DR UCSC; uc009pwv.2; mouse. DR CTD; 4016; -. DR MGI; MGI:106096; Loxl1. DR eggNOG; NOG77510; -. DR GeneTree; ENSGT00740000115025; -. DR HOGENOM; HOG000234262; -. DR HOVERGEN; HBG000226; -. DR InParanoid; P97873; -. DR KO; K14678; -. DR OrthoDB; EOG7SN8C6; -. DR TreeFam; TF326061; -. DR NextBio; 290996; -. DR PRO; PR:P97873; -. DR Bgee; P97873; -. DR CleanEx; MM_LOXL1; -. DR Genevestigator; P97873; -. DR GO; GO:0031012; C:extracellular matrix; IDA:MGI. DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell. DR GO; GO:0005578; C:proteinaceous extracellular matrix; IEA:Ensembl. DR GO; GO:0005507; F:copper ion binding; IEA:InterPro. DR GO; GO:0016641; F:oxidoreductase activity, acting on the CH-NH2 group of donors, oxygen as acceptor; IDA:MGI. DR InterPro; IPR001695; Lysyl_oxidase. DR InterPro; IPR019828; Lysyl_oxidase_CS. DR Pfam; PF01186; Lysyl_oxidase; 1. DR PRINTS; PR00074; LYSYLOXIDASE. DR PROSITE; PS00926; LYSYL_OXIDASE; 1. PE 2: Evidence at transcript level; KW Cleavage on pair of basic residues; Complete proteome; Copper; KW Disulfide bond; LTQ; Metal-binding; Oxidoreductase; KW Reference proteome; Secreted; Signal; TPQ. FT SIGNAL 1 28 Potential. FT PROPEP 29 94 By similarity. FT /FTId=PRO_0000018530. FT CHAIN 95 607 Lysyl oxidase homolog 1. FT /FTId=PRO_0000018531. FT REGION 403 607 Lysyl-oxidase like. FT METAL 482 482 Copper (Potential). FT METAL 484 484 Copper (Potential). FT METAL 486 486 Copper (Potential). FT MOD_RES 545 545 2',4',5'-topaquinone (By similarity). FT DISULFID 428 434 By similarity. FT DISULFID 481 530 By similarity. FT DISULFID 514 520 By similarity. FT DISULFID 541 551 By similarity. FT DISULFID 588 602 By similarity. FT CROSSLNK 510 545 Lysine tyrosylquinone (Lys-Tyr) (By FT similarity). FT CONFLICT 173 173 P -> S (in Ref. 2; AAH37999). FT CONFLICT 208 210 GAG -> HAS (in Ref. 2; AAH03973). FT CONFLICT 321 321 T -> I (in Ref. 2; AAH03973). FT CONFLICT 500 500 S -> A (in Ref. 3; AAB86802). SQ SEQUENCE 607 AA; 66506 MW; 7BA8144F09E96C94 CRC64; MALAGAGSQL RTLVWSACLC VLVHGQQAQP GQGSDPGRWR QLIQWENNGQ VYSLLNSGSE YVPAGPQRGE TSSRVLLAGA PQTSQRRSQG GPRRRQAPSL PLPGRVGSDT VRGQTRHPFG FGQVPDNWRE VAVGDSTGMA RARTSVSQQR HGGSASSSVS ASAFATTYRQ PSPYPQQFPY PQAPFVNQYE NYDPASRTYE QGYVYYRGAG GGMGAGAAAV ASAGVIYPFQ PRARYEDYGG GGGEEQPEYP AQGFYPAPER PYVPQPQPQP QPQPQPQPQP SDGLDRRYSH SLYNEGTPGF EQAYPDPSTD VSQAPAGAGG TYGGAGDPRL GWYPPYAANV PPEAYVPPRA VEPQPPFRVL EPPYLPVRSS DAPSQGGERN GAQQGRLSVG SVYRPNQNGR GLPDLVPDPN YVQASTYVQR AHLYSLRCAA EEKCLASTAY APEATDYDLR VLLRFPQRVK NQGTADFLPN RPRHTWEWHS CHQHYHSMDE FSHYDLLDAS TGKKVAEGHK ASFCLEDSTC DFGNLKRYAC TSHTQGLSPG CYDTYNADID CQWIDITDVQ PGNYILKVHV NPKYIVLESD FTNNVVRCNI HYTGRYVSTT NCKIVQS // ID LOXL2_MOUSE Reviewed; 776 AA. AC P58022; Q8BRE6; Q8BS86; Q8C4K0; Q9JJ39; DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot. DT 22-NOV-2005, sequence version 2. DT 19-MAR-2014, entry version 108. DE RecName: Full=Lysyl oxidase homolog 2; DE EC=1.4.3.13; DE AltName: Full=Lysyl oxidase-like protein 2; DE Flags: Precursor; GN Name=Loxl2; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC STRAIN=C57BL/6J; TISSUE=Embryo, and Head; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] OF 558-776 (ISOFORM 1). RX PubMed=10842102; DOI=10.1016/S0945-053X(00)00061-5; RA Jourdan-Le Saux C., Le Saux O., Gleyzal C., Sommer P., Csiszar K.; RT "The mouse lysyl oxidase-like 2 gene (mLOXL2) maps to chromosome 14 RT and is highly expressed in skin, lung and thymus."; RL Matrix Biol. 19:179-183(2000). RN [3] RP INDUCTION. RX PubMed=21835952; DOI=10.1182/blood-2010-10-313296; RA Bignon M., Pichol-Thievend C., Hardouin J., Malbouyres M., Brechot N., RA Nasciutti L., Barret A., Teillon J., Guillon E., Etienne E., Caron M., RA Joubert-Caron R., Monnot C., Ruggiero F., Muller L., Germain S.; RT "Lysyl oxidase-like protein-2 regulates sprouting angiogenesis and RT type IV collagen assembly in the endothelial basement membrane."; RL Blood 118:3979-3989(2011). RN [4] RP FUNCTION, AND TISSUE SPECIFICITY. RX PubMed=21071451; DOI=10.1074/jbc.M110.155622; RA Iftikhar M., Hurtado P., Bais M.V., Wigner N., Stephens D.N., RA Gerstenfeld L.C., Trackman P.C.; RT "Lysyl oxidase-like-2 (LOXL2) is a major isoform in chondrocytes and RT is critically required for differentiation."; RL J. Biol. Chem. 286:909-918(2011). CC -!- FUNCTION: Mediates the post-translational oxidative deamination of CC lysine residues on target proteins leading to the formation of CC deaminated lysine (allysine). When secreted in extracellular CC matrix, promotes cross-linking of extracellular matrix proteins by CC mediating oxidative deamination of peptidyl lysine residues in CC precursors to fibrous collagen and elastin. Acts as a regulator of CC sprouting angiogenesis, probably via collagen IV scaffolding. When CC nuclear, acts as a transcription corepressor and specifically CC mediates deamination of trimethylated 'Lys-4' of histone H3 CC (H3K4me3), a specific tag for epigenetic transcriptional CC activation. Involved in epithelial to mesenchymal transition (EMT) CC via interaction with SNAI1 and participates in repression of E- CC cadherin, probably by mediating deamination of histone H3 (By CC similarity). Acts as a regulator of chondrocyte differentiation, CC probably by regulating expression of factors that control CC chondrocyte differentiation. CC -!- CATALYTIC ACTIVITY: Peptidyl-L-lysyl-peptide + O(2) + H(2)O = CC peptidyl-allysyl-peptide + NH(3) + H(2)O(2). CC -!- COFACTOR: Copper (By similarity). CC -!- COFACTOR: Contains 1 lysine tyrosylquinone (By similarity). CC -!- ENZYME REGULATION: Specifically inhibited by a mouse monoclonal CC antibody AB0023, inhibition occurs in a non-competitive manner (By CC similarity). CC -!- SUBUNIT: Component of some chromatin repressor complex. Interacts CC with SNAI1 (By similarity). CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular CC matrix, basement membrane (By similarity). Nucleus (By CC similarity). Chromosome (By similarity). Note=Associated with CC chromatin (By similarity). It is unclear how LOXL2 is nuclear: it CC contains a clear signal sequence and is predicted to localize in CC the extracellular medium. However, different reports confirmed the CC intracellular location and its key role in transcription CC regulation. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P58022-1; Sequence=Displayed; CC Name=2; CC IsoId=P58022-2; Sequence=VSP_016231, VSP_016232; CC Note=No experimental confirmation available; CC -!- TISSUE SPECIFICITY: Ubiquitous. Highest expression in skin, lung CC and thymus. Present in chondrocytes: mainly expressed by CC chondrocytes in healing fractures and in epiphyseal growth plates CC (at protein level). CC -!- INDUCTION: Strongly induced in hypoxia. CC -!- PTM: The lysine tyrosylquinone cross-link (LTQ) is generated by CC condensation of the epsilon-amino group of a lysine with a CC topaquinone produced by oxidation of tyrosine (By similarity). CC -!- PTM: N-glycosylated. N-glycosylation on Asn-458 and Asn-646 may be CC essential for proper folding and secretion; may be composed of a CC fucosylated carbohydrates attached to a trimannose N-linked glycan CC core (By similarity). CC -!- SIMILARITY: Belongs to the lysyl oxidase family. CC -!- SIMILARITY: Contains 4 SRCR domains. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK034957; BAC28894.1; -; mRNA. DR EMBL; AK045019; BAC32186.1; -; mRNA. DR EMBL; AK081898; BAC38364.1; -; mRNA. DR EMBL; AK145323; BAE26367.1; -; mRNA. DR EMBL; AK159386; BAE35041.1; -; mRNA. DR EMBL; AF117951; AAF29046.1; -; mRNA. DR RefSeq; NP_201582.2; NM_033325.2. DR RefSeq; XP_003688982.2; XM_003688934.3. DR RefSeq; XP_006519810.1; XM_006519747.1. DR UniGene; Mm.116714; -. DR ProteinModelPortal; P58022; -. DR SMR; P58022; 71-162, 202-279, 325-429, 438-525. DR IntAct; P58022; 1. DR PhosphoSite; P58022; -. DR PRIDE; P58022; -. DR Ensembl; ENSMUST00000022660; ENSMUSP00000022660; ENSMUSG00000034205. [P58022-1] DR Ensembl; ENSMUST00000100420; ENSMUSP00000097987; ENSMUSG00000034205. [P58022-1] DR GeneID; 100862072; -. DR GeneID; 94352; -. DR KEGG; mmu:100862072; -. DR KEGG; mmu:94352; -. DR UCSC; uc007umn.3; mouse. [P58022-1] DR CTD; 4017; -. DR MGI; MGI:2137913; Loxl2. DR eggNOG; NOG40770; -. DR GeneTree; ENSGT00740000115380; -. DR HOGENOM; HOG000220841; -. DR HOVERGEN; HBG052336; -. DR InParanoid; P58022; -. DR KO; K00280; -. DR OMA; SSCANGM; -. DR OrthoDB; EOG7SN8C6; -. DR TreeFam; TF326061; -. DR ChiTaRS; LOXL2; mouse. DR NextBio; 352317; -. DR PRO; PR:P58022; -. DR Bgee; P58022; -. DR CleanEx; MM_LOXL2; -. DR Genevestigator; P58022; -. DR GO; GO:0005604; C:basement membrane; ISS:UniProtKB. DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell. DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB. DR GO; GO:0016020; C:membrane; IEA:InterPro. DR GO; GO:0005634; C:nucleus; ISS:UniProtKB. DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB. DR GO; GO:0005507; F:copper ion binding; IEA:InterPro. DR GO; GO:0035064; F:methylated histone residue binding; ISS:UniProtKB. DR GO; GO:0070492; F:oligosaccharide binding; ISS:UniProtKB. DR GO; GO:0004720; F:protein-lysine 6-oxidase activity; ISS:UniProtKB. DR GO; GO:0005044; F:scavenger receptor activity; IEA:InterPro. DR GO; GO:0003714; F:transcription corepressor activity; ISS:UniProtKB. DR GO; GO:0030199; P:collagen fibril organization; ISS:UniProtKB. DR GO; GO:0043542; P:endothelial cell migration; ISS:UniProtKB. DR GO; GO:0001935; P:endothelial cell proliferation; ISS:UniProtKB. DR GO; GO:0001837; P:epithelial to mesenchymal transition; ISS:UniProtKB. DR GO; GO:0016570; P:histone modification; ISS:UniProtKB. DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB. DR GO; GO:0032332; P:positive regulation of chondrocyte differentiation; IMP:UniProtKB. DR GO; GO:0018277; P:protein deamination; ISS:UniProtKB. DR GO; GO:0006898; P:receptor-mediated endocytosis; IEA:GOC. DR GO; GO:0046688; P:response to copper ion; ISS:UniProtKB. DR GO; GO:0001666; P:response to hypoxia; IDA:UniProtKB. DR GO; GO:0002040; P:sprouting angiogenesis; ISS:UniProtKB. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR InterPro; IPR001695; Lysyl_oxidase. DR InterPro; IPR019828; Lysyl_oxidase_CS. DR InterPro; IPR001190; SRCR. DR InterPro; IPR017448; Srcr_rcpt-rel. DR Pfam; PF01186; Lysyl_oxidase; 1. DR Pfam; PF00530; SRCR; 4. DR PRINTS; PR00074; LYSYLOXIDASE. DR PRINTS; PR00258; SPERACTRCPTR. DR SMART; SM00202; SR; 4. DR SUPFAM; SSF56487; SSF56487; 4. DR PROSITE; PS00926; LYSYL_OXIDASE; 1. DR PROSITE; PS00420; SRCR_1; 2. DR PROSITE; PS50287; SRCR_2; 4. PE 1: Evidence at protein level; KW Alternative splicing; Basement membrane; Chromatin regulator; KW Chromosome; Complete proteome; Copper; Disulfide bond; KW Extracellular matrix; Glycoprotein; LTQ; Metal-binding; Nucleus; KW Oxidoreductase; Reference proteome; Repeat; Repressor; Secreted; KW Signal; TPQ; Transcription; Transcription regulation. FT SIGNAL 1 25 Potential. FT CHAIN 26 776 Lysyl oxidase homolog 2. FT /FTId=PRO_0000042854. FT DOMAIN 61 162 SRCR 1. FT DOMAIN 191 305 SRCR 2. FT DOMAIN 329 428 SRCR 3. FT DOMAIN 438 546 SRCR 4. FT REGION 550 753 Lysyl-oxidase like (By similarity). FT METAL 628 628 Copper (Potential). FT METAL 630 630 Copper (Potential). FT METAL 632 632 Copper (Potential). FT MOD_RES 691 691 2',4',5'-topaquinone (By similarity). FT CARBOHYD 267 267 N-linked (GlcNAc...) (Potential). FT CARBOHYD 291 291 N-linked (GlcNAc...) (Potential). FT CARBOHYD 458 458 N-linked (GlcNAc...) (Potential). FT CARBOHYD 646 646 N-linked (GlcNAc...) (Potential). FT DISULFID 87 151 By similarity. FT DISULFID 100 161 By similarity. FT DISULFID 131 141 By similarity. FT DISULFID 221 294 By similarity. FT DISULFID 234 304 By similarity. FT DISULFID 268 278 By similarity. FT DISULFID 354 417 By similarity. FT DISULFID 367 427 By similarity. FT DISULFID 398 408 By similarity. FT DISULFID 467 532 By similarity. FT DISULFID 480 545 By similarity. FT DISULFID 514 524 By similarity. FT DISULFID 575 581 By similarity. FT DISULFID 627 675 By similarity. FT DISULFID 659 665 By similarity. FT DISULFID 687 697 By similarity. FT DISULFID 734 748 By similarity. FT CROSSLNK 655 691 Lysine tyrosylquinone (Lys-Tyr) (By FT similarity). FT VAR_SEQ 714 727 VVINPNYEVPESDF -> PSNRVLVRAGQTPY (in FT isoform 2). FT /FTId=VSP_016231. FT VAR_SEQ 728 776 Missing (in isoform 2). FT /FTId=VSP_016232. FT CONFLICT 320 320 K -> E (in Ref. 1; BAC32186). FT CONFLICT 558 560 IVQ -> HEE (in Ref. 2; AAF29046). SQ SEQUENCE 776 AA; 87003 MW; 9DE55C6F37DE5EEF CRC64; MELHFGSCLS GCLALLVLLP SLSLAQYEGW PYQLQYPEYF QQPAPEHHQR QVPSDVVKIQ VRLAGQKRKH NEGRVEVYYE GQWGTVCDDD FSIHAAHVVC RQVGYVEAKS WAASSSYGPG EGPIWLDNIY CTGKESTLAS CSSNGWGVTD CKHTEDVGVV CSEKRIPGFK FDNSLINQIE SLNIQVEDIR IRPILSAFRH RKPVTEGYVE VKEGKAWKQI CNKHWTAKNS HVVCGMFGFP AEKTYNPKAY KTFASRRKLR YWKFSMNCTG TEAHISSCKL GPSVTRDPVK NATCENGQPA VVSCVPSQIF SPDGPSRFRK AYKPEQPLVR LRGGAQVGEG RVEVLKNGEW GTICDDKWDL VSASVVCREL GFGTAKEAIT GSRLGQGIGP IHLNEVQCTG TEKSIIDCKF NTESQGCNHE EDAGVRCNIP IMGFQKKVRL NGGRNPYEGR VEVLTERNGS LVWGTVCGQN WGIVEAMVVC RQLGLGFASN AFQETWYWHG NIFANNVVMS GVKCSGTELS LAHCRHDEEV ACPEGGVRFG AGVACSETAP DLVLNAEIVQ QTAYLEDRPM SLLQCAMEEN CLSASAVHTD PTRGHRRLLR FSSQIHNNGQ SDFRPKNGRH AWIWHDCHRH YHSMEVFTYY DLLSLNGTKV AEGHKASFCL EDTECEGDIQ KSYECANFGE QGITMGCWDM YRHDIDCQWI DITDVPPGDY LFQVVINPNY EVPESDFSNN IMKCRSRYDG YRIWMYNCHV GGAFSEETEQ KFEHFSGLLN NQLSVQ // ID LOXE3_MOUSE Reviewed; 711 AA. AC Q9WV07; B1ASX3; DT 27-JAN-2003, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 2. DT 19-FEB-2014, entry version 97. DE RecName: Full=Hydroperoxide isomerase ALOXE3; DE EC=5.4.4.-; DE AltName: Full=Epidermis-type lipoxygenase 3; DE Short=Epidermal LOX-3; DE Short=e-LOX-3; DE Short=eLOX-3; DE EC=1.13.11.-; GN Name=Aloxe3; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=NMRI; TISSUE=Skin; RX PubMed=10366447; DOI=10.1006/geno.1999.5816; RA Kinzig A., Heidt M., Fuerstenberger G., Marks F., Krieg P.; RT "cDNA cloning, genomic structure and chromosomal localization of a RT novel epidermis-type lipoxygenase."; RL Genomics 58:158-164(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP FUNCTION AS A HYDROPEROXIDE ISOMERASE, AND CATALYTIC ACTIVITY. RX PubMed=17045234; DOI=10.1016/j.abb.2006.09.002; RA Yu Z., Schneider C., Boeglin W.E., Brash A.R.; RT "Human and mouse eLOX3 have distinct substrate specificities: RT implications for their linkage with lipoxygenases in skin."; RL Arch. Biochem. Biophys. 455:188-196(2006). RN [5] RP FUNCTION IN PPARG ACTIVATION. RX PubMed=20530198; DOI=10.1128/MCB.01806-08; RA Hallenborg P., Joergensen C., Petersen R.K., Feddersen S., Araujo P., RA Markt P., Langer T., Furstenberger G., Krieg P., Koppen A., RA Kalkhoven E., Madsen L., Kristiansen K.; RT "Epidermis-type lipoxygenase 3 regulates adipocyte differentiation and RT peroxisome proliferator-activated receptor gamma activity."; RL Mol. Cell. Biol. 30:4077-4091(2010). RN [6] RP FUNCTION IN SKIN BARRIER, AND DISRUPTION PHENOTYPE. RX PubMed=22832496; DOI=10.1038/jid.2012.250; RA Krieg P., Rosenberger S., de Juanes S., Latzko S., Hou J., Dick A., RA Kloz U., van der Hoeven F., Hausser I., Esposito I., Rauh M., RA Schneider H.; RT "Aloxe3 knockout mice reveal a function of epidermal lipoxygenase-3 as RT hepoxilin synthase and its pivotal role in barrier formation."; RL J. Invest. Dermatol. 133:172-180(2013). CC -!- FUNCTION: Non-heme iron-containing lipoxygenase which is atypical CC in that it displays a prominent hydroperoxide isomerase activity CC and a reduced dioxygenase activity compared to other CC lipoxygenases. The hydroperoxide isomerase activity catalyzes the CC isomerization of hydroperoxides, derived from arachidonic and CC linoleic acid by ALOX12B, into hepoxilin-type epoxyalcohols. The CC dioxygenase activity requires a step of activation of the enzyme CC by molecular oxygen. In presence of oxygen, oxygenates CC polyunsaturated fatty acids, including arachidonic acid, to CC produce fatty acid hydroperoxides. In the skin, acts downstream of CC ALOX12B on the linoleate moiety of esterified omega-hydroxyacyl- CC sphingosine (EOS) ceramides to produce an epoxy-ketone derivative, CC a crucial step in the conjugation of omega-hydroxyceramide to CC membrane proteins. Therefore plays a crucial role in the synthesis CC of corneocytes lipid envelope and the establishment of the skin CC barrier to water loss. In parallel, it may have a signaling CC function in barrier formation through the production of hepoxilins CC metabolites. Plays also a role in adipocyte differentiation CC through hepoxilin A3 and hepoxilin B3 production which in turn CC activate PPARG. Through the production of hepoxilins in the spinal CC cord, it may regulate inflammatory tactile allodynia. CC -!- CATALYTIC ACTIVITY: (5Z,8Z,10E,14Z)-(12R)-12-hydroperoxyicosa- CC 5,8,10,14-tetraenoate = (5Z,9E,14Z)-(8R,11R,12R)-8-hydroxy-11,12- CC hydroperoxyicosa-5,9,14-trienoate. CC -!- COFACTOR: Binds 1 iron ion per subunit (By similarity). CC -!- PATHWAY: Lipid metabolism; hydroperoxy eicosatetraenoic acid CC biosynthesis. CC -!- PATHWAY: Lipid metabolism; sphingolipid metabolism. CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- TISSUE SPECIFICITY: Skin specific. CC -!- DISRUPTION PHENOTYPE: Mice die within 5 to 12 hours after birth CC due to defective skin barrier function loosing around 2.5% of body CC weight per hour. Dehydratation through the skin is increased 4 CC folds. The outside-in barrier acquisition is also affected, the CC skin remaining permeable at E18.5 while it is impermeable in wild- CC type mice. The stratum corneum is more tightly packed while other CC layers are unaffected. Hyperkeratosis of the skin is observed but CC it is not associated with defects in epidermal differentiation CC while the ceramide composition of the epidermis is altered with an CC absence of ester-bound ceramides. CC -!- SIMILARITY: Belongs to the lipoxygenase family. CC -!- SIMILARITY: Contains 1 lipoxygenase domain. CC -!- SIMILARITY: Contains 1 PLAT domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; Y14695; CAB46101.1; -; mRNA. DR EMBL; AL645527; CAI35248.1; -; Genomic_DNA. DR EMBL; CH466601; EDL10481.1; -; Genomic_DNA. DR RefSeq; NP_035916.2; NM_011786.2. DR UniGene; Mm.41989; -. DR ProteinModelPortal; Q9WV07; -. DR SMR; Q9WV07; 4-711. DR STRING; 10090.ENSMUSP00000021268; -. DR PhosphoSite; Q9WV07; -. DR PaxDb; Q9WV07; -. DR PRIDE; Q9WV07; -. DR Ensembl; ENSMUST00000021268; ENSMUSP00000021268; ENSMUSG00000020892. DR GeneID; 23801; -. DR KEGG; mmu:23801; -. DR UCSC; uc007jpj.2; mouse. DR CTD; 59344; -. DR MGI; MGI:1345140; Aloxe3. DR eggNOG; NOG69653; -. DR GeneTree; ENSGT00550000074415; -. DR HOGENOM; HOG000234358; -. DR HOVERGEN; HBG005150; -. DR InParanoid; B1ASX3; -. DR OMA; RWKIYAP; -. DR OrthoDB; EOG7V49XR; -. DR TreeFam; TF105320; -. DR UniPathway; UPA00222; -. DR UniPathway; UPA00881; -. DR NextBio; 303419; -. DR PRO; PR:Q9WV07; -. DR ArrayExpress; Q9WV07; -. DR Bgee; Q9WV07; -. DR CleanEx; MM_ALOXE3; -. DR Genevestigator; Q9WV07; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0051120; F:hepoxilin A3 synthase activity; IDA:UniProtKB. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0016702; F:oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen; ISS:UniProtKB. DR GO; GO:0019369; P:arachidonic acid metabolic process; IDA:UniProtKB. DR GO; GO:0046513; P:ceramide biosynthetic process; IMP:UniProtKB. DR GO; GO:0061436; P:establishment of skin barrier; IMP:UniProtKB. DR GO; GO:0045444; P:fat cell differentiation; IMP:UniProtKB. DR GO; GO:0051122; P:hepoxilin biosynthetic process; IDA:UniProtKB. DR GO; GO:0043651; P:linoleic acid metabolic process; IDA:UniProtKB. DR GO; GO:0019372; P:lipoxygenase pathway; ISS:UniProtKB. DR GO; GO:0035357; P:peroxisome proliferator activated receptor signaling pathway; IMP:UniProtKB. DR GO; GO:0019233; P:sensory perception of pain; ISS:UniProtKB. DR Gene3D; 2.60.60.20; -; 1. DR InterPro; IPR008976; Lipase_LipOase. DR InterPro; IPR000907; LipOase. DR InterPro; IPR013819; LipOase_C. DR InterPro; IPR020834; LipOase_CS. DR InterPro; IPR020833; LipOase_Fe_BS. DR InterPro; IPR001885; LipOase_mml. DR InterPro; IPR001024; PLAT/LH2_dom. DR PANTHER; PTHR11771; PTHR11771; 1. DR Pfam; PF00305; Lipoxygenase; 1. DR Pfam; PF01477; PLAT; 1. DR PRINTS; PR00087; LIPOXYGENASE. DR PRINTS; PR00467; MAMLPOXGNASE. DR SMART; SM00308; LH2; 1. DR SUPFAM; SSF48484; SSF48484; 1. DR SUPFAM; SSF49723; SSF49723; 1. DR PROSITE; PS00711; LIPOXYGENASE_1; 1. DR PROSITE; PS00081; LIPOXYGENASE_2; 1. DR PROSITE; PS51393; LIPOXYGENASE_3; 1. DR PROSITE; PS50095; PLAT; 1. PE 1: Evidence at protein level; KW Complete proteome; Cytoplasm; Dioxygenase; Fatty acid metabolism; KW Iron; Isomerase; Lipid metabolism; Metal-binding; Oxidoreductase; KW Reference proteome. FT CHAIN 1 711 Hydroperoxide isomerase ALOXE3. FT /FTId=PRO_0000220692. FT DOMAIN 2 119 PLAT. FT DOMAIN 120 711 Lipoxygenase. FT METAL 408 408 Iron; catalytic (By similarity). FT METAL 413 413 Iron; catalytic (By similarity). FT METAL 588 588 Iron; catalytic (By similarity). FT METAL 592 592 Iron; catalytic (By similarity). FT METAL 711 711 Iron; via carboxylate; catalytic (By FT similarity). FT CONFLICT 138 138 Q -> R (in Ref. 1; CAB46101). FT CONFLICT 341 341 G -> S (in Ref. 1; CAB46101). FT CONFLICT 591 591 V -> F (in Ref. 1; CAB46101). SQ SEQUENCE 711 AA; 80473 MW; 85A75EE2AFF3000E CRC64; MAVYRLCVTT GSYLKAGTLD NIYATLVGTC GESPKQKLDR VGRDFASGSV QKYKVRCEAE LGEILLLRLH KERFAFFCKD PWYCSRICVT APDGSAVHFP CYQWIDGYCT VELRPGTART ICQDSLPLLL DHRKRELQAR QECYRWKIFA PGFPRMVDVS SFQEMESDKK FALTKTVPCA EQDDNSGNRY LPGFPMKIDI PSLLHMEPNI RYSATKTASL IFNALPASFG MKIRGLLDRK GSWKRLDDIR NIFWCHKTFT SEYVTEHWCE DSFFGYQYLN GVNPVMLHCL SSLPSKLPVT NDMVAPLLGP GTCLQTELER GHIFLADYWI LAEAPVHCIN GLQQYVTAPL CLLWLNPQGV LLPLAIQLSQ TPGPESPIFL PTDCELDWLL AKTWVRNSEF LVHENNTHFL CTHLLCEAFS MATLRQLPLC HPVYKLLLPH TRYTLQVNTI ARATLLNPDG LVDKVTSIGR QGLIYLMSTG LAHFTYTDFC LPDSIRARGV LTIPNYHYRD DGLKIWAAIE RFVSEIVSYY YPSDASVQQD CELQAWVGEI FAQAFLGRES SGFPSRLCTP GELVKYLTAI IFNCSAQHAA VNSGQHDFGA WMPNAPSSMR QPPPQTKGDT TMKSYLDTLP EVNTTCRNLL LFWLVSQEPK DQRPLGTYPD EHFTEEAPRQ SIAAFQNCLA QISKDIRERN QSLALPYAYL DPPLIENSVS I // ID LOXL4_MOUSE Reviewed; 757 AA. AC Q924C6; E9PXI3; DT 16-APR-2002, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 2. DT 19-MAR-2014, entry version 103. DE RecName: Full=Lysyl oxidase homolog 4; DE EC=1.4.3.-; DE AltName: Full=Lysyl oxidase-like protein 4; DE AltName: Full=Lysyl oxidase-related protein C; DE Flags: Precursor; GN Name=Loxl4; Synonyms=Loxc; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=11292829; DOI=10.1074/jbc.M100861200; RA Ito H., Akiyama H., Iguchi H., Iyama K., Miyamoto M., Ohsawa K., RA Nakamura T.; RT "Molecular cloning and biological activity of a novel lysyl oxidase- RT related gene expressed in cartilage."; RL J. Biol. Chem. 276:24023-24029(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). CC -!- FUNCTION: May modulate the formation of a collagenous CC extracellular matrix. CC -!- COFACTOR: Copper (By similarity). CC -!- COFACTOR: Contains 1 lysine tyrosylquinone (By similarity). CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space (Potential). CC -!- PTM: The lysine tyrosylquinone cross-link (LTQ) is generated by CC condensation of the epsilon-amino group of a lysine with a CC topaquinone produced by oxidation of tyrosine. CC -!- SIMILARITY: Belongs to the lysyl oxidase family. CC -!- SIMILARITY: Contains 4 SRCR domains. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF338440; AAK71933.1; -; mRNA. DR EMBL; AC124552; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; NP_444313.3; NM_053083.3. DR UniGene; Mm.178767; -. DR ProteinModelPortal; Q924C6; -. DR SMR; Q924C6; 44-133, 158-291, 307-531. DR IntAct; Q924C6; 1. DR PhosphoSite; Q924C6; -. DR PaxDb; Q924C6; -. DR PRIDE; Q924C6; -. DR Ensembl; ENSMUST00000026190; ENSMUSP00000026190; ENSMUSG00000025185. DR Ensembl; ENSMUST00000171432; ENSMUSP00000126686; ENSMUSG00000025185. DR GeneID; 67573; -. DR KEGG; mmu:67573; -. DR UCSC; uc008hns.2; mouse. DR CTD; 84171; -. DR MGI; MGI:1914823; Loxl4. DR eggNOG; NOG40770; -. DR GeneTree; ENSGT00740000115380; -. DR HOGENOM; HOG000220841; -. DR HOVERGEN; HBG052336; -. DR InParanoid; Q924C6; -. DR KO; K00280; -. DR OrthoDB; EOG7SN8C6; -. DR NextBio; 324941; -. DR PRO; PR:Q924C6; -. DR ArrayExpress; Q924C6; -. DR Bgee; Q924C6; -. DR CleanEx; MM_LOXL4; -. DR Genevestigator; Q924C6; -. DR GO; GO:0005576; C:extracellular region; IDA:MGI. DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell. DR GO; GO:0016020; C:membrane; IEA:InterPro. DR GO; GO:0043235; C:receptor complex; ISO:MGI. DR GO; GO:0005507; F:copper ion binding; IEA:InterPro. DR GO; GO:0004720; F:protein-lysine 6-oxidase activity; IDA:MGI. DR GO; GO:0005044; F:scavenger receptor activity; IEA:InterPro. DR GO; GO:0006898; P:receptor-mediated endocytosis; IEA:GOC. DR InterPro; IPR001695; Lysyl_oxidase. DR InterPro; IPR019828; Lysyl_oxidase_CS. DR InterPro; IPR001190; SRCR. DR InterPro; IPR017448; Srcr_rcpt-rel. DR Pfam; PF01186; Lysyl_oxidase; 1. DR Pfam; PF00530; SRCR; 4. DR PRINTS; PR00074; LYSYLOXIDASE. DR PRINTS; PR00258; SPERACTRCPTR. DR SMART; SM00202; SR; 4. DR SUPFAM; SSF56487; SSF56487; 4. DR PROSITE; PS00926; LYSYL_OXIDASE; 1. DR PROSITE; PS00420; SRCR_1; 1. DR PROSITE; PS50287; SRCR_2; 4. PE 2: Evidence at transcript level; KW Complete proteome; Copper; Disulfide bond; Glycoprotein; LTQ; KW Metal-binding; Oxidoreductase; Reference proteome; Repeat; Secreted; KW Signal; TPQ. FT SIGNAL 1 25 Potential. FT CHAIN 26 757 Lysyl oxidase homolog 4. FT /FTId=PRO_0000018536. FT DOMAIN 33 134 SRCR 1. FT DOMAIN 160 288 SRCR 2. FT DOMAIN 312 412 SRCR 3. FT DOMAIN 422 530 SRCR 4. FT REGION 534 737 Lysyl-oxidase like. FT METAL 612 612 Copper (Potential). FT METAL 614 614 Copper (Potential). FT METAL 616 616 Copper (Potential). FT MOD_RES 675 675 2',4',5'-topaquinone (By similarity). FT CARBOHYD 199 199 N-linked (GlcNAc...) (Potential). FT CARBOHYD 630 630 N-linked (GlcNAc...) (Potential). FT DISULFID 59 123 By similarity. FT DISULFID 72 133 By similarity. FT DISULFID 103 113 By similarity. FT DISULFID 192 277 By similarity. FT DISULFID 205 287 By similarity. FT DISULFID 252 262 By similarity. FT DISULFID 337 401 By similarity. FT DISULFID 350 411 By similarity. FT DISULFID 381 391 By similarity. FT DISULFID 451 516 By similarity. FT DISULFID 464 529 By similarity. FT DISULFID 498 508 By similarity. FT DISULFID 559 565 By similarity. FT DISULFID 611 659 By similarity. FT DISULFID 643 649 By similarity. FT DISULFID 671 681 By similarity. FT DISULFID 718 732 By similarity. FT CROSSLNK 639 675 Lysine tyrosylquinone (Lys-Tyr) (By FT similarity). FT CONFLICT 39 39 T -> A (in Ref. 1; AAK71933). FT CONFLICT 120 120 V -> I (in Ref. 1; AAK71933). FT CONFLICT 253 253 L -> F (in Ref. 1; AAK71933). FT CONFLICT 444 444 V -> G (in Ref. 1; AAK71933). FT CONFLICT 615 615 Y -> N (in Ref. 1; AAK71933). SQ SEQUENCE 757 AA; 84779 MW; 45E698867160955C CRC64; MMWPQPPTFS LFLLLLLSQA PSSRPQSSGT KKLRLVGPTD RPEEGRLEVL HQGQWGTVCD DDFALQEATV ACRQLGFESA LTWAHSAKYG QGEGPIWLDN VRCLGTEKTL DQCGSNGWGV SDCRHSEDVG VVCHPRRQHG YHSEKVSNAL GPQGRRLEEV RLKPILASAK RHSPVTEGAV EVRYDGHWRQ VCDQGWTMNN SRVVCGMLGF PSQTSVNSHY YRKVWNLKMK DPKSRLNSLT KKNSFWIHRV DCLGTEPHLA KCQVQVAPGR GKLRPACPGG MHAVVSCVAG PHFRRQKPKP TRKESHAEEL KVRLRSGAQV GEGRVEVLMN RQWGTVCDHR WNLISASVVC RQLGFGSARE ALFGAQLGQG LGPIHLSEVR CRGYERTLGD CLALEGSQNG CQHANDAAVR CNIPDMGFQN KVRLAGGRNS EEGVVEVQVE VNGVPRWGTV CSDHWGLTEA MVTCRQLGLG FANFALKDTW YWQGTPEAKE VVMSGVRCSG TEMALQQCQR HGPVHCSHGP GRFSAGVACM NSAPDLVMNA QLVQETAYLE DRPLSMLYCA HEENCLSKSA DHMDWPYGYR RLLRFSSQIY NLGRADFRPK AGRHSWIWHQ CHRHYHSIEV FTHYDLLTLN GSKVAEGHKA SFCLEDTNCP SGVQRRYACA NFGEQGVAVG CWDTYRHDID CQWVDITDVG PGDYIFQVVV NPTNDVAESD FSNNMIRCRC KYDGQRVWLH NCHTGDSYRA NAELSLEQEQ RLRNNLI // ID LOXL3_MOUSE Reviewed; 754 AA. AC Q9Z175; Q91VN8; Q9JJ39; DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 2. DT 19-MAR-2014, entry version 115. DE RecName: Full=Lysyl oxidase homolog 3; DE EC=1.4.3.-; DE AltName: Full=Lysyl oxidase-like protein 3; DE AltName: Full=Lysyl oxidase-related protein 2; DE Flags: Precursor; GN Name=Loxl3; Synonyms=Lor2; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. RC STRAIN=129/SvJ, and C57BL/6J; TISSUE=Muscle; RX PubMed=9927484; RA Jang W., Hua A., Spilson S.V., Miller W., Roe B.A., Meisler M.H.; RT "Comparative sequence of human and mouse BAC clones from the mnd2 RT region of chromosome 2p13."; RL Genome Res. 9:53-61(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Pituitary; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Mammary tumor; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- COFACTOR: Copper (By similarity). CC -!- COFACTOR: Contains 1 lysine tyrosylquinone (By similarity). CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space (Potential). CC -!- PTM: The lysine tyrosylquinone cross-link (LTQ) is generated by CC condensation of the epsilon-amino group of a lysine with a CC topaquinone produced by oxidation of tyrosine. CC -!- SIMILARITY: Belongs to the lysyl oxidase family. CC -!- SIMILARITY: Contains 4 SRCR domains. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF053368; AAC83205.1; -; mRNA. DR EMBL; AF084363; AAC95338.1; -; Genomic_DNA. DR EMBL; AK030548; BAC27016.1; -; mRNA. DR EMBL; CH466523; EDK99047.1; -; Genomic_DNA. DR EMBL; BC011298; AAH11298.1; -; mRNA. DR RefSeq; NP_038614.2; NM_013586.4. DR UniGene; Mm.380433; -. DR ProteinModelPortal; Q9Z175; -. DR SMR; Q9Z175; 57-145, 186-262, 305-526. DR IntAct; Q9Z175; 1. DR STRING; 10090.ENSMUSP00000000707; -. DR PhosphoSite; Q9Z175; -. DR PRIDE; Q9Z175; -. DR Ensembl; ENSMUST00000000707; ENSMUSP00000000707; ENSMUSG00000000693. DR GeneID; 16950; -. DR KEGG; mmu:16950; -. DR UCSC; uc009clt.1; mouse. DR CTD; 84695; -. DR MGI; MGI:1337004; Loxl3. DR eggNOG; NOG40770; -. DR GeneTree; ENSGT00740000115380; -. DR HOGENOM; HOG000220841; -. DR HOVERGEN; HBG052336; -. DR InParanoid; Q91VN8; -. DR KO; K00280; -. DR OMA; TWYWDSG; -. DR OrthoDB; EOG7SN8C6; -. DR TreeFam; TF326061; -. DR NextBio; 291000; -. DR PRO; PR:Q9Z175; -. DR ArrayExpress; Q9Z175; -. DR Bgee; Q9Z175; -. DR CleanEx; MM_LOXL3; -. DR Genevestigator; Q9Z175; -. DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell. DR GO; GO:0016020; C:membrane; IEA:InterPro. DR GO; GO:0005507; F:copper ion binding; IEA:InterPro. DR GO; GO:0016641; F:oxidoreductase activity, acting on the CH-NH2 group of donors, oxygen as acceptor; IEA:InterPro. DR GO; GO:0005044; F:scavenger receptor activity; IEA:InterPro. DR GO; GO:0001837; P:epithelial to mesenchymal transition; ISS:UniProtKB. DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB. DR GO; GO:0006898; P:receptor-mediated endocytosis; IEA:GOC. DR InterPro; IPR001695; Lysyl_oxidase. DR InterPro; IPR019828; Lysyl_oxidase_CS. DR InterPro; IPR001190; SRCR. DR InterPro; IPR017448; Srcr_rcpt-rel. DR Pfam; PF01186; Lysyl_oxidase; 1. DR Pfam; PF00530; SRCR; 4. DR PRINTS; PR00074; LYSYLOXIDASE. DR PRINTS; PR00258; SPERACTRCPTR. DR SMART; SM00202; SR; 4. DR SUPFAM; SSF56487; SSF56487; 4. DR PROSITE; PS00926; LYSYL_OXIDASE; 1. DR PROSITE; PS00420; SRCR_1; 1. DR PROSITE; PS50287; SRCR_2; 4. PE 2: Evidence at transcript level; KW Complete proteome; Copper; Disulfide bond; Glycoprotein; LTQ; KW Metal-binding; Oxidoreductase; Reference proteome; Repeat; Secreted; KW Signal; TPQ. FT SIGNAL 1 26 Potential. FT CHAIN 27 754 Lysyl oxidase homolog 3. FT /FTId=PRO_0000018534. FT DOMAIN 45 146 SRCR 1. FT DOMAIN 170 283 SRCR 2. FT DOMAIN 308 408 SRCR 3. FT DOMAIN 418 526 SRCR 4. FT REGION 530 733 Lysyl-oxidase like. FT METAL 608 608 Copper (Potential). FT METAL 610 610 Copper (Potential). FT METAL 612 612 Copper (Potential). FT MOD_RES 671 671 2',4',5'-topaquinone (By similarity). FT CARBOHYD 112 112 N-linked (GlcNAc...) (Potential). FT CARBOHYD 267 267 N-linked (GlcNAc...) (Potential). FT CARBOHYD 391 391 N-linked (GlcNAc...) (Potential). FT CARBOHYD 482 482 N-linked (GlcNAc...) (Potential). FT CARBOHYD 626 626 N-linked (GlcNAc...) (Potential). FT DISULFID 71 135 By similarity. FT DISULFID 84 145 By similarity. FT DISULFID 115 125 By similarity. FT DISULFID 202 272 By similarity. FT DISULFID 215 282 By similarity. FT DISULFID 249 259 By similarity. FT DISULFID 333 397 By similarity. FT DISULFID 346 407 By similarity. FT DISULFID 377 387 By similarity. FT DISULFID 447 512 By similarity. FT DISULFID 460 525 By similarity. FT DISULFID 493 503 By similarity. FT DISULFID 555 561 By similarity. FT DISULFID 607 655 By similarity. FT DISULFID 639 645 By similarity. FT DISULFID 667 677 By similarity. FT DISULFID 714 728 By similarity. FT CROSSLNK 635 671 Lysine tyrosylquinone (Lys-Tyr) (By FT similarity). FT CONFLICT 347 347 R -> P (in Ref. 1; AAC83205). SQ SEQUENCE 754 AA; 83740 MW; C3BF60F77696914D CRC64; MRAVSVWYCC PWGLLLLHCL CSFSVGSPSP SISPEKKVGS QGLRFRLAGF PRKPYEGRVE IQRAGEWGTI CDDDFTLQAA HVLCRELGFT EATGWTHSAK YGPGTGRIWL DNLSCRGTEG SVTECASRGW GNSDCTHDED AGVICKDQRL PGFSDSNVIE VEHQLQVEEV RLRPAVEWGR RPLPVTEGLV EVRLPEGWSQ VCDKGWSAHN SHVVCGMLGF PGEKRVNMAF YRMLAQKKQH SFGLHSVACV GTEAHLSLCS LEFYRANDTT RCSGGNPAVV SCVLGPLYAT FTGQKKQQHS KPQGEARVRL KGGAHQGEGR VEVLKAGTWG TVCDRKWDLQ AASVVCRELG FGTAREALSG ARMGQGMGAI HLSEVRCSGQ EPSLWRCPSK NITAEDCSHS QDAGVRCNLP YTGVETKIRL SGGRSRYEGR VEVQIGIPGH LRWGLICGDD WGTLEAMVAC RQLGLGYANH GLQETWYWDS GNVTEVVMSG VRCTGSELSL NQCAHHSSHI TCKKTGTRFT AGVICSETAS DLLLHSALVQ ETAYIEDRPL HMLYCAAEEN CLASSARSAN WPYGHRRLLR FSSQIHNLGR ADFRPKAGRH SWVWHECHGH YHSMDIFTHY DILTPNGTKV AEGHKASFCL EDTECQEDVS KRYECANFGE QGITVGCWDL YRHDIDCQWI DITDVKPGNY ILQVVINPNF EVAESDFTNN AMKCNCKYDG HRIWVHNCHI GDAFSEEANR RFERYPGQTS NQIV // ID LOX15_MOUSE Reviewed; 663 AA. AC P39654; Q4FJY9; Q5F2E3; Q6PHB2; DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot. DT 11-SEP-2007, sequence version 4. DT 19-FEB-2014, entry version 123. DE RecName: Full=Arachidonate 15-lipoxygenase; DE Short=15-LOX; DE EC=1.13.11.33; DE AltName: Full=12/15-lipoxygenase; DE Short=12/15-LO; DE AltName: Full=Arachidonate 12-lipoxygenase, leukocyte-type; DE Short=12-LOX; DE Short=L-12LO; DE EC=1.13.11.31; DE AltName: Full=Arachidonate omega-6 lipoxygenase; GN Name=Alox15; Synonyms=Alox12l; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, AND TISSUE RP SPECIFICITY. RC STRAIN=C57BL/6, and ICR; TISSUE=Spleen; RX PubMed=8188678; RA Chen X.-S., Kurre U., Jenkins N.A., Copeland N.G., Funk C.D.; RT "cDNA cloning, expression, mutagenesis of C-terminal isoleucine, RT genomic structure, and chromosomal localizations of murine 12- RT lipoxygenases."; RL J. Biol. Chem. 269:13979-13987(1994). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Macrophage; RX PubMed=7811740; DOI=10.1016/0005-2760(94)00199-9; RA Freire-Moar J., Alavi-Nassab A., Ng M., Mulkins M., Sigal E.; RT "Cloning and characterization of a murine macrophage lipoxygenase."; RL Biochim. Biophys. Acta 1254:112-116(1995). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Lung; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Ebert L., Muenstermann E., Schatten R., Henze S., Bohn E., RA Mollenhauer J., Wiemann S., Schick M., Korn B.; RT "Cloning of mouse full open reading frames in Gateway(R) system entry RT vector (pDONR201)."; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N, and FVB/N-3; TISSUE=Mammary tumor; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [7] RP DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY. RX PubMed=8798642; DOI=10.1074/jbc.271.39.24278; RA Sun D., Funk C.D.; RT "Disruption of 12/15-lipoxygenase expression in peritoneal RT macrophages. Enhanced utilization of the 5-lipoxygenase pathway and RT diminished oxidation of low density lipoprotein."; RL J. Biol. Chem. 271:24055-24062(1996). RN [8] RP FUNCTION IN MACROPHAGE. RX PubMed=10432118; DOI=10.1038/22572; RA Huang J.T., Welch J.S., Ricote M., Binder C.J., Willson T.M., RA Kelly C., Witztum J.L., Funk C.D., Conrad D., Glass C.K.; RT "Interleukin-4-dependent production of PPAR-gamma ligands in RT macrophages by 12/15-lipoxygenase."; RL Nature 400:378-382(1999). RN [9] RP FUNCTION IN ACTIN REGULATION, AND SUBCELLULAR LOCATION. RX PubMed=11278875; DOI=10.1074/jbc.M011276200; RA Miller Y.I., Chang M.K., Funk C.D., Feramisco J.R., Witztum J.L.; RT "12/15-lipoxygenase translocation enhances site-specific actin RT polymerization in macrophages phagocytosing apoptotic cells."; RL J. Biol. Chem. 276:19431-19439(2001). RN [10] RP FUNCTION IN BONE DEVELOPMENT, AND DISRUPTION PHENOTYPE. RX PubMed=14716014; DOI=10.1126/science.1090985; RA Klein R.F., Allard J., Avnur Z., Nikolcheva T., Rotstein D., RA Carlos A.S., Shea M., Waters R.V., Belknap J.K., Peltz G., RA Orwoll E.S.; RT "Regulation of bone mass in mice by the lipoxygenase gene Alox15."; RL Science 303:229-232(2004). RN [11] RP FUNCTION IN HEALING, AND TISSUE SPECIFICITY. RX PubMed=15708862; DOI=10.1074/jbc.M410638200; RA Gronert K., Maheshwari N., Khan N., Hassan I.R., Dunn M., RA Laniado Schwartzman M.; RT "A role for the mouse 12/15-lipoxygenase pathway in promoting RT epithelial wound healing and host defense."; RL J. Biol. Chem. 280:15267-15278(2005). RN [12] RP FUNCTION IN ER STRESS RESPONSE, DISRUPTION PHENOTYPE, AND INDUCTION. RX PubMed=22215650; DOI=10.1152/ajpendo.00373.2011; RA Cole B.K., Kuhn N.S., Green-Mitchell S.M., Leone K.A., Raab R.M., RA Nadler J.L., Chakrabarti S.K.; RT "12/15-Lipoxygenase signaling in the endoplasmic reticulum stress RT response."; RL Am. J. Physiol. 302:E654-E665(2012). RN [13] RP FUNCTION IN APOPTOTIC CELL CLEARANCE, DISRUPTION PHENOTYPE, AND TISSUE RP SPECIFICITY. RX PubMed=22503541; DOI=10.1016/j.immuni.2012.03.010; RA Uderhardt S., Herrmann M., Oskolkova O.V., Aschermann S., Bicker W., RA Ipseiz N., Sarter K., Frey B., Rothe T., Voll R., Nimmerjahn F., RA Bochkov V.N., Schett G., Kroenke G.; RT "12/15-lipoxygenase orchestrates the clearance of apoptotic cells and RT maintains immunologic tolerance."; RL Immunity 36:834-846(2012). CC -!- FUNCTION: Non-heme iron-containing dioxygenase that catalyzes the CC stereo-specific peroxidation of free and esterified CC polyunsaturated fatty acids generating a spectrum of bioactive CC lipid mediators. Converts arachidonic acid into 12- CC hydroperoxyeicosatetraenoic acid/12-HPETE and 15- CC hydroperoxyeicosatetraenoic acid/15-HPETE. Also converts linoleic CC acid to 13-hydroperoxyoctadecadienoic acid. May also act on (12S)- CC hydroperoxyeicosatetraenoic acid/(12S)-HPETE to produce hepoxilin CC A3. Probably plays an important role in the immune and CC inflammatory responses. Through the oxygenation of membrane-bound CC phosphatidylethanolamine in macrophages may favor clearance of CC apoptotic cells during inflammation by resident macrophages and CC prevent an autoimmune response associated with the clearance of CC apoptotic cells by inflammatory monocytes. In parallel, may CC regulate actin polymerization which is crucial for several CC biological processes, including macrophage function. May also CC regulate macrophage function through regulation of the peroxisome CC proliferator activated receptor signaling pathway. Finally, it is CC also involved in the cellular response to IL13/interleukin-13. CC Beside its role in the immune and inflammatory responses, may play CC a role in epithelial wound healing in the cornea maybe through CC production of lipoxin A4. May also play a role in endoplasmic CC reticulum stress response and the regulation of bone mass. CC -!- CATALYTIC ACTIVITY: Arachidonate + O(2) = (5Z,8Z,10E,14Z)-(12S)- CC 12-hydroperoxyicosa-5,8,10,14-tetraenoate. CC -!- CATALYTIC ACTIVITY: Arachidonate + O(2) = (5Z,8Z,11Z,13E)-(15S)- CC 15-hydroperoxyicosa-5,8,11,13-tetraenoate. CC -!- COFACTOR: Binds 1 iron ion per subunit. CC -!- PATHWAY: Lipid metabolism; hydroperoxy eicosatetraenoic acid CC biosynthesis. CC -!- SUBUNIT: Interacts with PEBP1; in response to IL13/interleukin-13, CC prevents the interaction of PEBP1 with RAF1 to activate the ERK CC signaling cascade (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol. Cell membrane. Lipid CC droplet (By similarity). Note=Translocates from the cytosol to the CC plasma membrane when stimulated by IL13/interleukin-13 and in CC macrophages binding apoptotic cells. CC -!- TISSUE SPECIFICITY: Found in pituitary and pineal glands as well CC as leukocytes, kidney, aorta, small intestine and cornea. Also CC expressed by resident peritoneal macrophages (at protein level). CC -!- INDUCTION: Up-regulated in response to endoplasmic reticulum CC stress (at protein level). CC -!- DISRUPTION PHENOTYPE: Mice are fertile and do not display overt CC phenotype. However, reduced endoplasmic reticulum stress response CC to high-fat diet is observed. Aged mice also display systemic CC autoimmunity, a significant and spontaneous production of several CC forms of autoantibodies being detected and glomerulonephritis and CC deposits of complement and immunoglobulins within their glomeruli CC being observed. They also display reduced bone mass. CC -!- SIMILARITY: Belongs to the lipoxygenase family. CC -!- SIMILARITY: Contains 1 lipoxygenase domain. CC -!- SIMILARITY: Contains 1 PLAT domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U04331; AAA20658.1; -; mRNA. DR EMBL; L34570; AAA64930.1; -; mRNA. DR EMBL; AK142371; BAE25045.1; -; mRNA. DR EMBL; CT010263; CAJ18471.1; -; mRNA. DR EMBL; AL596096; CAI51979.1; -; Genomic_DNA. DR EMBL; BC056625; AAH56625.1; -; mRNA. DR EMBL; BC081546; AAH81546.1; -; mRNA. DR PIR; B54075; B54075. DR RefSeq; NP_033790.3; NM_009660.3. DR UniGene; Mm.4584; -. DR ProteinModelPortal; P39654; -. DR SMR; P39654; 2-663. DR STRING; 10090.ENSMUSP00000019068; -. DR BindingDB; P39654; -. DR PhosphoSite; P39654; -. DR PaxDb; P39654; -. DR PRIDE; P39654; -. DR Ensembl; ENSMUST00000019068; ENSMUSP00000019068; ENSMUSG00000018924. DR GeneID; 11687; -. DR KEGG; mmu:11687; -. DR UCSC; uc007juo.1; mouse. DR CTD; 246; -. DR MGI; MGI:87997; Alox15. DR eggNOG; NOG133298; -. DR GeneTree; ENSGT00550000074415; -. DR HOGENOM; HOG000234358; -. DR HOVERGEN; HBG005150; -. DR InParanoid; P39654; -. DR KO; K00460; -. DR OMA; LTCWKDL; -. DR OrthoDB; EOG7B05CG; -. DR TreeFam; TF105320; -. DR UniPathway; UPA00881; -. DR NextBio; 279331; -. DR PRO; PR:P39654; -. DR ArrayExpress; P39654; -. DR Bgee; P39654; -. DR CleanEx; MM_ALOX15; -. DR Genevestigator; P39654; -. DR GO; GO:0005829; C:cytosol; IDA:UniProtKB. DR GO; GO:0005811; C:lipid particle; ISS:UniProtKB. DR GO; GO:0005634; C:nucleus; IEA:Ensembl. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0004052; F:arachidonate 12-lipoxygenase activity; IDA:UniProtKB. DR GO; GO:0050473; F:arachidonate 15-lipoxygenase activity; IDA:UniProtKB. DR GO; GO:0005506; F:iron ion binding; ISS:UniProtKB. DR GO; GO:0043277; P:apoptotic cell clearance; IMP:UniProtKB. DR GO; GO:0019369; P:arachidonic acid metabolic process; IDA:UniProtKB. DR GO; GO:0030282; P:bone mineralization; IMP:MGI. DR GO; GO:0035963; P:cellular response to interleukin-13; ISS:UniProtKB. DR GO; GO:0051122; P:hepoxilin biosynthetic process; ISS:UniProtKB. DR GO; GO:2001303; P:lipoxin A4 biosynthetic process; IMP:UniProtKB. DR GO; GO:0019372; P:lipoxygenase pathway; IDA:UniProtKB. DR GO; GO:0002820; P:negative regulation of adaptive immune response; IMP:UniProtKB. DR GO; GO:0006646; P:phosphatidylethanolamine biosynthetic process; IMP:UniProtKB. DR GO; GO:0030838; P:positive regulation of actin filament polymerization; IMP:UniProtKB. DR GO; GO:0010811; P:positive regulation of cell-substrate adhesion; ISS:UniProtKB. DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISS:UniProtKB. DR GO; GO:1901074; P:regulation of engulfment of apoptotic cell; IMP:UniProtKB. DR GO; GO:0035358; P:regulation of peroxisome proliferator activated receptor signaling pathway; IMP:UniProtKB. DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IMP:UniProtKB. DR GO; GO:0042060; P:wound healing; IMP:UniProtKB. DR Gene3D; 2.60.60.20; -; 1. DR InterPro; IPR008976; Lipase_LipOase. DR InterPro; IPR000907; LipOase. DR InterPro; IPR013819; LipOase_C. DR InterPro; IPR020834; LipOase_CS. DR InterPro; IPR020833; LipOase_Fe_BS. DR InterPro; IPR001885; LipOase_mml. DR InterPro; IPR001024; PLAT/LH2_dom. DR PANTHER; PTHR11771; PTHR11771; 1. DR Pfam; PF00305; Lipoxygenase; 1. DR Pfam; PF01477; PLAT; 1. DR PRINTS; PR00087; LIPOXYGENASE. DR PRINTS; PR00467; MAMLPOXGNASE. DR SMART; SM00308; LH2; 1. DR SUPFAM; SSF48484; SSF48484; 1. DR SUPFAM; SSF49723; SSF49723; 1. DR PROSITE; PS00711; LIPOXYGENASE_1; 1. DR PROSITE; PS00081; LIPOXYGENASE_2; 1. DR PROSITE; PS51393; LIPOXYGENASE_3; 1. DR PROSITE; PS50095; PLAT; 1. PE 1: Evidence at protein level; KW Cell membrane; Complete proteome; Cytoplasm; Dioxygenase; KW Fatty acid metabolism; Iron; Lipid droplet; Lipid metabolism; KW Membrane; Metal-binding; Oxidoreductase; Reference proteome. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 663 Arachidonate 15-lipoxygenase. FT /FTId=PRO_0000220686. FT DOMAIN 2 115 PLAT. FT DOMAIN 116 663 Lipoxygenase. FT METAL 361 361 Iron; catalytic (By similarity). FT METAL 366 366 Iron; catalytic (By similarity). FT METAL 541 541 Iron; catalytic (By similarity). FT METAL 545 545 Iron; catalytic (By similarity). FT METAL 663 663 Iron; via carboxylate; catalytic (By FT similarity). FT CONFLICT 37 37 K -> N (in Ref. 2; AAA64930). FT CONFLICT 119 119 E -> Q (in Ref. 2; AAA64930). FT CONFLICT 397 397 T -> N (in Ref. 2; AAA64930). FT CONFLICT 568 568 K -> T (in Ref. 4; CAJ18471 and 6; FT AAH56625/AAH81546). SQ SEQUENCE 663 AA; 75445 MW; 0D5412B4502B5799 CRC64; MGVYRIRVST GDSVYAGSNN EVYLWLIGQH GEASLGKLFR PCRNSEAEFK VDVSEYLGPL LFVRVQKWHY LKEDAWFCNW ISVKGPGDQG SEYTFPCYRW VQGTSILNLP EGTGCTVVED SQGLFRNHRE EELEERRSLY RWGNWKDGTI LNVAATSISD LPVDQRFRED KRLEFEASQV LGTMDTVINF PKNTVTCWKS LDDFNYVFKS GHTKMAERVR NSWKEDAFFG YQFLNGANPM VLKRSTCLPA RLVFPPGMEK LQAQLDEELK KGTLFEADFF LLDGIKANVI LCSQQYLAAP LVMLKLQPDG QLLPIAIQLE LPKTGSTPPP IFTPLDPPMD WLLAKCWVRS SDLQLHELQA HLLRGHLVAE VFAVATMRCL PSVHPVFKLL VPHLLYTMEI NVRARSDLIS ERGFFDKVMS TGGGGHLDLL KQAGAFLTYS SLCPPDDLAE RGLLDIDTCF YAKDALQLWQ VMNRYVVGMF DLYYKTDQAV QDDYELQSWC QEITEIGLQG AQDRGFPTSL QSRAQACHFI TMCIFTCTAQ HSSIHLGQLD WFYWVPNAPC TMRLPPPKTK DATMEKLMAT LPNPNQSTLQ INVVWLLGRR QAVMVPLGQH SEEHFPNPEA KAVLKKFREE LAALDKEIEI RNKSLDIPYE YLRPSLVENS VAI // ID LX12E_MOUSE Reviewed; 662 AA. AC P55249; Q91YW6; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 19-FEB-2014, entry version 114. DE RecName: Full=Arachidonate 12-lipoxygenase, epidermal-type; DE Short=12-LOX; DE EC=1.13.11.31; GN Name=Alox12e; Synonyms=Alox12-ps2, Aloxe; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY. RC STRAIN=C57BL/6 X 129/Sv; TISSUE=Epidermis; RX PubMed=8798535; DOI=10.1074/jbc.271.38.23338; RA Funk C.D., Keeney D.S., Oliw E.H., Boeglin W.E., Brash A.R.; RT "Functional expression and cellular localization of a mouse epidermal RT lipoxygenase."; RL J. Biol. Chem. 271:23338-23344(1996). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=129/Sv; TISSUE=Epidermis; RX PubMed=7492614; DOI=10.1016/0005-2760(95)00158-9; RA van Dijk K.W., Steketee K., Havekes L., Frants R., Hofker M.; RT "Genomic and cDNA cloning of a novel mouse lipoxygenase gene."; RL Biochim. Biophys. Acta 1259:4-8(1995). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION. RC STRAIN=NMRI; TISSUE=Skin; RX PubMed=9037187; DOI=10.1016/S0014-5793(96)01517-7; RA Kinzig A., Fuerstenberger G., Mueller F., Vogel S., Mueller-Decker K., RA Mincheva A., Lichter P., Marks F., Krieg P.; RT "Murine epidermal lipoxygenase (Aloxe) encodes a 12-lipoxygenase RT isoform."; RL FEBS Lett. 402:162-166(1997). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS LEU-260; LEU-453 RP AND SER-617. RC STRAIN=FVB/N; TISSUE=Mammary tumor; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: Non-heme iron-containing dioxygenase that probably CC catalyzes the stereo-specific peroxidation of free and esterified CC polyunsaturated fatty acids generating a spectrum of bioactive CC lipid mediators. May preferentially convert arachidonic acid to CC (12S)-hydroperoxyeicosatetraenoic acid/(12S)-HPETE. CC -!- CATALYTIC ACTIVITY: Arachidonate + O(2) = (5Z,8Z,10E,14Z)-(12S)- CC 12-hydroperoxyicosa-5,8,10,14-tetraenoate. CC -!- COFACTOR: Binds 1 iron ion per subunit (By similarity). CC -!- PATHWAY: Lipid metabolism; hydroperoxy eicosatetraenoic acid CC biosynthesis. CC -!- SUBCELLULAR LOCATION: Cytoplasm (Potential). CC -!- TISSUE SPECIFICITY: Expressed in epidermis. CC -!- SIMILARITY: Belongs to the lipoxygenase family. CC -!- SIMILARITY: Contains 1 lipoxygenase domain. CC -!- SIMILARITY: Contains 1 PLAT domain. CC -!- CAUTION: Was originally thought to be an arachidonate 8- CC lipoxygenase and was called LOX8. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U39200; AAC52869.1; -; mRNA. DR EMBL; U24181; AAC52324.1; -; Genomic_DNA. DR EMBL; X99252; CAA67625.1; -; mRNA. DR EMBL; BC013751; AAH13751.1; -; mRNA. DR EMBL; BC051047; AAH51047.1; -; mRNA. DR RefSeq; NP_663717.1; NM_145684.1. DR UniGene; Mm.274093; -. DR ProteinModelPortal; P55249; -. DR SMR; P55249; 4-662. DR PhosphoSite; P55249; -. DR PRIDE; P55249; -. DR Ensembl; ENSMUST00000019051; ENSMUSP00000019051; ENSMUSG00000018907. DR GeneID; 11685; -. DR KEGG; mmu:11685; -. DR UCSC; uc007jun.1; mouse. DR CTD; 11685; -. DR MGI; MGI:1274790; Alox12e. DR eggNOG; NOG133298; -. DR HOGENOM; HOG000234358; -. DR HOVERGEN; HBG005150; -. DR InParanoid; P55249; -. DR KO; K00458; -. DR OMA; KFLGRRQ; -. DR OrthoDB; EOG7B05CG; -. DR TreeFam; TF105320; -. DR UniPathway; UPA00881; -. DR NextBio; 279323; -. DR PRO; PR:P55249; -. DR ArrayExpress; P55249; -. DR Bgee; P55249; -. DR CleanEx; MM_ALOX12E; -. DR Genevestigator; P55249; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004052; F:arachidonate 12-lipoxygenase activity; IEA:UniProtKB-EC. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0019369; P:arachidonic acid metabolic process; IMP:UniProtKB. DR GO; GO:0019372; P:lipoxygenase pathway; IMP:UniProtKB. DR Gene3D; 2.60.60.20; -; 1. DR InterPro; IPR008976; Lipase_LipOase. DR InterPro; IPR000907; LipOase. DR InterPro; IPR013819; LipOase_C. DR InterPro; IPR020834; LipOase_CS. DR InterPro; IPR020833; LipOase_Fe_BS. DR InterPro; IPR001885; LipOase_mml. DR InterPro; IPR001024; PLAT/LH2_dom. DR PANTHER; PTHR11771; PTHR11771; 1. DR Pfam; PF00305; Lipoxygenase; 1. DR Pfam; PF01477; PLAT; 1. DR PRINTS; PR00087; LIPOXYGENASE. DR PRINTS; PR00467; MAMLPOXGNASE. DR SMART; SM00308; LH2; 1. DR SUPFAM; SSF48484; SSF48484; 1. DR SUPFAM; SSF49723; SSF49723; 1. DR PROSITE; PS00711; LIPOXYGENASE_1; 1. DR PROSITE; PS00081; LIPOXYGENASE_2; 1. DR PROSITE; PS51393; LIPOXYGENASE_3; 1. DR PROSITE; PS50095; PLAT; 1. PE 2: Evidence at transcript level; KW Complete proteome; Cytoplasm; Dioxygenase; Fatty acid metabolism; KW Iron; Lipid metabolism; Metal-binding; Oxidoreductase; KW Reference proteome. FT CHAIN 1 662 Arachidonate 12-lipoxygenase, epidermal- FT type. FT /FTId=PRO_0000220688. FT DOMAIN 2 114 PLAT. FT DOMAIN 115 662 Lipoxygenase. FT METAL 360 360 Iron; catalytic (By similarity). FT METAL 365 365 Iron; catalytic (By similarity). FT METAL 540 540 Iron; catalytic (By similarity). FT METAL 662 662 Iron; via carboxylate; catalytic (By FT similarity). FT VARIANT 260 260 V -> L (in strain:FVB/N). FT VARIANT 453 453 V -> L (in strain:FVB/N). FT VARIANT 617 617 P -> S (in strain:FVB/N). FT CONFLICT 619 619 P -> A (in Ref. 2; AAC52324). SQ SEQUENCE 662 AA; 75456 MW; D67768415EE988F7 CRC64; MVKYKILVAT GDSVFAGSAN LVHLWLVGEH GEADLGKQLR PLLGRKTELE VDVPLHLGRL LAVKLRKQKG LLDSDWFCKS ITVQGPGTQG EAFFPCYSWV QGKETICLTE GTALKVTDDT QNLFRKYREQ ELENRRNVYR WGSWKEGLIL PIAGSTERDL PRNQRFMKDK DLDFSLSLVK ELKNFAIKGT LDFVSRVQKL EDYQKVFPHT KTALPERVRG SWKEDALFGY QFLNGANPML LRRSMRLPAR LVLPPGMEDV QTQLEKELKA GSLFEVDFSL LDGVKPNIII FKQQYVTAPL VMLKLQPDGR LLPMVIQLQP PRHGCPPPLL FLPSDPPMAW LLAKIWVRSS DFQLHQLQSH LLRGHLMAEV ISVATMRSLP SLHPIYKLLA PHFRYTMEIN TLARNNLVSE WGIFDLVVST GSGGHVDILQ RATSCLTYRS FCPPDDLADR GLVGVKSSLY AQDALRLWEI ISRYVERMVE LFYRSDTDVK EDPELQVWCR EVTEVGLLGA QDRGFPLSLE SRAELCRFVA MCIFTCTGQH ASTHLGQLDW YAWIPNGPCT MRKPPPISKD VTERDIVDSL PCLQQARMQI TVTKFLGRRQ PVMVALGQHK EEYFSGPRPR DVLKQFQEEL AIMDKEIEVR NASLDLPYEY LRPSLVENSV TI // ID LX12B_MOUSE Reviewed; 701 AA. AC O70582; DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1998, sequence version 1. DT 19-FEB-2014, entry version 107. DE RecName: Full=Arachidonate 12-lipoxygenase, 12R-type; DE Short=12R-LOX; DE Short=12R-lipoxygenase; DE EC=1.13.11.-; DE AltName: Full=Epidermis-type lipoxygenase 12; DE AltName: Full=Epidermis-type lipoxygenase 2; DE Short=e-LOX 2; GN Name=Alox12b; Synonyms=Aloxe2; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY. RC STRAIN=NMRI; TISSUE=Epidermis; RX PubMed=9518531; DOI=10.1016/S0005-2760(97)00214-2; RA Krieg P., Kinzig A., Heidt M., Marks F., Fuerstenberger G.; RT "cDNA cloning of a 8-lipoxygenase and a novel epidermis-type RT lipoxygenase from phorbol ester-treated mouse skin."; RL Biochim. Biophys. Acta 1391:7-12(1998). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE. RC STRAIN=C57BL/6 X SJL; RX PubMed=9837935; DOI=10.1074/jbc.273.50.33540; RA Sun D., McDonnell M., Chen X.-S., Lakkis M.M., Li H., Isaacs S.N., RA Elsea S.H., Patel P.I., Funk C.D.; RT "Human 12(R)-lipoxygenase and the mouse ortholog. Molecular cloning, RT expression, and gene chromosomal assignment."; RL J. Biol. Chem. 273:33540-33547(1998). RN [3] RP FUNCTION IN ARACHIDONATE METABOLISM, CATALYTIC ACTIVITY, REACTION RP MECHANISM, PATHWAY, AND MUTAGENESIS OF PHE-390; GLY-441; ALA-455 AND RP VAL-631. RX PubMed=16129665; DOI=10.1074/jbc.M508260200; RA Meruvu S., Walther M., Ivanov I., Hammarstroem S., Fuerstenberger G., RA Krieg P., Reddanna P., Kuhn H.; RT "Sequence determinants for the reaction specificity of murine (12R)- RT lipoxygenase: targeted substrate modification and site-directed RT mutagenesis."; RL J. Biol. Chem. 280:36633-36641(2005). RN [4] RP FUNCTION IN SKIN BARRIER, AND DISRUPTION PHENOTYPE. RX PubMed=17403930; DOI=10.1083/jcb.200612116; RA Epp N., Fuerstenberger G., Mueller K., de Juanes S., Leitges M., RA Hausser I., Thieme F., Liebisch G., Schmitz G., Krieg P.; RT "12R-lipoxygenase deficiency disrupts epidermal barrier function."; RL J. Cell Biol. 177:173-182(2007). RN [5] RP FUNCTION IN SKIN BARRIER, AND PATHWAY. RX PubMed=17429434; DOI=10.1038/sj.jid.5700825; RA Moran J.L., Qiu H., Turbe-Doan A., Yun Y., Boeglin W.E., Brash A.R., RA Beier D.R.; RT "A mouse mutation in the 12R-lipoxygenase, Alox12b, disrupts formation RT of the epidermal permeability barrier."; RL J. Invest. Dermatol. 127:1893-1897(2007). RN [6] RP FUNCTION IN SKIN BARRIER, AND DISRUPTION PHENOTYPE. RX PubMed=21558561; DOI=10.1074/jbc.M111.251496; RA Zheng Y., Yin H., Boeglin W.E., Elias P.M., Crumrine D., Beier D.R., RA Brash A.R.; RT "Lipoxygenases mediate the effect of essential fatty acid in skin RT barrier formation: a proposed role in releasing omega-hydroxyceramide RT for construction of the corneocyte lipid envelope."; RL J. Biol. Chem. 286:24046-24056(2011). CC -!- FUNCTION: Non-heme iron-containing dioxygenase that catalyzes the CC stereo-specific peroxidation of free and esterified CC polyunsaturated fatty acids generating a spectrum of bioactive CC lipid mediators. Mainly converts arachidonic acid to (12R)- CC hydroperoxyeicosatetraenoic acid/(12R)-HPETE and minor CC stereoisomers. In the skin, acts upstream of ALOXE3 on the CC lineolate moiety of esterified omega-hydroxyacyl-sphingosine (EOS) CC ceramides to produce an epoxy-ketone derivative, a crucial step in CC the conjugation of omega-hydroxyceramide to membrane proteins. CC Therefore plays a crucial role in the synthesis of corneocytes CC lipid envelope and the establishment of the skin barrier to water CC loss. May also play a role in the regulation of the expression of CC airway mucins. CC -!- CATALYTIC ACTIVITY: Arachidonate + O(2) = (5Z,8Z,10E,14Z)-(12R)- CC 12-hydroperoxyicosa-5,8,10,14-tetraenoate. CC -!- COFACTOR: Binds 1 iron ion per subunit (By similarity). CC -!- PATHWAY: Lipid metabolism; hydroperoxy eicosatetraenoic acid CC biosynthesis. CC -!- PATHWAY: Lipid metabolism; sphingolipid metabolism. CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- TISSUE SPECIFICITY: Expressed in skin epidermis and other CC stratified epithelia including tongue and forestomach. Low levels CC of expression are found in trachea, brain and lung. Not expressed CC in intestine, liver, kidney, adipose tissue, muscle or CC hematopoietic cells. CC -!- DEVELOPMENTAL STAGE: In the embryo, expression begins at day 15.5. CC -!- DISRUPTION PHENOTYPE: Mice die within 3 to 5 hours after birth due CC to defective skin barrier function loosing around 30% of body CC weight within 3 hours. Dehydration through the skin is increased 8 CC folds. The outside-in barrier acquisition is also affected, the CC skin remaining permeable at E18.5 while it is impermeable in wild- CC type mice. The stratum corneum is more tightly packed while other CC layers are unaffected. Processing of filaggrin/FG is aberrant and CC the skin displays structural abnormalities. The cornified envelope CC is more fragile and the ceramide composition of the epidermis is CC altered. CC -!- MISCELLANEOUS: Mummy, a recessive ethylnitrosurea-induced mutant CC has a nonsense mutation in the catalytic domain of Lox12b, CC resulting in truncation of the protein by 68 amino acids. The CC affected mice are born with red, shiny skin that dessicates and CC appears scaly. They probably die of dehydration like mice with CC targeted disruption of the gene (PubMed:17429434). CC -!- SIMILARITY: Belongs to the lipoxygenase family. CC -!- SIMILARITY: Contains 1 lipoxygenase domain. CC -!- SIMILARITY: Contains 1 PLAT domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; Y14334; CAA74714.1; -; mRNA. DR EMBL; AF059251; AAC79681.1; -; mRNA. DR RefSeq; NP_033789.1; NM_009659.2. DR UniGene; Mm.340329; -. DR ProteinModelPortal; O70582; -. DR SMR; O70582; 2-701. DR PhosphoSite; O70582; -. DR PRIDE; O70582; -. DR Ensembl; ENSMUST00000036424; ENSMUSP00000035250; ENSMUSG00000032807. DR GeneID; 11686; -. DR KEGG; mmu:11686; -. DR UCSC; uc007jpk.1; mouse. DR CTD; 242; -. DR MGI; MGI:1274782; Alox12b. DR eggNOG; NOG69653; -. DR HOGENOM; HOG000234358; -. DR HOVERGEN; HBG005150; -. DR InParanoid; O70582; -. DR KO; K08021; -. DR OMA; YHFPAYQ; -. DR OrthoDB; EOG7V49XR; -. DR TreeFam; TF105320; -. DR UniPathway; UPA00222; -. DR UniPathway; UPA00881; -. DR NextBio; 279327; -. DR PRO; PR:O70582; -. DR ArrayExpress; O70582; -. DR Bgee; O70582; -. DR CleanEx; MM_ALOX12B; -. DR Genevestigator; O70582; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004052; F:arachidonate 12-lipoxygenase activity; IDA:UniProtKB. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:1990136; F:linoleate 9S-lipoxygenase activity; IDA:UniProtKB. DR GO; GO:0019369; P:arachidonic acid metabolic process; IDA:UniProtKB. DR GO; GO:0046513; P:ceramide biosynthetic process; IMP:UniProtKB. DR GO; GO:0061436; P:establishment of skin barrier; IMP:UniProtKB. DR GO; GO:0051122; P:hepoxilin biosynthetic process; ISS:UniProtKB. DR GO; GO:0043651; P:linoleic acid metabolic process; IDA:UniProtKB. DR GO; GO:0019372; P:lipoxygenase pathway; ISS:UniProtKB. DR GO; GO:0010628; P:positive regulation of gene expression; ISS:UniProtKB. DR GO; GO:0043410; P:positive regulation of MAPK cascade; ISS:UniProtKB. DR GO; GO:0070257; P:positive regulation of mucus secretion; ISS:UniProtKB. DR GO; GO:0006497; P:protein lipidation; IMP:UniProtKB. DR Gene3D; 2.60.60.20; -; 1. DR InterPro; IPR008976; Lipase_LipOase. DR InterPro; IPR000907; LipOase. DR InterPro; IPR013819; LipOase_C. DR InterPro; IPR020834; LipOase_CS. DR InterPro; IPR020833; LipOase_Fe_BS. DR InterPro; IPR001885; LipOase_mml. DR InterPro; IPR001024; PLAT/LH2_dom. DR PANTHER; PTHR11771; PTHR11771; 1. DR Pfam; PF00305; Lipoxygenase; 1. DR Pfam; PF01477; PLAT; 1. DR PRINTS; PR00087; LIPOXYGENASE. DR PRINTS; PR00467; MAMLPOXGNASE. DR SMART; SM00308; LH2; 1. DR SUPFAM; SSF48484; SSF48484; 1. DR SUPFAM; SSF49723; SSF49723; 1. DR PROSITE; PS00711; LIPOXYGENASE_1; 1. DR PROSITE; PS00081; LIPOXYGENASE_2; 1. DR PROSITE; PS51393; LIPOXYGENASE_3; 1. DR PROSITE; PS50095; PLAT; 1. PE 1: Evidence at protein level; KW Complete proteome; Cytoplasm; Dioxygenase; Fatty acid metabolism; KW Iron; Lipid metabolism; Metal-binding; Oxidoreductase; Polymorphism; KW Reference proteome. FT CHAIN 1 701 Arachidonate 12-lipoxygenase, 12R-type. FT /FTId=PRO_0000220690. FT DOMAIN 2 119 PLAT. FT DOMAIN 120 701 Lipoxygenase. FT METAL 398 398 Iron; catalytic (By similarity). FT METAL 403 403 Iron; catalytic (By similarity). FT METAL 578 578 Iron; catalytic (By similarity). FT METAL 582 582 Iron; catalytic (By similarity). FT METAL 701 701 Iron; via carboxylate; catalytic (By FT similarity). FT VARIANT 9 9 A -> V (in strain: C57BL/6 X SJL). FT VARIANT 351 351 M -> V (in strain: C57BL/6 X SJL). FT VARIANT 361 361 T -> I (in strain: C57BL/6 X SJL). FT MUTAGEN 390 390 F->A: Reduced enzymatic activity and FT altered stereoselectivity of the FT oxygenation reaction. FT MUTAGEN 390 390 F->W: Loss of enzymatic activity. FT MUTAGEN 441 441 G->A: Reduced enzymatic activity and FT changed stereoselectivity of the FT oxygenation reaction. FT MUTAGEN 441 441 G->V: Loss of enzymatic activity. FT MUTAGEN 455 455 A->I,W: Reduced enzymatic activity and FT altered stereoselectivity of the FT oxygenation reaction. FT MUTAGEN 631 631 V->A,G: Increased enzymatic activity and FT changed stereoselectivity of the FT oxygenation reaction to produce (11R)- FT HPETE preferentially instead of (12R)- FT HPETE. SQ SEQUENCE 701 AA; 80578 MW; FAE3A3B8D2AA142E CRC64; MATYKVKVAT GTDFFSGTLD SISLTIVGTQ GESHKQRLNH FGRDFATGAV DDYTVQCQQD LGELIIIRLH KEPHSFLAKD PWYCNYVQIC APDCRVYHFP AYQWMDGYET LALREATGKI TADDTLPILL EHRQEEIRAK KDFYHWRVFV PGLPNYVDIP SYHPPPRRCR NPNRPEWDGY IPGFPILINI KATRFLNSNL RFSFVKTASF FYRLGPMALA FKLRGLVDRK RSWKRLKDIK NIFPATKSVV SEYVAEHWTE DSFFGYQYLN GINPGLIRRC TQIPDKFPVT DEMVAPFLGE GTCLQAELER GNIYLADYRI LDGIPTVELN GQQQHHCAPM CLLHFGPDGN MMPIAIQLSQ TPGPDCPIFL PNDSEWDWLL AKTWVRYAEF YSHEAVAHLL ESHLIGEAFC LALLRNLPMC HPLYKLLIPH TRYNVQINSI GRALLLNKGG LSARAMSLGL EGFAQVMVRG LSELTYKSLC IPNDFVERGV QDLPGYYFRD DSLAVWYAME RYVTEIITYY YPNDAAVEGD PELQCWVQEI FKECLLGRES SGFPTCLRTI PELIEYVTMV MYTCSARHAA VNSGQLEYTS WMPNFPSSMR NPPMQTKGLT TLQTYMDTLP DVKTTCIVLL VLWTLCREPD DRRPLGHFPD IHFVEEGPRR SIEAFRQNLN QISHNIRQRN KCLTLPYYYL DPVLIENSIS I // ID LYOX_MOUSE Reviewed; 411 AA. AC P28301; DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-1992, sequence version 1. DT 19-MAR-2014, entry version 118. DE RecName: Full=Protein-lysine 6-oxidase; DE EC=1.4.3.13; DE AltName: Full=Lysyl oxidase; DE AltName: Full=Ras excision protein; DE Flags: Precursor; GN Name=Lox; Synonyms=Rrg; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=1678898; DOI=10.1126/science.1678898; RA Kenyon K., Contente S., Trackman P.C., Tang J., Kagan H.M., RA Friedman R.M.; RT "Lysyl oxidase and rrg messenger RNA."; RL Science 253:802-802(1991). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=NIH Swiss; RX PubMed=8100214; DOI=10.1006/geno.1993.1202; RA Contente S., Csiszar K., Kenyon K., Friedman R.M.; RT "Structure of the mouse lysyl oxidase gene."; RL Genomics 16:395-400(1993). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N-3; TISSUE=Mammary gland; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP ROLE OF PROPEPTIDE. RX PubMed=16251195; DOI=10.1074/jbc.M506832200; RA Thomassin L., Werneck C.C., Broekelmann T.J., Gleyzal C., RA Hornstra I.K., Mecham R.P., Sommer P.; RT "The Pro-regions of lysyl oxidase and lysyl oxidase-like 1 are RT required for deposition onto elastic fibers."; RL J. Biol. Chem. 280:42848-42855(2005). RN [5] RP PROTEOLYTIC CLEAVAGE BY BMP1. RX PubMed=20181949; DOI=10.1074/jbc.M109.088864; RA Maruhashi T., Kii I., Saito M., Kudo A.; RT "Interaction between periostin and BMP-1 promotes proteolytic RT activation of lysyl oxidase."; RL J. Biol. Chem. 285:13294-13303(2010). CC -!- FUNCTION: Responsible for the post-translational oxidative CC deamination of peptidyl lysine residues in precursors to fibrous CC collagen and elastin. CC -!- FUNCTION: Regulator of Ras expression. May play a role in tumor CC suppression. CC -!- CATALYTIC ACTIVITY: Peptidyl-L-lysyl-peptide + O(2) + H(2)O = CC peptidyl-allysyl-peptide + NH(3) + H(2)O(2). CC -!- COFACTOR: Copper (By similarity). CC -!- COFACTOR: Contains 1 lysine tyrosylquinone (By similarity). CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space. CC -!- PTM: The lysine tyrosylquinone cross-link (LTQ) is generated by CC condensation of the epsilon-amino group of a lysine with a CC topaquinone produced by oxidation of tyrosine. CC -!- PTM: Proteolytically activated by BMP1. CC -!- MISCELLANEOUS: The propeptide plays a role in directing the CC deposition of this enzyme to elastic fibers, via interaction with CC tropoelastin. CC -!- SIMILARITY: Belongs to the lysyl oxidase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M65142; AAA19032.1; -; mRNA. DR EMBL; M65143; AAA20185.1; -; mRNA. DR EMBL; L04262; AAA99899.1; -; Genomic_DNA. DR EMBL; L04263; AAA99899.1; JOINED; Genomic_DNA. DR EMBL; L04264; AAA99899.1; JOINED; Genomic_DNA. DR EMBL; BC018439; AAH18439.1; -; mRNA. DR PIR; A47005; OXMSL. DR RefSeq; NP_001273110.1; NM_001286181.1. DR RefSeq; NP_001273111.1; NM_001286182.1. DR RefSeq; NP_034858.2; NM_010728.3. DR UniGene; Mm.172; -. DR UniGene; Mm.488403; -. DR BioGrid; 201191; 3. DR IntAct; P28301; 4. DR MINT; MINT-1549500; -. DR PhosphoSite; P28301; -. DR PaxDb; P28301; -. DR PRIDE; P28301; -. DR Ensembl; ENSMUST00000025409; ENSMUSP00000025409; ENSMUSG00000024529. DR Ensembl; ENSMUST00000171470; ENSMUSP00000129247; ENSMUSG00000024529. DR GeneID; 16948; -. DR KEGG; mmu:16948; -. DR UCSC; uc008exe.1; mouse. DR CTD; 4015; -. DR MGI; MGI:96817; Lox. DR eggNOG; NOG69196; -. DR HOGENOM; HOG000234262; -. DR HOVERGEN; HBG000226; -. DR InParanoid; P28301; -. DR KO; K00277; -. DR OMA; YSDDNPY; -. DR OrthoDB; EOG7SN8C6; -. DR TreeFam; TF326061; -. DR NextBio; 290992; -. DR PRO; PR:P28301; -. DR ArrayExpress; P28301; -. DR Bgee; P28301; -. DR CleanEx; MM_LOX; -. DR Genevestigator; P28301; -. DR GO; GO:0005581; C:collagen; IDA:MGI. DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell. DR GO; GO:0005634; C:nucleus; IEA:Ensembl. DR GO; GO:0005507; F:copper ion binding; IEA:Ensembl. DR GO; GO:0004720; F:protein-lysine 6-oxidase activity; IDA:MGI. DR GO; GO:0001568; P:blood vessel development; IMP:MGI. DR GO; GO:0030199; P:collagen fibril organization; IMP:MGI. DR GO; GO:0048251; P:elastic fiber assembly; IMP:MGI. DR GO; GO:0030324; P:lung development; IMP:MGI. DR GO; GO:0042493; P:response to drug; IEA:Ensembl. DR GO; GO:0048545; P:response to steroid hormone; IEA:Ensembl. DR GO; GO:0042060; P:wound healing; IEA:Ensembl. DR InterPro; IPR001695; Lysyl_oxidase. DR InterPro; IPR019828; Lysyl_oxidase_CS. DR Pfam; PF01186; Lysyl_oxidase; 1. DR PRINTS; PR00074; LYSYLOXIDASE. DR PROSITE; PS00926; LYSYL_OXIDASE; 1. PE 1: Evidence at protein level; KW Complete proteome; Copper; Disulfide bond; Glycoprotein; LTQ; KW Metal-binding; Oxidoreductase; Reference proteome; Secreted; Signal; KW TPQ. FT SIGNAL 1 21 Potential. FT PROPEP 22 162 By similarity. FT /FTId=PRO_0000018522. FT CHAIN 163 411 Protein-lysine 6-oxidase. FT /FTId=PRO_0000018523. FT REGION 207 411 Lysyl-oxidase like. FT METAL 286 286 Copper (Potential). FT METAL 288 288 Copper (Potential). FT METAL 290 290 Copper (Potential). FT MOD_RES 349 349 2',4',5'-topaquinone (By similarity). FT CARBOHYD 91 91 N-linked (GlcNAc...) (Potential). FT CARBOHYD 138 138 N-linked (GlcNAc...) (Potential). FT DISULFID 232 238 By similarity. FT DISULFID 285 334 By similarity. FT DISULFID 318 324 By similarity. FT DISULFID 345 355 By similarity. FT DISULFID 392 406 By similarity. FT CROSSLNK 314 349 Lysine tyrosylquinone (Lys-Tyr) (By FT similarity). FT CONFLICT 333 333 A -> G (in Ref. 2; AAA99899). SQ SEQUENCE 411 AA; 46701 MW; DBC0563A9C0AEB52 CRC64; MRFAWAVLLL GPLQLCPLLR CAPQTPREPP AAPGAWRQTI QWENNGQVFS LLSLGAQYQP QRRRDPSATA RRPDGDAASQ PRTPILLLRD NRTASTRART PSPSGVAAGR PRPAARHWFQ AGFSPSGARD GASRRAANRT ASPQPPQLSN LRPPSHIDRM VGDDPYNPYK YSDDNPYYNY YDTYERPRPG SRNRPGYGTG YFQYGLPDLV PDPYYIQAST YVQKMSMYNL RCAAEENCLA SSAYRADVRD YDHRVLLRFP QRVKNQGTSD FLPSRPRYSW EWHSCHQHYH SMDEFSHYDL LDANTQRRVA EGHKASFCLE DTSCDYGYHR RFACTAHTQG LSPGCYDTYA ADIDCQWIDI TDVQPGNYIL KVSVNPSYLV PESDYTNNVV RCDIRYTGHH AYASGCTISP Y // ID M2GD_MOUSE Reviewed; 869 AA. AC Q9DBT9; B1B1D0; Q8R1S7; DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 19-MAR-2014, entry version 97. DE RecName: Full=Dimethylglycine dehydrogenase, mitochondrial; DE EC=1.5.8.4; DE AltName: Full=ME2GLYDH; DE Flags: Precursor; GN Name=Dmgdh; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Lung; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 237-869. RC TISSUE=Liver; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-141; LYS-310; LYS-312; RP LYS-427; LYS-469; LYS-516; LYS-648; LYS-786 AND LYS-788, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., RA Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). RN [5] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-107; LYS-141; LYS-161; RP LYS-216; LYS-328; LYS-353; LYS-427; LYS-469; LYS-516; LYS-648; LYS-757 RP AND LYS-786, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Liver; RX PubMed=23576753; DOI=10.1073/pnas.1302961110; RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., RA Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.; RT "Label-free quantitative proteomics of the lysine acetylome in RT mitochondria identifies substrates of SIRT3 in metabolic pathways."; RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013). CC -!- CATALYTIC ACTIVITY: N,N-dimethylglycine + electron-transfer CC flavoprotein + H(2)O = sarcosine + formaldehyde + reduced CC electron-transfer flavoprotein. CC -!- COFACTOR: Binds 1 FAD covalently per monomer (By similarity). CC -!- PATHWAY: Amine and polyamine degradation; betaine degradation; CC sarcosine from betaine: step 2/2. CC -!- SUBCELLULAR LOCATION: Mitochondrion (By similarity). CC -!- SIMILARITY: Belongs to the GcvT family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK004755; BAB23536.1; -; mRNA. DR EMBL; CT030023; CAO77970.1; -; Genomic_DNA. DR EMBL; AC131739; CAO77970.1; JOINED; Genomic_DNA. DR EMBL; BC024126; AAH24126.1; -; mRNA. DR RefSeq; NP_083048.1; NM_028772.3. DR UniGene; Mm.21789; -. DR ProteinModelPortal; Q9DBT9; -. DR SMR; Q9DBT9; 44-851. DR IntAct; Q9DBT9; 2. DR MINT; MINT-1840379; -. DR PhosphoSite; Q9DBT9; -. DR PaxDb; Q9DBT9; -. DR PRIDE; Q9DBT9; -. DR Ensembl; ENSMUST00000048001; ENSMUSP00000039663; ENSMUSG00000042102. DR GeneID; 74129; -. DR KEGG; mmu:74129; -. DR UCSC; uc007rll.1; mouse. DR CTD; 29958; -. DR MGI; MGI:1921379; Dmgdh. DR eggNOG; COG0665; -. DR GeneTree; ENSGT00530000063120; -. DR HOGENOM; HOG000251716; -. DR HOVERGEN; HBG081945; -. DR InParanoid; B1B1D0; -. DR KO; K00315; -. DR OMA; AGFWARE; -. DR OrthoDB; EOG7CCBQB; -. DR TreeFam; TF314735; -. DR UniPathway; UPA00291; UER00433. DR NextBio; 339854; -. DR PRO; PR:Q9DBT9; -. DR Bgee; Q9DBT9; -. DR CleanEx; MM_DMGDH; -. DR Genevestigator; Q9DBT9; -. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR GO; GO:0004047; F:aminomethyltransferase activity; IEA:InterPro. DR GO; GO:0047865; F:dimethylglycine dehydrogenase activity; IEA:UniProtKB-EC. DR GO; GO:0006579; P:amino-acid betaine catabolic process; IEA:UniProtKB-UniPathway. DR GO; GO:0006546; P:glycine catabolic process; IEA:InterPro. DR GO; GO:0032259; P:methylation; IEA:GOC. DR Gene3D; 3.30.1360.120; -; 2. DR InterPro; IPR006076; FAD-dep_OxRdtase. DR InterPro; IPR013977; GCV_T_C. DR InterPro; IPR006222; GCV_T_N. DR InterPro; IPR027266; TrmE/GcvT_dom1. DR Pfam; PF01266; DAO; 1. DR Pfam; PF01571; GCV_T; 1. DR Pfam; PF08669; GCV_T_C; 1. PE 1: Evidence at protein level; KW Acetylation; Complete proteome; FAD; Flavoprotein; Mitochondrion; KW Oxidoreductase; Reference proteome; Transit peptide. FT TRANSIT 1 43 Mitochondrion (Potential). FT CHAIN 44 869 Dimethylglycine dehydrogenase, FT mitochondrial. FT /FTId=PRO_0000010768. FT MOD_RES 84 84 Tele-8alpha-FAD histidine (By FT similarity). FT MOD_RES 107 107 N6-acetyllysine. FT MOD_RES 141 141 N6-acetyllysine; alternate. FT MOD_RES 141 141 N6-succinyllysine; alternate. FT MOD_RES 161 161 N6-acetyllysine. FT MOD_RES 216 216 N6-acetyllysine. FT MOD_RES 310 310 N6-succinyllysine. FT MOD_RES 312 312 N6-succinyllysine. FT MOD_RES 328 328 N6-acetyllysine. FT MOD_RES 353 353 N6-acetyllysine. FT MOD_RES 427 427 N6-acetyllysine; alternate. FT MOD_RES 427 427 N6-succinyllysine; alternate. FT MOD_RES 469 469 N6-acetyllysine; alternate. FT MOD_RES 469 469 N6-succinyllysine; alternate. FT MOD_RES 516 516 N6-acetyllysine; alternate. FT MOD_RES 516 516 N6-succinyllysine; alternate. FT MOD_RES 648 648 N6-acetyllysine; alternate. FT MOD_RES 648 648 N6-succinyllysine; alternate. FT MOD_RES 757 757 N6-acetyllysine. FT MOD_RES 786 786 N6-acetyllysine; alternate. FT MOD_RES 786 786 N6-succinyllysine; alternate. FT MOD_RES 788 788 N6-succinyllysine. FT CONFLICT 758 758 T -> A (in Ref. 3; AAH24126). SQ SEQUENCE 869 AA; 97255 MW; D415C743105A0547 CRC64; MLRPGALRLR GLALRGSPRR PSSAGLREGQ ESPASPPEWK DRAETVIIGG GCVGVSLAYH LAKAGMRDVV LMEKSELTAG STWHAAGLTT YFHPGINLKK IHYDSIKLYE RLEEETGQVV GFHQPGSIRL ATTPVRVDEF KYQMTRTNWH ATEQYIIEPE KIHELFPLLN MNKILAGLYN PGDGHIDPYS LTMALAAGAR KYGALLKYPA PVTSLKPRPD GTWDVETPQG SVRANRIVNA AGFWAREVGK MIGLDHPLIP VQHQYVVTST IPEVKALKRE LPVLRDLEGS YYLRQERDGL LFGPYESQEK MKLQASWVTH GVPPGFGKEL FESDLDRISD HLEAAMEMIP VLKKADIINV VNGPITYSPD ILPMVGPHQG VRNYWVATGF GYGIIHAGGV GKFLSDWILH GEPPFDLIEL DPNRYGKWTT TQYTEAKARE SYGFNNIVGY PKEERFAGRP TQRVSGLYKT LKSKCSMGFH AGWEQPHWFY KPGQDTQYRP SFRRTNWFEP VGSEYKQVMQ RVGVIDLSPF GKFNIKGRDS TQLLDHLFAN VIPKVGFTNI SHMLTPRGRV YAELTVSQQS PGEFLLITGS GSELHDLRWI EEAAFRGGYD VEIQNITDEF GVLGVAGPYA RRVLQKLTSE DLSDDAFKFL QTKSFNISDI PVTAIRISYT GELGWELYHR REDSATLYER IMSAGQEEGI GDFGTYALNA LRLEKAFRAW GSEMNCDTNP LEAGLEYFVK LNKPADFIGK QALKQIKTEG LKRRLVCLTV ATDDVDPEGN ESIWYKGKVV GNTTSGSYSY SIQKSLAFAY VPVQLSEVGQ QVEVELLGKN YPATIIQEPL VLTEPARARL QKDGKKTNLE KGPSRTTKL // ID MAON_MOUSE Reviewed; 604 AA. AC Q8BMF3; Q499F4; DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 2. DT 19-MAR-2014, entry version 94. DE RecName: Full=NADP-dependent malic enzyme, mitochondrial; DE Short=NADP-ME; DE EC=1.1.1.40; DE AltName: Full=Malic enzyme 3; DE Flags: Precursor; GN Name=Me3; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Olfactory bulb; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=CD-1; TISSUE=Neural stem cell; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP PROTEIN SEQUENCE OF 71-92 AND 481-506, AND MASS SPECTROMETRY. RC TISSUE=Hippocampus; RA Lubec G., Klug S.; RL Submitted (MAR-2007) to UniProtKB. CC -!- CATALYTIC ACTIVITY: (S)-malate + NADP(+) = pyruvate + CO(2) + CC NADPH. CC -!- CATALYTIC ACTIVITY: Oxaloacetate = pyruvate + CO(2). CC -!- COFACTOR: Divalent metal cations. Prefers magnesium or manganese CC (By similarity). CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix (By similarity). CC -!- SIMILARITY: Belongs to the malic enzymes family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK032196; BAC27751.1; -; mRNA. DR EMBL; BC099935; AAH99935.1; -; mRNA. DR RefSeq; NP_852072.2; NM_181407.4. DR RefSeq; XP_006507252.1; XM_006507189.1. DR RefSeq; XP_006507253.1; XM_006507190.1. DR UniGene; Mm.334011; -. DR ProteinModelPortal; Q8BMF3; -. DR SMR; Q8BMF3; 48-602. DR IntAct; Q8BMF3; 1. DR MINT; MINT-4111524; -. DR STRING; 10090.ENSMUSP00000032856; -. DR PhosphoSite; Q8BMF3; -. DR PaxDb; Q8BMF3; -. DR PRIDE; Q8BMF3; -. DR Ensembl; ENSMUST00000032856; ENSMUSP00000032856; ENSMUSG00000030621. DR GeneID; 109264; -. DR KEGG; mmu:109264; -. DR UCSC; uc009igd.1; mouse. DR CTD; 10873; -. DR MGI; MGI:1916679; Me3. DR eggNOG; COG0281; -. DR GeneTree; ENSGT00390000000754; -. DR HOGENOM; HOG000042486; -. DR HOVERGEN; HBG000746; -. DR InParanoid; Q499F4; -. DR KO; K00029; -. DR OMA; DFAYKHN; -. DR OrthoDB; EOG7G4QF0; -. DR TreeFam; TF300537; -. DR NextBio; 361849; -. DR PRO; PR:Q8BMF3; -. DR ArrayExpress; Q8BMF3; -. DR Bgee; Q8BMF3; -. DR CleanEx; MM_ME3; -. DR Genevestigator; Q8BMF3; -. DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR GO; GO:0004471; F:malate dehydrogenase (decarboxylating) (NAD+) activity; IEA:InterPro. DR GO; GO:0004473; F:malate dehydrogenase (decarboxylating) (NADP+) activity; ISS:UniProtKB. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR GO; GO:0008948; F:oxaloacetate decarboxylase activity; IEA:UniProtKB-EC. DR GO; GO:0006108; P:malate metabolic process; ISS:UniProtKB. DR GO; GO:0006090; P:pyruvate metabolic process; ISS:UniProtKB. DR Gene3D; 3.40.50.10380; -; 1. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR015884; Malic_enzyme_CS. DR InterPro; IPR012301; Malic_N_dom. DR InterPro; IPR012302; Malic_NAD-bd. DR InterPro; IPR001891; Malic_OxRdtase. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Pfam; PF00390; malic; 1. DR Pfam; PF03949; Malic_M; 1. DR PIRSF; PIRSF000106; ME; 1. DR PRINTS; PR00072; MALOXRDTASE. DR SMART; SM00919; Malic_M; 1. DR PROSITE; PS00331; MALIC_ENZYMES; 1. PE 1: Evidence at protein level; KW Complete proteome; Direct protein sequencing; Metal-binding; KW Mitochondrion; NADP; Oxidoreductase; Reference proteome; KW Transit peptide. FT TRANSIT 1 ? Mitochondrion (Potential). FT CHAIN ? 604 NADP-dependent malic enzyme, FT mitochondrial. FT /FTId=PRO_0000018540. FT ACT_SITE 137 137 Proton donor (By similarity). FT ACT_SITE 208 208 Proton acceptor (By similarity). FT METAL 280 280 Divalent metal cation (By similarity). FT METAL 281 281 Divalent metal cation (By similarity). FT METAL 304 304 Divalent metal cation (By similarity). FT BINDING 190 190 NADP (By similarity). FT BINDING 304 304 NADP (By similarity). FT BINDING 443 443 NADP (By similarity). FT SITE 304 304 Important for activity (By similarity). FT CONFLICT 113 113 L -> H (in Ref. 1; BAC27751). FT CONFLICT 338 338 G -> D (in Ref. 1; BAC27751). SQ SEQUENCE 604 AA; 67098 MW; F667B01B116A5918 CRC64; MGAALGTGAR LTSVPRIACS SLRRQAPSAP AQGCHSKSGP PRPVPLKKRG YDVTRNPHLN KGMAFTLEER LQLGIHGLIP PCFLSQDVQL LRIMRYYENQ QSDLDKYIIL MTLQDRNEKL FYRVLTSDVE KFMPIVYTPT VGLACQHYGL TFRRPRGLFI TIHDKGHIAT MLNSWPEDNI KAVVVTDGER ILGLGDLGCY GMGIPVGKLA LYTACGGVNP QQCLPVLLDV GTNNEELLRD PLYIGLKHQR VRGEEYDDLL DEFMQAVTDK FGINCLIQFE DFANANAFRL LNKYRNKYCM FNDDIQGTAS VAVAGILAAL RITKNRLSNH VFVFQGAGEA AMGIAHLLVM ALEKEGIPKT EAIKKIWMVD SKGLIVKGRS HLNHEKEMFA QDHPEVNSLE EVVRLVKPTA IIGVAAIAGA FTEQILRDMA SFHERPIVFA LSNPTSKAEC TAEKCYRVTE GRGIFASGSP FKSVTLEDGR TFTPGQGNNA YVFPGVALGV IAGGIRHIPD EIFLLTAEQI AQEVSEQHLS QGRLYPPLST IRDVSLRIAV KVLDYAYKHN LASYYPEPKD KEAFVKSLIY TPDYDSFSLD TYSWPKEAMS VQKV // ID MAOX_MOUSE Reviewed; 572 AA. AC P06801; Q9DBF9; DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 2. DT 19-FEB-2014, entry version 123. DE RecName: Full=NADP-dependent malic enzyme; DE Short=NADP-ME; DE EC=1.1.1.40; DE AltName: Full=Malic enzyme 1; GN Name=Me1; Synonyms=Mod-1, Mod1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=3805042; RA Bagchi S., Wise L.S., Brown M.L., Bregman D., Sul H.S., Rubin C.S.; RT "Structure and expression of murine malic enzyme mRNA. RT Differentiation-dependent accumulation of two forms of malic enzyme RT mRNA in 3T3-L1 cells."; RL J. Biol. Chem. 262:1558-1565(1987). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Liver; RX PubMed=3541755; DOI=10.1111/j.1749-6632.1986.tb15522.x; RA Bagchi S., Wise L.S., Brown M.L., Sul H.S., Bregman D.B., Rubin C.S.; RT "Regulation and structure of murine malic enzyme mRNA."; RL Ann. N. Y. Acad. Sci. 478:77-92(1986). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Liver, and Testis; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [4] RP PROTEIN SEQUENCE OF 428-445, AND MASS SPECTROMETRY. RC TISSUE=Hippocampus; RA Lubec G., Klug S.; RL Submitted (MAR-2007) to UniProtKB. CC -!- CATALYTIC ACTIVITY: (S)-malate + NADP(+) = pyruvate + CO(2) + CC NADPH. CC -!- CATALYTIC ACTIVITY: Oxaloacetate = pyruvate + CO(2). CC -!- COFACTOR: Divalent metal cations. Prefers magnesium or manganese CC (By similarity). CC -!- SUBUNIT: Homotetramer. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the malic enzymes family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; J02652; AAA39727.1; -; mRNA. DR EMBL; M26756; AAA39489.1; -; mRNA. DR EMBL; AK004980; BAB23716.1; -; mRNA. DR EMBL; AK077968; BAC37086.1; -; mRNA. DR PIR; A26683; DEMSMX. DR RefSeq; NP_001185862.1; NM_001198933.1. DR RefSeq; NP_032641.2; NM_008615.2. DR UniGene; Mm.148155; -. DR ProteinModelPortal; P06801; -. DR SMR; P06801; 15-555. DR IntAct; P06801; 4. DR MINT; MINT-1855632; -. DR PhosphoSite; P06801; -. DR REPRODUCTION-2DPAGE; P06801; -. DR SWISS-2DPAGE; P06801; -. DR PaxDb; P06801; -. DR PRIDE; P06801; -. DR Ensembl; ENSMUST00000034989; ENSMUSP00000034989; ENSMUSG00000032418. DR GeneID; 17436; -. DR KEGG; mmu:17436; -. DR UCSC; uc009qxs.2; mouse. DR CTD; 4199; -. DR MGI; MGI:97043; Me1. DR eggNOG; COG0281; -. DR GeneTree; ENSGT00390000000754; -. DR HOGENOM; HOG000042486; -. DR HOVERGEN; HBG000746; -. DR InParanoid; Q9DBF9; -. DR KO; K00029; -. DR OMA; VKEMAAH; -. DR OrthoDB; EOG7G4QF0; -. DR TreeFam; TF300537; -. DR ChiTaRS; ME1; mouse. DR NextBio; 292072; -. DR PRO; PR:P06801; -. DR Bgee; P06801; -. DR CleanEx; MM_ME1; -. DR Genevestigator; P06801; -. DR GO; GO:0005829; C:cytosol; ISS:UniProtKB. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR GO; GO:0004471; F:malate dehydrogenase (decarboxylating) (NAD+) activity; IEA:InterPro. DR GO; GO:0004473; F:malate dehydrogenase (decarboxylating) (NADP+) activity; ISS:UniProtKB. DR GO; GO:0030145; F:manganese ion binding; ISS:UniProtKB. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR GO; GO:0008948; F:oxaloacetate decarboxylase activity; IEA:UniProtKB-EC. DR GO; GO:0006108; P:malate metabolic process; ISS:UniProtKB. DR GO; GO:0051262; P:protein tetramerization; IDA:MGI. DR GO; GO:0009725; P:response to hormone; ISS:UniProtKB. DR Gene3D; 3.40.50.10380; -; 1. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR015884; Malic_enzyme_CS. DR InterPro; IPR012301; Malic_N_dom. DR InterPro; IPR012302; Malic_NAD-bd. DR InterPro; IPR001891; Malic_OxRdtase. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Pfam; PF00390; malic; 1. DR Pfam; PF03949; Malic_M; 1. DR PIRSF; PIRSF000106; ME; 1. DR PRINTS; PR00072; MALOXRDTASE. DR SMART; SM00919; Malic_M; 1. DR PROSITE; PS00331; MALIC_ENZYMES; 1. PE 1: Evidence at protein level; KW Acetylation; Complete proteome; Cytoplasm; Direct protein sequencing; KW Metal-binding; NADP; Oxidoreductase; Reference proteome. FT CHAIN 1 572 NADP-dependent malic enzyme. FT /FTId=PRO_0000160193. FT NP_BIND 301 318 NADP (By similarity). FT ACT_SITE 102 102 Proton donor (By similarity). FT ACT_SITE 173 173 Proton acceptor (By similarity). FT METAL 245 245 Divalent metal cation (By similarity). FT METAL 246 246 Divalent metal cation (By similarity). FT METAL 269 269 Divalent metal cation (By similarity). FT BINDING 155 155 NADP (By similarity). FT BINDING 269 269 NADP (By similarity). FT SITE 269 269 Important for activity (By similarity). FT MOD_RES 1 1 N-acetylmethionine (By similarity). FT CONFLICT 408 408 N -> S (in Ref. 1; AAA39727 and 2; FT AAA39489). FT CONFLICT 418 419 EQ -> DE (in Ref. 1; AAA39727 and 2; FT AAA39489). FT CONFLICT 482 482 A -> R (in Ref. 1; AAA39727 and 2; FT AAA39489). SQ SEQUENCE 572 AA; 63954 MW; D6BBF93FBEDAB1BE CRC64; MEPRAPRRRH THQRGYLLTR DPHLNKDLAF TLEERQQLNI HGLLPPCIIS QELQVLRIIK NFERLNSDFD RYLLLMDLQD RNEKLFYSVL MSDVEKFMPI VYTPTVGLAC QQYSLAFRKP RGLFISIHDK GHIASVLNAW PEDVVKAIVV TDGERILGLG DLGCNGMGIP VGKLALYTAC GGVNPQQCLP ITLDVGTENE ELLKDPLYIG LRHRRVRGPE YDAFLDEFME AASSKYGMNC LIQFEDFANR NAFRLLNKYR NKYCTFNDDI QGTASVAVAG LLAALRITKN KLSDQTVLFQ GAGEAALGIA HLVVMAMEKE GLSKENARKK IWLVDSKGLI VKGRASLTEE KEVFAHEHEE MKNLEAIVQK IKPTALIGVA AIGGAFTEQI LKDMAAFNER PIIFALSNPT SKAECSAEQC YKVTKGRAIF ASGSPFDPVT LPDGRTLFPG QGNNSYVFPG VALGVVACGL RHIDDKVFLT TAEVISQQVS DKHLQEGRLY PPLNTIRGVS LKIAVKIVQD AYKEKMATVY PEPQNKEEFV SSQMYSTNYD QILPDCYPWP AEVQKIQTKV NQ // ID MAOM_MOUSE Reviewed; 589 AA. AC Q99KE1; Q3TBM8; DT 09-NOV-2004, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 19-FEB-2014, entry version 104. DE RecName: Full=NAD-dependent malic enzyme, mitochondrial; DE Short=NAD-ME; DE EC=1.1.1.38; DE AltName: Full=Malic enzyme 2; DE Flags: Precursor; GN Name=Me2; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J, and NOD; TISSUE=Spleen, and Thymus; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Mammary tumor; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- CATALYTIC ACTIVITY: (S)-malate + NAD(+) = pyruvate + CO(2) + NADH. CC -!- CATALYTIC ACTIVITY: Oxaloacetate = pyruvate + CO(2). CC -!- COFACTOR: Divalent metal cations. Prefers magnesium or manganese CC (By similarity). CC -!- ENZYME REGULATION: Subject to allosteric activation by fumarate CC (By similarity). CC -!- SUBUNIT: Homotetramer (By similarity). CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix (By similarity). CC -!- MISCELLANEOUS: This isoenzyme can also use NADP(+) but is more CC effective with NAD(+) (By similarity). CC -!- SIMILARITY: Belongs to the malic enzymes family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK042289; BAC31216.1; -; mRNA. DR EMBL; AK050933; BAC34467.1; -; mRNA. DR EMBL; AK050980; BAC34483.1; -; mRNA. DR EMBL; AK156403; BAE33701.1; -; mRNA. DR EMBL; AK171157; BAE42281.1; -; mRNA. DR EMBL; BC004709; AAH04709.1; -; mRNA. DR RefSeq; NP_663469.1; NM_145494.2. DR UniGene; Mm.36817; -. DR ProteinModelPortal; Q99KE1; -. DR SMR; Q99KE1; 23-573. DR IntAct; Q99KE1; 1. DR MINT; MINT-4101121; -. DR STRING; 10090.ENSMUSP00000025439; -. DR PhosphoSite; Q99KE1; -. DR REPRODUCTION-2DPAGE; Q99KE1; -. DR PaxDb; Q99KE1; -. DR PRIDE; Q99KE1; -. DR Ensembl; ENSMUST00000025439; ENSMUSP00000025439; ENSMUSG00000024556. DR GeneID; 107029; -. DR KEGG; mmu:107029; -. DR UCSC; uc008fox.1; mouse. DR CTD; 4200; -. DR MGI; MGI:2147351; Me2. DR eggNOG; COG0281; -. DR GeneTree; ENSGT00390000000754; -. DR HOGENOM; HOG000042486; -. DR HOVERGEN; HBG000746; -. DR InParanoid; Q99KE1; -. DR KO; K00027; -. DR OMA; FRYPEPE; -. DR OrthoDB; EOG7G4QF0; -. DR TreeFam; TF300537; -. DR ChiTaRS; ME2; mouse. DR NextBio; 358536; -. DR PRO; PR:Q99KE1; -. DR ArrayExpress; Q99KE1; -. DR Bgee; Q99KE1; -. DR CleanEx; MM_ME2; -. DR Genevestigator; Q99KE1; -. DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR GO; GO:0004471; F:malate dehydrogenase (decarboxylating) (NAD+) activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR GO; GO:0008948; F:oxaloacetate decarboxylase activity; IEA:UniProtKB-EC. DR GO; GO:0006108; P:malate metabolic process; IEA:InterPro. DR Gene3D; 3.40.50.10380; -; 1. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR015884; Malic_enzyme_CS. DR InterPro; IPR012301; Malic_N_dom. DR InterPro; IPR012302; Malic_NAD-bd. DR InterPro; IPR001891; Malic_OxRdtase. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Pfam; PF00390; malic; 1. DR Pfam; PF03949; Malic_M; 1. DR PIRSF; PIRSF000106; ME; 1. DR PRINTS; PR00072; MALOXRDTASE. DR SMART; SM00919; Malic_M; 1. DR PROSITE; PS00331; MALIC_ENZYMES; 1. PE 2: Evidence at transcript level; KW Acetylation; Allosteric enzyme; Complete proteome; Metal-binding; KW Mitochondrion; NAD; Oxidoreductase; Reference proteome; KW Transit peptide. FT TRANSIT 1 18 Mitochondrion (By similarity). FT CHAIN 19 589 NAD-dependent malic enzyme, FT mitochondrial. FT /FTId=PRO_0000018538. FT NP_BIND 311 328 NAD (By similarity). FT ACT_SITE 112 112 Proton donor (By similarity). FT ACT_SITE 183 183 Proton acceptor (By similarity). FT METAL 255 255 Divalent metal cation (By similarity). FT METAL 256 256 Divalent metal cation (By similarity). FT METAL 279 279 Divalent metal cation (By similarity). FT BINDING 165 165 NAD (By similarity). FT BINDING 279 279 NAD (By similarity). FT BINDING 421 421 NAD (By similarity). FT SITE 279 279 Important for activity (By similarity). FT MOD_RES 156 156 N6-acetyllysine (By similarity). FT MOD_RES 224 224 N6-acetyllysine (By similarity). FT MOD_RES 240 240 N6-acetyllysine (By similarity). FT MOD_RES 272 272 N6-acetyllysine (By similarity). FT MOD_RES 346 346 N6-acetyllysine (By similarity). SQ SEQUENCE 589 AA; 65799 MW; CD77AD5744B08CAB CRC64; MFSRLRAVTT PCTLTCRRVH LKEKGKPLML NPRTNKGMAF TLQERQMLGL QGLLPPKIET QDIQALRFHR NLKKMTSPLE KYIYIMGIQE RNEKLFYRIL QDDIESLMPI VYTPTVGLAC CQYGHIFRRP KGLFISISDR GHVRSIVDNW PENHVKAVVV TDGERILGLG DLGVYGMGIP VGKLCLYTAC AGIQPEKCLP VCIDVGTDNM ALLKDPFYMG LYQKRDRSQL YDDLMDEFMK AITDRYGRNT LIQFEDFGNH NAFRFLRKYQ QKYCTFNDDI QGTAAVALSG LLAAQRVINK PVSEHKILFL GAGEAALGIA NLIVLSMVES GLSEEEAQRK IWMFDKSGLL VKGRTASIDS NQEPYAHAAP ESIPATFEDA VNKLKPSVII GVAGAGPLFT HGVIKAMASI NERPIIFALS NPTAQAECTA EDAYTLTEGR CLFASGSPFE PVKLQDGRVF TPGQGNNAYI FPGVALAVIL CEARHISDTV FLEAAKALTT QLTDAELAQG RLYPSLANIQ EVSANIAIKL AEYLYANKMA FRYPEPEDKA RYVRERIWRS NYVSLLPDVY DWPESSLTPP QITEEKLPH // ID MDH1B_MOUSE Reviewed; 500 AA. AC Q5F204; Q80YT6; Q9D988; DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 19-FEB-2014, entry version 83. DE RecName: Full=Putative malate dehydrogenase 1B; DE EC=1.1.1.-; GN Name=Mdh1b; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Testis; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 284-500. RC STRAIN=C57BL/6J; TISSUE=Testis; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 2 family. CC -!- SEQUENCE CAUTION: CC Sequence=AAH50786.1; Type=Erroneous initiation; CC Sequence=BAB24922.1; Type=Erroneous initiation; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AL732462; CAI51863.1; -; Genomic_DNA. DR EMBL; AL645534; CAI51863.1; JOINED; Genomic_DNA. DR EMBL; AL645534; CAI51917.1; -; Genomic_DNA. DR EMBL; AC099637; CAI51917.1; JOINED; Genomic_DNA. DR EMBL; BC050786; AAH50786.1; ALT_INIT; mRNA. DR EMBL; AK007262; BAB24922.1; ALT_INIT; mRNA. DR RefSeq; NP_083972.3; NM_029696.4. DR UniGene; Mm.30494; -. DR ProteinModelPortal; Q5F204; -. DR SMR; Q5F204; 131-457. DR PRIDE; Q5F204; -. DR Ensembl; ENSMUST00000114094; ENSMUSP00000109728; ENSMUSG00000025963. DR GeneID; 76668; -. DR KEGG; mmu:76668; -. DR UCSC; uc007bgj.1; mouse. DR CTD; 130752; -. DR MGI; MGI:1923918; Mdh1b. DR eggNOG; COG0039; -. DR GeneTree; ENSGT00530000063410; -. DR HOGENOM; HOG000006952; -. DR HOVERGEN; HBG108123; -. DR InParanoid; Q5F204; -. DR OMA; IWGNISG; -. DR OrthoDB; EOG7M0NS0; -. DR TreeFam; TF329007; -. DR NextBio; 345589; -. DR PRO; PR:Q5F204; -. DR Bgee; Q5F204; -. DR Genevestigator; Q5F204; -. DR GO; GO:0016615; F:malate dehydrogenase activity; IEA:InterPro. DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR GO; GO:0006108; P:malate metabolic process; IEA:InterPro. DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.720; -; 1. DR Gene3D; 3.90.110.10; -; 1. DR InterPro; IPR022383; Lactate/malate_DH_C. DR InterPro; IPR015955; Lactate_DH/Glyco_Ohase_4_C. DR InterPro; IPR010945; Malate_DH_type2. DR InterPro; IPR016040; NAD(P)-bd_dom. DR PANTHER; PTHR23382; PTHR23382; 1. DR Pfam; PF02866; Ldh_1_C; 1. DR SUPFAM; SSF56327; SSF56327; 1. PE 2: Evidence at transcript level; KW Complete proteome; NAD; Oxidoreductase; Reference proteome; KW Tricarboxylic acid cycle. FT CHAIN 1 500 Putative malate dehydrogenase 1B. FT /FTId=PRO_0000331436. FT CONFLICT 10 10 A -> E (in Ref. 2; AAH50786). SQ SEQUENCE 500 AA; 56297 MW; 9D7DB6688A93B9CF CRC64; MAKFVIAGKA NCPYYAKAEL LADYLQKNLP DFRIFKITQH PDKWEDWVED VCERNMWDHR TSPIIWRELL DRGGRGLLLG GYNEFLEHAQ LYYGVTSNMT TELMMVIAKE NMQTHTEQQL DKETMKDLIS PLQVWIASAG TYVCCHLIPL LLSGEVFGMH TEISLTLFDQ EQREDCLRSI VMETQDLASP VLRTVSFCTT VKEAFLQAQV IIILDDSTEE EVYSLESCLR SRVPLCRLYG YLIEKNAHKS VKVIVGGKNF VNLKTTLLMQ YAPNIASNII AVALGVEGQA KAVLARKMKT TSANIKDVII WGNITGNNYV DLRKAKVYNY ESAVKGPPGH YHSVLSLIFD REWITKEFVQ TLKILSSTGK QFGGILAAHS IATTLKYWYH GSPPGEIVSL GVMSEGQFDI PEGIVFSMPV KFENGTWVVL TDLEDISLSE KTLSRLTGDL IQEKLVACGD LLTFQPIEED PKDNEPSNTG MNEEKEQPGS DDSDEKNEDQ // ID MDHC_MOUSE Reviewed; 334 AA. AC P14152; Q3TP22; Q80Y13; Q9DB45; DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 19-MAR-2014, entry version 137. DE RecName: Full=Malate dehydrogenase, cytoplasmic; DE EC=1.1.1.37; DE AltName: Full=Cytosolic malate dehydrogenase; GN Name=Mdh1; Synonyms=Mor2; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=3312200; RA Joh T., Takeshima H., Tsuzuki T., Setoyama C., Shimada K., Tanase S., RA Kuramitsu S., Kagamiyama H., Morino Y.; RT "Cloning and sequence analysis of cDNAs encoding mammalian cytosolic RT malate dehydrogenase. Comparison of the amino acid sequences of RT mammalian and bacterial malate dehydrogenase."; RL J. Biol. Chem. 262:15127-15131(1987). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=C3H/He; TISSUE=Liver; RX PubMed=3172222; DOI=10.1016/0022-2836(88)90270-7; RA Setoyama C., Joh T., Tsuzuki T., Shimada K.; RT "Structural organization of the mouse cytosolic malate dehydrogenase RT gene: comparison with that of the mouse mitochondrial malate RT dehydrogenase gene."; RL J. Mol. Biol. 202:355-364(1988). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Cerebellum, Mammary gland, and Stomach; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6; TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP PROTEIN SEQUENCE OF 80-92; 126-142; 171-199; 206-230; 299-310 AND RP 325-334, AND MASS SPECTROMETRY. RC STRAIN=C57BL/6; TISSUE=Brain, and Hippocampus; RA Lubec G., Klug S., Kang S.U.; RL Submitted (APR-2007) to UniProtKB. RN [7] RP ISGYLATION. RX PubMed=16139798; DOI=10.1016/j.bbrc.2005.08.132; RA Giannakopoulos N.V., Luo J.K., Papov V., Zou W., Lenschow D.J., RA Jacobs B.S., Borden E.C., Li J., Virgin H.W., Zhang D.E.; RT "Proteomic identification of proteins conjugated to ISG15 in mouse and RT human cells."; RL Biochem. Biophys. Res. Commun. 336:496-506(2005). RN [8] RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-110; LYS-214; LYS-298 AND RP LYS-318, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Liver; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., RA Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). RN [9] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-118, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23576753; DOI=10.1073/pnas.1302961110; RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., RA Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.; RT "Label-free quantitative proteomics of the lysine acetylome in RT mitochondria identifies substrates of SIRT3 in metabolic pathways."; RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013). CC -!- CATALYTIC ACTIVITY: (S)-malate + NAD(+) = oxaloacetate + NADH. CC -!- SUBUNIT: Homodimer. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- PTM: ISGylated. CC -!- PTM: Acetylation at Lys-118 dramatically enhances enzymatic CC activity and promotes adipogenic differentiation (By similarity). CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 2 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M29462; AAA39510.1; -; mRNA. DR EMBL; M36084; AAA37423.1; -; Genomic_DNA. DR EMBL; AK005237; BAB23897.1; -; mRNA. DR EMBL; AK164785; BAE37915.1; -; mRNA. DR EMBL; AK168545; BAE40421.1; -; mRNA. DR EMBL; AL663049; CAI24411.1; -; Genomic_DNA. DR EMBL; BC050940; AAH50940.2; -; mRNA. DR PIR; S02654; DEMSMC. DR RefSeq; NP_032644.3; NM_008618.3. DR UniGene; Mm.212703; -. DR ProteinModelPortal; P14152; -. DR SMR; P14152; 2-334. DR IntAct; P14152; 7. DR MINT; MINT-1869753; -. DR ChEMBL; CHEMBL2176827; -. DR PhosphoSite; P14152; -. DR COMPLUYEAST-2DPAGE; P14152; -. DR REPRODUCTION-2DPAGE; P14152; -. DR SWISS-2DPAGE; P14152; -. DR UCD-2DPAGE; P14152; -. DR PaxDb; P14152; -. DR PRIDE; P14152; -. DR Ensembl; ENSMUST00000102874; ENSMUSP00000099938; ENSMUSG00000020321. DR GeneID; 17449; -. DR KEGG; mmu:17449; -. DR UCSC; uc007idv.2; mouse. DR CTD; 4190; -. DR MGI; MGI:97051; Mdh1. DR eggNOG; COG0039; -. DR GeneTree; ENSGT00530000063410; -. DR HOGENOM; HOG000220953; -. DR HOVERGEN; HBG006340; -. DR InParanoid; P14152; -. DR KO; K00025; -. DR OMA; NCLIASK; -. DR OrthoDB; EOG78H3TM; -. DR TreeFam; TF105826; -. DR ChiTaRS; MDH1; mouse. DR NextBio; 292088; -. DR PRO; PR:P14152; -. DR ArrayExpress; P14152; -. DR Bgee; P14152; -. DR CleanEx; MM_MDH1; -. DR Genevestigator; P14152; -. DR GO; GO:0005813; C:centrosome; IEA:Ensembl. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR GO; GO:0030060; F:L-malate dehydrogenase activity; IEA:UniProtKB-EC. DR GO; GO:0051287; F:NAD binding; IEA:Ensembl. DR GO; GO:0044262; P:cellular carbohydrate metabolic process; IEA:InterPro. DR GO; GO:0006108; P:malate metabolic process; IEA:Ensembl. DR GO; GO:0006734; P:NADH metabolic process; IEA:Ensembl. DR GO; GO:0006107; P:oxaloacetate metabolic process; IEA:Ensembl. DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.720; -; 1. DR Gene3D; 3.90.110.10; -; 1. DR HAMAP; MF_01517; Malate_dehydrog_2; 1. DR InterPro; IPR001557; L-lactate/malate_DH. DR InterPro; IPR022383; Lactate/malate_DH_C. DR InterPro; IPR001236; Lactate/malate_DH_N. DR InterPro; IPR015955; Lactate_DH/Glyco_Ohase_4_C. DR InterPro; IPR001252; Malate_DH_AS. DR InterPro; IPR011274; Malate_DH_NAD-dep_euk. DR InterPro; IPR010945; Malate_DH_type2. DR InterPro; IPR016040; NAD(P)-bd_dom. DR PANTHER; PTHR23382; PTHR23382; 1. DR Pfam; PF02866; Ldh_1_C; 1. DR Pfam; PF00056; Ldh_1_N; 1. DR PIRSF; PIRSF000102; Lac_mal_DH; 1. DR SUPFAM; SSF56327; SSF56327; 1. DR TIGRFAMs; TIGR01759; MalateDH-SF1; 1. DR TIGRFAMs; TIGR01758; MDH_euk_cyt; 1. DR PROSITE; PS00068; MDH; 1. PE 1: Evidence at protein level; KW Acetylation; Complete proteome; Cytoplasm; Direct protein sequencing; KW NAD; Oxidoreductase; Phosphoprotein; Reference proteome; KW Tricarboxylic acid cycle; Ubl conjugation. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 334 Malate dehydrogenase, cytoplasmic. FT /FTId=PRO_0000113410. FT NP_BIND 11 17 NAD (By similarity). FT NP_BIND 129 131 NAD (By similarity). FT ACT_SITE 187 187 Proton acceptor (By similarity). FT BINDING 92 92 Substrate (By similarity). FT BINDING 98 98 Substrate (By similarity). FT BINDING 105 105 NAD (By similarity). FT BINDING 112 112 NAD (By similarity). FT BINDING 131 131 Substrate (By similarity). FT BINDING 162 162 Substrate (By similarity). FT MOD_RES 2 2 N-acetylserine (By similarity). FT MOD_RES 110 110 N6-succinyllysine. FT MOD_RES 118 118 N6-acetyllysine. FT MOD_RES 121 121 N6-acetyllysine (By similarity). FT MOD_RES 214 214 N6-succinyllysine. FT MOD_RES 298 298 N6-acetyllysine; alternate (By FT similarity). FT MOD_RES 298 298 N6-succinyllysine; alternate. FT MOD_RES 318 318 N6-succinyllysine. FT MOD_RES 333 333 Phosphoserine (By similarity). FT CONFLICT 92 92 R -> I (in Ref. 3; BAB23897). FT CONFLICT 177 177 D -> N (in Ref. 3; BAE37915). FT CONFLICT 288 288 F -> L (in Ref. 1 and 2). SQ SEQUENCE 334 AA; 36511 MW; 3B9F00372AA939DF CRC64; MSEPIRVLVT GAAGQIAYSL LYSIGNGSVF GKDQPIILVL LDITPMMGVL DGVLMELQDC ALPLLQDVIA TDKEEIAFKD LDVAVLVGSM PRREGMERKD LLKANVKIFK SQGTALEKYA KKSVKVIVVG NPANTNCLTA SKSAPSIPKE NFSCLTRLDH NRAKSQIALK LGVTADDVKN VIIWGNHSST QYPDVNHAKV KLQGKEVGVY EALKDDSWLK GEFITTVQQR GAAVIKARKL SSAMSAAKAI ADHIRDIWFG TPEGEFVSMG VISDGNSYGV PDDLLYSFPV VIKNKTWKFV EGLPINDFSR EKMDLTAKEL TEEKETAFEF LSSA // ID MDHM_MOUSE Reviewed; 338 AA. AC P08249; Q0QF44; Q8CF79; Q8R1P0; DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2007, sequence version 3. DT 19-MAR-2014, entry version 146. DE RecName: Full=Malate dehydrogenase, mitochondrial; DE EC=1.1.1.37; DE Flags: Precursor; GN Name=Mdh2; Synonyms=Mor1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=3038184; DOI=10.1021/bi00383a017; RA Joh T., Takeshima H., Tsuzuki T., Shimada K., Tanase S., Morino Y.; RT "Cloning and sequence analysis of cDNAs encoding mammalian RT mitochondrial malate dehydrogenase."; RL Biochemistry 26:2515-2520(1987). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=3379635; DOI=10.1016/0022-2836(88)90328-2; RA Takeshima H., Joh T., Tsuzuki T., Shimada K., Matsukado Y.; RT "Structural organization of the mouse mitochondrial malate RT dehydrogenase gene."; RL J. Mol. Biol. 200:1-11(1988). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=BALB/c, and C57BL/6J; TISSUE=Cerebellum, and Kidney; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Mammary tumor; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 22-322. RC TISSUE=Liver; RX PubMed=16751257; DOI=10.1093/molbev/msl027; RA Kullberg M., Nilsson M.A., Arnason U., Harley E.H., Janke A.; RT "Housekeeping genes for phylogenetic analysis of eutherian RT relationships."; RL Mol. Biol. Evol. 23:1493-1503(2006). RN [6] RP PROTEIN SEQUENCE OF 27-45; 53-74; 79-104; 166-185; 192-239; 242-257; RP 282-296 AND 308-324, AND MASS SPECTROMETRY. RC STRAIN=C57BL/6, and OF1; TISSUE=Brain, and Hippocampus; RA Lubec G., Kang S.U., Klug S., Yang J.W., Zigmond M., Sunyer B., RA Chen W.-Q.; RL Submitted (JAN-2009) to UniProtKB. RN [7] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-239, SUCCINYLATION [LARGE RP SCALE ANALYSIS] AT LYS-78; LYS-91; LYS-185; LYS-203; LYS-215; LYS-239; RP LYS-269; LYS-296; LYS-301; LYS-307; LYS-314; LYS-324 AND LYS-335, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic fibroblast, and Liver; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., RA Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). RN [8] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-78; LYS-91; LYS-165; RP LYS-185; LYS-215; LYS-239; LYS-296; LYS-301; LYS-307; LYS-314; RP LYS-324; LYS-329 AND LYS-335, AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23576753; DOI=10.1073/pnas.1302961110; RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., RA Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.; RT "Label-free quantitative proteomics of the lysine acetylome in RT mitochondria identifies substrates of SIRT3 in metabolic pathways."; RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013). CC -!- CATALYTIC ACTIVITY: (S)-malate + NAD(+) = oxaloacetate + NADH. CC -!- ENZYME REGULATION: Enzyme activity is enhanced by acetylation (By CC similarity). CC -!- SUBUNIT: Homodimer. CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix. CC -!- PTM: Acetylation is enhanced by up to 67% after treatment either CC with trichostin A (TCA) or with nicotinamide (NAM) with the CC appearance of tri-and tetraacetylations. Glucose also increases CC acetylation by about 60% (By similarity). Acetylation of Lys-239 CC and Lys-314 is observed in liver mitochondria from fasted mice but CC not from fed mice. CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 1 family. CC -!- SEQUENCE CAUTION: CC Sequence=BAC24986.1; Type=Frameshift; Positions=39; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M16229; AAA39509.1; -; mRNA. DR EMBL; X07295; CAA30274.1; -; Genomic_DNA. DR EMBL; X07296; CAA30274.1; JOINED; Genomic_DNA. DR EMBL; X07297; CAA30274.1; JOINED; Genomic_DNA. DR EMBL; X07298; CAA30274.1; JOINED; Genomic_DNA. DR EMBL; X07299; CAA30274.1; JOINED; Genomic_DNA. DR EMBL; X07300; CAA30274.1; JOINED; Genomic_DNA. DR EMBL; X07301; CAA30274.1; JOINED; Genomic_DNA. DR EMBL; AK002305; BAC24986.1; ALT_FRAME; mRNA. DR EMBL; AK167809; BAE39836.1; -; mRNA. DR EMBL; AK160553; BAE35869.1; -; mRNA. DR EMBL; AK135162; BAE22447.1; -; mRNA. DR EMBL; BC023482; AAH23482.1; -; mRNA. DR EMBL; DQ402950; ABD77283.1; -; mRNA. DR PIR; S01350; DEMSMM. DR RefSeq; NP_032643.2; NM_008617.2. DR UniGene; Mm.297096; -. DR ProteinModelPortal; P08249; -. DR SMR; P08249; 25-337. DR BioGrid; 201467; 3. DR IntAct; P08249; 7. DR MINT; MINT-4101644; -. DR PhosphoSite; P08249; -. DR REPRODUCTION-2DPAGE; P08249; -. DR SWISS-2DPAGE; P08249; -. DR UCD-2DPAGE; P08249; -. DR PaxDb; P08249; -. DR PRIDE; P08249; -. DR Ensembl; ENSMUST00000019323; ENSMUSP00000019323; ENSMUSG00000019179. DR GeneID; 17448; -. DR KEGG; mmu:17448; -. DR UCSC; uc008zyz.1; mouse. DR CTD; 4191; -. DR MGI; MGI:97050; Mdh2. DR eggNOG; COG0039; -. DR GeneTree; ENSGT00390000016686; -. DR HOGENOM; HOG000213792; -. DR HOVERGEN; HBG001662; -. DR InParanoid; P08249; -. DR KO; K00026; -. DR OMA; VEVKGFA; -. DR OrthoDB; EOG74R1R7; -. DR TreeFam; TF300834; -. DR ChiTaRS; Mdh2; mouse. DR NextBio; 292084; -. DR PRO; PR:P08249; -. DR ArrayExpress; P08249; -. DR Bgee; P08249; -. DR CleanEx; MM_MDH2; -. DR Genevestigator; P08249; -. DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:MGI. DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell. DR GO; GO:0005634; C:nucleus; IEA:Ensembl. DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl. DR GO; GO:0030060; F:L-malate dehydrogenase activity; IDA:MGI. DR GO; GO:0046554; F:malate dehydrogenase (NADP+) activity; IEA:Ensembl. DR GO; GO:0044262; P:cellular carbohydrate metabolic process; IEA:InterPro. DR GO; GO:0006475; P:internal protein amino acid acetylation; ISS:UniProtKB. DR GO; GO:0006108; P:malate metabolic process; ISA:MGI. DR GO; GO:0006734; P:NADH metabolic process; IEA:Ensembl. DR GO; GO:0006107; P:oxaloacetate metabolic process; IEA:Ensembl. DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.720; -; 1. DR Gene3D; 3.90.110.10; -; 1. DR InterPro; IPR001557; L-lactate/malate_DH. DR InterPro; IPR022383; Lactate/malate_DH_C. DR InterPro; IPR001236; Lactate/malate_DH_N. DR InterPro; IPR015955; Lactate_DH/Glyco_Ohase_4_C. DR InterPro; IPR001252; Malate_DH_AS. DR InterPro; IPR010097; Malate_DH_type1. DR InterPro; IPR016040; NAD(P)-bd_dom. DR PANTHER; PTHR11540; PTHR11540; 1. DR PANTHER; PTHR11540:SF1; PTHR11540:SF1; 1. DR Pfam; PF02866; Ldh_1_C; 1. DR Pfam; PF00056; Ldh_1_N; 1. DR PIRSF; PIRSF000102; Lac_mal_DH; 1. DR SUPFAM; SSF56327; SSF56327; 1. DR TIGRFAMs; TIGR01772; MDH_euk_gproteo; 1. DR PROSITE; PS00068; MDH; 1. PE 1: Evidence at protein level; KW Acetylation; Complete proteome; Direct protein sequencing; KW Mitochondrion; NAD; Oxidoreductase; Reference proteome; KW Transit peptide; Tricarboxylic acid cycle. FT TRANSIT 1 24 Mitochondrion. FT CHAIN 25 338 Malate dehydrogenase, mitochondrial. FT /FTId=PRO_0000018629. FT NP_BIND 31 37 NAD (By similarity). FT NP_BIND 140 142 NAD (By similarity). FT ACT_SITE 200 200 Proton acceptor (By similarity). FT BINDING 57 57 NAD (By similarity). FT BINDING 104 104 Substrate. FT BINDING 110 110 Substrate. FT BINDING 117 117 NAD (By similarity). FT BINDING 142 142 Substrate. FT BINDING 176 176 Substrate. FT BINDING 251 251 NAD (By similarity). FT MOD_RES 78 78 N6-acetyllysine; alternate. FT MOD_RES 78 78 N6-succinyllysine; alternate. FT MOD_RES 91 91 N6-acetyllysine; alternate. FT MOD_RES 91 91 N6-succinyllysine; alternate. FT MOD_RES 165 165 N6-acetyllysine. FT MOD_RES 185 185 N6-acetyllysine; alternate. FT MOD_RES 185 185 N6-succinyllysine; alternate. FT MOD_RES 203 203 N6-succinyllysine. FT MOD_RES 215 215 N6-acetyllysine; alternate. FT MOD_RES 215 215 N6-succinyllysine; alternate. FT MOD_RES 239 239 N6-acetyllysine; alternate. FT MOD_RES 239 239 N6-malonyllysine; alternate (By FT similarity). FT MOD_RES 239 239 N6-succinyllysine; alternate. FT MOD_RES 269 269 N6-succinyllysine. FT MOD_RES 296 296 N6-acetyllysine; alternate. FT MOD_RES 296 296 N6-succinyllysine; alternate. FT MOD_RES 301 301 N6-acetyllysine; alternate. FT MOD_RES 301 301 N6-succinyllysine; alternate. FT MOD_RES 307 307 N6-acetyllysine; alternate. FT MOD_RES 307 307 N6-malonyllysine; alternate (By FT similarity). FT MOD_RES 307 307 N6-succinyllysine; alternate. FT MOD_RES 314 314 N6-acetyllysine; alternate. FT MOD_RES 314 314 N6-succinyllysine; alternate. FT MOD_RES 324 324 N6-acetyllysine; alternate. FT MOD_RES 324 324 N6-succinyllysine; alternate. FT MOD_RES 328 328 N6-acetyllysine; alternate (By FT similarity). FT MOD_RES 328 328 N6-succinyllysine; alternate (By FT similarity). FT MOD_RES 329 329 N6-acetyllysine; alternate. FT MOD_RES 329 329 N6-malonyllysine; alternate (By FT similarity). FT MOD_RES 335 335 N6-acetyllysine; alternate. FT MOD_RES 335 335 N6-succinyllysine; alternate. FT CONFLICT 76 76 N -> K (in Ref. 1; AAA39509). FT CONFLICT 269 269 K -> L (in Ref. 1; AAA39509 and 2; FT CAA30274). SQ SEQUENCE 338 AA; 35611 MW; 99D13BB2099C19F1 CRC64; MLSALARPAG AALRRSFSTS AQNNAKVAVL GASGGIGQPL SLLLKNSPLV SRLTLYDIAH TPGVAADLSH IETRANVKGY LGPEQLPDCL KGCDVVVIPA GVPRKPGMTR DDLFNTNATI VATLTAACAQ HCPEAMVCII ANPVNSTIPI TAEVFKKHGV YNPNKIFGVT TLDIVRANTF VAELKGLDPA RVNVPVIGGH AGKTIIPLIS QCTPKVDFPQ DQLATLTGRI QEAGTEVVKA KAGAGSATLS MAYAGARFVF SLVDAMNGKE GVVECSFVQS KETECTYFST PLLLGKKGLE KNLGIGKITP FEEKMIAEAI PELKASIKKG EDFVKNMK // ID MECR_MOUSE Reviewed; 373 AA. AC Q9DCS3; Q99L39; DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot. DT 26-APR-2005, sequence version 2. DT 19-MAR-2014, entry version 98. DE RecName: Full=Trans-2-enoyl-CoA reductase, mitochondrial; DE EC=1.3.1.38; DE Flags: Precursor; GN Name=Mecr; Synonyms=Nrbf1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Kidney; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Mammary tumor; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-267, SUCCINYLATION [LARGE RP SCALE ANALYSIS] AT LYS-61; LYS-252; LYS-267 AND LYS-316, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic fibroblast, and Liver; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., RA Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). RN [4] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-61 AND LYS-252, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23576753; DOI=10.1073/pnas.1302961110; RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., RA Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.; RT "Label-free quantitative proteomics of the lysine acetylome in RT mitochondria identifies substrates of SIRT3 in metabolic pathways."; RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013). CC -!- FUNCTION: Oxidoreductase with a preference for short and medium CC chain substrates, including trans-2-hexenoyl-CoA (C6), trans-2- CC decenoyl-CoA (C10), and trans-2-hexadecenoyl-CoA (C16). May play a CC role in mitochondrial fatty acid synthesis (By similarity). CC -!- CATALYTIC ACTIVITY: Acyl-CoA + NADP(+) = trans-2,3-dehydroacyl-CoA CC + NADPH. CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SUBCELLULAR LOCATION: Mitochondrion (By similarity). CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase CC family. Quinone oxidoreductase subfamily. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK002533; BAB22169.1; -; mRNA. DR EMBL; BC003864; AAH03864.1; -; mRNA. DR RefSeq; NP_079573.2; NM_025297.2. DR UniGene; Mm.192706; -. DR ProteinModelPortal; Q9DCS3; -. DR SMR; Q9DCS3; 38-373. DR IntAct; Q9DCS3; 2. DR MINT; MINT-4128719; -. DR PhosphoSite; Q9DCS3; -. DR PaxDb; Q9DCS3; -. DR PRIDE; Q9DCS3; -. DR Ensembl; ENSMUST00000030742; ENSMUSP00000030742; ENSMUSG00000028910. DR GeneID; 26922; -. DR KEGG; mmu:26922; -. DR UCSC; uc008vae.2; mouse. DR CTD; 51102; -. DR MGI; MGI:1349441; Mecr. DR eggNOG; COG0604; -. DR GeneTree; ENSGT00740000115589; -. DR HOGENOM; HOG000294683; -. DR HOVERGEN; HBG052446; -. DR InParanoid; Q9DCS3; -. DR KO; K07512; -. DR OMA; CSTLWRV; -. DR OrthoDB; EOG78M024; -. DR TreeFam; TF312886; -. DR NextBio; 304813; -. DR PRO; PR:Q9DCS3; -. DR ArrayExpress; Q9DCS3; -. DR Bgee; Q9DCS3; -. DR CleanEx; MM_MECR; -. DR Genevestigator; Q9DCS3; -. DR GO; GO:0005829; C:cytosol; ISO:MGI. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR GO; GO:0005634; C:nucleus; ISO:MGI. DR GO; GO:0016922; F:ligand-dependent nuclear receptor binding; ISO:MGI. DR GO; GO:0019166; F:trans-2-enoyl-CoA reductase (NADPH) activity; IEA:UniProtKB-EC. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.720; -; 1. DR Gene3D; 3.90.180.10; -; 1. DR InterPro; IPR013149; ADH_C. DR InterPro; IPR013154; ADH_GroES-like. DR InterPro; IPR002085; ADH_SF_Zn-type. DR InterPro; IPR011032; GroES-like. DR InterPro; IPR016040; NAD(P)-bd_dom. DR PANTHER; PTHR11695; PTHR11695; 1. DR Pfam; PF08240; ADH_N; 1. DR Pfam; PF00107; ADH_zinc_N; 1. DR SUPFAM; SSF50129; SSF50129; 1. PE 1: Evidence at protein level; KW Acetylation; Complete proteome; Fatty acid biosynthesis; KW Fatty acid metabolism; Lipid biosynthesis; Lipid metabolism; KW Mitochondrion; NADP; Oxidoreductase; Reference proteome; KW Transit peptide. FT TRANSIT 1 53 Mitochondrion (Potential). FT CHAIN 54 373 Trans-2-enoyl-CoA reductase, FT mitochondrial. FT /FTId=PRO_0000000889. FT NP_BIND 193 196 NADP (By similarity). FT NP_BIND 216 218 NADP (By similarity). FT NP_BIND 285 288 NADP (By similarity). FT NP_BIND 310 312 NADP (By similarity). FT BINDING 167 167 NADP (By similarity). FT BINDING 368 368 NADP (By similarity). FT MOD_RES 61 61 N6-acetyllysine; alternate. FT MOD_RES 61 61 N6-succinyllysine; alternate. FT MOD_RES 252 252 N6-acetyllysine; alternate. FT MOD_RES 252 252 N6-succinyllysine; alternate. FT MOD_RES 267 267 N6-acetyllysine; alternate. FT MOD_RES 267 267 N6-succinyllysine; alternate. FT MOD_RES 316 316 N6-succinyllysine. FT CONFLICT 69 69 E -> K (in Ref. 1; BAB22169). SQ SEQUENCE 373 AA; 40343 MW; EBA9A61A46386AEE CRC64; MLVSQRVTGA RARAPQLAGL LEAWYRHGRT TSSYSALSEP SRVRALVYGN HGDPAKVVQL KNLELTAVEG SDVHVRMLAA PINPSDINMI QGNYGLLPKL PAVGGNEGVG QVIAVGSSVS ALKPGDWVIP ANAGLGTWRT EAVFSEEALI GIPKDIPLQS AATLGVNPCT AYRMLVDFEQ LQPGDSVIQN ASNSGVGQAV IQIASALRLK TINVVRDRPD IKKLTDRLKD LGADYVLTEE ELRMPETKTI FKDLPLPRLA LNCVGGKSST ELLRHLAPGG TMVTYGGMAK QPVTASVSLL IFKDLKLRGF WLSQWKKNHS PDEFKELILT LCNLIRQGRL TAPSCSEVPL QGYQQALEAS MKPFVSSKQI LTM // ID MICA1_MOUSE Reviewed; 1048 AA. AC Q8VDP3; D3Z4C6; E9PXR1; Q3TB77; Q3TBH9; Q3TX89; DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2002, sequence version 1. DT 19-MAR-2014, entry version 108. DE RecName: Full=Protein-methionine sulfoxide oxidase MICAL1; DE EC=1.14.13.-; DE AltName: Full=Molecule interacting with CasL protein 1; DE Short=MICAL-1; DE Short=mMical1; DE AltName: Full=NEDD9-interacting protein with calponin homology and LIM domains; GN Name=Mical1; Synonyms=Mical, Nical; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC STRAIN=C57BL/6J, and NOD; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Mammary tumor; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP INTERACTION WITH RAB8A. RX PubMed=18094055; DOI=10.1091/mbc.E07-06-0551; RA Yamamura R., Nishimura N., Nakatsuji H., Arase S., Sasaki T.; RT "The interaction of JRAB/MICAL-L2 with Rab8 and Rab13 coordinates the RT assembly of tight junctions and adherens junctions."; RL Mol. Biol. Cell 19:971-983(2008). RN [5] RP FUNCTION, AND INTERACTION WITH STK38 AND STK38L. RX PubMed=21730291; DOI=10.1128/MCB.01389-10; RA Zhou Y., Adolfs Y., Pijnappel W.W., Fuller S.J., Van der Schors R.C., RA Li K.W., Sugden P.H., Smit A.B., Hergovich A., Pasterkamp R.J.; RT "MICAL-1 is a negative regulator of MST-NDR kinase signaling and RT apoptosis."; RL Mol. Cell. Biol. 31:3603-3615(2011). RN [6] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=23911929; DOI=10.1016/j.molcel.2013.06.019; RA Lee B.C., Peterfi Z., Hoffmann F.W., Moore R.E., Kaya A., Avanesov A., RA Tarrago L., Zhou Y., Weerapana E., Fomenko D.E., Hoffmann P.R., RA Gladyshev V.N.; RT "MsrB1 and MICALs regulate actin assembly and macrophage function via RT reversible stereoselective methionine oxidation."; RL Mol. Cell 51:397-404(2013). RN [7] RP X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 1-489 IN COMPLEX WITH FAD. RX PubMed=16275925; DOI=10.1073/pnas.0504997102; RA Siebold C., Berrow N., Walter T.S., Harlos K., Owens R.J., RA Stuart D.I., Terman J.R., Kolodkin A.L., Pasterkamp R.J., Jones E.Y.; RT "High-resolution structure of the catalytic region of MICAL (molecule RT interacting with CasL), a multidomain flavoenzyme-signaling RT molecule."; RL Proc. Natl. Acad. Sci. U.S.A. 102:16836-16841(2005). CC -!- FUNCTION: Monooxygenase that promotes depolymerization of F-actin CC by mediating oxidation of specific methionine residues on actin. CC Acts by modifying actin subunits through the addition of oxygen to CC form methionine-sulfoxide, leading to promote actin filament CC severing and prevent repolymerization. Acts as a cytoskeletal CC regulator that connects NEDD9 to intermediate filaments. Also acts CC as a negative regulator of apoptosis via its interaction with CC STK38 and STK38L; acts by antagonizing STK38 and STK38L activation CC by MST1/STK4. CC -!- CATALYTIC ACTIVITY: [protein]-methionine + NADPH + O(2) = CC [protein]-methionine-sulfoxide + NADP(+) + H(2)O. CC -!- COFACTOR: FAD. CC -!- SUBUNIT: Associates with the SH3 domain of NEDD9. Interacts with CC VIM and PLXNA3. Interacts with RAB1B (By similarity). Interacts CC with STK38 and STK38L. Interacts with RAB8A. CC -!- INTERACTION: CC Q91VJ4:Stk38; NbExp=9; IntAct=EBI-4394891, EBI-2527046; CC A4GW50:Stk38l (xeno); NbExp=2; IntAct=EBI-4394891, EBI-4404035; CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Cytoplasm, CC cytoskeleton (By similarity). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q8VDP3-1; Sequence=Displayed; CC Name=2; CC IsoId=Q8VDP3-2; Sequence=VSP_042591; CC Name=3; CC IsoId=Q8VDP3-3; Sequence=VSP_042592; CC -!- DOMAIN: The C-terminal coiled coil part contains the plexin- CC interacting region. CC -!- SIMILARITY: Belongs to the Mical family. CC -!- SIMILARITY: Contains 1 CH (calponin-homology) domain. CC -!- SIMILARITY: Contains 1 LIM zinc-binding domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK159369; BAE35027.1; -; mRNA. DR EMBL; AK170881; BAE42090.1; -; mRNA. DR EMBL; AK171234; BAE42330.1; -; mRNA. DR EMBL; AK171411; BAE42437.1; -; mRNA. DR EMBL; AK171429; BAE42447.1; -; mRNA. DR EMBL; AK171479; BAE42481.1; -; mRNA. DR EMBL; AC153360; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC021477; AAH21477.1; -; mRNA. DR EMBL; BC034682; AAH34682.1; -; mRNA. DR RefSeq; NP_001157905.1; NM_001164433.1. DR RefSeq; NP_612188.1; NM_138315.2. DR UniGene; Mm.290431; -. DR PDB; 2BRA; X-ray; 2.00 A; A/B=1-484. DR PDB; 2BRY; X-ray; 1.45 A; A/B=1-489. DR PDB; 2C4C; X-ray; 2.90 A; A/B=1-489. DR PDBsum; 2BRA; -. DR PDBsum; 2BRY; -. DR PDBsum; 2C4C; -. DR ProteinModelPortal; Q8VDP3; -. DR SMR; Q8VDP3; 7-489, 506-612, 673-741. DR IntAct; Q8VDP3; 4. DR STRING; 10090.ENSMUSP00000019967; -. DR PhosphoSite; Q8VDP3; -. DR PaxDb; Q8VDP3; -. DR PRIDE; Q8VDP3; -. DR Ensembl; ENSMUST00000019967; ENSMUSP00000019967; ENSMUSG00000019823. [Q8VDP3-1] DR Ensembl; ENSMUST00000099934; ENSMUSP00000097519; ENSMUSG00000019823. [Q8VDP3-2] DR Ensembl; ENSMUST00000119962; ENSMUSP00000113783; ENSMUSG00000019823. [Q8VDP3-3] DR GeneID; 171580; -. DR KEGG; mmu:171580; -. DR UCSC; uc007exn.2; mouse. [Q8VDP3-1] DR UCSC; uc007exp.2; mouse. [Q8VDP3-2] DR CTD; 64780; -. DR MGI; MGI:2385847; Mical1. DR eggNOG; COG5069; -. DR GeneTree; ENSGT00640000091174; -. DR HOGENOM; HOG000047263; -. DR HOVERGEN; HBG052474; -. DR OMA; KQCLLRL; -. DR OrthoDB; EOG769ZHM; -. DR TreeFam; TF324129; -. DR ChiTaRS; MICAL1; mouse. DR EvolutionaryTrace; Q8VDP3; -. DR NextBio; 371076; -. DR PRO; PR:Q8VDP3; -. DR ArrayExpress; Q8VDP3; -. DR Bgee; Q8VDP3; -. DR Genevestigator; Q8VDP3; -. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell. DR GO; GO:0003779; F:actin binding; IDA:UniProtKB. DR GO; GO:0071949; F:FAD binding; ISS:UniProtKB. DR GO; GO:0016709; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen; IDA:UniProtKB. DR GO; GO:0017124; F:SH3 domain binding; ISS:UniProtKB. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0030042; P:actin filament depolymerization; IDA:UniProtKB. DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB. DR GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IMP:UniProtKB. DR GO; GO:0001933; P:negative regulation of protein phosphorylation; IMP:UniProtKB. DR GO; GO:0019417; P:sulfur oxidation; IDA:UniProtKB. DR Gene3D; 1.10.418.10; -; 1. DR Gene3D; 2.10.110.10; -; 1. DR InterPro; IPR001715; CH-domain. DR InterPro; IPR022735; DUF3585. DR InterPro; IPR002938; mOase_FAD-bd. DR InterPro; IPR001781; Znf_LIM. DR Pfam; PF00307; CH; 1. DR Pfam; PF12130; DUF3585; 1. DR Pfam; PF01494; FAD_binding_3; 1. DR Pfam; PF00412; LIM; 1. DR SMART; SM00033; CH; 1. DR SMART; SM00132; LIM; 1. DR SUPFAM; SSF47576; SSF47576; 1. DR PROSITE; PS50021; CH; 1. DR PROSITE; PS00478; LIM_DOMAIN_1; 1. DR PROSITE; PS50023; LIM_DOMAIN_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Actin-binding; Alternative splicing; Coiled coil; KW Complete proteome; Cytoplasm; Cytoskeleton; FAD; Flavoprotein; KW LIM domain; Metal-binding; Monooxygenase; NADP; Oxidoreductase; KW Phosphoprotein; Reference proteome; Zinc. FT CHAIN 1 1048 Protein-methionine sulfoxide oxidase FT MICAL1. FT /FTId=PRO_0000075843. FT DOMAIN 507 608 CH. FT DOMAIN 681 743 LIM zinc-binding. FT NP_BIND 95 123 FAD. FT REGION 1 489 Monooxygenase domain. FT COILED 847 867 Potential. FT COILED 906 949 Potential. FT COILED 974 1031 Potential. FT BINDING 95 95 FAD. FT BINDING 114 114 FAD. FT BINDING 116 116 FAD. FT BINDING 121 121 FAD. FT BINDING 123 123 FAD. FT BINDING 393 393 FAD. FT MOD_RES 616 616 Phosphoserine (By similarity). FT VAR_SEQ 87 159 Missing (in isoform 2). FT /FTId=VSP_042591. FT VAR_SEQ 192 192 S -> D (in isoform 3). FT /FTId=VSP_042592. FT CONFLICT 871 871 P -> H (in Ref. 1; BAE35027). FT HELIX 9 19 FT HELIX 23 37 FT HELIX 44 53 FT TURN 58 60 FT HELIX 61 71 FT HELIX 74 79 FT TURN 80 84 FT STRAND 86 90 FT HELIX 94 105 FT STRAND 109 115 FT STRAND 124 126 FT HELIX 129 136 FT TURN 137 139 FT HELIX 140 143 FT TURN 145 148 FT STRAND 154 156 FT HELIX 157 170 FT STRAND 174 178 FT STRAND 180 185 FT STRAND 194 200 FT HELIX 204 207 FT STRAND 211 216 FT STRAND 228 233 FT STRAND 238 245 FT HELIX 250 253 FT TURN 263 266 FT HELIX 269 277 FT STRAND 281 298 FT HELIX 300 305 FT STRAND 308 311 FT HELIX 316 319 FT TURN 322 324 FT HELIX 327 341 FT TURN 342 346 FT STRAND 357 359 FT STRAND 361 365 FT STRAND 367 373 FT STRAND 375 381 FT STRAND 384 390 FT HELIX 392 394 FT HELIX 400 402 FT HELIX 405 424 FT HELIX 429 440 FT HELIX 441 445 FT TURN 448 450 FT HELIX 455 457 FT HELIX 462 464 FT STRAND 466 468 FT HELIX 476 482 FT STRAND 483 485 SQ SEQUENCE 1048 AA; 116785 MW; C31A392A4AE222FC CRC64; MASPASTNPA HDHFETFVQA QLCQDVLSSF QGLCRALGVE SGGGLSQYHK IKAQLNYWSA KSLWAKLDKR ASQPVYQQGQ ACTNTKCLVV GAGPCGLRAA VELALLGARV VLVEKRIKFS RHNVLHLWPF TIHDLRALGA KKFYGRFCTG TLDHISIRQL QLLLLKVALL LGVEIHWGVK FTGLQPPPRK GSGWRAQLQP NPPAQLASYE FDVLISAAGG KFVPEGFTIR EMRGKLAIGI TANFVNGRTV EETQVPEISG VARIYNQKFF QSLLKATGID LENIVYYKDE THYFVMTAKK QCLLRLGVLR QDLSETDQLL GKANVVPEAL QRFARAAADF ATHGKLGKLE FAQDARGRPD VAAFDFTSMM RAESSARVQE KHGARLLLGL VGDCLVEPFW PLGTGVARGF LAAFDAAWMV KRWAEGAGPL EVLAERESLY QLLSQTSPEN MHRNVAQYGL DPATRYPNLN LRAVTPNQVQ DLYDMMDKEH AQRKSDEPDS RKTTTGSAGT EELLHWCQEQ TAGFPGVHVT DFSSSWADGL ALCALVHHLQ PGLLEPSELQ GMGALEATTW ALRVAEHELG ITPVLSAQAV MAGSDPLGLI AYLSHFHSAF KNTSHSSGLV SQPSGTPSAI LFLGKLQRSL QRTRAKVDEE TPSTEEPPVS EPSMSPNTPE LSEHQEAGAE ELCELCGKHL YILERFCVDG HFFHRSCFCC HTCEATLWPG GYGQHPGDGH FYCLQHLPQE DQKEADNNGS LESQELPTPG DSNMQPDPSS PPVTRVSPVP SPSQPARRLI RLSSLERLRL SSLNIIPDSG AEPPPKPPRS CSDLARESLK SSFVGWGVPV QAPQVPEAIE KGDDEEEEEE EEEEEEEPLP PLEPELEQTL LTLAKNPGAM TKYPTWRRTL MRRAKEEEMK RFCKAQAIQR RLNEIEATMR ELEAEGTKLE LALRKESSSP EQQKKLWLDQ LLRLIQKKNS LVTEEAELMI TVQELDLEEK QRQLDHELRG YMNREETMKT EADLQSENQV LRKLLEVVNQ RDALIQFQEE RRLREMPA // ID MICA2_MOUSE Reviewed; 960 AA. AC Q8BML1; F6ZD54; F8WJF1; Q14DP1; Q3TR48; Q3UPU6; Q5DU17; DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 19-MAR-2014, entry version 89. DE RecName: Full=Protein-methionine sulfoxide oxidase MICAL2; DE EC=1.14.13.-; DE AltName: Full=Molecule interacting with CasL protein 2; DE Short=MICAL-2; DE Short=mMical2; GN Name=Mical2; Synonyms=Kiaa0750; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Brain; RA Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O., RA Koga H.; RT "Prediction of the coding sequences of mouse homologues of KIAA gene. RT The complete nucleotide sequences of mouse KIAA-homologous cDNAs RT identified by screening of terminal sequences of cDNA clones randomly RT sampled from size-fractionated libraries."; RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3). RC STRAIN=C57BL/6J; TISSUE=Aorta, Eye, Pituitary, and Vein; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP INTERACTION WITH PLXNA4. RX PubMed=12110185; DOI=10.1016/S0092-8674(02)00794-8; RA Terman J.R., Mao T., Pasterkamp R.J., Yu H.-H., Kolodkin A.L.; RT "MICALs, a family of conserved flavoprotein oxidoreductases, function RT in plexin-mediated axonal repulsion."; RL Cell 109:887-900(2002). RN [6] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=23911929; DOI=10.1016/j.molcel.2013.06.019; RA Lee B.C., Peterfi Z., Hoffmann F.W., Moore R.E., Kaya A., Avanesov A., RA Tarrago L., Zhou Y., Weerapana E., Fomenko D.E., Hoffmann P.R., RA Gladyshev V.N.; RT "MsrB1 and MICALs regulate actin assembly and macrophage function via RT reversible stereoselective methionine oxidation."; RL Mol. Cell 51:397-404(2013). CC -!- FUNCTION: Monooxygenase that promotes depolymerization of F-actin CC by mediating oxidation of specific methionine residues on actin. CC Acts by modifying actin subunits through the addition of oxygen to CC form methionine-sulfoxide, leading to promote actin filament CC severing and prevent repolymerization. CC -!- CATALYTIC ACTIVITY: [protein]-methionine + NADPH + O(2) = CC [protein]-methionine-sulfoxide + NADP(+) + H(2)O. CC -!- COFACTOR: FAD (By similarity). CC -!- SUBUNIT: Interacts with RAB1B (By similarity). Interacts with VIM CC and PLXNA4. CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Cytoplasm, CC cytoskeleton (By similarity). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q8BML1-1; Sequence=Displayed; CC Name=2; CC IsoId=Q8BML1-2; Sequence=VSP_042597, VSP_042599; CC Note=No experimental confirmation available; CC Name=3; CC IsoId=Q8BML1-3; Sequence=VSP_042598; CC Note=No experimental confirmation available; CC -!- SIMILARITY: Belongs to the Mical family. CC -!- SIMILARITY: Contains 1 CH (calponin-homology) domain. CC -!- SIMILARITY: Contains 1 LIM zinc-binding domain. CC -!- SEQUENCE CAUTION: CC Sequence=BAD90416.1; Type=Erroneous initiation; Note=Translation N-terminally shortened; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK220353; BAD90416.1; ALT_INIT; mRNA. DR EMBL; AK030608; BAC27044.1; -; mRNA. DR EMBL; AK138935; BAE23824.1; -; mRNA. DR EMBL; AK143191; BAE25298.1; -; mRNA. DR EMBL; AK163078; BAE37182.1; -; mRNA. DR EMBL; AC100153; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC132392; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC166834; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC111895; AAI11896.1; -; mRNA. DR EMBL; BC112415; AAI12416.1; -; mRNA. DR RefSeq; NP_001180234.1; NM_001193305.1. DR RefSeq; NP_796256.1; NM_177282.5. DR RefSeq; XP_006508017.1; XM_006507954.1. DR UniGene; Mm.488195; -. DR UniGene; Mm.52312; -. DR ProteinModelPortal; Q8BML1; -. DR SMR; Q8BML1; 16-488, 511-629, 749-807. DR STRING; 10090.ENSMUSP00000102260; -. DR PhosphoSite; Q8BML1; -. DR PaxDb; Q8BML1; -. DR PRIDE; Q8BML1; -. DR Ensembl; ENSMUST00000037991; ENSMUSP00000047639; ENSMUSG00000038244. [Q8BML1-2] DR Ensembl; ENSMUST00000050149; ENSMUSP00000051163; ENSMUSG00000038244. [Q8BML1-1] DR Ensembl; ENSMUST00000106648; ENSMUSP00000102259; ENSMUSG00000038244. [Q8BML1-3] DR GeneID; 320878; -. DR KEGG; mmu:320878; -. DR UCSC; uc009jgm.2; mouse. [Q8BML1-3] DR UCSC; uc009jgn.2; mouse. [Q8BML1-1] DR UCSC; uc009jgo.2; mouse. [Q8BML1-2] DR CTD; 9645; -. DR MGI; MGI:2444947; Mical2. DR eggNOG; COG5069; -. DR GeneTree; ENSGT00640000091174; -. DR HOGENOM; HOG000047263; -. DR HOVERGEN; HBG052474; -. DR OMA; CSVCATT; -. DR OrthoDB; EOG769ZHM; -. DR TreeFam; TF324129; -. DR ChiTaRS; MICAL2; mouse. DR NextBio; 397627; -. DR PRO; PR:Q8BML1; -. DR ArrayExpress; Q8BML1; -. DR Bgee; Q8BML1; -. DR Genevestigator; Q8BML1; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell. DR GO; GO:0003779; F:actin binding; IDA:UniProtKB. DR GO; GO:0071949; F:FAD binding; ISS:UniProtKB. DR GO; GO:0016709; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen; IDA:UniProtKB. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0030042; P:actin filament depolymerization; IDA:UniProtKB. DR GO; GO:0019417; P:sulfur oxidation; IDA:UniProtKB. DR Gene3D; 1.10.418.10; -; 1. DR Gene3D; 2.10.110.10; -; 1. DR InterPro; IPR001715; CH-domain. DR InterPro; IPR002938; mOase_FAD-bd. DR InterPro; IPR003042; Rng_hydrolase-like. DR InterPro; IPR001781; Znf_LIM. DR Pfam; PF00307; CH; 1. DR Pfam; PF01494; FAD_binding_3; 1. DR Pfam; PF00412; LIM; 1. DR PRINTS; PR00420; RNGMNOXGNASE. DR SMART; SM00033; CH; 1. DR SMART; SM00132; LIM; 1. DR SUPFAM; SSF47576; SSF47576; 1. DR PROSITE; PS50021; CH; 1. DR PROSITE; PS00478; LIM_DOMAIN_1; 1. DR PROSITE; PS50023; LIM_DOMAIN_2; 1. PE 1: Evidence at protein level; KW Actin-binding; Alternative splicing; Complete proteome; Cytoplasm; KW Cytoskeleton; FAD; Flavoprotein; LIM domain; Metal-binding; KW Monooxygenase; NADP; Oxidoreductase; Reference proteome; Zinc. FT CHAIN 1 960 Protein-methionine sulfoxide oxidase FT MICAL2. FT /FTId=PRO_0000075845. FT DOMAIN 516 619 CH. FT DOMAIN 751 813 LIM zinc-binding. FT NP_BIND 97 125 FAD (By similarity). FT REGION 2 494 Monooxygenase domain (By similarity). FT BINDING 97 97 FAD (By similarity). FT BINDING 116 116 FAD (By similarity). FT BINDING 118 118 FAD (By similarity). FT BINDING 123 123 FAD (By similarity). FT BINDING 125 125 FAD (By similarity). FT BINDING 398 398 FAD (By similarity). FT VAR_SEQ 736 736 Q -> QDCRRVSGIGKPVLCSASRPPGTSCCPKLEESTPRL FT PPPLKRQFSSTVATGQVLRELNQVPASGECPSRPWRARAKS FT DLQLGGVENLATLPRTCQGALALSGVLRRLQQVEEKVLQKR FT AQNLANREFHTKNIKEKAAHLASMFGHGDLPQDKLLSKRVP FT HAHPPSPPSCLPSPHPAAASSPPAADSVSPARKLTVGKVSS FT GIGAAAEVLVNLYLNDHRPKTQATSPDL (in isoform FT 2). FT /FTId=VSP_042597. FT VAR_SEQ 799 960 GKFYCKPHFVHCKTSSKQRKRRAELNQQREEEGTWQEQEAP FT RRDVPTESSCAVAAISTPEGSPPGTSTSFFRKALSWPLRLT FT RGLLNLPQSLLRWMQGLQEAAGHHVRDNAHNYCFMFELLSL FT GLLLLWAFSKVLAAMYRESEESLENIRSWLLRFIPVKLQ FT -> GNPRGQESTSLWPWSQM (in isoform 3). FT /FTId=VSP_042598. FT VAR_SEQ 863 960 GTSTSFFRKALSWPLRLTRGLLNLPQSLLRWMQGLQEAAGH FT HVRDNAHNYCFMFELLSLGLLLLWAFSKVLAAMYRESEESL FT ENIRSWLLRFIPVKLQ -> VRFSLPVLHPLLG (in FT isoform 2). FT /FTId=VSP_042599. SQ SEQUENCE 960 AA; 110072 MW; 0D70BBA2144730E2 CRC64; MGENEDEKQA QASQVFENFV QATTCKGTLQ AFNILTCLLD LDPLDHRNFY SQLKSKVNTW KAKALWHKLD KRGSHKEYKR GKACSNTKCL IVGGGPCGLR TAIELAYLGA KVVVVEKRDT FSRNNVLHLW PFTIHDLRGL GAKKFYGKFC AGSIDHISIR QLQLILFKVA LMLGVEVHVN VEFVRVLEPP EDQENQKVGW RAEFLPADHA LSDFEFDVII GADGHRNTLE GFRRKEFRGK LAIAITANFI NRNSTAEAKV EEISGVAFIF NQKFFQDLKE ETGIDLENIV YYKDSTHYFV MTAKKQSLLD KGVILNDYID TEMLLCSENV NQDNLLSYAR EAADFATNYQ LPSLDFAINH NGQPDVAMFD FTSMYASENA ALMRERQAHQ LLVALVGDSL LEPFWPMGTG CARGFLAAFD TAWMVKSWDQ GTPPLEVLAE RESLYRLLPQ TTPENINKNF EQYTLDPATR YPNLNLHCVR PHQVKHLYIT KEMDRFPLER WGSVRRSVSL SRRESDIRPN KLLTWCQQQT KGYQHVRVTD LTTSWRSGLA LCAIIHSFRP ELINFDSLNE DDAVENNQLA FDVAKREFGI LPVTTGKEMA STQEPDKLSM VMYLSKFYEL FRGTPLRPMD SWRKNYGENA DFGLGKTFIQ NNYLNLTLPR KRTPRVDTQT EENDMNKRRR QGFNHLEELP SFSSRSLGSS QEYAKESGSQ NKVKHMANQL LAKFEENTRN PSVVKQESPR KAFPLSLGGR DTCYFCKKRV YMIERLSAEG HFFHQECFRC SVCSATLRLA AYAFDCDEGK FYCKPHFVHC KTSSKQRKRR AELNQQREEE GTWQEQEAPR RDVPTESSCA VAAISTPEGS PPGTSTSFFR KALSWPLRLT RGLLNLPQSL LRWMQGLQEA AGHHVRDNAH NYCFMFELLS LGLLLLWAFS KVLAAMYRES EESLENIRSW LLRFIPVKLQ // ID MICA3_MOUSE Reviewed; 1993 AA. AC Q8CJ19; B2RR77; Q3UGQ8; Q3V160; Q69ZY5; Q80TE8; Q8BXB1; DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot. DT 13-JUL-2010, sequence version 2. DT 19-MAR-2014, entry version 96. DE RecName: Full=Protein-methionine sulfoxide oxidase MICAL3; DE EC=1.14.13.-; DE AltName: Full=Molecule interacting with CasL protein 3; DE Short=MICAL-3; GN Name=Mical3; Synonyms=Kiaa0819, Kiaa1364; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3). RC TISSUE=Testis; RA Korenbaum E., Hust H., Munck M., Noegel A.A.; RT "Flavoprotein oxidoreductase MICAL-3 is associated with spermatid RT development."; RL Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE RP SEQUENCE [LARGE SCALE MRNA] OF 1526-1993 (ISOFORM 1). RC TISSUE=Brain; RX PubMed=12693553; DOI=10.1093/dnares/10.1.35; RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S., RA Nakajima D., Nagase T., Ohara O., Koga H.; RT "Prediction of the coding sequences of mouse homologues of KIAA gene: RT II. The complete nucleotide sequences of 400 mouse KIAA-homologous RT cDNAs identified by screening of terminal sequences of cDNA clones RT randomly sampled from size-fractionated libraries."; RL DNA Res. 10:35-48(2003). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). RC TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-695 (ISOFORMS 1/2), AND RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1740 (ISOFORM 4). RC STRAIN=C57BL/6J; TISSUE=Head, and Testis; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). CC -!- FUNCTION: Monooxygenase that promotes depolymerization of F-actin CC by mediating oxidation of specific methionine residues on actin. CC Acts by modifying actin subunits through the addition of oxygen to CC form methionine-sulfoxide, leading to promote actin filament CC severing and prevent repolymerization. Involved in exocytic CC vesicles tethering and fusion: the monooxygenase activity is CC required for this process (By similarity). CC -!- CATALYTIC ACTIVITY: [protein]-methionine + NADPH + O(2) = CC [protein]-methionine-sulfoxide + NADP(+) + H(2)O. CC -!- COFACTOR: FAD (By similarity). CC -!- SUBUNIT: Interacts with RAB1B. Interacts with ERC1 and RAB8A (By CC similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Cytoplasm, CC cytoskeleton (By similarity). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; CC IsoId=Q8CJ19-1; Sequence=Displayed; CC Name=2; CC IsoId=Q8CJ19-2; Sequence=VSP_039491, VSP_039492; CC Note=No experimental confirmation available; CC Name=3; CC IsoId=Q8CJ19-3; Sequence=VSP_039493, VSP_039494; CC Name=4; CC IsoId=Q8CJ19-4; Sequence=VSP_039490, VSP_039495; CC -!- SIMILARITY: Belongs to the Mical family. CC -!- SIMILARITY: Contains 1 CH (calponin-homology) domain. CC -!- SIMILARITY: Contains 1 LIM zinc-binding domain. CC -!- SEQUENCE CAUTION: CC Sequence=BAC65779.1; Type=Erroneous initiation; Note=Translation N-terminally shortened; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF536756; AAN06715.1; -; mRNA. DR EMBL; AK173033; BAD32311.1; -; mRNA. DR EMBL; AK122497; BAC65779.1; ALT_INIT; mRNA. DR EMBL; AC079443; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC083894; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC138257; AAI38258.1; -; mRNA. DR EMBL; AK132669; BAE21292.1; -; mRNA. DR EMBL; AK147803; BAE28149.1; -; mRNA. DR EMBL; AK048201; BAC33271.1; -; mRNA. DR RefSeq; NP_001257404.1; NM_001270475.1. DR RefSeq; NP_700445.2; NM_153396.3. DR RefSeq; XP_006505862.1; XM_006505799.1. DR RefSeq; XP_006505863.1; XM_006505800.1. DR RefSeq; XP_006505866.1; XM_006505803.1. DR UniGene; Mm.122399; -. DR UniGene; Mm.491728; -. DR ProteinModelPortal; Q8CJ19; -. DR SMR; Q8CJ19; 9-489, 515-630, 762-818. DR BioGrid; 228787; 5. DR IntAct; Q8CJ19; 5. DR STRING; 10090.ENSMUSP00000096056; -. DR PhosphoSite; Q8CJ19; -. DR PaxDb; Q8CJ19; -. DR PRIDE; Q8CJ19; -. DR Ensembl; ENSMUST00000077159; ENSMUSP00000076402; ENSMUSG00000003178. [Q8CJ19-3] DR GeneID; 194401; -. DR KEGG; mmu:194401; -. DR UCSC; uc009dnw.1; mouse. [Q8CJ19-1] DR UCSC; uc009dnx.1; mouse. [Q8CJ19-4] DR UCSC; uc009dnz.2; mouse. [Q8CJ19-3] DR UCSC; uc009doa.1; mouse. [Q8CJ19-2] DR CTD; 57553; -. DR MGI; MGI:2442733; Mical3. DR eggNOG; COG5069; -. DR GeneTree; ENSGT00640000091174; -. DR HOGENOM; HOG000047263; -. DR HOVERGEN; HBG081827; -. DR InParanoid; Q8CJ19; -. DR OMA; STGIRRQ; -. DR OrthoDB; EOG769ZHM; -. DR TreeFam; TF324129; -. DR ChiTaRS; MICAL3; mouse. DR NextBio; 371593; -. DR PRO; PR:Q8CJ19; -. DR Bgee; Q8CJ19; -. DR Genevestigator; Q8CJ19; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell. DR GO; GO:0003779; F:actin binding; ISS:UniProtKB. DR GO; GO:0071949; F:FAD binding; ISS:UniProtKB. DR GO; GO:0016709; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen; ISS:UniProtKB. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0030042; P:actin filament depolymerization; ISS:UniProtKB. DR GO; GO:0006887; P:exocytosis; IEA:UniProtKB-KW. DR Gene3D; 1.10.418.10; -; 1. DR Gene3D; 2.10.110.10; -; 1. DR InterPro; IPR001715; CH-domain. DR InterPro; IPR022735; DUF3585. DR InterPro; IPR002938; mOase_FAD-bd. DR InterPro; IPR003042; Rng_hydrolase-like. DR InterPro; IPR001781; Znf_LIM. DR Pfam; PF00307; CH; 1. DR Pfam; PF12130; DUF3585; 1. DR Pfam; PF01494; FAD_binding_3; 1. DR Pfam; PF00412; LIM; 1. DR PRINTS; PR00420; RNGMNOXGNASE. DR SMART; SM00033; CH; 1. DR SMART; SM00132; LIM; 1. DR SUPFAM; SSF47576; SSF47576; 1. DR PROSITE; PS50021; CH; 1. DR PROSITE; PS00478; LIM_DOMAIN_1; 1. DR PROSITE; PS50023; LIM_DOMAIN_2; 1. PE 2: Evidence at transcript level; KW Actin-binding; Alternative splicing; Coiled coil; Complete proteome; KW Cytoplasm; Cytoskeleton; Exocytosis; FAD; Flavoprotein; LIM domain; KW Metal-binding; Monooxygenase; NADP; Oxidoreductase; Phosphoprotein; KW Reference proteome; Zinc. FT CHAIN 1 1993 Protein-methionine sulfoxide oxidase FT MICAL3. FT /FTId=PRO_0000075847. FT DOMAIN 518 621 CH. FT DOMAIN 762 824 LIM zinc-binding. FT NP_BIND 88 117 FAD (Potential). FT NP_BIND 97 125 FAD (By similarity). FT REGION 2 494 Monooxygenase domain (By similarity). FT COILED 1817 1983 Potential. FT COMPBIAS 688 691 Poly-Glu. FT BINDING 97 97 FAD (By similarity). FT BINDING 116 116 FAD (By similarity). FT BINDING 118 118 FAD (By similarity). FT BINDING 123 123 FAD (By similarity). FT BINDING 125 125 FAD (By similarity). FT BINDING 398 398 FAD (By similarity). FT MOD_RES 649 649 Phosphoserine (By similarity). FT MOD_RES 887 887 Phosphothreonine (By similarity). FT MOD_RES 1335 1335 Phosphoserine (By similarity). FT MOD_RES 1339 1339 Phosphothreonine (By similarity). FT MOD_RES 1369 1369 Phosphoserine (By similarity). FT MOD_RES 1382 1382 Phosphoserine (By similarity). FT MOD_RES 1452 1452 Phosphothreonine (By similarity). FT VAR_SEQ 1 871 Missing (in isoform 4). FT /FTId=VSP_039490. FT VAR_SEQ 748 774 GSIKKEFPQNLGGSDTCYFCQKRVYVM -> VSPKLSSRMT FT TWYRKEGLHAAISQALV (in isoform 2). FT /FTId=VSP_039491. FT VAR_SEQ 775 1993 Missing (in isoform 2). FT /FTId=VSP_039492. FT VAR_SEQ 810 864 GKFYCKPHYCYRLSGYAQRKRPAVAPLSGKEVKGALQDGPT FT ADANGLASVAASSA -> EFSPNFWTSASYHVPVALPATVM FT PMCLLYHPSQVLVCLEGGPAFMSPVLFNDTNS (in FT isoform 3). FT /FTId=VSP_039493. FT VAR_SEQ 865 1993 Missing (in isoform 3). FT /FTId=VSP_039494. FT VAR_SEQ 1016 1061 Missing (in isoform 4). FT /FTId=VSP_039495. FT CONFLICT 281 281 A -> T (in Ref. 1; AAN06715). FT CONFLICT 1249 1249 P -> H (in Ref. 5; BAE28149). SQ SEQUENCE 1993 AA; 223721 MW; 5059DCB5EF4DB091 CRC64; MEERKQETTN QAHVLFDRFV QATTCKGTLR AFQELCDHLE LKPKDYRSFY HKLKSKLNYW KAKALWAKLD KRGSHKDYKK GKACTNTKCL IIGAGPCGLR TAIDLSLLGA KVVVIEKRDA FSRNNVLHLW PFTIHDLRGL GAKKFYGKFC AGAIDHISIR QLQLILLKVA LILGIEIHVN VEFQGLVQPP EDQENERIGW RALVHPKTHP VSEYEFEVII GGDGRRNTLE GFRRKEFRGK LAIAITANFI NRNTTAEAKV EEISGVAFIF NQKFFQELRE ATGIDLENIV YYKDDTHYFV MTAKKQSLLD KGVILHDYTD TELLLSRENV DQEALLNYAR EAADFSTQQQ LPSLDFAINH YGQPDVAMFD FTCMYASENA ALVREQNGHQ LLVALVGDSL LEPFWPMGTG IARGFLAAMD SAWMVRSWSL GTSPLEVLAE RESIYRLLPQ TTPENVSKNF SQYSIDPVTR YPNININFLR PSQVRHLYDS GETKDIHLEM ENMVNPRTTP KLTRNESVAR SSKLLGWCQR QTEGYSGVNV TDLTMSWKSG LALCAIIHRY RPDLIDFDSL DEQNVEKNNQ LAFDIAEKEL GISPIMTGKE MASVGEPDKL SMVMYLTQFY EMFKDSLSSS DTLDLNAEEK AVLIASTKSP ISFLSKLGQT ISRKRSPKDK KEKDSDGAGK RRKTSQSEEE EPPRSYKGER PTLVSTLTDR RMDAAVGNQN KVKYMATQLL AKFEENAPAQ STGVRRQGSI KKEFPQNLGG SDTCYFCQKR VYVMERLSAE GKFFHRSCFK CEYCATTLRL SAYAYDIEDG KFYCKPHYCY RLSGYAQRKR PAVAPLSGKE VKGALQDGPT ADANGLASVA ASSAERSPGT SMNGLEEPSI AKRLRGTPER IELENYRRSV RQVEELEEVP EETQAEHNLS SVLDKGTEED VASSSSESEM EEEEEEDDED DHLPTSDLGG VPWKEAVRIH ALLKGRSEEE LEASKNFEPE EEEEEEEYEE EDEEYEEEEE EESSEAGNKR LQQIITAADP LAIQADVHWT HIREREAEER MLPTSESSTS RAPLDEDDLE EDADSEPAET EGEAAEDGDP GDTGAELDDQ HWSDDIPSDA EAEHRLQSQA KVKAELELRV SENEEEKPSD APKQEERGTS QVSSPSQPPE KQVGVFSPAR SPGTEEAKSP LATKVKSPEE PLFPTPLLLR EKPKAEVPEE QKAVLSPIRS QPVALPEARS PTSPTSLQPE SLLAPPTPPT PPPTQLPICS QPQPSSDASI PSPTKSPIRF QPVPAKTSTP LTPLPVKSQG DPKDRLSGPL AVEEVLKRSD LVEEFWMKSA EIRRSLGLTP VDRSKGSEPS LPSPASKPIS LKSYSVDKSP QDEGLCLLKP PSVPKRLGLP KSAGDQPPLL TPKSPSDKEL RSSQEERRDL SSSSGLGLHD SSSNMKTLGS QSFNTSDSTM LTPPSSPPPP PPPNEEPATL RRKPHQTFER REASIIPPPT PASFMRPPRE PAQPPREEVR KSFVESVDEI PFADDVEDTY DDKTEDSSLQ EKFFTPPSCW SRSEKLQAKE NGRLPPLEQD VPPQKRGLPL VSAEAKELAE ERMRAREKSV KSQALRDAMA KQLSRMQAME MVSSRSHTAQ SQGKELGSES TRHPSLRGTQ EPTLKHEATS EEILSPPSDS GGPDGSVTSS EGSSGKSKKR SSLFSPRRNK KEKKTKGEAR PPEKPSPGLP EDVVAKPKSL WKSVFSGYKK DKKKKSDEKS CSSTPSSGAT VDSGQRRASP MVRAELQLRR QLSFSEDSDL SSDDILERSS QKSKREPRTY TEEELSAKLT RRVQKAARRQ AKQEELKRLH RAQIIQRQLE QVEEKQRQLE ERGVAVEKAL RGEAGMGKKD DPKLMQEWFK LVQEKNAMVR YESELMIFAR ELELEDRQSR LQQELRERMA VEDHLKTEGE LSEEKKILNE MLEVVEQRDS LVALLEEQRL REKEEDKDLE AAMLCKGFSL DWS // ID MINA_MOUSE Reviewed; 465 AA. AC Q8CD15; Q8QZX1; Q9CQ03; DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot. DT 23-OCT-2007, sequence version 2. DT 19-MAR-2014, entry version 81. DE RecName: Full=Bifunctional lysine-specific demethylase and histidyl-hydroxylase MINA; DE EC=1.14.11.-; DE AltName: Full=Histone lysine demethylase MINA; DE AltName: Full=MYC-induced nuclear antigen; GN Name=Mina; Synonyms=Mina53; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE RP SPECIFICITY, DEVELOPMENTAL STAGE, AND INDUCTION. RC TISSUE=Stomach; RX PubMed=16533354; DOI=10.1111/j.1365-2605.2005.00572.x; RA Tsuneoka M., Nishimune Y., Ohta K., Teye K., Tanaka H., Soejima M., RA Iida H., Inokuchi T., Kimura H., Koda Y.; RT "Expression of Mina53, a product of a Myc target gene in mouse RT testis."; RL Int. J. Androl. 29:323-330(2006). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Embryo, Embryonic testis, and Pancreas; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6, and FVB/N; TISSUE=Kidney, and Olfactory epithelium; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: Oxygenase that can act as both a histone lysine CC demethylase and a ribosomal histidine hydroxylase. Is involved in CC the demethylation of trimethylated 'Lys-9' on histone H3 CC (H3K9me3), leading to an increase in ribosomal RNA expression. CC Also catalyzes the hydroxylation of 60S ribosomal protein L27a on CC 'His-39' (By similarity). May play an important role in cell CC growth and survival. May be involved in ribosome biogenesis, most CC likely during the assembly process of pre-ribosomal particles. CC -!- CATALYTIC ACTIVITY: L-histidine-[60S ribosomal protein L27a] + 2- CC oxoglutarate + O(2) = (3S)-3-hydroxy-L-histidine-[60S ribosomal CC protein L27a] + succinate + CO(2). CC -!- COFACTOR: Binds 1 Fe(2+) ion per subunit (By similarity). CC -!- SUBCELLULAR LOCATION: Nucleus. Nucleus, nucleolus. CC -!- TISSUE SPECIFICITY: Predominantly expressed in testis. Expressed CC at high levels in spleen, thymus, and colon, but barely detectable CC in brain, skeletal muscle, and seminal vesicle (at protein level). CC -!- DEVELOPMENTAL STAGE: In testis, expressed in the nuclei of CC spermatogonia at all stages of the seminiferous epithelial cycle, CC and in meiotic prophase cells such as preleptotene, leptotene and CC zygotene, and weakly in early pachytene spermatocytes, but is CC absent in late pachytene spermatocytes, spermatids and mature CC sperm (at protein level). CC -!- INDUCTION: Up-regulated in experimentally-induced cryptorchid CC testis. CC -!- SIMILARITY: Belongs to the MINA53/NO66 family. CC -!- SIMILARITY: Contains 1 JmjC domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AB177385; BAD60965.1; -; mRNA. DR EMBL; AK007810; BAB25275.1; -; mRNA. DR EMBL; AK013451; BAB28860.1; -; mRNA. DR EMBL; AK031671; BAC27503.1; -; mRNA. DR EMBL; BC023462; AAH23462.1; -; mRNA. DR EMBL; BC025109; AAH25109.1; -; mRNA. DR EMBL; BC058242; AAH58242.1; -; mRNA. DR RefSeq; NP_080186.3; NM_025910.3. DR RefSeq; XP_006522542.1; XM_006522479.1. DR UniGene; Mm.289150; -. DR ProteinModelPortal; Q8CD15; -. DR SMR; Q8CD15; 31-465. DR IntAct; Q8CD15; 1. DR MINT; MINT-4115257; -. DR PhosphoSite; Q8CD15; -. DR PaxDb; Q8CD15; -. DR PRIDE; Q8CD15; -. DR DNASU; 67014; -. DR Ensembl; ENSMUST00000023407; ENSMUSP00000023407; ENSMUSG00000022724. DR Ensembl; ENSMUST00000160571; ENSMUSP00000125297; ENSMUSG00000022724. DR GeneID; 67014; -. DR KEGG; mmu:67014; -. DR UCSC; uc007zph.2; mouse. DR CTD; 84864; -. DR MGI; MGI:1914264; Mina. DR eggNOG; NOG83808; -. DR GeneTree; ENSGT00390000000083; -. DR HOGENOM; HOG000007965; -. DR HOVERGEN; HBG055265; -. DR InParanoid; Q8CD15; -. DR OMA; STYQNNS; -. DR OrthoDB; EOG7T1RBJ; -. DR TreeFam; TF318659; -. DR ChiTaRS; MINA; mouse. DR NextBio; 323310; -. DR PRO; PR:Q8CD15; -. DR ArrayExpress; Q8CD15; -. DR Bgee; Q8CD15; -. DR CleanEx; MM_MINA; -. DR Genevestigator; Q8CD15; -. DR GO; GO:0005829; C:cytosol; IDA:MGI. DR GO; GO:0005730; C:nucleolus; ISO:MGI. DR GO; GO:0005667; C:transcription factor complex; IPI:MGI. DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0001191; F:RNA polymerase II transcription factor binding transcription factor activity involved in negative regulation of transcription; IGI:MGI. DR GO; GO:0042127; P:regulation of cell proliferation; ISO:MGI. DR GO; GO:0042254; P:ribosome biogenesis; IEA:UniProtKB-KW. DR InterPro; IPR003347; JmjC_dom. DR InterPro; IPR013109; NO66/MINA. DR PANTHER; PTHR13096:SF0; PTHR13096:SF0; 1. DR Pfam; PF08007; Cupin_4; 1. DR SMART; SM00558; JmjC; 1. DR PROSITE; PS51184; JMJC; 1. PE 1: Evidence at protein level; KW Complete proteome; Dioxygenase; Iron; Metal-binding; Nucleus; KW Oxidoreductase; Phosphoprotein; Reference proteome; KW Ribosome biogenesis; Transcription; Transcription regulation. FT CHAIN 1 465 Bifunctional lysine-specific demethylase FT and histidyl-hydroxylase MINA. FT /FTId=PRO_0000308378. FT DOMAIN 139 271 JmjC. FT METAL 179 179 Iron; catalytic (By similarity). FT METAL 181 181 Iron; catalytic (By similarity). FT METAL 240 240 Iron; catalytic (By similarity). FT MOD_RES 309 309 Phosphoserine (By similarity). FT CONFLICT 15 15 A -> E (in Ref. 3; AAH25109/AAH23462). FT CONFLICT 107 107 S -> N (in Ref. 2; BAC27503). FT CONFLICT 440 440 D -> E (in Ref. 3; AAH25109/AAH23462). SQ SEQUENCE 465 AA; 53517 MW; E0504FE459FFC47A CRC64; MPKKVQPTGD ENEEASVPCK RVKEELPETL SVLNFDSPSS FFESLISPIK VETFFKEFWE QKPLLIQRDD PVLAKYYQSL FSLSDLKRLC KKGVYYGRDV NVCRSISGKK KVLNKDGRAH FLQLRKDFDQ KRATIQFHQP QRYKDELWRI QEKLECYFGS LVGSNVYMTP AGSQGLPPHY DDVEVFILQL EGTKHWRLYS PTVPLAHEYS VESEDRIGTP THDFLLKPGD LLYFPRGTIH QAETPSGLAY SIHLTISTYQ NNSWGDCLLD SISGFVFDIA KEDVALRSGM PRRMLLNVET PADVTRKLSG FLRTLADQLE GREELLSSDM KKDFVKHRLP PFFEGNGTET MDPGKQLPRL DNIIRLQFKD HIVLTVGPDK NPFDEAQQKV VYIYHSLKNV RQMHMIGEEE ESEIFGLRFP LSHVDALKQI WCGSPIRVKD LKLDTDEEKE NLALSLWSES LIQVL // ID MIOX_MOUSE Reviewed; 285 AA. AC Q9QXN5; Q5S8D0; Q91WQ8; DT 12-FEB-2003, integrated into UniProtKB/Swiss-Prot. DT 08-NOV-2005, sequence version 2. DT 19-FEB-2014, entry version 108. DE RecName: Full=Inositol oxygenase; DE EC=1.13.99.1; DE AltName: Full=Aldehyde reductase-like 6; DE AltName: Full=Myo-inositol oxygenase; DE Short=MI oxygenase; DE AltName: Full=Renal-specific oxidoreductase; GN Name=Miox; Synonyms=Aldrl6, Rsor; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY. RC TISSUE=Kidney; RX PubMed=10944187; DOI=10.1073/pnas.160266197; RA Yang Q., Dixit B., Wada J., Tian Y., Wallner E.I., Srivastva S.K., RA Kanwar Y.S.; RT "Identification of a renal-specific oxido-reductase in newborn RT diabetic mice."; RL Proc. Natl. Acad. Sci. U.S.A. 97:9896-9901(2000). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=C57BL/6; TISSUE=Kidney; RX PubMed=15504367; DOI=10.1016/j.bbrc.2004.09.209; RA Arner R.J., Prabhu K.S., Reddy C.C.; RT "Molecular cloning, expression, and characterization of myo-inositol RT oxygenase from mouse, rat, and human kidney."; RL Biochem. Biophys. Res. Commun. 324:1386-1392(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Kidney; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH IRON AND RP MYO-INOSITOL, AND COFACTOR. RX PubMed=17012379; DOI=10.1073/pnas.0605143103; RA Brown P.M., Caradoc-Davies T.T., Dickson J.M., Cooper G.J., RA Loomes K.M., Baker E.N.; RT "Crystal structure of a substrate complex of myo-inositol oxygenase, a RT di-iron oxygenase with a key role in inositol metabolism."; RL Proc. Natl. Acad. Sci. U.S.A. 103:15032-15037(2006). RN [5] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH IRON AND RP MYO-INOSITOL, AND COFACTOR. RX PubMed=18364358; DOI=10.1074/jbc.M800348200; RA Thorsell A.G., Persson C., Voevodskaya N., Busam R.D., Hammarstrom M., RA Graslund S., Graslund A., Hallberg B.M.; RT "Structural and biophysical characterization of human myo-inositol RT oxygenase."; RL J. Biol. Chem. 283:15209-15216(2008). CC -!- CATALYTIC ACTIVITY: Myo-inositol + O(2) = D-glucuronate + H(2)O. CC -!- COFACTOR: Binds 2 iron ions per subunit. CC -!- PATHWAY: Polyol metabolism; myo-inositol degradation into D- CC glucuronate; D-glucuronate from myo-inositol: step 1/1. CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- TISSUE SPECIFICITY: Kidney specific. Renal proximal tubules. CC -!- SIMILARITY: Belongs to the myo-inositol oxygenase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF197127; AAF25202.1; -; mRNA. DR EMBL; AY738257; AAV65815.1; -; mRNA. DR EMBL; BC013543; AAH13543.1; -; mRNA. DR RefSeq; NP_064361.2; NM_019977.2. DR UniGene; Mm.158200; -. DR PDB; 2HUO; X-ray; 2.00 A; A=1-285. DR PDB; 3BXD; X-ray; 2.00 A; A=1-285. DR PDBsum; 2HUO; -. DR PDBsum; 3BXD; -. DR ProteinModelPortal; Q9QXN5; -. DR SMR; Q9QXN5; 28-285. DR IntAct; Q9QXN5; 1. DR MINT; MINT-4102022; -. DR PhosphoSite; Q9QXN5; -. DR REPRODUCTION-2DPAGE; Q9QXN5; -. DR PaxDb; Q9QXN5; -. DR PRIDE; Q9QXN5; -. DR DNASU; 56727; -. DR Ensembl; ENSMUST00000023282; ENSMUSP00000023282; ENSMUSG00000022613. DR GeneID; 56727; -. DR KEGG; mmu:56727; -. DR UCSC; uc007xgc.1; mouse. DR CTD; 55586; -. DR MGI; MGI:1891725; Miox. DR eggNOG; NOG135479; -. DR GeneTree; ENSGT00390000016211; -. DR HOGENOM; HOG000163182; -. DR HOVERGEN; HBG039556; -. DR InParanoid; Q9QXN5; -. DR KO; K00469; -. DR OMA; NFYREQH; -. DR OrthoDB; EOG7DZ8KD; -. DR TreeFam; TF300089; -. DR BRENDA; 1.13.99.1; 3474. DR SABIO-RK; Q9QXN5; -. DR UniPathway; UPA00111; UER00527. DR EvolutionaryTrace; Q9QXN5; -. DR NextBio; 313210; -. DR PRO; PR:Q9QXN5; -. DR ArrayExpress; Q9QXN5; -. DR Bgee; Q9QXN5; -. DR CleanEx; MM_MIOX; -. DR Genevestigator; Q9QXN5; -. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0016234; C:inclusion body; ISS:UniProtKB. DR GO; GO:0004033; F:aldo-keto reductase (NADP) activity; IDA:UniProtKB. DR GO; GO:0008199; F:ferric iron binding; ISS:UniProtKB. DR GO; GO:0050113; F:inositol oxygenase activity; ISS:UniProtKB. DR GO; GO:0050661; F:NADP binding; IEA:Ensembl. DR GO; GO:0016651; F:oxidoreductase activity, acting on NAD(P)H; IDA:UniProtKB. DR GO; GO:0019310; P:inositol catabolic process; ISS:UniProtKB. DR InterPro; IPR018170; Aldo/ket_reductase_CS. DR InterPro; IPR007828; Inositol_oxygenase. DR PANTHER; PTHR12588; PTHR12588; 1. DR Pfam; PF05153; DUF706; 1. DR PROSITE; PS00063; ALDOKETO_REDUCTASE_3; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Cytoplasm; Iron; Metal-binding; KW Oxidoreductase; Reference proteome. FT CHAIN 1 285 Inositol oxygenase. FT /FTId=PRO_0000079149. FT REGION 85 88 Substrate binding. FT REGION 141 142 Substrate binding. FT REGION 220 221 Substrate binding. FT METAL 98 98 Iron 1. FT METAL 123 123 Iron 1. FT METAL 124 124 Iron 1. FT METAL 124 124 Iron 2. FT METAL 194 194 Iron 2. FT METAL 220 220 Iron 2. FT METAL 253 253 Iron 1. FT BINDING 29 29 Substrate. FT BINDING 127 127 Substrate. FT CONFLICT 65 65 S -> G (in Ref. 1; AAF25202). FT STRAND 31 33 FT HELIX 37 50 FT HELIX 53 63 FT HELIX 73 79 FT HELIX 80 82 FT HELIX 95 109 FT HELIX 114 122 FT HELIX 125 132 FT HELIX 136 138 FT STRAND 145 148 FT TURN 155 159 FT HELIX 165 168 FT TURN 170 172 FT STRAND 173 176 FT HELIX 185 187 FT HELIX 194 204 FT HELIX 211 219 FT HELIX 223 226 FT TURN 232 234 FT HELIX 237 255 FT HELIX 264 278 SQ SEQUENCE 285 AA; 33164 MW; C6877BFF2B60D1A7 CRC64; MKVDVGPDPS LVYRPDVDPE MAKSKDSFRN YTSGPLLDRV FTTYKLMHTH QTVDFVSRKR IQYGSFSYKK MTIMEAVGML DDLVDESDPD VDFPNSFHAF QTAEGIRKAH PDKDWFHLVG LLHDLGKIMA LWGEPQWAVV GDTFPVGCRP QASVVFCDST FQDNPDLQDP RYSTELGMYQ PHCGLENVLM SWGHDEYLYQ MMKFNKFSLP SEAFYMIRFH SFYPWHTGGD YRQLCSQQDL DMLPWVQEFN KFDLYTKCPD LPDVESLRPY YQGLIDKYCP GTLSW // ID MMSA_MOUSE Reviewed; 535 AA. AC Q9EQ20; Q3TDA2; Q8CIB4; DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2001, sequence version 1. DT 19-MAR-2014, entry version 103. DE RecName: Full=Methylmalonate-semialdehyde dehydrogenase [acylating], mitochondrial; DE Short=MMSDH; DE Short=Malonate-semialdehyde dehydrogenase [acylating]; DE EC=1.2.1.18; DE EC=1.2.1.27; DE AltName: Full=Aldehyde dehydrogenase family 6 member A1; DE Flags: Precursor; GN Name=Aldh6a1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Liver; RA Yang B.-Z., Zhang L.-F., Roe C.R., Ding J.-H.; RT "Mouse methylmalonate-semialdehyde dehydrogenase (MMSDH) cDNA and gene RT map."; RL Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J, and NOD; TISSUE=Cecum, Kidney, and Spleen; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Liver; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-47; LYS-52; LYS-55; RP LYS-76; LYS-117; LYS-129; LYS-364; LYS-376; LYS-391 AND LYS-517, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., RA Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). RN [5] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-47; LYS-52; LYS-55; LYS-76; RP LYS-87; LYS-117; LYS-129; LYS-298; LYS-330; LYS-331; LYS-364; LYS-376 RP AND LYS-500, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Liver; RX PubMed=23576753; DOI=10.1073/pnas.1302961110; RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., RA Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.; RT "Label-free quantitative proteomics of the lysine acetylome in RT mitochondria identifies substrates of SIRT3 in metabolic pathways."; RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013). CC -!- FUNCTION: Plays a role in valine and pyrimidine metabolism. Binds CC fatty acyl-CoA (By similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-3-oxopropanoate + CoA + H(2)O + CC NAD(+) = propanoyl-CoA + HCO(3)(-) + NADH. CC -!- CATALYTIC ACTIVITY: 3-oxopropanoate + CoA + NAD(P)(+) = acetyl-CoA CC + CO(2) + NAD(P)H. CC -!- SUBUNIT: Homotetramer (By similarity). CC -!- SUBCELLULAR LOCATION: Mitochondrion (By similarity). CC -!- PTM: Acetylation of Lys-55; Lys-117 and Lys-331 is observed in CC liver mitochondria from fasted mice but not from fed mice. CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF297860; AAG44988.1; -; mRNA. DR EMBL; AK033587; BAC28375.1; -; mRNA. DR EMBL; AK147146; BAE27715.1; -; mRNA. DR EMBL; AK155814; BAE33445.1; -; mRNA. DR EMBL; AK169915; BAE41455.1; -; mRNA. DR EMBL; AK170305; BAE41702.1; -; mRNA. DR EMBL; AK171581; BAE42539.1; -; mRNA. DR EMBL; AK171896; BAE42726.1; -; mRNA. DR EMBL; BC033440; AAH33440.1; -; mRNA. DR RefSeq; NP_598803.1; NM_134042.2. DR UniGene; Mm.247510; -. DR ProteinModelPortal; Q9EQ20; -. DR SMR; Q9EQ20; 9-516. DR IntAct; Q9EQ20; 4. DR MINT; MINT-1860357; -. DR STRING; 10090.ENSMUSP00000082288; -. DR PhosphoSite; Q9EQ20; -. DR REPRODUCTION-2DPAGE; Q8CIB4; -. DR REPRODUCTION-2DPAGE; Q9EQ20; -. DR PaxDb; Q9EQ20; -. DR PRIDE; Q9EQ20; -. DR Ensembl; ENSMUST00000085192; ENSMUSP00000082288; ENSMUSG00000021238. DR GeneID; 104776; -. DR KEGG; mmu:104776; -. DR UCSC; uc007ofk.2; mouse. DR CTD; 4329; -. DR MGI; MGI:1915077; Aldh6a1. DR eggNOG; COG1012; -. DR GeneTree; ENSGT00720000108597; -. DR HOGENOM; HOG000271507; -. DR HOVERGEN; HBG105023; -. DR InParanoid; Q9EQ20; -. DR KO; K00140; -. DR OMA; ISNVKPN; -. DR OrthoDB; EOG7J70F8; -. DR TreeFam; TF105651; -. DR ChiTaRS; ALDH6A1; mouse. DR NextBio; 357280; -. DR PRO; PR:Q9EQ20; -. DR ArrayExpress; Q9EQ20; -. DR Bgee; Q9EQ20; -. DR CleanEx; MM_ALDH6A1; -. DR Genevestigator; Q9EQ20; -. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR GO; GO:0005634; C:nucleus; IEA:Ensembl. DR GO; GO:0018478; F:malonate-semialdehyde dehydrogenase (acetylating) activity; IEA:UniProtKB-EC. DR GO; GO:0004491; F:methylmalonate-semialdehyde dehydrogenase (acylating) activity; IEA:UniProtKB-EC. DR GO; GO:0050873; P:brown fat cell differentiation; IDA:MGI. DR Gene3D; 3.40.309.10; -; 1. DR Gene3D; 3.40.605.10; -; 1. DR InterPro; IPR016161; Ald_DH/histidinol_DH. DR InterPro; IPR016163; Ald_DH_C. DR InterPro; IPR016160; Ald_DH_CS. DR InterPro; IPR016162; Ald_DH_N. DR InterPro; IPR015590; Aldehyde_DH_dom. DR InterPro; IPR010061; MeMal-semiAld_DH. DR PANTHER; PTHR11699:SF27; PTHR11699:SF27; 1. DR Pfam; PF00171; Aldedh; 1. DR SUPFAM; SSF53720; SSF53720; 1. DR TIGRFAMs; TIGR01722; MMSDH; 1. DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1. PE 1: Evidence at protein level; KW Acetylation; Complete proteome; Mitochondrion; NAD; Oxidoreductase; KW Reference proteome; Transit peptide. FT TRANSIT 1 32 Mitochondrion (By similarity). FT CHAIN 33 535 Methylmalonate-semialdehyde dehydrogenase FT [acylating], mitochondrial. FT /FTId=PRO_0000320299. FT NP_BIND 209 213 NAD (Potential). FT NP_BIND 261 266 NAD (Potential). FT ACT_SITE 317 317 Nucleophile (By similarity). FT BINDING 417 417 NAD (Potential). FT MOD_RES 47 47 N6-acetyllysine; alternate. FT MOD_RES 47 47 N6-succinyllysine; alternate. FT MOD_RES 52 52 N6-acetyllysine; alternate. FT MOD_RES 52 52 N6-succinyllysine; alternate. FT MOD_RES 55 55 N6-acetyllysine; alternate. FT MOD_RES 55 55 N6-succinyllysine; alternate. FT MOD_RES 76 76 N6-acetyllysine; alternate. FT MOD_RES 76 76 N6-succinyllysine; alternate. FT MOD_RES 87 87 N6-acetyllysine. FT MOD_RES 117 117 N6-acetyllysine; alternate. FT MOD_RES 117 117 N6-succinyllysine; alternate. FT MOD_RES 129 129 N6-acetyllysine; alternate. FT MOD_RES 129 129 N6-succinyllysine; alternate. FT MOD_RES 298 298 N6-acetyllysine. FT MOD_RES 330 330 N6-acetyllysine. FT MOD_RES 331 331 N6-acetyllysine. FT MOD_RES 364 364 N6-acetyllysine; alternate. FT MOD_RES 364 364 N6-succinyllysine; alternate. FT MOD_RES 376 376 N6-acetyllysine; alternate. FT MOD_RES 376 376 N6-succinyllysine; alternate. FT MOD_RES 391 391 N6-succinyllysine. FT MOD_RES 500 500 N6-acetyllysine. FT MOD_RES 517 517 N6-succinyllysine. FT CONFLICT 55 55 K -> R (in Ref. 2; BAE41702). FT CONFLICT 141 141 G -> C (in Ref. 3; AAH33440). FT CONFLICT 211 211 S -> P (in Ref. 2; BAE41702). SQ SEQUENCE 535 AA; 57916 MW; 1EF4ED4C4FE2284D CRC64; MAAAVAAAAA MRSRILQVSS KVNATWYPAS SFSSSSVPTV KLFIDGKFVE SKSDKWIDIH NPATNEVVGR VPQSTKAEMD AAVESCKRAF PAWADTSILS RQQVLLRYQQ LIKENLKEIA RLITLEQGKT LADAEGDVFR GLQVVEHACS VTSLMLGETM PSITKDMDLY SYRLPLGVCA GIAPFNFPAM IPLWMFPMAM VCGNTFLMKP SERVPGATML LAKLLQDSGA PDGTLNIIHG QHDAVNFICD HPDIKAISFV GSNQAGEYIF ERGSRNGKRV QANMGAKNHG VVMPDANKEN TLNQLVGAAF GAAGQRCMAL STAILVGEAK KWLPELVDRA KNLRVNAGDQ PGADLGPLIT PQAKERVCNL IDSGTKEGAS ILLDGRRIKV KGYENGNFVG PTIISNVKPS MTCYKEEIFG PVLVVLETET LDEAIKIVND NPYGNGTAIF TTNGATARKY AHMVDVGQVG VNVPIPVPLP MFSFTGSRSS FRGDTNFYGK QGIQFYTQLK TITSQWKEED ATLSSPAVVM PTMGR // ID MOSC2_MOUSE Reviewed; 338 AA. AC Q922Q1; DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 19-MAR-2014, entry version 81. DE RecName: Full=MOSC domain-containing protein 2, mitochondrial; DE EC=1.-.-.-; DE AltName: Full=Mitochondrial amidoxime reducing component 2; DE Short=mARC1; DE AltName: Full=Moco sulfurase C-terminal domain-containing protein 2; DE AltName: Full=Molybdenum cofactor sulfurase C-terminal domain-containing protein 2; DE Flags: Precursor; GN Name=Marc2; Synonyms=Mg87, Mosc2; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Spinal ganglion; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Mammary tumor; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP PEROXISOMAL SUBCELLULAR LOCATION. RC TISSUE=Kidney; RX PubMed=17768142; DOI=10.1074/mcp.M700169-MCP200; RA Wiese S., Gronemeyer T., Ofman R., Kunze M., Grou C.P., Almeida J.A., RA Eisenacher M., Stephan C., Hayen H., Schollenberger L., Korosec T., RA Waterham H.R., Schliebs W., Erdmann R., Berger J., Meyer H.E., RA Just W., Azevedo J.E., Wanders R.J., Warscheid B.; RT "Proteomics characterization of mouse kidney peroxisomes by tandem RT mass spectrometry and protein correlation profiling."; RL Mol. Cell. Proteomics 6:2045-2057(2007). RN [4] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-156, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23576753; DOI=10.1073/pnas.1302961110; RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., RA Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.; RT "Label-free quantitative proteomics of the lysine acetylome in RT mitochondria identifies substrates of SIRT3 in metabolic pathways."; RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013). CC -!- FUNCTION: As a component of the benzamidoxime prodrug-converting CC complex required to reduce N-hydroxylated prodrugs, such as CC benzamidoxime. Also able to reduce N(omega)-hydroxy-L-arginine CC (NOHA) and N(omega)-hydroxy-N(delta)-methyl-L-arginine (NHAM) into CC L-arginine and N(delta)-methyl-L-arginine, respectively (By CC similarity). CC -!- COFACTOR: Molybdenum (By similarity). CC -!- SUBUNIT: Component of a complex composed of cytochrome b5, NADH- CC cytochrome b5 reductase (CYB5R3) and MOSC2 (By similarity). CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane; Peripheral CC membrane protein. Peroxisome. CC -!- SIMILARITY: Contains 1 MOSC domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK051230; BAC34565.1; -; mRNA. DR EMBL; BC006888; AAH06888.1; -; mRNA. DR RefSeq; NP_598445.1; NM_133684.3. DR UniGene; Mm.177724; -. DR ProteinModelPortal; Q922Q1; -. DR IntAct; Q922Q1; 5. DR MINT; MINT-1860682; -. DR STRING; 10090.ENSMUSP00000066715; -. DR PhosphoSite; Q922Q1; -. DR PaxDb; Q922Q1; -. DR PRIDE; Q922Q1; -. DR Ensembl; ENSMUST00000068725; ENSMUSP00000066715; ENSMUSG00000073481. DR GeneID; 67247; -. DR KEGG; mmu:67247; -. DR UCSC; uc007dyq.1; mouse. DR CTD; 54996; -. DR MGI; MGI:1914497; Marc2. DR eggNOG; COG3217; -. DR GeneTree; ENSGT00530000063150; -. DR HOGENOM; HOG000180196; -. DR HOVERGEN; HBG081982; -. DR InParanoid; Q922Q1; -. DR OMA; VAQWFTN; -. DR OrthoDB; EOG7WT41P; -. DR TreeFam; TF316807; -. DR NextBio; 324002; -. DR PRO; PR:Q922Q1; -. DR ArrayExpress; Q922Q1; -. DR Bgee; Q922Q1; -. DR CleanEx; MM_MOSC2; -. DR Genevestigator; Q922Q1; -. DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:MGI. DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell. DR GO; GO:0030151; F:molybdenum ion binding; IEA:Ensembl. DR GO; GO:0043546; F:molybdopterin cofactor binding; IEA:Ensembl. DR GO; GO:0008940; F:nitrate reductase activity; IEA:Ensembl. DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro. DR GO; GO:0042126; P:nitrate metabolic process; IEA:Ensembl. DR InterPro; IPR005302; MoCF_Sase_C. DR InterPro; IPR005303; MOSC_N. DR InterPro; IPR011037; Pyrv_Knase-like_insert_dom. DR Pfam; PF03473; MOSC; 1. DR Pfam; PF03476; MOSC_N; 1. DR SUPFAM; SSF50800; SSF50800; 2. DR PROSITE; PS51340; MOSC; 1. PE 1: Evidence at protein level; KW Acetylation; Complete proteome; Membrane; Mitochondrion; KW Mitochondrion outer membrane; Molybdenum; Oxidoreductase; Peroxisome; KW Reference proteome; Transit peptide. FT TRANSIT 1 35 Mitochondrion (Potential). FT CHAIN 36 338 MOSC domain-containing protein 2, FT mitochondrial. FT /FTId=PRO_0000273342. FT DOMAIN 188 336 MOSC. FT MOD_RES 156 156 N6-acetyllysine. SQ SEQUENCE 338 AA; 38194 MW; 436E6C7224B807DA CRC64; MGSSSSTALA RLGLPGQPRS TWLGVAALGL AAVALGTVAW RRTRPRRRRQ LQQVGTVSKV WIYPIKSCKG VSVCETECTD MGLRCGKVRD RFWMVVKEDG HMVTARQEPR LVLVSITLEN NYLTLEAPGM EQIVLPIKLP SSNKIHNCRL FGLDIKGRDC GDEVAQWFTN YLKTQAYRLV QFDTSMKGRT TKKLYPSESY LQNYEVAYPD CSPVHLISEA SLVDLNTRLK KKVKMEYFRP NIVVSGCEAF EEDTWDELLI GDVEMKRVLS CPRCVLTTVD PDTGIIDRKE PLETLKSYRL CDPSVKSIYQ SSPLFGMYFS VEKLGSLRVG DPVYRMVD // ID MOSC1_MOUSE Reviewed; 340 AA. AC Q9CW42; Q8R2L6; DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 19-MAR-2014, entry version 72. DE RecName: Full=MOSC domain-containing protein 1, mitochondrial; DE EC=1.-.-.-; DE AltName: Full=Mitochondrial amidoxime reducing component 1; DE Short=mARC1; DE AltName: Full=Moco sulfurase C-terminal domain-containing protein 1; DE AltName: Full=Molybdenum cofactor sulfurase C-terminal domain-containing protein 1; GN Name=Marc1; Synonyms=Mosc1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Liver, and Mammary gland; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 161-340. RC STRAIN=C57BL/6J; TISSUE=Mammary gland; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION. RX PubMed=12865426; DOI=10.1074/jbc.M304940200; RA Da Cruz S., Xenarios I., Langridge J., Vilbois F., Parone P.A., RA Martinou J.-C.; RT "Proteomic analysis of the mouse liver mitochondrial inner membrane."; RL J. Biol. Chem. 278:41566-41571(2003). CC -!- FUNCTION: As a component of an N-hydroxylated prodrug-converting CC complex required to reduce N-hydroxylated prodrugs, such as CC benzamidoxime. Also able to reduce N(omega)-hydroxy-L-arginine CC (NOHA) and N(omega)-hydroxy-N(delta)-methyl-L-arginine (NHAM) into CC L-arginine and N(delta)-methyl-L-arginine, respectively (By CC similarity). CC -!- COFACTOR: Molybdenum (By similarity). CC -!- SUBUNIT: Component of a complex composed of cytochrome b5, NADH- CC cytochrome b5 reductase and MOSC1 (By similarity). CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane; Single-pass CC type II membrane protein (By similarity). Note=Mitochondrial CC import is mediated by AA 1-44 and requires ATP (By similarity). CC -!- SIMILARITY: Contains 1 MOSC domain. CC -!- SEQUENCE CAUTION: CC Sequence=AAH28441.1; Type=Erroneous initiation; CC Sequence=BAB23724.1; Type=Frameshift; Positions=53; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK004989; BAB23724.1; ALT_FRAME; mRNA. DR EMBL; BC028441; AAH28441.1; ALT_INIT; mRNA. DR RefSeq; XP_006497254.1; XM_006497191.1. DR UniGene; Mm.272457; -. DR ProteinModelPortal; Q9CW42; -. DR SMR; Q9CW42; 61-192. DR IntAct; Q9CW42; 2. DR MINT; MINT-1848620; -. DR PhosphoSite; Q9CW42; -. DR PaxDb; Q9CW42; -. DR PRIDE; Q9CW42; -. DR Ensembl; ENSMUST00000048462; ENSMUSP00000035804; ENSMUSG00000026621. DR GeneID; 66112; -. DR UCSC; uc007dyp.1; mouse. DR MGI; MGI:1913362; Marc1. DR eggNOG; COG3217; -. DR GeneTree; ENSGT00530000063150; -. DR HOGENOM; HOG000180196; -. DR HOVERGEN; HBG081982; -. DR PRO; PR:Q9CW42; -. DR ArrayExpress; Q9CW42; -. DR Bgee; Q9CW42; -. DR CleanEx; MM_MOSC1; -. DR Genevestigator; Q9CW42; -. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:MGI. DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell. DR GO; GO:0030151; F:molybdenum ion binding; IEA:InterPro. DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW. DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro. DR InterPro; IPR005302; MoCF_Sase_C. DR InterPro; IPR005303; MOSC_N. DR InterPro; IPR011037; Pyrv_Knase-like_insert_dom. DR Pfam; PF03473; MOSC; 1. DR Pfam; PF03476; MOSC_N; 1. DR SUPFAM; SSF50800; SSF50800; 2. DR PROSITE; PS51340; MOSC; 1. PE 1: Evidence at protein level; KW Complete proteome; Membrane; Mitochondrion; KW Mitochondrion outer membrane; Molybdenum; Oxidoreductase; KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix. FT CHAIN 1 340 MOSC domain-containing protein 1, FT mitochondrial. FT /FTId=PRO_0000273336. FT TOPO_DOM 1 24 Mitochondrial matrix (By similarity). FT TRANSMEM 25 44 Helical; Signal-anchor for type II FT membrane protein; (Potential). FT TOPO_DOM 45 340 Cytoplasmic (By similarity). FT DOMAIN 191 338 MOSC. FT CONFLICT 251 251 V -> I (in Ref. 2; AAH28441). SQ SEQUENCE 340 AA; 37979 MW; 2EB4A29C10E7DC50 CRC64; MGAGSWALTL FGFSAFRVPG QPRSTWLGVA ALGLAAVALG TVAWRRARPR RRRRLQQVGT VAQLWIYPIK SCKGLSVSEA ECTAMGLRYG HLRDRFWLVI NEEGNMVTAR QEPRLVLISL TCEDDTLTLS AAYTKDLLLP ITPPATNPLL QCRVHGLEIQ GRDCGEDAAQ WVSSFLKMQS CRLVHFEPHM RPRSSRQMKA VFRTKDQVAY SDASPFLVLS EASLEDLNSR LERRVKATNF RPNIVISGCG VYAEDSWNEV LIGDVELKRV MACTRCLLTT VDPDTGISDR KEPLETLKSY RLCDPSEQAL YGKLPIFGQY FALENPGTIR VGDPVYLLGQ // ID MOXD1_MOUSE Reviewed; 613 AA. AC Q9CXI3; Q6PFA8; Q8BUZ7; Q8R394; Q9JJA6; DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 19-FEB-2014, entry version 78. DE RecName: Full=DBH-like monooxygenase protein 1; DE EC=1.14.17.-; DE AltName: Full=DBH-related protein; DE AltName: Full=Monooxygenase X; DE Flags: Precursor; GN Name=Moxd1; Synonyms=Dbhr, Mox; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Head, Ovary, and Uterus; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Czech II; TISSUE=Mammary tumor; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP IDENTIFICATION. RC TISSUE=Embryo; RX PubMed=11397006; DOI=10.1006/dbio.2001.0275; RA Knecht A.K., Bronner-Fraser M.; RT "DBHR, a gene with homology to dopamine beta-hydroxylase, is expressed RT in the neural crest throughout early development."; RL Dev. Biol. 234:365-375(2001). RN [4] RP IDENTIFICATION, TISSUE SPECIFICITY, GLYCOSYLATION, AND SUBCELLULAR RP LOCATION. RX PubMed=15337741; DOI=10.1074/jbc.M407486200; RA Xin X., Mains R.E., Eipper B.A.; RT "Monooxygenase X, a member of the copper-dependent monooxygenase RT family localized to the endoplasmic reticulum."; RL J. Biol. Chem. 279:48159-48167(2004). CC -!- COFACTOR: Binds 2 copper ions per subunit (By similarity). CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass CC type I membrane protein. CC -!- TISSUE SPECIFICITY: Broadly exprressed, with highest levels in CC salivary gland and ovary. CC -!- PTM: N-glycosylated. CC -!- SIMILARITY: Belongs to the copper type II ascorbate-dependent CC monooxygenase family. CC -!- SIMILARITY: Contains 1 DOMON domain. CC -!- SEQUENCE CAUTION: CC Sequence=BAC38265.1; Type=Frameshift; Positions=580; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AB041606; BAA95089.1; -; mRNA. DR EMBL; AK014340; BAB29283.1; -; mRNA. DR EMBL; AK030274; BAC26871.1; -; mRNA. DR EMBL; AK081586; BAC38265.1; ALT_FRAME; mRNA. DR EMBL; BC025892; AAH25892.1; -; mRNA. DR EMBL; BC057652; AAH57652.1; -; mRNA. DR RefSeq; NP_067484.2; NM_021509.5. DR UniGene; Mm.285934; -. DR ProteinModelPortal; Q9CXI3; -. DR SMR; Q9CXI3; 197-472. DR PhosphoSite; Q9CXI3; -. DR PRIDE; Q9CXI3; -. DR Ensembl; ENSMUST00000095784; ENSMUSP00000093460; ENSMUSG00000020000. DR GeneID; 59012; -. DR KEGG; mmu:59012; -. DR UCSC; uc007equ.1; mouse. DR CTD; 26002; -. DR MGI; MGI:1921582; Moxd1. DR eggNOG; NOG286384; -. DR GeneTree; ENSGT00530000063085; -. DR HOGENOM; HOG000037925; -. DR HOVERGEN; HBG100597; -. DR InParanoid; Q9CXI3; -. DR OMA; SCTLSTK; -. DR OrthoDB; EOG7XDBFB; -. DR TreeFam; TF320698; -. DR NextBio; 314560; -. DR PRO; PR:Q9CXI3; -. DR Bgee; Q9CXI3; -. DR CleanEx; MM_MOXD1; -. DR Genevestigator; Q9CXI3; -. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005507; F:copper ion binding; IEA:InterPro. DR GO; GO:0016715; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced ascorbate as one donor, and incorporation of one atom of oxygen; IEA:InterPro. DR Gene3D; 2.60.120.230; -; 1. DR Gene3D; 2.60.120.310; -; 1. DR InterPro; IPR014784; Cu2_ascorb_mOase-like_C. DR InterPro; IPR000323; Cu2_ascorb_mOase_N. DR InterPro; IPR000945; DBH-rel. DR InterPro; IPR005018; DOMON_domain. DR InterPro; IPR028463; MOXD1. DR InterPro; IPR008977; PHM/PNGase_F_dom. DR PANTHER; PTHR10157; PTHR10157; 1. DR PANTHER; PTHR10157:SF21; PTHR10157:SF21; 1. DR Pfam; PF01082; Cu2_monooxygen; 1. DR Pfam; PF03351; DOMON; 1. DR PRINTS; PR00767; DBMONOXGNASE. DR SMART; SM00664; DoH; 1. DR SUPFAM; SSF49742; SSF49742; 2. DR PROSITE; PS50836; DOMON; 1. PE 1: Evidence at protein level; KW Complete proteome; Copper; Disulfide bond; Endoplasmic reticulum; KW Glycoprotein; Membrane; Metal-binding; Monooxygenase; Oxidoreductase; KW Reference proteome; Signal; Transmembrane; Transmembrane helix. FT SIGNAL 1 19 Potential. FT CHAIN 20 613 DBH-like monooxygenase protein 1. FT /FTId=PRO_0000305218. FT TOPO_DOM 20 587 Lumenal (Potential). FT TRANSMEM 588 608 Helical; (Potential). FT DOMAIN 35 148 DOMON. FT ACT_SITE 203 203 Potential. FT ACT_SITE 389 389 Potential. FT METAL 235 235 Copper A (By similarity). FT METAL 236 236 Copper A (By similarity). FT METAL 307 307 Copper A (By similarity). FT METAL 389 389 Copper B (By similarity). FT METAL 391 391 Copper B (By similarity). FT METAL 464 464 Copper B (By similarity). FT CARBOHYD 114 114 N-linked (GlcNAc...) (Potential). FT CARBOHYD 247 247 N-linked (GlcNAc...) (Potential). FT CARBOHYD 476 476 N-linked (GlcNAc...) (Potential). FT CARBOHYD 517 517 N-linked (GlcNAc...) (Potential). FT DISULFID 205 257 By similarity. FT DISULFID 242 269 By similarity. FT DISULFID 364 480 By similarity. FT DISULFID 368 550 By similarity. FT DISULFID 443 465 By similarity. FT CONFLICT 11 11 A -> V (in Ref. 2; AAH57652). FT CONFLICT 131 131 V -> A (in Ref. 2; AAH25892/AAH57652). FT CONFLICT 133 133 D -> V (in Ref. 1; BAA95089). FT CONFLICT 185 185 P -> L (in Ref. 2; AAH25892/AAH57652). FT CONFLICT 513 513 K -> R (in Ref. 1; BAC38265). FT CONFLICT 609 609 S -> N (in Ref. 2; AAH25892/AAH57652). FT CONFLICT 612 612 G -> D (in Ref. 2; AAH25892/AAH57652). SQ SEQUENCE 613 AA; 69678 MW; 4A202563373AC927 CRC64; MCGWPLLVLW ALLPATAAGS PGRSYPHRVV LDPEGKYWLH WGRQGERLAF RLEVRTNGYV GFGFSPTGSM AAADIVVGGV AHGRPYLQDY FTNADRELEK DAQQDYHLDY AMENSTHTVI EFSRELHTCD VNDKSLTDST VRVIWAYHHD DPGESGPKYH DLNRGTRSLR LLNPEKANVV STVLPYFDLV NQNVPIPNKG TTYWCQMFKI PTFQEKHHVI KVEPIIERGH ENLVHHILVY QCSSNFNDSV LDFGHECYHP NMPDAFLTCE TVILAWGIGG EGFTYPPHVG LSLGMPLDPR YVLLEVHYDN PARRKGLIDS SGLRVFHTTD IRRYDAGVIE AGLWVSLFHT IPPGMPEFHS EGHCTLECLE EALGAEKPSG IHVFAVLLHA HLAGKGIRLR HFRKGEEMKL LAYDDDYDFN FQEFQYLREE QTILPGDNLI TECRYNTKDR AVMTWGGLST RNEMCLSYLL YYPRVNLTRC SSIPDIMEQL QFIGVKEIYR PVTTWPFIIK SPKQYRNLSF MDAMNKFKWT KKEGLSFNKL VLSLPVNVRC SKTDNAEWSI QGMTAIPPDI KRPYEAEPLV CEKAASPPLH GIFSLRLLTC ALLLGSMLSS QGL // ID MOXD2_MOUSE Reviewed; 619 AA. AC Q7TT41; Q91XT2; DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2003, sequence version 1. DT 19-FEB-2014, entry version 69. DE RecName: Full=DBH-like monooxygenase protein 2; DE EC=1.14.17.-; DE AltName: Full=Dopamine-beta-hydroxylase-like protein; DE Flags: Precursor; GN Name=Moxd2; Synonyms=Dbhl, Dbhl1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=11160223; RA Chen F., Rowen L., Hood L., Rothenberg E.V.; RT "Differential transcriptional regulation of individual TCR V beta RT segments before gene rearrangement."; RL J. Immunol. 166:1771-1780(2001). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=C57BL/6; TISSUE=Thymus; RA Matsuda M., Horseman N.D.; RT "Thymus-specific expression of dopamine beta-hydroxylase-like gene RT mRNA in mice."; RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases. RN [3] RP IDENTIFICATION. RC TISSUE=Embryo; RX PubMed=11397006; DOI=10.1006/dbio.2001.0275; RA Knecht A.K., Bronner-Fraser M.; RT "DBHR, a gene with homology to dopamine beta-hydroxylase, is expressed RT in the neural crest throughout early development."; RL Dev. Biol. 234:365-375(2001). RN [4] RP TISSUE SPECIFICITY. RX PubMed=15337741; DOI=10.1074/jbc.M407486200; RA Xin X., Mains R.E., Eipper B.A.; RT "Monooxygenase X, a member of the copper-dependent monooxygenase RT family localized to the endoplasmic reticulum."; RL J. Biol. Chem. 279:48159-48167(2004). CC -!- COFACTOR: Binds 2 copper ions per subunit (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane CC protein (Potential). CC -!- TISSUE SPECIFICITY: Expressed at low levels in thymus and testis. CC -!- SIMILARITY: Belongs to the copper type II ascorbate-dependent CC monooxygenase family. CC -!- SIMILARITY: Contains 1 DOMON domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000663; AAB69054.1; -; Genomic_DNA. DR EMBL; AB065134; BAB62024.1; -; mRNA. DR RefSeq; NP_647457.2; NM_139296.2. DR UniGene; Mm.207087; -. DR ProteinModelPortal; Q7TT41; -. DR SMR; Q7TT41; 201-473. DR STRING; 10090.ENSMUSP00000031937; -. DR PaxDb; Q7TT41; -. DR PRIDE; Q7TT41; -. DR DNASU; 194357; -. DR Ensembl; ENSMUST00000031937; ENSMUSP00000031937; ENSMUSG00000029885. DR GeneID; 194357; -. DR KEGG; mmu:194357; -. DR UCSC; uc009bnh.1; mouse. DR CTD; 194357; -. DR MGI; MGI:2388042; Moxd2. DR eggNOG; NOG286384; -. DR GeneTree; ENSGT00530000063085; -. DR HOGENOM; HOG000004745; -. DR HOVERGEN; HBG099586; -. DR InParanoid; Q7TT41; -. DR OMA; NVEWTPE; -. DR OrthoDB; EOG73NG2W; -. DR TreeFam; TF320698; -. DR NextBio; 371580; -. DR PRO; PR:Q7TT41; -. DR Bgee; Q7TT41; -. DR CleanEx; MM_MOXD2; -. DR Genevestigator; Q7TT41; -. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005507; F:copper ion binding; IEA:InterPro. DR GO; GO:0016715; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced ascorbate as one donor, and incorporation of one atom of oxygen; IEA:InterPro. DR Gene3D; 2.60.120.230; -; 1. DR Gene3D; 2.60.120.310; -; 1. DR InterPro; IPR014784; Cu2_ascorb_mOase-like_C. DR InterPro; IPR000323; Cu2_ascorb_mOase_N. DR InterPro; IPR000945; DBH-rel. DR InterPro; IPR005018; DOMON_domain. DR InterPro; IPR028464; Moxd2. DR InterPro; IPR008977; PHM/PNGase_F_dom. DR PANTHER; PTHR10157; PTHR10157; 1. DR PANTHER; PTHR10157:SF2; PTHR10157:SF2; 1. DR Pfam; PF01082; Cu2_monooxygen; 1. DR Pfam; PF03351; DOMON; 1. DR PRINTS; PR00767; DBMONOXGNASE. DR SMART; SM00664; DoH; 1. DR SUPFAM; SSF49742; SSF49742; 2. DR PROSITE; PS50836; DOMON; 1. PE 2: Evidence at transcript level; KW Complete proteome; Copper; Disulfide bond; Glycoprotein; Membrane; KW Metal-binding; Monooxygenase; Oxidoreductase; Reference proteome; KW Signal; Transmembrane; Transmembrane helix. FT SIGNAL 1 21 Potential. FT CHAIN 22 619 DBH-like monooxygenase protein 2. FT /FTId=PRO_0000305224. FT TOPO_DOM 22 594 Extracellular (Potential). FT TRANSMEM 595 615 Helical; (Potential). FT TOPO_DOM 616 619 Cytoplasmic (Potential). FT DOMAIN 40 156 DOMON. FT ACT_SITE 209 209 Potential. FT ACT_SITE 390 390 Potential. FT METAL 241 241 Copper A (By similarity). FT METAL 242 242 Copper A (By similarity). FT METAL 309 309 Copper A (By similarity). FT METAL 390 390 Copper B (By similarity). FT METAL 392 392 Copper B (By similarity). FT METAL 465 465 Copper B (By similarity). FT CARBOHYD 250 250 N-linked (GlcNAc...) (Potential). FT CARBOHYD 405 405 N-linked (GlcNAc...) (Potential). FT CARBOHYD 477 477 N-linked (GlcNAc...) (Potential). FT DISULFID 211 261 By similarity. FT DISULFID 248 271 By similarity. FT DISULFID 366 481 By similarity. FT DISULFID 444 466 By similarity. FT CONFLICT 289 289 D -> G (in Ref. 2; BAB62024). FT CONFLICT 561 561 L -> V (in Ref. 2; BAB62024). SQ SEQUENCE 619 AA; 69397 MW; 74518832AD5E1A63 CRC64; MACVLLFRLF LLLVLAAFSQ GKRLGPTSPL RYSRFLDPSR AVFLRWDFDY EAEIITFELQ VQTTGWVGLG ITDRYTFVGS DLVVGGVLPN GNVYFSDQHL LDEDTLEQDG SQDAELLRLT EDAVSTTMRF SRPFRTCDPH DRDITSDTMR VLAAYGPDDI PKMSREHTFV KSIFLLQMLQ YDDQDAPEDT IIHDLKISNF IIPEDDTTYA CTFLPLPIVS KKHHIYKFEP ILVERNETMV HHVLVYACGN SSVLPTGIGE CYGSDPAFSL CSHVIAGWAV GGLSYQFPDD VGISIGTPFD PQWIRLEIHY SNFQNLPGIR DTSGMRLFYT SHLRKYDMGV LQLGISVFPI HFIPPGAEAF LSYGLCKTDK FEELNGAPVS DIYISACLLH THLAGRSLQA LQYRNGTQLQ VVCKDFSYDF NLQESRDLPH PVVIKPGDEL LIECHYQTLD RDFMTFGGAS TINEMCLIFF FYYPRINISS CMGYPDIIYV TNELGEEASE NPMENLMVLD NVEWTPENIK KAEKACKESQ QTVLIKTIDE EVENTTGWIP DIIPTPRGPC LESTGGKVEP QDNTPAGFRA VPLALSGSNT ATLRPLPMIA VLFLQGSLSC LLAMLQTGV // ID MSMO1_MOUSE Reviewed; 293 AA. AC Q9CRA4; Q543V8; DT 22-FEB-2003, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 19-FEB-2014, entry version 96. DE RecName: Full=Methylsterol monooxygenase 1; DE EC=1.14.13.72; DE AltName: Full=C-4 methylsterol oxidase; GN Name=Msmo1; Synonyms=Sc4mol; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; RC TISSUE=Amnion, Bone marrow, Cerebellum, Embryo, Liver, and Placenta; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Mammary tumor; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- CATALYTIC ACTIVITY: 4,4-dimethyl-5-alpha-cholest-7-en-3-beta-ol + CC NAD(P)H + O(2) = 4-beta-hydroxymethyl-4-alpha-methyl-5-alpha- CC cholest-7-en-3-beta-ol + NAD(P)(+) + H(2)O. CC -!- CATALYTIC ACTIVITY: 4-beta-hydroxymethyl-4-alpha-methyl-5-alpha- CC cholest-7-en-3-beta-ol + NAD(P)H + O(2) = 3-beta-hydroxy-4-beta- CC methyl-5-alpha-cholest-7-ene-4-alpha-carbaldehyde + NAD(P)(+) + 2 CC H(2)O. CC -!- CATALYTIC ACTIVITY: 3-beta-hydroxy-4-beta-methyl-5-alpha-cholest- CC 7-ene-4-alpha-carbaldehyde + NAD(P)H + O(2) = 3-beta-hydroxy-4- CC beta-methyl-5-alpha-cholest-7-ene-4-alpha-carboxylate + NAD(P)(+) CC + H(2)O. CC -!- COFACTOR: Iron (Probable). CC -!- PATHWAY: Steroid biosynthesis; zymosterol biosynthesis; zymosterol CC from lanosterol: step 3/6. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass CC membrane protein (Probable). CC -!- DOMAIN: The histidine box domains may contain the active site CC and/or be involved in metal ion binding. CC -!- SIMILARITY: Belongs to the sterol desaturase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK005090; BAB23811.1; -; mRNA. DR EMBL; AK005441; BAB24035.1; -; mRNA. DR EMBL; AK045059; BAC32201.1; -; mRNA. DR EMBL; AK146684; BAE27358.1; -; mRNA. DR EMBL; AK151135; BAE30143.1; -; mRNA. DR EMBL; AK169017; BAE40814.1; -; mRNA. DR EMBL; BC006802; AAH06802.1; -; mRNA. DR RefSeq; NP_079712.1; NM_025436.2. DR UniGene; Mm.30119; -. DR ProteinModelPortal; Q9CRA4; -. DR PhosphoSite; Q9CRA4; -. DR PaxDb; Q9CRA4; -. DR PRIDE; Q9CRA4; -. DR Ensembl; ENSMUST00000034015; ENSMUSP00000034015; ENSMUSG00000031604. DR GeneID; 66234; -. DR KEGG; mmu:66234; -. DR UCSC; uc009lux.1; mouse. DR CTD; 66234; -. DR MGI; MGI:1913484; Sc4mol. DR eggNOG; COG3000; -. DR GeneTree; ENSGT00530000063017; -. DR HOGENOM; HOG000162289; -. DR HOVERGEN; HBG051504; -. DR InParanoid; Q9CRA4; -. DR KO; K07750; -. DR OMA; DSQFIAY; -. DR OrthoDB; EOG747PJB; -. DR TreeFam; TF354294; -. DR UniPathway; UPA00770; UER00756. DR ChiTaRS; MSMO1; mouse. DR NextBio; 321041; -. DR PRO; PR:Q9CRA4; -. DR ArrayExpress; Q9CRA4; -. DR Bgee; Q9CRA4; -. DR CleanEx; MM_SC4MOL; -. DR Genevestigator; Q9CRA4; -. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0000254; F:C-4 methylsterol oxidase activity; IEA:UniProtKB-EC. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro. DR GO; GO:0016126; P:sterol biosynthetic process; IEA:UniProtKB-KW. DR InterPro; IPR006694; Fatty_acid_hydroxylase. DR Pfam; PF04116; FA_hydroxylase; 1. PE 2: Evidence at transcript level; KW Complete proteome; Endoplasmic reticulum; Iron; Lipid biosynthesis; KW Lipid metabolism; Membrane; NAD; Oxidoreductase; Reference proteome; KW Steroid biosynthesis; Steroid metabolism; Sterol biosynthesis; KW Sterol metabolism; Transmembrane; Transmembrane helix. FT CHAIN 1 293 Methylsterol monooxygenase 1. FT /FTId=PRO_0000117034. FT TRANSMEM 55 75 Helical; (Potential). FT TRANSMEM 100 120 Helical; (Potential). FT TRANSMEM 199 219 Helical; (Potential). FT MOTIF 157 161 Histidine box-1. FT MOTIF 170 174 Histidine box-2. FT MOTIF 249 255 Histidine box-3. SQ SEQUENCE 293 AA; 34772 MW; 0A275DE7B5D4DB52 CRC64; MATNKSVGVF SSASLAVEYV DSLLPENPLQ EPFKNAWVYM LDNYTKFQIA TWGSLIVHEA IYFLFSLPGF LFQFIPYMRK YKIQKDKPET FEGQWKCLKK ILFNHFFIQL PLICGTYYFT EFFNIPYDWE RMPRWYLTLA RCLGCAVIED TWHYFLHRLL HHKRIYKYIH KVHHEFQAPF GIEAEYAHPL ETLILGTGFF IGIVLLCDHV ILLWAWVTIR LLETIDVHSG YDIPLNPLNL VPFYTGARHH DFHHMNFIGN YASTFTWWDK LFGTDAQYHA YIEKSKKLGK KSD // ID MSRA_MOUSE Reviewed; 233 AA. AC Q9D6Y7; Q5EBQ7; Q91WK9; Q9DCY2; DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 19-MAR-2014, entry version 93. DE RecName: Full=Mitochondrial peptide methionine sulfoxide reductase; DE EC=1.8.4.11; DE AltName: Full=Peptide-methionine (S)-S-oxide reductase; DE Short=Peptide Met(O) reductase; DE AltName: Full=Protein-methionine-S-oxide reductase; DE Short=PMSR; DE Flags: Precursor; GN Name=Msra; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4). RC STRAIN=C57BL/6J; TISSUE=Spinal cord, and Tongue; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3). RC TISSUE=Brain, and Kidney; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP PARTIAL PROTEIN SEQUENCE, MASS SPECTROMETRY, ALTERNATIVE SPLICING, AND RP SUBCELLULAR LOCATION. RX PubMed=15924425; DOI=10.1021/bi0501131; RA Kim H.Y., Gladyshev V.N.; RT "Role of structural and functional elements of mouse methionine-S- RT sulfoxide reductase in its subcellular distribution."; RL Biochemistry 44:8059-8067(2005). RN [5] RP MYRISTOYLATION (ISOFORM 2), AND ALTERNATIVE INITIATION. RX PubMed=20368336; DOI=10.1074/jbc.M110.119701; RA Kim G., Cole N.B., Lim J.C., Zhao H., Levine R.L.; RT "Dual sites of protein initiation control the localization and RT myristoylation of methionine sulfoxide reductase A."; RL J. Biol. Chem. 285:18085-18094(2010). RN [6] RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-104 AND LYS-183, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., RA Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). RN [7] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-104 AND LYS-183, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23576753; DOI=10.1073/pnas.1302961110; RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., RA Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.; RT "Label-free quantitative proteomics of the lysine acetylome in RT mitochondria identifies substrates of SIRT3 in metabolic pathways."; RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013). CC -!- FUNCTION: Has an important function as a repair enzyme for CC proteins that have been inactivated by oxidation. Catalyzes the CC reversible oxidation-reduction of methionine sulfoxide in proteins CC to methionine (By similarity). CC -!- CATALYTIC ACTIVITY: Peptide-L-methionine + thioredoxin disulfide + CC H(2)O = peptide-L-methionine (S)-S-oxide + thioredoxin. CC -!- CATALYTIC ACTIVITY: L-methionine + thioredoxin disulfide + H(2)O = CC L-methionine (S)-S-oxide + thioredoxin. CC -!- SUBCELLULAR LOCATION: Isoform 1: Mitochondrion. CC -!- SUBCELLULAR LOCATION: Isoform 2: Cytoplasm. Nucleus. Membrane; CC Lipid-anchor. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing, Alternative initiation; Named isoforms=4; CC Comment=Only about 25% of mRNAs are initiated at the CC mitochondrial isoform 1 codon. According to PubMed=15924425, CC differential subcellular targeting is not due alternative CC initiation; CC Name=1; CC IsoId=Q9D6Y7-1; Sequence=Displayed; CC Note=Mitochondrial; CC Name=2; CC IsoId=Q9D6Y7-2; Sequence=VSP_042133; CC Note=Cytoplasmic. Contains a N-myristoyl glycine at position 2. CC Produced by alternative initiation; CC Name=3; CC IsoId=Q9D6Y7-3; Sequence=VSP_041409; CC Name=4; CC IsoId=Q9D6Y7-4; Sequence=VSP_041408; CC -!- SIMILARITY: Belongs to the MsrA Met sulfoxide reductase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK002356; BAB22035.1; -; mRNA. DR EMBL; AK009822; BAB26522.1; -; mRNA. DR EMBL; AK049714; BAC33889.1; -; mRNA. DR EMBL; AK018338; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; CH466535; EDL36048.1; -; Genomic_DNA. DR EMBL; BC014738; AAH14738.1; -; mRNA. DR EMBL; BC089311; AAH89311.1; -; mRNA. DR RefSeq; NP_001240641.1; NM_001253712.1. DR RefSeq; NP_001240643.1; NM_001253714.1. DR RefSeq; NP_001240644.1; NM_001253715.1. DR RefSeq; NP_001240645.1; NM_001253716.1. DR RefSeq; NP_080598.2; NM_026322.4. DR UniGene; Mm.26713; -. DR PDB; 2L90; NMR; -; A=22-233. DR PDBsum; 2L90; -. DR ProteinModelPortal; Q9D6Y7; -. DR SMR; Q9D6Y7; 22-232. DR IntAct; Q9D6Y7; 4. DR MINT; MINT-1854772; -. DR PhosphoSite; Q9D6Y7; -. DR PaxDb; Q9D6Y7; -. DR PRIDE; Q9D6Y7; -. DR Ensembl; ENSMUST00000067927; ENSMUSP00000065754; ENSMUSG00000054733. [Q9D6Y7-1] DR GeneID; 110265; -. DR KEGG; mmu:110265; -. DR UCSC; uc007uig.2; mouse. [Q9D6Y7-4] DR UCSC; uc007uih.2; mouse. [Q9D6Y7-3] DR UCSC; uc007uii.2; mouse. [Q9D6Y7-1] DR CTD; 4482; -. DR MGI; MGI:106916; Msra. DR eggNOG; COG0225; -. DR GeneTree; ENSGT00390000003823; -. DR HOGENOM; HOG000263862; -. DR HOVERGEN; HBG006401; -. DR InParanoid; Q5EBQ7; -. DR KO; K07304; -. DR OMA; GEWWDAE; -. DR OrthoDB; EOG76X610; -. DR TreeFam; TF353884; -. DR BRENDA; 1.8.4.11; 3474. DR ChiTaRS; MSRA; mouse. DR NextBio; 363659; -. DR PRO; PR:Q9D6Y7; -. DR Bgee; Q9D6Y7; -. DR CleanEx; MM_MSRA; -. DR Genevestigator; Q9D6Y7; -. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0008113; F:peptide-methionine (S)-S-oxide reductase activity; IEA:UniProtKB-EC. DR GO; GO:0030091; P:protein repair; IEA:InterPro. DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro. DR Gene3D; 3.30.1060.10; -; 1. DR HAMAP; MF_01401; MsrA; 1. DR InterPro; IPR028427; Met_Sox_Rdtase. DR InterPro; IPR002569; Met_Sox_Rdtase_MsrA. DR PANTHER; PTHR10173; PTHR10173; 1. DR Pfam; PF01625; PMSR; 1. DR SUPFAM; SSF55068; SSF55068; 1. DR TIGRFAMs; TIGR00401; msrA; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative initiation; KW Alternative splicing; Complete proteome; Cytoplasm; KW Direct protein sequencing; Lipoprotein; Membrane; Mitochondrion; KW Myristate; Nucleus; Oxidoreductase; Reference proteome; KW Transit peptide. FT TRANSIT 1 20 Mitochondrion (By similarity). FT CHAIN 21 233 Mitochondrial peptide methionine FT sulfoxide reductase. FT /FTId=PRO_0000138627. FT MOD_RES 104 104 N6-acetyllysine; alternate. FT MOD_RES 104 104 N6-succinyllysine; alternate. FT MOD_RES 183 183 N6-acetyllysine; alternate. FT MOD_RES 183 183 N6-succinyllysine; alternate. FT VAR_SEQ 1 45 MLSASRRALQLLSSANPVRRMGDSASKVISAEEALPGRTEP FT IPVT -> MSK (in isoform 4). FT /FTId=VSP_041408. FT VAR_SEQ 1 20 Missing (in isoform 2). FT /FTId=VSP_042133. FT VAR_SEQ 69 108 Missing (in isoform 3). FT /FTId=VSP_041409. FT CONFLICT 20 20 R -> G (in Ref. 1; BAB22035). FT CONFLICT 156 156 R -> P (in Ref. 1; AK018338). FT CONFLICT 187 187 G -> V (in Ref. 1; BAB22035). FT HELIX 24 26 FT TURN 31 33 FT TURN 49 51 FT STRAND 55 58 FT STRAND 64 69 FT HELIX 73 81 FT STRAND 83 95 FT HELIX 103 106 FT STRAND 114 121 FT TURN 123 125 FT HELIX 128 137 FT STRAND 144 147 FT STRAND 150 152 FT STRAND 158 160 FT HELIX 164 182 FT TURN 183 185 FT HELIX 204 206 FT HELIX 209 212 FT TURN 228 230 SQ SEQUENCE 233 AA; 25988 MW; B16EFE01BE751242 CRC64; MLSASRRALQ LLSSANPVRR MGDSASKVIS AEEALPGRTE PIPVTAKHHV SGNRTVEPFP EGTQMAVFGM GCFWGAERKF WVLKGVYSTQ VGFAGGHTRN PTYKEVCSEK TGHAEVVRVV YRPEHISFEE LLKVFWENHD PTQGMRQGND FGTQYRSAVY PTSAVQMEAA LRSKEEYQKV LSKHNFGPIT TDIREGQVFY YAEDYHQQYL SKNPDGYCGL GGTGVSCPMA IKK // ID MSRB2_MOUSE Reviewed; 175 AA. AC Q78J03; DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 19-MAR-2014, entry version 75. DE RecName: Full=Methionine-R-sulfoxide reductase B2, mitochondrial; DE Short=MsrB2; DE EC=1.8.4.-; DE Flags: Precursor; GN Name=Msrb2; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Mammary tumor; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP FUNCTION, SUBCELLULAR LOCATION, ENZYME REGULATION, AND COFACTOR. RX PubMed=14699060; DOI=10.1091/mbc.E03-08-0629; RA Kim H.-Y., Gladyshev V.N.; RT "Methionine sulfoxide reduction in mammals: characterization of RT methionine-R-sulfoxide reductases."; RL Mol. Biol. Cell 15:1055-1064(2004). RN [4] RP FUNCTION. RX PubMed=23911929; DOI=10.1016/j.molcel.2013.06.019; RA Lee B.C., Peterfi Z., Hoffmann F.W., Moore R.E., Kaya A., Avanesov A., RA Tarrago L., Zhou Y., Weerapana E., Fomenko D.E., Hoffmann P.R., RA Gladyshev V.N.; RT "MsrB1 and MICALs regulate actin assembly and macrophage function via RT reversible stereoselective methionine oxidation."; RL Mol. Cell 51:397-404(2013). CC -!- FUNCTION: Methionine-sulfoxide reductase that specifically reduces CC methionine (R)-sulfoxide back to methionine. While in many cases, CC methionine oxidation is the result of random oxidation following CC oxidative stress, methionine oxidation is also a post- CC translational modification that takes place on specific residue. CC Upon oxidative stress, may play a role in the preservation of CC mitochondrial integrity by decreasing the intracellular reactive CC oxygen species build-up through its scavenging role, hence CC contributing to cell survival and protein maintenance. CC -!- CATALYTIC ACTIVITY: L-methionine + oxidized thioredoxin = L- CC methionine R-oxide + reduced thioredoxin. CC -!- COFACTOR: Binds 1 zinc ion per subunit. CC -!- ENZYME REGULATION: Inhibited by high concentrations of substrate. CC -!- SUBCELLULAR LOCATION: Mitochondrion. CC -!- SIMILARITY: Belongs to the MsrB Met sulfoxide reductase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AL928806; CAM21786.1; -; Genomic_DNA. DR EMBL; BC021619; AAH21619.1; -; mRNA. DR RefSeq; NP_083895.1; NM_029619.2. DR UniGene; Mm.27166; -. DR PDB; 2L1U; NMR; -; A=45-175. DR PDBsum; 2L1U; -. DR ProteinModelPortal; Q78J03; -. DR SMR; Q78J03; 45-175. DR IntAct; Q78J03; 1. DR PhosphoSite; Q78J03; -. DR PaxDb; Q78J03; -. DR PRIDE; Q78J03; -. DR Ensembl; ENSMUST00000023856; ENSMUSP00000023856; ENSMUSG00000023094. DR GeneID; 76467; -. DR KEGG; mmu:76467; -. DR UCSC; uc008imf.2; mouse. DR CTD; 22921; -. DR MGI; MGI:1923717; Msrb2. DR eggNOG; COG0229; -. DR GeneTree; ENSGT00510000046802; -. DR HOGENOM; HOG000243424; -. DR HOVERGEN; HBG002192; -. DR InParanoid; Q78J03; -. DR KO; K07305; -. DR OMA; WERDESH; -. DR OrthoDB; EOG7VHSZD; -. DR TreeFam; TF329147; -. DR NextBio; 345204; -. DR PRO; PR:Q78J03; -. DR Bgee; Q78J03; -. DR Genevestigator; Q78J03; -. DR GO; GO:0005739; C:mitochondrion; IDA:HGNC. DR GO; GO:0003779; F:actin binding; IDA:UniProtKB. DR GO; GO:0033743; F:peptide-methionine (R)-S-oxide reductase activity; IDA:UniProtKB. DR GO; GO:0008270; F:zinc ion binding; IDA:HGNC. DR GO; GO:0030041; P:actin filament polymerization; IDA:UniProtKB. DR GO; GO:0030091; P:protein repair; IDA:HGNC. DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro. DR Gene3D; 2.170.150.20; -; 1. DR InterPro; IPR028427; Met_Sox_Rdtase. DR InterPro; IPR002579; Met_Sox_Rdtase_MsrB. DR InterPro; IPR011057; Mss4-like. DR PANTHER; PTHR10173; PTHR10173; 1. DR Pfam; PF01641; SelR; 1. DR SUPFAM; SSF51316; SSF51316; 1. DR TIGRFAMs; TIGR00357; TIGR00357; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Metal-binding; Mitochondrion; KW Oxidoreductase; Reference proteome; Transit peptide; Zinc. FT TRANSIT 1 42 Mitochondrion (Potential). FT CHAIN 43 175 Methionine-R-sulfoxide reductase B2, FT mitochondrial. FT /FTId=PRO_0000327243. FT ACT_SITE 162 162 Nucleophile (By similarity). FT METAL 83 83 Zinc (By similarity). FT METAL 86 86 Zinc (By similarity). FT METAL 139 139 Zinc (By similarity). FT METAL 142 142 Zinc (By similarity). FT HELIX 48 51 FT HELIX 55 61 FT HELIX 70 72 FT STRAND 79 87 FT STRAND 89 92 FT HELIX 93 95 FT TURN 98 101 FT STRAND 104 108 FT HELIX 116 119 FT STRAND 122 127 FT STRAND 134 142 FT STRAND 147 150 FT HELIX 156 158 FT STRAND 160 163 FT STRAND 168 175 SQ SEQUENCE 175 AA; 19157 MW; 916771737762C6A6 CRC64; MARLLRALRG LPLLQAPGRL ARGCAGSGSK DTGSLTKSKR SLSEADWQKK LTPEQFYVTR EKGTEAPFSG MYLNNKETGM YHCVCCDSPL FSSEKKYCSG TGWPSFSEAY GSKGSDESHT GILRRLDTSL GCPRMEVVCK QCEAHLGHVF PDGPKPTGQR FCINSVALKF KPSKP // ID MSRB1_MOUSE Reviewed; 116 AA. AC Q9JLC3; Q545U8; DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot. DT 26-FEB-2008, sequence version 3. DT 19-FEB-2014, entry version 100. DE RecName: Full=Methionine-R-sulfoxide reductase B1; DE Short=MsrB1; DE EC=1.8.4.-; DE AltName: Full=Selenoprotein R; DE Short=SelR; DE AltName: Full=Selenoprotein X; DE Short=SelX; GN Name=Msrb1; Synonyms=Sepr, Sepx1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=10567350; DOI=10.1074/jbc.274.48.33888; RA Kryukov G.V., Kryukov V.M., Gladyshev V.N.; RT "New mammalian selenocysteine-containing proteins identified with an RT algorithm that searches for selenocysteine insertion sequence RT elements."; RL J. Biol. Chem. 274:33888-33897(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Heart, and Kidney; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6; TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP ENZYME ACTIVITY, AND ZINC-BINDING. RX PubMed=11929995; DOI=10.1073/pnas.072603099; RA Kryukov G.V., Kumar R.A., Koc A., Sun Z., Gladyshev V.N.; RT "Selenoprotein R is a zinc-containing stereo-specific methionine RT sulfoxide reductase."; RL Proc. Natl. Acad. Sci. U.S.A. 99:4245-4250(2002). RN [5] RP FUNCTION, COFACTOR, AND SUBCELLULAR LOCATION. RX PubMed=14699060; DOI=10.1091/mbc.E03-08-0629; RA Kim H.-Y., Gladyshev V.N.; RT "Methionine sulfoxide reduction in mammals: characterization of RT methionine-R-sulfoxide reductases."; RL Mol. Biol. Cell 15:1055-1064(2004). RN [6] RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION. RX PubMed=23911929; DOI=10.1016/j.molcel.2013.06.019; RA Lee B.C., Peterfi Z., Hoffmann F.W., Moore R.E., Kaya A., Avanesov A., RA Tarrago L., Zhou Y., Weerapana E., Fomenko D.E., Hoffmann P.R., RA Gladyshev V.N.; RT "MsrB1 and MICALs regulate actin assembly and macrophage function via RT reversible stereoselective methionine oxidation."; RL Mol. Cell 51:397-404(2013). RN [7] RP STRUCTURE BY NMR. RX PubMed=19636847; DOI=10.1007/s12104-007-9039-7; RA Sal L.S., Aachmann F.L., Kim H.Y., Gladyshev V.N., Dikiy A.; RT "NMR assignments of 1H, 13C and 15N spectra of methionine sulfoxide RT reductase B1 from Mus musculus."; RL Biomol. NMR. Assign. 1:131-133(2007). CC -!- FUNCTION: Methionine-sulfoxide reductase that specifically reduces CC methionine (R)-sulfoxide back to methionine. While in many cases, CC methionine oxidation is the result of random oxidation following CC oxidative stress, methionine oxidation is also a post- CC translational modification that takes place on specific residue. CC Acts as a regulator of actin assembly by reducing methionine (R)- CC sulfoxide mediated by MICALs (MICAL1, MICAL2 or MICAL3) on actin, CC thereby promoting filament repolymerization. Plays a role in CC innate immunity by reducing oxidized actin, leading to actin CC repolymerization in macrophages. CC -!- CATALYTIC ACTIVITY: L-methionine + oxidized thioredoxin = L- CC methionine R-oxide + reduced thioredoxin. CC -!- COFACTOR: Binds 1 zinc ion per subunit. CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cytoplasm, cytoskeleton. CC -!- SIMILARITY: Belongs to the MsrB Met sulfoxide reductase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF195142; AAF13697.1; -; mRNA. DR EMBL; AK002339; BAC55245.1; -; mRNA. DR EMBL; AK002652; BAE43148.1; -; mRNA. DR EMBL; AK003112; BAC55248.1; -; mRNA. DR EMBL; AK003624; BAC55249.1; -; mRNA. DR EMBL; BC090646; AAH90646.1; -; mRNA. DR RefSeq; NP_038787.1; NM_013759.2. DR UniGene; Mm.28212; -. DR PDB; 2KV1; NMR; -; A=1-116. DR PDBsum; 2KV1; -. DR ProteinModelPortal; Q9JLC3; -. DR SMR; Q9JLC3; 1-116. DR Ensembl; ENSMUST00000101800; ENSMUSP00000099300; ENSMUSG00000075705. DR Ensembl; ENSMUST00000115262; ENSMUSP00000110917; ENSMUSG00000075705. DR GeneID; 27361; -. DR KEGG; mmu:27361; -. DR UCSC; uc008ayh.1; mouse. DR CTD; 51734; -. DR MGI; MGI:1351642; Msrb1. DR eggNOG; COG0229; -. DR GeneTree; ENSGT00510000047678; -. DR HOGENOM; HOG000243424; -. DR HOVERGEN; HBG002192; -. DR InParanoid; Q9JLC3; -. DR KO; K07305; -. DR OMA; LKVSCGK; -. DR OrthoDB; EOG7VHSZD; -. DR TreeFam; TF329147; -. DR EvolutionaryTrace; Q9JLC3; -. DR NextBio; 305236; -. DR PRO; PR:Q9JLC3; -. DR Bgee; Q9JLC3; -. DR CleanEx; MM_SEPX1; -. DR Genevestigator; Q9JLC3; -. DR GO; GO:0005737; C:cytoplasm; IDA:MGI. DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell. DR GO; GO:0005634; C:nucleus; IDA:MGI. DR GO; GO:0003779; F:actin binding; IDA:UniProtKB. DR GO; GO:0070191; F:methionine-R-sulfoxide reductase activity; IDA:MGI. DR GO; GO:0033743; F:peptide-methionine (R)-S-oxide reductase activity; IDA:UniProtKB. DR GO; GO:0008270; F:zinc ion binding; IDA:HGNC. DR GO; GO:0030041; P:actin filament polymerization; IDA:UniProtKB. DR GO; GO:0045087; P:innate immune response; IMP:UniProtKB. DR GO; GO:0030091; P:protein repair; IDA:HGNC. DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro. DR Gene3D; 2.170.150.20; -; 1. DR InterPro; IPR028427; Met_Sox_Rdtase. DR InterPro; IPR002579; Met_Sox_Rdtase_MsrB. DR InterPro; IPR011057; Mss4-like. DR PANTHER; PTHR10173; PTHR10173; 1. DR Pfam; PF01641; SelR; 1. DR SUPFAM; SSF51316; SSF51316; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Cytoplasm; Cytoskeleton; Immunity; KW Innate immunity; Metal-binding; Nucleus; Oxidoreductase; KW Reference proteome; Selenocysteine; Zinc. FT CHAIN 1 116 Methionine-R-sulfoxide reductase B1. FT /FTId=PRO_0000140322. FT ACT_SITE 95 95 Nucleophile (By similarity). FT METAL 23 23 Zinc (By similarity). FT METAL 26 26 Zinc (By similarity). FT METAL 71 71 Zinc (By similarity). FT METAL 74 74 Zinc (By similarity). FT NON_STD 95 95 Selenocysteine. FT HELIX 12 14 FT STRAND 19 23 FT TURN 24 26 FT STRAND 41 43 FT STRAND 56 59 FT STRAND 61 63 FT STRAND 67 70 FT TURN 72 75 FT STRAND 79 81 FT TURN 87 90 FT TURN 98 100 FT STRAND 101 105 FT STRAND 107 109 SQ SEQUENCE 116 AA; 12788 MW; 7DE4E5EE86CAA333 CRC64; MSFCSFFGGE VFQNHFEPGV YVCAKCSYEL FSSHSKYAHS SPWPAFTETI HPDSVTKCPE KNRPEALKVS CGKCGNGLGH EFLNDGPKRG QSRFUIFSSS LKFVPKGKEA AASQGH // ID MSRB3_MOUSE Reviewed; 253 AA. AC Q8BU85; DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot. DT 05-APR-2011, sequence version 2. DT 19-MAR-2014, entry version 90. DE RecName: Full=Methionine-R-sulfoxide reductase B3, mitochondrial; DE Short=MsrB3; DE EC=1.8.4.-; DE Flags: Precursor; GN Name=Msrb3; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 20-253. RC STRAIN=C57BL/6J; TISSUE=Lung, and Urinary bladder; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 48-253. RC TISSUE=Olfactory epithelium; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP IDENTIFICATION, AND SUBCELLULAR LOCATION. RX PubMed=15249228; DOI=10.1016/j.bbrc.2004.06.078; RA Kim H.Y., Gladyshev V.N.; RT "Characterization of mouse endoplasmic reticulum methionine-R- RT sulfoxide reductase."; RL Biochem. Biophys. Res. Commun. 320:1277-1283(2004). RN [5] RP TISSUE SPECIFICITY. RX PubMed=21185009; DOI=10.1016/j.ajhg.2010.11.010; RA Ahmed Z.M., Yousaf R., Lee B.C., Khan S.N., Lee S., Lee K., RA Husnain T., Rehman A.U., Bonneux S., Ansar M., Ahmad W., Leal S.M., RA Gladyshev V.N., Belyantseva I.A., Van Camp G., Riazuddin S., RA Friedman T.B., Riazuddin S.; RT "Functional null mutations of MSRB3 encoding methionine sulfoxide RT reductase are associated with human deafness DFNB74."; RL Am. J. Hum. Genet. 88:19-29(2011). RN [6] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-102, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic fibroblast; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., RA Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). CC -!- FUNCTION: Catalyzes the reduction of free and protein-bound CC methionine sulfoxide to methionine (By similarity). CC -!- CATALYTIC ACTIVITY: L-methionine + oxidized thioredoxin = L- CC methionine R-oxide + reduced thioredoxin. CC -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity). CC -!- SUBUNIT: Monomer (By similarity). CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum. Note=Not detected in CC the mitochondrion. CC -!- TISSUE SPECIFICITY: Widely expressed. Detected in the sensory CC epithelia of the organ of Corti and vestibular end organs as early CC as P2 up to adulthood (at protein level). In the organ of Corti, CC present in inner and outer hair cells and, to a lesser extent, in CC supporting cells (at protein level). In hair cells, distributed CC throughout the cell body. Barely detectable level in stereocilia. CC Also observed in spiral ganglion neurons, but not in the stria CC vascularis. In the vestibular end organs, found throughout the CC sensory epithelium, but more intense expression in hair cells than CC in supporting cells (at protein level). In vestibular hair cells, CC present within cell bodies and to a lesser extent in kinocilia. CC Barely detectable in stereocilia. CC -!- DEVELOPMENTAL STAGE: Expressed in temporal bones at 15 dpc through CC postnatal 30, levels decrease thereafter, but is still present in CC the inner ear at P180. CC -!- MISCELLANEOUS: Contains a signal peptide followed by a CC mitochondrial transit peptide within a single transcript. However, CC the protein is detected exclusively within the endoplasmic CC reticulum. This contasts with other species, including Homo CC sapiens, where the signal and transit peptides are encoded on 2 CC mutually exclusive exons (PubMed:15249228), and where alternative CC splicing leads to the synthesis of either the endoplasmic CC reticulum resident form or the mitochondrial form. CC -!- SIMILARITY: Belongs to the MsrB Met sulfoxide reductase family. CC -!- SEQUENCE CAUTION: CC Sequence=AAH96447.1; Type=Erroneous initiation; Note=Translation N-terminally extended; CC Sequence=BAC39776.1; Type=Erroneous initiation; Note=Translation N-terminally extended; CC Sequence=BAE23258.1; Type=Erroneous initiation; Note=Translation N-terminally extended; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AC138388; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AK086975; BAC39776.1; ALT_INIT; mRNA. DR EMBL; AK137163; BAE23258.1; ALT_INIT; mRNA. DR EMBL; BC096447; AAH96447.1; ALT_INIT; mRNA. DR RefSeq; NP_796066.1; NM_177092.4. DR RefSeq; XP_006513827.1; XM_006513764.1. DR RefSeq; XP_006513828.1; XM_006513765.1. DR UniGene; Mm.169755; -. DR ProteinModelPortal; Q8BU85; -. DR SMR; Q8BU85; 79-238. DR IntAct; Q8BU85; 2. DR MINT; MINT-4112541; -. DR STRING; 10090.ENSMUSP00000089781; -. DR PhosphoSite; Q8BU85; -. DR PaxDb; Q8BU85; -. DR PRIDE; Q8BU85; -. DR Ensembl; ENSMUST00000092143; ENSMUSP00000089781; ENSMUSG00000051236. DR GeneID; 320183; -. DR KEGG; mmu:320183; -. DR UCSC; uc007hfh.2; mouse. DR CTD; 253827; -. DR MGI; MGI:2443538; Msrb3. DR eggNOG; COG0229; -. DR GeneTree; ENSGT00510000046802; -. DR HOGENOM; HOG000243424; -. DR HOVERGEN; HBG002192; -. DR InParanoid; Q8BU85; -. DR KO; K07305; -. DR OrthoDB; EOG7VHSZD; -. DR TreeFam; TF329147; -. DR ChiTaRS; MSRB3; mouse. DR NextBio; 396199; -. DR PRO; PR:Q8BU85; -. DR ArrayExpress; Q8BU85; -. DR Bgee; Q8BU85; -. DR Genevestigator; Q8BU85; -. DR GO; GO:0005783; C:endoplasmic reticulum; ISS:HGNC. DR GO; GO:0005739; C:mitochondrion; ISA:MGI. DR GO; GO:0033743; F:peptide-methionine (R)-S-oxide reductase activity; ISS:HGNC. DR GO; GO:0008270; F:zinc ion binding; ISS:HGNC. DR GO; GO:0030091; P:protein repair; ISS:HGNC. DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro. DR Gene3D; 2.170.150.20; -; 1. DR HAMAP; MF_01400; MsrB; 1. DR InterPro; IPR028427; Met_Sox_Rdtase. DR InterPro; IPR002579; Met_Sox_Rdtase_MsrB. DR InterPro; IPR011057; Mss4-like. DR PANTHER; PTHR10173; PTHR10173; 1. DR Pfam; PF01641; SelR; 1. DR SUPFAM; SSF51316; SSF51316; 1. DR TIGRFAMs; TIGR00357; TIGR00357; 1. PE 1: Evidence at protein level; KW Acetylation; Complete proteome; Endoplasmic reticulum; Metal-binding; KW Oxidoreductase; Reference proteome; Signal; Zinc. FT SIGNAL 1 56 Potential. FT CHAIN 57 253 Methionine-R-sulfoxide reductase B3, FT mitochondrial. FT /FTId=PRO_0000327241. FT MOTIF 250 253 Endoplasmic reticulum retention signal. FT ACT_SITE 218 218 Nucleophile (By similarity). FT METAL 146 146 Zinc (By similarity). FT METAL 149 149 Zinc (By similarity). FT METAL 195 195 Zinc (By similarity). FT METAL 198 198 Zinc (By similarity). FT MOD_RES 102 102 N6-acetyllysine. SQ SEQUENCE 253 AA; 26832 MW; 361264F3C605ADB5 CRC64; MPPAAPSVAR SREGGGIGQR RLVFPKSARR TLPCPIALCL GLCLAAAAAT TTRASAAAFA SAGDTTAMSA FNLLHLVTKS QPVAPRACGL PSGSCRDKKN CKVVFSQQEL RKRLTPLQYH VTQEKGTESA FEGEYTHHKD PGIYKCVVCG TPLFKSETKF DSGSGWPAFH DVISSEAIEF TDDFSYGMHR VETSCSQCGA HLGHIFDDGP RPTGKRYCIN SASLSFTPAD SSEAEGSGIK ESGSPAAADR AEL // ID MTD2L_MOUSE Reviewed; 338 AA. AC D3YZG8; DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot. DT 20-APR-2010, sequence version 1. DT 19-FEB-2014, entry version 35. DE RecName: Full=Probable bifunctional methylenetetrahydrofolate dehydrogenase/cyclohydrolase 2; DE AltName: Full=NADP-dependent methylenetetrahydrofolate dehydrogenase 2-like protein; DE Short=MTHFD2-like; DE Includes: DE RecName: Full=NAD-dependent methylenetetrahydrofolate dehydrogenase; DE EC=1.5.1.15; DE Includes: DE RecName: Full=Methenyltetrahydrofolate cyclohydrolase; DE EC=3.5.4.9; GN Name=Mthfd2l; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 5,10-methylenetetrahydrofolate + NAD(+) = CC 5,10-methenyltetrahydrofolate + NADH. CC -!- CATALYTIC ACTIVITY: 5,10-methenyltetrahydrofolate + H(2)O = 10- CC formyltetrahydrofolate. CC -!- COFACTOR: Magnesium (By similarity). CC -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion. CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral CC membrane protein; Matrix side (By similarity). CC -!- SIMILARITY: Belongs to the tetrahydrofolate CC dehydrogenase/cyclohydrolase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AC109311; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC157938; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH466617; EDL05299.1; -; Genomic_DNA. DR RefSeq; NP_081064.1; NM_026788.1. DR UniGene; Mm.153030; -. DR ProteinModelPortal; D3YZG8; -. DR SMR; D3YZG8; 42-332. DR PhosphoSite; D3YZG8; -. DR PRIDE; D3YZG8; -. DR Ensembl; ENSMUST00000071652; ENSMUSP00000071578; ENSMUSG00000029376. DR GeneID; 665563; -. DR KEGG; mmu:665563; -. DR UCSC; uc008ybp.2; mouse. DR CTD; 441024; -. DR MGI; MGI:1915871; Mthfd2l. DR GeneTree; ENSGT00730000110817; -. DR HOGENOM; HOG000218242; -. DR KO; K13403; -. DR OMA; DLKHKIQ; -. DR OrthoDB; EOG7CG70C; -. DR TreeFam; TF323998; -. DR UniPathway; UPA00193; -. DR NextBio; 427797; -. DR PRO; PR:D3YZG8; -. DR Bgee; D3YZG8; -. DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005739; C:mitochondrion; IBA:RefGenome. DR GO; GO:0004477; F:methenyltetrahydrofolate cyclohydrolase activity; IBA:RefGenome. DR GO; GO:0004487; F:methylenetetrahydrofolate dehydrogenase (NAD+) activity; IBA:RefGenome. DR GO; GO:0004488; F:methylenetetrahydrofolate dehydrogenase (NADP+) activity; IBA:RefGenome. DR GO; GO:0009396; P:folic acid-containing compound biosynthetic process; IEA:InterPro. DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0006730; P:one-carbon metabolic process; IBA:RefGenome. DR GO; GO:0006164; P:purine nucleotide biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0035999; P:tetrahydrofolate interconversion; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.720; -; 1. DR HAMAP; MF_01576; THF_DHG_CYH; 1. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR000672; THF_DH/CycHdrlase. DR InterPro; IPR020630; THF_DH/CycHdrlase_cat_dom. DR InterPro; IPR020867; THF_DH/CycHdrlase_CS. DR InterPro; IPR020631; THF_DH/CycHdrlase_NAD-bd_dom. DR Pfam; PF00763; THF_DHG_CYH; 1. DR Pfam; PF02882; THF_DHG_CYH_C; 1. DR PRINTS; PR00085; THFDHDRGNASE. DR PROSITE; PS00767; THF_DHG_CYH_2; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Complete proteome; Histidine biosynthesis; KW Hydrolase; Magnesium; Membrane; Methionine biosynthesis; KW Mitochondrion; Mitochondrion inner membrane; Multifunctional enzyme; KW NAD; One-carbon metabolism; Oxidoreductase; Purine biosynthesis; KW Reference proteome. FT CHAIN 1 338 Probable bifunctional FT methylenetetrahydrofolate FT dehydrogenase/cyclohydrolase 2. FT /FTId=PRO_0000413328. SQ SEQUENCE 338 AA; 36438 MW; 71A447A15C918D8E CRC64; MATRARGFSL LRGRLGRGPV RAPGVAERAW RGFGSSGRRH EAVIISGTNM AKQIQKEIQQ GVESWIALGN RRPHLSIILV GDNPASHTYV RNKIKAASAV GICSELIIKP KNVSQEELLD ITDQLNMDPR VSGILVQLPL PDHVDERTIC NGIAPEKDVD GFHIINIGRL CLDQHSLIPA TASAVWEIIK RAGIETFGKN VVVAGRSKNV GMPIAMLLHT DGEHERPGGD ATVTIAHRYT PREQLKAHTQ LADIIIVAAG IPRLITADMV REGAAVIDVG INYIQDPVTG KTKLVGDVDF EAVKKKASFI TPVPGGVGPM TVAMLLKNTL LAAKNIAY // ID MTDC_MOUSE Reviewed; 350 AA. AC P18155; Q3TMN4; DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1990, sequence version 1. DT 19-FEB-2014, entry version 128. DE RecName: Full=Bifunctional methylenetetrahydrofolate dehydrogenase/cyclohydrolase, mitochondrial; DE Includes: DE RecName: Full=NAD-dependent methylenetetrahydrofolate dehydrogenase; DE EC=1.5.1.15; DE Includes: DE RecName: Full=Methenyltetrahydrofolate cyclohydrolase; DE EC=3.5.4.9; DE Flags: Precursor; GN Name=Mthfd2; Synonyms=Nmdmc; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 36-55. RX PubMed=2647744; RA Belanger C., Mackenzie R.E.; RT "Isolation and characterization of cDNA clones encoding the murine RT NAD-dependent methylenetetrahydrofolate dehydrogenase- RT methenyltetrahydrofolate cyclohydrolase."; RL J. Biol. Chem. 264:4837-4843(1989). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=1999293; DOI=10.1016/0378-1119(91)90064-I; RA Belanger C., Mackenzie R.E.; RT "Structural organization of the murine gene encoding NAD-dependent RT methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate RT cyclohydrolase."; RL Gene 97:283-288(1991). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Salivary gland; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-34. RX PubMed=1843253; DOI=10.1093/nar/19.16.4341; RA Belanger C., Peri K.G., Mackenzie R.E.; RT "Analysis of the promoter region of the gene encoding NAD-dependent RT methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate RT cyclohydrolase."; RL Nucleic Acids Res. 19:4341-4345(1991). CC -!- CATALYTIC ACTIVITY: 5,10-methylenetetrahydrofolate + NAD(+) = CC 5,10-methenyltetrahydrofolate + NADH. CC -!- CATALYTIC ACTIVITY: 5,10-methenyltetrahydrofolate + H(2)O = 10- CC formyltetrahydrofolate. CC -!- COFACTOR: Magnesium. CC -!- SUBUNIT: Homodimer. CC -!- SUBCELLULAR LOCATION: Mitochondrion. CC -!- MISCELLANEOUS: This NAD-dependent bifunctional enzyme has very CC different kinetic properties than the larger NADP-dependent CC trifunctional enzyme and is unique in that it requires formation CC of an enzyme-magnesium complex to allow binding of NAD. CC -!- SIMILARITY: Belongs to the tetrahydrofolate CC dehydrogenase/cyclohydrolase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; J04627; AAA39827.1; -; mRNA. DR EMBL; M63445; AAA39828.1; -; Genomic_DNA. DR EMBL; M63415; AAA39828.1; JOINED; Genomic_DNA. DR EMBL; M63439; AAA39828.1; JOINED; Genomic_DNA. DR EMBL; M63440; AAA39828.1; JOINED; Genomic_DNA. DR EMBL; M63441; AAA39828.1; JOINED; Genomic_DNA. DR EMBL; M63442; AAA39828.1; JOINED; Genomic_DNA. DR EMBL; M63443; AAA39828.1; JOINED; Genomic_DNA. DR EMBL; M63444; AAA39828.1; JOINED; Genomic_DNA. DR EMBL; AK076019; BAC36124.1; -; mRNA. DR EMBL; AK159680; BAE35283.1; -; mRNA. DR EMBL; AK165840; BAE38407.1; -; mRNA. DR EMBL; BC019511; AAH19511.1; -; mRNA. DR EMBL; S52980; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR PIR; A33267; A33267. DR RefSeq; NP_032664.1; NM_008638.2. DR UniGene; Mm.443; -. DR UniGene; Mm.475021; -. DR ProteinModelPortal; P18155; -. DR SMR; P18155; 37-336. DR PhosphoSite; P18155; -. DR PaxDb; P18155; -. DR PRIDE; P18155; -. DR Ensembl; ENSMUST00000005810; ENSMUSP00000005810; ENSMUSG00000005667. DR GeneID; 17768; -. DR KEGG; mmu:17768; -. DR UCSC; uc009cne.2; mouse. DR CTD; 10797; -. DR MGI; MGI:1338850; Mthfd2. DR eggNOG; COG0190; -. DR GeneTree; ENSGT00730000110817; -. DR HOGENOM; HOG000218242; -. DR HOVERGEN; HBG006411; -. DR InParanoid; P18155; -. DR KO; K13403; -. DR OMA; MLLNANC; -. DR OrthoDB; EOG7CG70C; -. DR TreeFam; TF323998; -. DR BRENDA; 1.5.1.15; 3474. DR SABIO-RK; P18155; -. DR ChiTaRS; Mthfd2; mouse. DR NextBio; 292477; -. DR PRO; PR:P18155; -. DR Bgee; P18155; -. DR Genevestigator; P18155; -. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR GO; GO:0000287; F:magnesium ion binding; IEA:Ensembl. DR GO; GO:0004477; F:methenyltetrahydrofolate cyclohydrolase activity; IBA:RefGenome. DR GO; GO:0004487; F:methylenetetrahydrofolate dehydrogenase (NAD+) activity; IBA:RefGenome. DR GO; GO:0004488; F:methylenetetrahydrofolate dehydrogenase (NADP+) activity; IBA:RefGenome. DR GO; GO:0042301; F:phosphate ion binding; IEA:Ensembl. DR GO; GO:0009396; P:folic acid-containing compound biosynthetic process; IEA:InterPro. DR GO; GO:0006730; P:one-carbon metabolic process; IBA:RefGenome. DR GO; GO:0046653; P:tetrahydrofolate metabolic process; IEA:Ensembl. DR Gene3D; 3.40.50.720; -; 1. DR HAMAP; MF_01576; THF_DHG_CYH; 1. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR000672; THF_DH/CycHdrlase. DR InterPro; IPR020630; THF_DH/CycHdrlase_cat_dom. DR InterPro; IPR020867; THF_DH/CycHdrlase_CS. DR InterPro; IPR020631; THF_DH/CycHdrlase_NAD-bd_dom. DR Pfam; PF00763; THF_DHG_CYH; 1. DR Pfam; PF02882; THF_DHG_CYH_C; 1. DR PRINTS; PR00085; THFDHDRGNASE. DR PROSITE; PS00766; THF_DHG_CYH_1; 1. DR PROSITE; PS00767; THF_DHG_CYH_2; 1. PE 1: Evidence at protein level; KW Acetylation; Complete proteome; Direct protein sequencing; Hydrolase; KW Magnesium; Mitochondrion; Multifunctional enzyme; NAD; KW One-carbon metabolism; Oxidoreductase; Reference proteome; KW Transit peptide. FT TRANSIT 1 35 Mitochondrion. FT CHAIN 36 350 Bifunctional methylenetetrahydrofolate FT dehydrogenase/cyclohydrolase, FT mitochondrial. FT /FTId=PRO_0000034050. FT MOD_RES 50 50 N6-acetyllysine (By similarity). SQ SEQUENCE 350 AA; 37863 MW; 896AD40D9154E9D7 CRC64; MASVSLLSAL AVRLLRPTHG CHPRLQPFHL AAVRNEAVVI SGRKLAQQIK QEVQQEVEEW VASGNKRPHL SVILVGDNPA SHSYVLNKTR AAAEVGINSE TIVKPASVSE EELLNSIRKL NNDENVDGLL VQLPLPEHID ERKVCNAVSP DKDVDGFHVI NVGRMCLDQY SMLPATPWGV WEIIKRTGIP TLGKNVVVAG RSKNVGMPIA MLLHTDGAHE RPGGDATVTI SHRYTPKEQL KKHTILADIV ISAAGIPNLI TADMIKEGAA VIDVGINRVQ DPVTAKPKLV GDVDFEGVKK KAGYITPVPG GVGPMTVAML MKNTIIAAKK VLRPEELEVF KSKQRGVATN // ID MTHR_MOUSE Reviewed; 654 AA. AC Q9WU20; Q8CDE4; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 2. DT 22-JAN-2014, entry version 95. DE RecName: Full=Methylenetetrahydrofolate reductase; DE EC=1.5.1.20; GN Name=Mthfr; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=9680386; DOI=10.1007/s003359900838; RA Goyette P., Pai A., Milos R., Frosst P., Tran P., Chen Z., Chan M., RA Rozen R.; RT "Gene structure of human and mouse methylenetetrahydrofolate reductase RT (MTHFR)."; RL Mamm. Genome 9:652-656(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Testis; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6; TISSUE=Brain, and Olfactory epithelium; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: Catalyzes the conversion of 5,10- CC methylenetetrahydrofolate to 5-methyltetrahydrofolate, a co- CC substrate for homocysteine remethylation to methionine. CC -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC -!- COFACTOR: FAD (By similarity). CC -!- ENZYME REGULATION: Allosterically regulated by S- CC adenosylmethionine (By similarity). CC -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion. CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF105998; AAD20313.1; -; Genomic_DNA. DR EMBL; AF105988; AAD20313.1; JOINED; Genomic_DNA. DR EMBL; AF105989; AAD20313.1; JOINED; Genomic_DNA. DR EMBL; AF105990; AAD20313.1; JOINED; Genomic_DNA. DR EMBL; AF105991; AAD20313.1; JOINED; Genomic_DNA. DR EMBL; AF105992; AAD20313.1; JOINED; Genomic_DNA. DR EMBL; AF105993; AAD20313.1; JOINED; Genomic_DNA. DR EMBL; AF105994; AAD20313.1; JOINED; Genomic_DNA. DR EMBL; AF105995; AAD20313.1; JOINED; Genomic_DNA. DR EMBL; AF105996; AAD20313.1; JOINED; Genomic_DNA. DR EMBL; AF105997; AAD20313.1; JOINED; Genomic_DNA. DR EMBL; AK030192; BAC26832.1; -; mRNA. DR EMBL; AL606929; CAM14896.1; -; Genomic_DNA. DR EMBL; CH466594; EDL14794.1; -; Genomic_DNA. DR EMBL; CH466594; EDL14796.1; -; Genomic_DNA. DR EMBL; CH466594; EDL14797.1; -; Genomic_DNA. DR EMBL; BC051017; AAH51017.1; -; mRNA. DR EMBL; BC052466; AAH52466.1; -; mRNA. DR RefSeq; NP_034970.2; NM_010840.3. DR UniGene; Mm.89959; -. DR ProteinModelPortal; Q9WU20; -. DR SMR; Q9WU20; 59-337. DR PhosphoSite; Q9WU20; -. DR PaxDb; Q9WU20; -. DR PRIDE; Q9WU20; -. DR Ensembl; ENSMUST00000097788; ENSMUSP00000095395; ENSMUSG00000029009. DR GeneID; 17769; -. DR KEGG; mmu:17769; -. DR UCSC; uc008vtu.2; mouse. DR CTD; 4524; -. DR MGI; MGI:106639; Mthfr. DR eggNOG; COG0685; -. DR GeneTree; ENSGT00390000012490; -. DR HOGENOM; HOG000246234; -. DR HOVERGEN; HBG006414; -. DR InParanoid; Q8CDE4; -. DR KO; K00297; -. DR OrthoDB; EOG7TF7B4; -. DR BRENDA; 1.5.1.15; 3474. DR UniPathway; UPA00193; -. DR NextBio; 292481; -. DR PRO; PR:Q9WU20; -. DR ArrayExpress; Q9WU20; -. DR Bgee; Q9WU20; -. DR CleanEx; MM_MTHFR; -. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IMP:MGI. DR GO; GO:0009086; P:methionine biosynthetic process; IMP:MGI. DR GO; GO:0035999; P:tetrahydrofolate interconversion; IEA:UniProtKB-UniPathway. DR InterPro; IPR004621; Fadh2_euk. DR InterPro; IPR003171; Mehydrof_redctse. DR Pfam; PF02219; MTHFR; 1. DR TIGRFAMs; TIGR00677; fadh2_euk; 1. PE 2: Evidence at transcript level; KW Allosteric enzyme; Complete proteome; FAD; Flavoprotein; NADP; KW Oxidoreductase; Reference proteome. FT CHAIN 1 654 Methylenetetrahydrofolate reductase. FT /FTId=PRO_0000190247. FT NP_BIND 62 67 NAD (By similarity). FT NP_BIND 93 94 NAD and FAD (By similarity). FT NP_BIND 156 158 FAD (By similarity). FT NP_BIND 173 174 FAD (By similarity). FT NP_BIND 200 203 FAD (By similarity). FT ACT_SITE 62 62 Proton donor/acceptor (By similarity). FT BINDING 126 126 FAD (By similarity). FT BINDING 158 158 Substrate (By similarity). FT BINDING 196 196 FAD (By similarity). FT BINDING 209 209 FAD (By similarity). FT BINDING 216 216 FAD (By similarity). FT BINDING 227 227 Substrate (By similarity). FT BINDING 320 320 Substrate (By similarity). FT BINDING 324 324 Substrate (By similarity). FT CONFLICT 303 303 S -> R (in Ref. 1; AAD20313). SQ SEQUENCE 654 AA; 74580 MW; 96E625014D8F4838 CRC64; MVNEARGSGS PNPRSEGSSS GSESSKDSSR CSTPSLDPER HERLREKMRR RMDSGDKWFS LEFFPPRTAE GAVNLISRFD RMAAGGPLFV DVTWHPAGDP GSDKETSSMM IASTAVNYCG LETILHMTCC QQRPEEITGH LHRAKQLGLK NIMALRGDPV GDHWEAEEGG FSYATDLVKH IRTEFADYFD ICVAGYPRGH PDAESFEDDL KHLKEKVSAG ADFIITQLFF EASTFFSFVK ACTEIGISCP ILPGIFPIQG YTSLRQLVKL SKLEVPQKIK DVIEPIKDND AAIRNYGIEL AVSLCRELLD SGLVPGLHFY TLNREVATME VLKQLGMWTE DPRRPLPWAL SAHPKRREED VRPIFWASRP KSYIYRTQDW DEFPNGRWGN SSSPAFGELK DYYLFYLKSK SPREELLKMW GEELTSEESV FEVFEHYLSG EPNRHGYRVT CLPWNDEPLA AETSLMKEEL LRVNRLGILT INSQPNINAK PSSDPVVGWG PSGGYVFQKA YLEFFTSRET VEALLQVLKT YELRVNYHIV DVKGENITNA PELQPNAVTW GIFPGREIIQ PTVVDPISFM FWKDEAFALW IEQWGKLYEE ESPSRMIIQY IHDNYFLVNL VDNEFPLDSC LWQVVEDTFE LLNRHPTERE TQAP // ID MTND_MOUSE Reviewed; 179 AA. AC Q99JT9; DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 19-FEB-2014, entry version 103. DE RecName: Full=1,2-dihydroxy-3-keto-5-methylthiopentene dioxygenase; DE EC=1.13.11.54; DE AltName: Full=Acireductone dioxygenase (Fe(2+)-requiring); DE Short=ARD; DE Short=Fe-ARD; DE AltName: Full=Membrane-type 1 matrix metalloproteinase cytoplasmic tail-binding protein 1; DE Short=MTCBP-1; GN Name=Adi1; Synonyms=Mtcbp1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Mammary tumor; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.06 ANGSTROMS) IN COMPLEX WITH DIVALENT METAL RP ION, COFACTOR, AND SUBUNIT. RX PubMed=16783794; DOI=10.1002/prot.20947; RA Xu Q., Schwarzenbacher R., Krishna S.S., McMullan D., Agarwalla S., RA Quijano K., Abdubek P., Ambing E., Axelrod H., Biorac T., RA Canaves J.M., Chiu H.J., Elsliger M.A., Grittini C., Grzechnik S.K., RA DiDonato M., Hale J., Hampton E., Han G.W., Haugen J., Hornsby M., RA Jaroszewski L., Klock H.E., Knuth M.W., Koesema E., Kreusch A., RA Kuhn P., Miller M.D., Moy K., Nigoghossian E., Paulsen J., Reyes R., RA Rife C., Spraggon G., Stevens R.C., van den Bedem H., Velasquez J., RA White A., Wolf G., Hodgson K.O., Wooley J., Deacon A.M., Godzik A., RA Lesley S.A., Wilson I.A.; RT "Crystal structure of acireductone dioxygenase (ARD) from Mus musculus RT at 2.06 angstrom resolution."; RL Proteins 64:808-813(2006). CC -!- FUNCTION: Catalyzes the formation of formate and 2-keto-4- CC methylthiobutyrate (KMTB) from 1,2-dihydroxy-3-keto-5- CC methylthiopentene (DHK-MTPene). Also down-regulates cell migration CC mediated by MMP14 (By similarity). CC -!- CATALYTIC ACTIVITY: 1,2-dihydroxy-5-(methylthio)pent-1-en-3-one + CC O(2) = 4-(methylthio)-2-oxobutanoate + formate. CC -!- COFACTOR: Binds 1 iron ion per monomer. Can also use other CC divalent metal cations. CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via CC salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose CC 1-phosphate: step 5/6. CC -!- SUBUNIT: Monomer. Interacts with MMP14 (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By CC similarity). Cell membrane; Peripheral membrane protein; CC Cytoplasmic side (By similarity). Note=Localizes to the plasma CC membrane when complexed to MMP14 (By similarity). CC -!- SIMILARITY: Belongs to the acireductone dioxygenase (ARD) family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK145831; BAE26682.1; -; mRNA. DR EMBL; BC005695; AAH05695.1; -; mRNA. DR RefSeq; NP_598813.1; NM_134052.2. DR UniGene; Mm.291504; -. DR PDB; 1VR3; X-ray; 2.06 A; A=1-179. DR PDBsum; 1VR3; -. DR ProteinModelPortal; Q99JT9; -. DR SMR; Q99JT9; 1-179. DR STRING; 10090.ENSMUSP00000020957; -. DR PhosphoSite; Q99JT9; -. DR PaxDb; Q99JT9; -. DR PRIDE; Q99JT9; -. DR DNASU; 104923; -. DR Ensembl; ENSMUST00000020957; ENSMUSP00000020957; ENSMUSG00000020629. DR GeneID; 104923; -. DR KEGG; mmu:104923; -. DR UCSC; uc007nfv.1; mouse. DR CTD; 55256; -. DR MGI; MGI:2144929; Adi1. DR eggNOG; COG1791; -. DR GeneTree; ENSGT00390000008195; -. DR HOGENOM; HOG000201071; -. DR HOVERGEN; HBG081992; -. DR InParanoid; Q99JT9; -. DR KO; K08967; -. DR OMA; YEEKLKM; -. DR OrthoDB; EOG73FQP0; -. DR TreeFam; TF300231; -. DR BRENDA; 1.13.11.53; 3474. DR UniPathway; UPA00904; UER00878. DR EvolutionaryTrace; Q99JT9; -. DR NextBio; 357366; -. DR PRO; PR:Q99JT9; -. DR ArrayExpress; Q99JT9; -. DR Bgee; Q99JT9; -. DR CleanEx; MM_ADI1; -. DR Genevestigator; Q99JT9; -. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl. DR GO; GO:0005634; C:nucleus; ISS:UniProtKB. DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB. DR GO; GO:0010309; F:acireductone dioxygenase [iron(II)-requiring] activity; IEA:UniProtKB-HAMAP. DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0016491; F:oxidoreductase activity; ISS:UniProtKB. DR GO; GO:0019509; P:L-methionine salvage from methylthioadenosine; ISS:UniProtKB. DR Gene3D; 2.60.120.10; -; 1. DR HAMAP; MF_03154; Salvage_MtnD_euk; 1. DR InterPro; IPR004313; Acireductn_dOase_family. DR InterPro; IPR027496; MTCBP-1_eukaryotes. DR InterPro; IPR014710; RmlC-like_jellyroll. DR InterPro; IPR011051; RmlC_Cupin. DR PANTHER; PTHR23418; PTHR23418; 1. DR Pfam; PF03079; ARD; 1. DR SUPFAM; SSF51182; SSF51182; 1. PE 1: Evidence at protein level; KW 3D-structure; Amino-acid biosynthesis; Cell membrane; KW Complete proteome; Cytoplasm; Dioxygenase; Iron; Membrane; KW Metal-binding; Methionine biosynthesis; Nucleus; Oxidoreductase; KW Reference proteome. FT CHAIN 1 179 1,2-dihydroxy-3-keto-5-methylthiopentene FT dioxygenase. FT /FTId=PRO_0000162943. FT METAL 88 88 Iron or nickel. FT METAL 90 90 Iron or nickel. FT METAL 94 94 Iron or nickel. FT METAL 133 133 Iron or nickel. FT STRAND 3 7 FT HELIX 28 33 FT STRAND 37 40 FT HELIX 43 45 FT HELIX 50 59 FT STRAND 63 70 FT TURN 71 73 FT HELIX 77 85 FT STRAND 94 108 FT STRAND 114 120 FT STRAND 123 127 FT STRAND 133 137 FT STRAND 143 152 FT STRAND 158 160 FT HELIX 166 177 SQ SEQUENCE 179 AA; 21524 MW; 02CE7B89181EBEFE CRC64; MVQAWYMDES TADPRKPHRA QPDRPVSLEQ LRTLGVLYWK LDADKYENDP ELEKIRKMRN YSWMDIITIC KDTLPNYEEK IKMFFEEHLH LDEEIRYILE GSGYFDVRDK EDKWIRISME KGDMITLPAG IYHRFTLDEK NYVKAMRLFV GEPVWTPYNR PADHFDARVQ YMSFLEGTA // ID MTRR_MOUSE Reviewed; 696 AA. AC Q8C1A3; Q3U2C6; Q8R0Y3; DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot. DT 31-MAY-2011, sequence version 2. DT 19-MAR-2014, entry version 92. DE RecName: Full=Methionine synthase reductase; DE Short=MSR; DE EC=1.16.1.8; GN Name=Mtrr; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J, and NOD; TISSUE=Corpora quadrigemina, and Skin; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Liver; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP DISRUPTION PHENOTYPE. RX PubMed=18413293; DOI=10.1016/j.ymgme.2008.03.004; RA Deng L., Elmore C.L., Lawrance A.K., Matthews R.G., Rozen R.; RT "Methionine synthase reductase deficiency results in adverse RT reproductive outcomes and congenital heart defects in mice."; RL Mol. Genet. Metab. 94:336-342(2008). RN [5] RP FUNCTION, AND DISRUPTION PHENOTYPE. RX PubMed=24074862; DOI=10.1016/j.cell.2013.09.002; RA Padmanabhan N., Jia D., Geary-Joo C., Wu X., Ferguson-Smith A.C., RA Fung E., Bieda M.C., Snyder F.F., Gravel R.A., Cross J.C., RA Watson E.D.; RT "Mutation in folate metabolism causes epigenetic instability and RT transgenerational effects on development."; RL Cell 155:81-93(2013). CC -!- FUNCTION: Involved in the reductive regeneration of cob(I)alamin CC (vitamin B12) cofactor required for the maintenance of methionine CC synthase in a functional state. Necessary for utilization of CC methylgroups from the folate cycle, thereby affecting CC transgenerational epigenetic inheritance. Folate pathway donates CC methyl groups necessary for cellular methylation and affects CC different pathways such as DNA methylation, possibly explaining CC the transgenerational epigenetic inheritance effects. CC -!- CATALYTIC ACTIVITY: 2 [methionine synthase]-methylcob(I)alamin + 2 CC S-adenosylhomocysteine + NADP(+) = 2 [methionine synthase]- CC cob(II)alamin + NADPH + 2 S-adenosyl-L-methionine. CC -!- COFACTOR: FAD (By similarity). CC -!- COFACTOR: FMN (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- DISRUPTION PHENOTYPE: Female mice have more resorptions and more CC delayed embryos per litter as well as embryonic delays and CC defects: placentae of mothers are smaller and their embryos are CC smaller and display myocardial hypoplasia and a higher incidence CC of ventricular septal defects per litter (PubMed:18413293). CC Epigenetic transmission of developmental disorders between CC generations: a hypomorphic mutation disrupts folate metabolism and CC is associated with effects on offspring development that are CC transmitted transgenerationally. The epigenetic influences caused CC by Mtrr hypomorphic deficiency in mice leads to 2 distinctive CC phenotypes: (1) an atypical uterine environment in their wild-type CC daughters that causes growth defects in their wild-type CC grandprogeny and (2) congenital malformations in their wild-type CC grandprogeny due to epigenetic inheritance via the germline, the CC effects of which persist for at least up to 4 wild-type CC generations after an Mtrr-deficient maternal ancestor. These CC effects are associated with altered DNA methylation patterns CC (PubMed:24074862). CC -!- SIMILARITY: Contains 1 FAD-binding FR-type domain. CC -!- SIMILARITY: Contains 1 flavodoxin-like domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK028628; BAC26039.1; -; mRNA. DR EMBL; AK155359; BAE33215.1; -; mRNA. DR EMBL; AK163449; BAE37348.1; -; mRNA. DR EMBL; CH466563; EDL37004.1; -; Genomic_DNA. DR EMBL; BC025942; AAH25942.1; -; mRNA. DR RefSeq; NP_766068.1; NM_172480.2. DR RefSeq; XP_006517242.1; XM_006517179.1. DR RefSeq; XP_006517243.1; XM_006517180.1. DR RefSeq; XP_006517244.1; XM_006517181.1. DR RefSeq; XP_006517245.1; XM_006517182.1. DR UniGene; Mm.205514; -. DR ProteinModelPortal; Q8C1A3; -. DR SMR; Q8C1A3; 2-696. DR STRING; 10090.ENSMUSP00000039810; -. DR PRIDE; Q8C1A3; -. DR Ensembl; ENSMUST00000045827; ENSMUSP00000039810; ENSMUSG00000034617. DR GeneID; 210009; -. DR KEGG; mmu:210009; -. DR UCSC; uc007rby.1; mouse. DR CTD; 4552; -. DR MGI; MGI:1891037; Mtrr. DR eggNOG; COG0369; -. DR GeneTree; ENSGT00620000087711; -. DR HOGENOM; HOG000007485; -. DR HOVERGEN; HBG108376; -. DR InParanoid; Q8C1A3; -. DR KO; K00597; -. DR OrthoDB; EOG7NCV31; -. DR TreeFam; TF105716; -. DR NextBio; 372826; -. DR PRO; PR:Q8C1A3; -. DR Bgee; Q8C1A3; -. DR Genevestigator; Q8C1A3; -. DR GO; GO:0005829; C:cytosol; IBA:RefGenome. DR GO; GO:0045111; C:intermediate filament cytoskeleton; IEA:Ensembl. DR GO; GO:0005634; C:nucleus; IEA:Ensembl. DR GO; GO:0030586; F:[methionine synthase] reductase activity; IBA:RefGenome. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; ISS:UniProtKB. DR GO; GO:0010181; F:FMN binding; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0016709; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen; IBA:RefGenome. DR GO; GO:0006306; P:DNA methylation; IMP:UniProtKB. DR GO; GO:0046655; P:folic acid metabolic process; IMP:UniProtKB. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:UniProtKB-KW. DR Gene3D; 1.20.990.10; -; 1. DR InterPro; IPR003097; FAD-binding_1. DR InterPro; IPR017927; Fd_Rdtase_FAD-bd. DR InterPro; IPR001094; Flavdoxin. DR InterPro; IPR008254; Flavodoxin/NO_synth. DR InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase. DR InterPro; IPR023173; NADPH_Cyt_P450_Rdtase_dom3. DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd. DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl. DR Pfam; PF00667; FAD_binding_1; 1. DR Pfam; PF00258; Flavodoxin_1; 1. DR Pfam; PF00175; NAD_binding_1; 1. DR PRINTS; PR00369; FLAVODOXIN. DR PRINTS; PR00371; FPNCR. DR SUPFAM; SSF63380; SSF63380; 1. DR PROSITE; PS51384; FAD_FR; 1. DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1. PE 2: Evidence at transcript level; KW Amino-acid biosynthesis; Complete proteome; Cytoplasm; FAD; KW Flavoprotein; FMN; Methionine biosynthesis; NADP; Oxidoreductase; KW Phosphoprotein; Reference proteome. FT CHAIN 1 696 Methionine synthase reductase. FT /FTId=PRO_0000409308. FT DOMAIN 4 147 Flavodoxin-like. FT DOMAIN 269 531 FAD-binding FR-type. FT NP_BIND 10 14 FMN (By similarity). FT NP_BIND 93 124 FMN (By similarity). FT NP_BIND 449 452 FAD (By similarity). FT NP_BIND 485 488 FAD (By similarity). FT NP_BIND 608 609 NADP (By similarity). FT NP_BIND 622 624 NADP (By similarity). FT REGION 166 245 Hinge (By similarity). FT BINDING 289 289 NADP (By similarity). FT BINDING 657 657 NADP (By similarity). FT BINDING 695 695 FAD (By similarity). FT MOD_RES 171 171 Phosphoserine (By similarity). FT CONFLICT 90 90 R -> Q (in Ref. 1; BAC26039/BAE37348). FT CONFLICT 190 190 V -> F (in Ref. 3; AAH25942). FT CONFLICT 198 198 V -> M (in Ref. 1; BAC26039/BAE37348). FT CONFLICT 482 482 P -> L (in Ref. 1; BAC26039/BAE37348). FT CONFLICT 508 508 A -> V (in Ref. 1; BAC26039/BAE37348). FT CONFLICT 513 513 T -> A (in Ref. 1; BAC26039/BAE37348). FT CONFLICT 645 645 I -> V (in Ref. 1; BAC26039/BAE37348). SQ SEQUENCE 696 AA; 77518 MW; 740E3A5D9440FC81 CRC64; MRRFLLLYAT QRGQAKAIAE EISEQAVSHG FSADLHCISE SEKYDLKTET GPLVMVVSTT GTGDPPDTAR KFVKEIHNKT LPTDYFAHLR YGLLGLGDSE YTYFCNGGKV IDKRLQELGA QRFYDTGHAD DCVGLELVVE PWIDGLWAAL TKHFKSLGGQ ENMSDTLSRA SDAPLSTAMK PELLHIQSQV ELLRLEDVGE RDSELREQNE TNRGQQGRIE DFDSSLVHSV PPLSQSSLSI PAVPPEYLEV HLQESLGQEE NQASVPSGDP SFQVPISKAI RLTTNDAVKS TLLLELDISK IEFSHQPGDS FNVTCPNSDR EVEELLQRLQ LADKRAHRVI LKIKTDTKKK GAALPAHVPE GRSLQFILTW CLEIRAVPKK AFLRALAEHT SSATEKRRLQ ELCSKQGAAD YNRFIRDASV CLLDLLLTFP SCQPPLSLLL EHLPKLQPRP YSCASSSLRH PDKLHFVFNI VEFPPSTTAA SPRKGVCTGW LATLVAPFLQ PNTDVSNADS GDTLAPEIRI SPRATNAFHL PEDPSAPIIM VGPGTGVAPF VGFLQHREKL QEQHPDGKFG AMWLFFGCRH KDRDYLFREE LRHFLKTGVL THLKVSFSRD AAPDGEEAPA KYVQDNLQRH SQQVARTLLQ ENGYIYVCGD AKNMAKDVND TLIGIISNEA GVDKLEAMKT LATLKQEKRY LQDIWS // ID NB5R1_MOUSE Reviewed; 305 AA. AC Q9DB73; Q91W81; DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 19-MAR-2014, entry version 92. DE RecName: Full=NADH-cytochrome b5 reductase 1; DE Short=b5R.1; DE EC=1.6.2.2; DE AltName: Full=NAD(P)H:quinone oxidoreductase type 3 polypeptide A2; GN Name=Cyb5r1; Synonyms=Nqo3a2; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC STRAIN=C57BL/6J; TISSUE=Cerebellum; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC STRAIN=FVB/N; TISSUE=Kidney, and Salivary gland; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: NADH-cytochrome b5 reductases are involved in CC desaturation and elongation of fatty acids, cholesterol CC biosynthesis, drug metabolism, and, in erythrocyte, methemoglobin CC reduction (By similarity). CC -!- CATALYTIC ACTIVITY: NADH + 2 ferricytochrome b5 = NAD(+) + H(+) + CC 2 ferrocytochrome b5. CC -!- COFACTOR: FAD (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein CC (Potential). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9DB73-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9DB73-2; Sequence=VSP_025557, VSP_025558; CC Note=No experimental confirmation available; CC -!- SIMILARITY: Belongs to the flavoprotein pyridine nucleotide CC cytochrome reductase family. CC -!- SIMILARITY: Contains 1 FAD-binding FR-type domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK005159; BAB23850.1; -; mRNA. DR EMBL; AK159663; BAE35270.1; -; mRNA. DR EMBL; AK167178; BAE39313.1; -; mRNA. DR EMBL; BC016266; AAH16266.1; -; mRNA. DR EMBL; BC024618; AAH24618.1; -; mRNA. DR RefSeq; NP_082333.1; NM_028057.2. DR UniGene; Mm.280230; -. DR UniGene; Mm.490981; -. DR ProteinModelPortal; Q9DB73; -. DR SMR; Q9DB73; 36-305. DR PhosphoSite; Q9DB73; -. DR PaxDb; Q9DB73; -. DR PRIDE; Q9DB73; -. DR Ensembl; ENSMUST00000027726; ENSMUSP00000027726; ENSMUSG00000026456. [Q9DB73-1] DR Ensembl; ENSMUST00000154237; ENSMUSP00000133385; ENSMUSG00000026456. [Q9DB73-2] DR GeneID; 72017; -. DR KEGG; mmu:72017; -. DR UCSC; uc007cru.1; mouse. [Q9DB73-1] DR CTD; 51706; -. DR MGI; MGI:1919267; Cyb5r1. DR eggNOG; COG0543; -. DR GeneTree; ENSGT00390000008881; -. DR HOGENOM; HOG000175005; -. DR HOVERGEN; HBG052580; -. DR InParanoid; Q9DB73; -. DR KO; K00326; -. DR OMA; RYPSRFK; -. DR TreeFam; TF314333; -. DR ChiTaRS; CYB5R1; mouse. DR NextBio; 335228; -. DR PRO; PR:Q9DB73; -. DR ArrayExpress; Q9DB73; -. DR Bgee; Q9DB73; -. DR CleanEx; MM_CYB5R1; -. DR Genevestigator; Q9DB73; -. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR GO; GO:0004128; F:cytochrome-b5 reductase activity, acting on NAD(P)H; IEA:UniProtKB-EC. DR GO; GO:0016126; P:sterol biosynthetic process; IEA:UniProtKB-KW. DR InterPro; IPR017927; Fd_Rdtase_FAD-bd. DR InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase. DR InterPro; IPR001834; NADH-Cyt_B5_reductase. DR InterPro; IPR008333; OxRdtase_FAD-bd_dom. DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd. DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl. DR Pfam; PF00970; FAD_binding_6; 1. DR Pfam; PF00175; NAD_binding_1; 1. DR PRINTS; PR00406; CYTB5RDTASE. DR PRINTS; PR00371; FPNCR. DR SUPFAM; SSF63380; SSF63380; 1. DR PROSITE; PS51384; FAD_FR; 1. PE 2: Evidence at transcript level; KW Alternative splicing; Complete proteome; FAD; Flavoprotein; KW Lipid biosynthesis; Lipid metabolism; Membrane; NAD; Oxidoreductase; KW Reference proteome; Steroid biosynthesis; Steroid metabolism; KW Sterol biosynthesis; Sterol metabolism; Transmembrane; KW Transmembrane helix. FT CHAIN 1 305 NADH-cytochrome b5 reductase 1. FT /FTId=PRO_0000287546. FT TRANSMEM 8 28 Helical; (Potential). FT DOMAIN 44 156 FAD-binding FR-type. FT NP_BIND 136 166 FAD (By similarity). FT NP_BIND 175 210 FAD (By similarity). FT VAR_SEQ 159 228 GNFNIQPNKKSPPELRVAKKLGMIAGGTGITPMLQLIRAIL FT KVPEDPTQCFLLFANQTERDIILREDLEE -> ESACVHGC FT TWAKSPEATMLYGKADFTLWRLPEETYASPSFTKDFPLAKD FT QKRKLFSSSHGDDPSTVPCLW (in isoform 2). FT /FTId=VSP_025557. FT VAR_SEQ 229 305 Missing (in isoform 2). FT /FTId=VSP_025558. SQ SEQUENCE 305 AA; 34135 MW; 847B9AAFD99ED035 CRC64; MGIQPSPVLL ASLGVGLLTL LGLALGTYLV RRSRRPQVTL QDPDEKYLLR LLDKTTVSHN TRRFRFALPT AHHILGLPVG KHVYLSARID GSLVIRPYTP VTSDEDQGYV DLVIKVYLKG VHPKFPEGGK MSQYLDSLKI GDMVEFRGPS GLLSYAGKGN FNIQPNKKSP PELRVAKKLG MIAGGTGITP MLQLIRAILK VPEDPTQCFL LFANQTERDI ILREDLEELQ AQYPNRFKLW FTLDSPPEDW TYSKGFVTAD MIQEHLPAPA EDVLLLLCGP PPMVQLACHP NLDKLGYSQK MRFTY // ID NB5R4_MOUSE Reviewed; 528 AA. AC Q3TDX8; E9Q129; Q3TJH3; Q3U012; Q6VXY4; Q6VXY5; Q8BJV8; Q8BTI5; AC Q8R3H8; Q99LY4; Q99P29; DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot. DT 28-JUN-2011, sequence version 3. DT 19-MAR-2014, entry version 86. DE RecName: Full=Cytochrome b5 reductase 4; DE EC=1.6.2.2; DE AltName: Full=Flavohemoprotein b5/b5R; DE Short=b5+b5R; DE AltName: Full=N-terminal cytochrome b5 and cytochrome b5 oxidoreductase domain-containing protein; DE AltName: Full=cb5/cb5R; GN Name=Cyb5r4; Synonyms=Ncb5or; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT RP ASP-THR-LEU-PRO-ARG-ASP-VAL-THR-156 INS. RC STRAIN=C57BL/6J, and NOD; TISSUE=Eye, Liver, Spinal cord, and Spleen; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT RP ASP-THR-LEU-PRO-ARG-ASP-VAL-THR-156 INS. RC STRAIN=Czech II, and FVB/N; TISSUE=Mammary tumor; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] OF 35-528 (ISOFORM 1), AND VARIANT RP ASP-THR-LEU-PRO-ARG-ASP-VAL-THR-156 INS. RX PubMed=10611283; DOI=10.1073/pnas.96.26.14742; RA Zhu H., Qiu H., Yoon H.-W., Huang S., Bunn H.F.; RT "Identification of a cytochrome b-type NAD(P)H oxidoreductase RT ubiquitously expressed in human cells."; RL Proc. Natl. Acad. Sci. U.S.A. 96:14742-14747(1999). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 35-528 (ISOFORMS 1 AND 2), VARIANT RP ASP-THR-LEU-PRO-ARG-ASP-VAL-THR-156 INS, AND TISSUE SPECIFICITY. RC STRAIN=Swiss; TISSUE=Testis; RX PubMed=14962668; DOI=10.1016/j.ygeno.2003.08.020; RA Curry B.J., Roman S.D., Wallace C.A., Scott R., Miriami E., RA Aitken R.J.; RT "Identification and characterization of a novel splice variant of RT mouse and rat cytochrome b5/cytochrome b5 reductase."; RL Genomics 83:425-438(2004). RN [6] RP FUNCTION, AND DISRUPTION PHENOTYPE. RX PubMed=15247412; DOI=10.1073/pnas.0404044101; RA Xie J., Zhu H., Larade K., Ladoux A., Seguritan A., Chu M., Ito S., RA Bronson R.T., Leiter E.H., Zhang C.-Y., Rosen E.D., Bunn H.F.; RT "Absence of a reductase, NCB5OR, causes insulin-deficient diabetes."; RL Proc. Natl. Acad. Sci. U.S.A. 101:10750-10755(2004). RN [7] RP TISSUE SPECIFICITY. RX PubMed=16814408; DOI=10.1016/j.bbaexp.2006.05.002; RA Larade K., Bunn H.F.; RT "Promoter characterization and transcriptional regulation of Ncb5or, a RT novel reductase necessary for pancreatic beta-cell maintenance."; RL Biochim. Biophys. Acta 1759:257-262(2006). CC -!- FUNCTION: NADH-cytochrome b5 reductase involved in endoplasmic CC reticulum stress response pathway. Plays a critical role in CC protecting pancreatic beta-cells against oxidant stress, possibly CC by protecting the cell from excess buildup of reactive oxygen CC species (ROS). CC -!- CATALYTIC ACTIVITY: NADH + 2 ferricytochrome b5 = NAD(+) + H(+) + CC 2 ferrocytochrome b5. CC -!- COFACTOR: FAD (By similarity). CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum. Note=Soluble protein CC (By similarity). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q3TDX8-4; Sequence=Displayed; CC Name=2; Synonyms=cb5/cb5rDelta12; CC IsoId=Q3TDX8-5; Sequence=VSP_041453; CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. Isoform 2 is expressed CC in testis, brain, skeletal muscle and in the male germline. CC -!- DISRUPTION PHENOTYPE: Mice display insulin-deficient diabetes. CC Embryos and fetus develop normally. At 4 weeks of age, mice show CC have normal blood glucose levels but impaired glucose tolerance. CC Isolated islets have markedly impaired glucose- or arginine- CC stimulated insulin secretion. By 7 weeks of age, they develop CC severe hyperglycemia with markedly decreased serum insulin levels CC and nearly normal insulin tolerance. As the animals age, there is CC a progressive loss of beta cells in pancreatic islets, but there CC is no loss of alpha, delta, or PP cells. 4 week-old mice have CC enhanced sensitivity to the diabetogenic agent streptozotocin. CC -!- SIMILARITY: Belongs to the flavoprotein pyridine nucleotide CC cytochrome reductase family. CC -!- SIMILARITY: Contains 1 CS domain. CC -!- SIMILARITY: Contains 1 cytochrome b5 heme-binding domain. CC -!- SIMILARITY: Contains 1 FAD-binding FR-type domain. CC -!- SEQUENCE CAUTION: CC Sequence=AAH25438.1; Type=Erroneous initiation; Note=Translation N-terminally extended; CC Sequence=BAC41118.1; Type=Erroneous initiation; Note=Translation N-terminally extended; CC Sequence=BAE34044.1; Type=Erroneous initiation; Note=Translation N-terminally extended; CC Sequence=BAE42908.1; Type=Erroneous initiation; Note=Translation N-terminally extended; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK078682; BAC37357.1; -; mRNA. DR EMBL; AK090159; BAC41118.1; ALT_INIT; mRNA. DR EMBL; AK157312; BAE34044.1; ALT_INIT; mRNA. DR EMBL; AK167436; BAE39522.1; -; mRNA. DR EMBL; AK169937; BAE41470.1; -; mRNA. DR EMBL; AK172252; BAE42908.1; ALT_INIT; mRNA. DR EMBL; AC156793; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC025438; AAH25438.1; ALT_INIT; mRNA. DR EMBL; BC002170; AAH02170.1; -; mRNA. DR EMBL; AF338818; AAK08116.1; -; mRNA. DR EMBL; AY321368; AAQ83900.1; -; mRNA. DR EMBL; AY321369; AAQ83901.1; -; mRNA. DR RefSeq; NP_077157.2; NM_024195.2. DR RefSeq; XP_006511262.1; XM_006511199.1. DR UniGene; Mm.30166; -. DR ProteinModelPortal; Q3TDX8; -. DR SMR; Q3TDX8; 51-137, 174-263, 282-502. DR IntAct; Q3TDX8; 1. DR PhosphoSite; Q3TDX8; -. DR PRIDE; Q3TDX8; -. DR Ensembl; ENSMUST00000168529; ENSMUSP00000126119; ENSMUSG00000032872. [Q3TDX8-4] DR Ensembl; ENSMUST00000173126; ENSMUSP00000134460; ENSMUSG00000032872. [Q3TDX8-5] DR GeneID; 266690; -. DR KEGG; mmu:266690; -. DR UCSC; uc009qyc.2; mouse. [Q3TDX8-4] DR UCSC; uc009qyf.2; mouse. [Q3TDX8-5] DR CTD; 51167; -. DR MGI; MGI:2386848; Cyb5r4. DR eggNOG; COG0543; -. DR GeneTree; ENSGT00390000008881; -. DR HOVERGEN; HBG108174; -. DR InParanoid; Q3TDX8; -. DR OMA; DSVIVDH; -. DR OrthoDB; EOG718KBZ; -. DR TreeFam; TF313874; -. DR ChiTaRS; CYB5R4; mouse. DR NextBio; 392180; -. DR PRO; PR:Q3TDX8; -. DR ArrayExpress; Q3TDX8; -. DR Bgee; Q3TDX8; -. DR CleanEx; MM_CYB5R4; -. DR Genevestigator; Q3TDX8; -. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl. DR GO; GO:0004128; F:cytochrome-b5 reductase activity, acting on NAD(P)H; IDA:MGI. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:Ensembl. DR GO; GO:0020037; F:heme binding; ISA:MGI. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0016174; F:NAD(P)H oxidase activity; IEA:Ensembl. DR GO; GO:0003958; F:NADPH-hemoprotein reductase activity; IEA:Ensembl. DR GO; GO:0048468; P:cell development; IMP:MGI. DR GO; GO:0006091; P:generation of precursor metabolites and energy; IEA:Ensembl. DR GO; GO:0042593; P:glucose homeostasis; IMP:MGI. DR GO; GO:0042168; P:heme metabolic process; ISA:MGI. DR GO; GO:0030073; P:insulin secretion; IMP:MGI. DR GO; GO:0006739; P:NADP metabolic process; IEA:Ensembl. DR GO; GO:0046677; P:response to antibiotic; IMP:MGI. DR GO; GO:0006801; P:superoxide metabolic process; IEA:Ensembl. DR Gene3D; 3.10.120.10; -; 1. DR InterPro; IPR007052; CS_dom. DR InterPro; IPR001199; Cyt_B5-like_heme/steroid-bd. DR InterPro; IPR018506; Cyt_B5_heme-BS. DR InterPro; IPR017927; Fd_Rdtase_FAD-bd. DR InterPro; IPR008978; HSP20-like_chaperone. DR InterPro; IPR001834; NADH-Cyt_B5_reductase. DR InterPro; IPR008333; OxRdtase_FAD-bd_dom. DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd. DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl. DR Pfam; PF04969; CS; 1. DR Pfam; PF00173; Cyt-b5; 1. DR Pfam; PF00970; FAD_binding_6; 1. DR Pfam; PF00175; NAD_binding_1; 1. DR PRINTS; PR00406; CYTB5RDTASE. DR PRINTS; PR00363; CYTOCHROMEB5. DR SUPFAM; SSF49764; SSF49764; 1. DR SUPFAM; SSF55856; SSF55856; 1. DR SUPFAM; SSF63380; SSF63380; 1. DR PROSITE; PS51203; CS; 1. DR PROSITE; PS00191; CYTOCHROME_B5_1; 1. DR PROSITE; PS50255; CYTOCHROME_B5_2; 1. DR PROSITE; PS51384; FAD_FR; 1. PE 2: Evidence at transcript level; KW Acetylation; Alternative splicing; Complete proteome; KW Endoplasmic reticulum; FAD; Flavoprotein; Heme; Iron; Metal-binding; KW NAD; Oxidoreductase; Polymorphism; Reference proteome. FT CHAIN 1 528 Cytochrome b5 reductase 4. FT /FTId=PRO_0000410469. FT DOMAIN 54 130 Cytochrome b5 heme-binding. FT DOMAIN 172 263 CS. FT DOMAIN 280 392 FAD-binding FR-type. FT NP_BIND 372 387 FAD (By similarity). FT NP_BIND 399 431 FAD (By similarity). FT METAL 89 89 Iron (heme axial ligand) (By similarity). FT METAL 112 112 Iron (heme axial ligand) (By similarity). FT MOD_RES 1 1 N-acetylmethionine (By similarity). FT VAR_SEQ 326 376 Missing (in isoform 2). FT /FTId=VSP_041453. FT VARIANT 156 156 S -> SDTLPRDVT. FT CONFLICT 171 171 D -> G (in Ref. 1; BAE34044/BAE41470/ FT BAE42908, 4; AAK08116 and 5; AAQ83900/ FT AAQ83901). FT CONFLICT 216 216 V -> I (in Ref. 3; AAH25438). FT CONFLICT 300 300 F -> L (in Ref. 1; BAE34044/BAE41470/ FT BAE42908, 3; AAH02170, 4; AAK08116 and 5; FT AAQ83900/AAQ83901). FT CONFLICT 336 336 V -> L (in Ref. 1; BAE34044). FT CONFLICT 339 339 S -> P (in Ref. 1; BAE41470). FT CONFLICT 356 356 C -> Y (in Ref. 1; BAE34044/BAE41470/ FT BAE42908, 3; AAH02170/AAH25438, 4; FT AAK08116 and 5; AAQ83900). FT CONFLICT 388 388 D -> N (in Ref. 1; BAE34044/BAE41470/ FT BAE42908, 3; AAH02170/AAH25438, 4; FT AAK08116 and 5; AAQ83900/AAQ83901). FT CONFLICT 393 393 K -> T (in Ref. 3; AAH25438). FT CONFLICT 438 438 E -> D (in Ref. 1; BAC37357). FT CONFLICT 504 504 P -> Q (in Ref. 1; BAE39522). SQ SEQUENCE 528 AA; 59716 MW; 8CF34CE865980A66 CRC64; MLNVPSQAFP APGSQQRVSS QGRSKVPLKQ GRSLMDWIRL TKSGKDLTGL KGGLIEVTEE ELKKHNKKED CWICIRGFVY NVSPYMEYHP GGEDELMRAA GADGTDLFNE VHRWVNYESM LKECLVGRMA VKPAVPKDCH EGKRVLNGML PKSQMSDTLP RDVTDTLPRE DLSSPSYDWF QTESSVTIVV YTKQKNISLD SVIVDLQDDS LRAEAVIKDH SYLVHVGLSH EVQENFSVRV IENVGKIEIV LQKKESVSWQ CLGDHLEKHD SFIPKKDTGL YYRRCQLISK EDVTHDTRLF CLMLPPSTHL QVPVGQHVYL KLSVTGAEIV KPYTPVSDSL LSDFKEPVLS PNKYICFLIK IYPAGLFTPE LDRLQIGDFI SVSGPEGDFK VSKLQEVEDL FLLAAGTGFT PMVTVLNYAL SHMSSLRKVK LMFFNKTEDD IIWRCQLEKL ALREKRFDVE FVLSAPSPEW NGKQGHISRA LLSEFLQRSS ENSRAFLCIC GPTPFTDEGI RLLHDLNFSD DEIHGFTA // ID NB5R2_MOUSE Reviewed; 276 AA. AC Q3KNK3; Q3UGG1; Q8BUG7; DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot. DT 15-MAY-2007, sequence version 2. DT 19-MAR-2014, entry version 64. DE RecName: Full=NADH-cytochrome b5 reductase 2; DE Short=b5R.2; DE EC=1.6.2.2; GN Name=Cyb5r2; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC STRAIN=C57BL/6J; TISSUE=Kidney; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: NADH-cytochrome b5 reductases are involved in CC desaturation and elongation of fatty acids, cholesterol CC biosynthesis, drug metabolism, and, in erythrocyte, methemoglobin CC reduction. Responsible for NADH-dependent lucigenin CC chemiluminescence in spermatozoa by reducing both lucigenin and 2- CC [4-iodophenyl]-3-[4-nitrophenyl]-5-[2,4-disulfophenyl]-2H CC tetrazolium monosodium salt (WST-1) (By similarity). CC -!- CATALYTIC ACTIVITY: NADH + 2 ferricytochrome b5 = NAD(+) + H(+) + CC 2 ferrocytochrome b5. CC -!- COFACTOR: FAD (By similarity). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q3KNK3-1; Sequence=Displayed; CC Name=2; CC IsoId=Q3KNK3-2; Sequence=VSP_025560; CC Note=No experimental confirmation available; CC -!- SIMILARITY: Belongs to the flavoprotein pyridine nucleotide CC cytochrome reductase family. CC -!- SIMILARITY: Contains 1 FAD-binding FR-type domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK085272; BAC39408.1; -; mRNA. DR EMBL; AK147952; BAE28247.1; -; mRNA. DR EMBL; BC107238; AAI07239.1; -; mRNA. DR EMBL; BC107239; AAI07240.1; -; mRNA. DR RefSeq; NP_001192156.1; NM_001205227.1. DR RefSeq; NP_796190.1; NM_177216.4. DR RefSeq; XP_006508012.1; XM_006507949.1. DR RefSeq; XP_006508013.1; XM_006507950.1. DR UniGene; Mm.132828; -. DR ProteinModelPortal; Q3KNK3; -. DR SMR; Q3KNK3; 9-276. DR PhosphoSite; Q3KNK3; -. DR PaxDb; Q3KNK3; -. DR PRIDE; Q3KNK3; -. DR Ensembl; ENSMUST00000052438; ENSMUSP00000050061; ENSMUSG00000048065. [Q3KNK3-2] DR GeneID; 320635; -. DR KEGG; mmu:320635; -. DR UCSC; uc009jbi.2; mouse. [Q3KNK3-1] DR UCSC; uc012frx.2; mouse. [Q3KNK3-2] DR CTD; 51700; -. DR MGI; MGI:2444415; Cyb5r2. DR eggNOG; COG0543; -. DR GeneTree; ENSGT00390000008881; -. DR HOGENOM; HOG000175005; -. DR HOVERGEN; HBG052580; -. DR InParanoid; Q3KNK3; -. DR KO; K00326; -. DR OMA; VHHLGMI; -. DR OrthoDB; EOG7CZK69; -. DR TreeFam; TF314333; -. DR NextBio; 397113; -. DR PRO; PR:Q3KNK3; -. DR Bgee; Q3KNK3; -. DR CleanEx; MM_CYB5R2; -. DR Genevestigator; Q3KNK3; -. DR GO; GO:0016020; C:membrane; IEA:Ensembl. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR GO; GO:0004128; F:cytochrome-b5 reductase activity, acting on NAD(P)H; IEA:UniProtKB-EC. DR GO; GO:0016126; P:sterol biosynthetic process; IEA:UniProtKB-KW. DR InterPro; IPR017927; Fd_Rdtase_FAD-bd. DR InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase. DR InterPro; IPR001834; NADH-Cyt_B5_reductase. DR InterPro; IPR008333; OxRdtase_FAD-bd_dom. DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd. DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl. DR Pfam; PF00970; FAD_binding_6; 1. DR Pfam; PF00175; NAD_binding_1; 1. DR PRINTS; PR00406; CYTB5RDTASE. DR PRINTS; PR00371; FPNCR. DR SUPFAM; SSF63380; SSF63380; 1. DR PROSITE; PS51384; FAD_FR; 1. PE 2: Evidence at transcript level; KW Alternative splicing; Complete proteome; FAD; Flavoprotein; KW Lipid biosynthesis; Lipid metabolism; NAD; Oxidoreductase; KW Reference proteome; Steroid biosynthesis; Steroid metabolism; KW Sterol biosynthesis; Sterol metabolism. FT CHAIN 1 276 NADH-cytochrome b5 reductase 2. FT /FTId=PRO_0000287549. FT DOMAIN 15 127 FAD-binding FR-type. FT NP_BIND 107 137 FAD (By similarity). FT NP_BIND 146 181 FAD (By similarity). FT VAR_SEQ 130 130 G -> GCQTRAAEVKNIFIFLG (in isoform 2). FT /FTId=VSP_025560. FT CONFLICT 132 132 L -> I (in Ref. 2; AAI07239). FT CONFLICT 267 267 S -> G (in Ref. 2; AAI07239). FT CONFLICT 275 275 I -> T (in Ref. 2; AAI07239). SQ SEQUENCE 276 AA; 31360 MW; 56596AF2F33F33E3 CRC64; MSVKKKDLIT LQDPEAKYPL PLIEKEQISH NTRRFRFGLP SPDHVLGLPV GNYVHLLAQI NNELVIRAYT PVSSDDDQGF VDLIIKIYFK NVHPKYPEGG KMTQYLENMK IGDTILFRGP TGRLFYNEPG TLLIKANKTS EPEKKLVHHL GMIAGGTGIT PMLQLIRHIT KDTSDETRMS LLFANQTEED ILLRKELEEV ATTHHKQFNL WYTLDRPPSD WKYSSGFVSA DMIKEHLPPP GEDTLILVCG PPPLIQAAAH PSLEQLSYTK DMIFIY // ID NB5R5_MOUSE Reviewed; 316 AA. AC B1AS42; B1AS41; Q571N5; Q80W48; Q99KB7; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 08-APR-2008, sequence version 1. DT 19-MAR-2014, entry version 48. DE RecName: Full=NADH-cytochrome b5 reductase-like; DE EC=1.6.2.2; GN Name=Cyb5rl; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4). RC STRAIN=ICR; TISSUE=Embryonic tail; RX PubMed=15449545; DOI=10.1093/dnares/11.2.127; RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., RA Saga Y., Kitamura H., Nakagawa T., Nagase T., Ohara O., Koga H.; RT "Prediction of the coding sequences of mouse homologues of FLJ genes: RT the complete nucleotide sequences of 110 mouse FLJ-homologous cDNAs RT identified by screening of terminal sequences of cDNA clones randomly RT sampled from size-fractionated libraries."; RL DNA Res. 11:127-135(2004). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3). RC STRAIN=FVB/N; TISSUE=Liver, and Mammary tumor; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: NADH-cytochrome b5 reductases are involved in CC desaturation and elongation of fatty acids, cholesterol CC biosynthesis, drug metabolism, and, in erythrocyte, methemoglobin CC reduction (By similarity). CC -!- CATALYTIC ACTIVITY: NADH + 2 ferricytochrome b5 = NAD(+) + H(+) + CC 2 ferrocytochrome b5. CC -!- COFACTOR: FAD (By similarity). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; CC IsoId=B1AS42-1; Sequence=Displayed; CC Name=2; CC IsoId=B1AS42-2; Sequence=VSP_033851; CC Note=No experimental confirmation available; CC Name=3; CC IsoId=B1AS42-3; Sequence=VSP_033849, VSP_033850; CC Note=No experimental confirmation available; CC Name=4; CC IsoId=B1AS42-4; Sequence=VSP_033848, VSP_033852, VSP_033853; CC Note=No experimental confirmation available; CC -!- SIMILARITY: Belongs to the flavoprotein pyridine nucleotide CC cytochrome reductase family. CC -!- SIMILARITY: Contains 1 FAD-binding FR-type domain. CC -!- SIMILARITY: Contains 1 Oxidoreductase-like domain. CC -!- SEQUENCE CAUTION: CC Sequence=AAH04750.1; Type=Erroneous initiation; CC Sequence=BAD90340.1; Type=Erroneous initiation; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK220154; BAD90340.1; ALT_INIT; mRNA. DR EMBL; AL607132; CAM46300.2; -; Genomic_DNA. DR EMBL; AL607132; CAM46301.1; -; Genomic_DNA. DR EMBL; BC004750; AAH04750.1; ALT_INIT; mRNA. DR EMBL; BC043687; AAH43687.1; -; mRNA. DR RefSeq; NP_780680.1; NM_175471.2. DR RefSeq; XP_006503024.1; XM_006502961.1. DR RefSeq; XP_006503029.1; XM_006502966.1. DR UniGene; Mm.44608; -. DR ProteinModelPortal; B1AS42; -. DR SMR; B1AS42; 74-293. DR PaxDb; B1AS42; -. DR PRIDE; B1AS42; -. DR Ensembl; ENSMUST00000030364; ENSMUSP00000030364; ENSMUSG00000028621. [B1AS42-2] DR Ensembl; ENSMUST00000106756; ENSMUSP00000102367; ENSMUSG00000028621. [B1AS42-3] DR Ensembl; ENSMUST00000106758; ENSMUSP00000102369; ENSMUSG00000028621. [B1AS42-1] DR GeneID; 230582; -. DR KEGG; mmu:230582; -. DR UCSC; uc008tzb.1; mouse. [B1AS42-3] DR UCSC; uc008tzc.1; mouse. [B1AS42-2] DR UCSC; uc008tzd.1; mouse. [B1AS42-1] DR CTD; 606495; -. DR MGI; MGI:1919657; Cyb5rl. DR eggNOG; COG0543; -. DR GeneTree; ENSGT00540000072126; -. DR HOGENOM; HOG000008210; -. DR HOVERGEN; HBG108175; -. DR InParanoid; B1AS42; -. DR OMA; TKDIARC; -. DR OrthoDB; EOG7HXCSB; -. DR TreeFam; TF336549; -. DR NextBio; 379943; -. DR PRO; PR:B1AS42; -. DR ArrayExpress; B1AS42; -. DR Bgee; B1AS42; -. DR Genevestigator; B1AS42; -. DR GO; GO:0004128; F:cytochrome-b5 reductase activity, acting on NAD(P)H; IEA:UniProtKB-EC. DR InterPro; IPR017927; Fd_Rdtase_FAD-bd. DR InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase. DR InterPro; IPR001834; NADH-Cyt_B5_reductase. DR InterPro; IPR019180; Oxidoreductase-like_N. DR InterPro; IPR008333; OxRdtase_FAD-bd_dom. DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd. DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl. DR Pfam; PF00970; FAD_binding_6; 1. DR Pfam; PF00175; NAD_binding_1; 1. DR Pfam; PF09791; Oxidored-like; 1. DR PRINTS; PR00406; CYTB5RDTASE. DR PRINTS; PR00371; FPNCR. DR SUPFAM; SSF63380; SSF63380; 1. DR PROSITE; PS51384; FAD_FR; 1. PE 2: Evidence at transcript level; KW Alternative splicing; Complete proteome; FAD; Flavoprotein; NAD; KW Oxidoreductase; Reference proteome. FT CHAIN 1 316 NADH-cytochrome b5 reductase-like. FT /FTId=PRO_0000337042. FT DOMAIN 17 53 Oxidoreductase-like. FT DOMAIN 76 178 FAD-binding FR-type. FT NP_BIND 158 173 FAD (By similarity). FT NP_BIND 183 215 FAD (By similarity). FT VAR_SEQ 1 85 Missing (in isoform 4). FT /FTId=VSP_033848. FT VAR_SEQ 1 60 Missing (in isoform 3). FT /FTId=VSP_033849. FT VAR_SEQ 61 67 KQPPESQ -> MNNKDLE (in isoform 3). FT /FTId=VSP_033850. FT VAR_SEQ 146 180 Missing (in isoform 2). FT /FTId=VSP_033851. FT VAR_SEQ 250 283 EVSPEQLPWSYRDKTHFGRLGQELVAELVACCRR -> ASP FT SPSYRGGSRLTEVLDQGGARTGPVCLTLLSL (in FT isoform 4). FT /FTId=VSP_033852. FT VAR_SEQ 284 316 Missing (in isoform 4). FT /FTId=VSP_033853. SQ SEQUENCE 316 AA; 35884 MW; A5D49CF710DD7AFA CRC64; MAETEEEEDS EAWLRLKPVE PLPSQCCGSG CSPCVFDLYY RDLERWETAR ARNDRSLLSG KQPPESQSCS AKLSPETFLA FHISTMEKVT KDTYLVRFTL PGNSRLGLRP GQHLILRGVV DGLEIQRAYT PISPVTAEGY FDVLIKCYRT GLMSQYVESW RTGDTAFWRG PFGSFLYEPK KYGELLMLAA GTGLAPMVPI LQSITDDEDD ETFVTLVGCF KTFEGIYLKT FFQEQARFWN VQTFFVLSQE VSPEQLPWSY RDKTHFGRLG QELVAELVAC CRRKPFTLVC GSPAFNEDMA RCLLSAGLTE DSYFLF // ID NB5R3_MOUSE Reviewed; 301 AA. AC Q9DCN2; DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 19-MAR-2014, entry version 109. DE RecName: Full=NADH-cytochrome b5 reductase 3; DE Short=B5R; DE Short=Cytochrome b5 reductase; DE EC=1.6.2.2; DE AltName: Full=Diaphorase-1; DE Contains: DE RecName: Full=NADH-cytochrome b5 reductase 3 membrane-bound form; DE Contains: DE RecName: Full=NADH-cytochrome b5 reductase 3 soluble form; GN Name=Cyb5r3; Synonyms=Dia1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=ILS, and ISS; RX PubMed=11471062; DOI=10.1007/s00335-001-1001-x; RA Ehringer M.A., Thompson J., Conroy O., Xu Y., Yang F., Canniff J., RA Beeson M., Gordon L., Bennett B., Johnson T.E., Sikela J.M.; RT "High-throughput sequence identification of gene coding variants RT within alcohol-related QTLs."; RL Mamm. Genome 12:657-663(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Kidney; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=129, C57BL/6, and FVB/N; RC TISSUE=Brain, Kidney, and Mammary tumor; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP PROTEIN SEQUENCE OF 127-135, AND MASS SPECTROMETRY. RC STRAIN=C57BL/6; TISSUE=Brain; RA Lubec G., Kang S.U.; RL Submitted (APR-2007) to UniProtKB. RN [5] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-120, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=16916647; DOI=10.1016/j.molcel.2006.06.026; RA Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T., RA Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.; RT "Substrate and functional diversity of lysine acetylation revealed by RT a proteomics survey."; RL Mol. Cell 23:607-618(2006). RN [6] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-42 AND LYS-50, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic fibroblast; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., RA Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). RN [7] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-42, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23576753; DOI=10.1073/pnas.1302961110; RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., RA Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.; RT "Label-free quantitative proteomics of the lysine acetylome in RT mitochondria identifies substrates of SIRT3 in metabolic pathways."; RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013). CC -!- FUNCTION: Desaturation and elongation of fatty acids, cholesterol CC biosynthesis, drug metabolism, and, in erythrocyte, methemoglobin CC reduction (By similarity). CC -!- CATALYTIC ACTIVITY: NADH + 2 ferricytochrome b5 = NAD(+) + H(+) + CC 2 ferrocytochrome b5. CC -!- COFACTOR: FAD (By similarity). CC -!- SUBUNIT: Component of a complex composed of cytochrome b5, NADH- CC cytochrome b5 reductase (CYB5R3) and MOSC2 (By similarity). CC -!- SUBCELLULAR LOCATION: Isoform 1: Endoplasmic reticulum membrane; CC Lipid-anchor; Cytoplasmic side (By similarity). Mitochondrion CC outer membrane; Lipid-anchor; Cytoplasmic side (By similarity). CC -!- SUBCELLULAR LOCATION: Isoform 2: Cytoplasm, cytosol (By CC similarity). Note=Produces the soluble form found in erythrocytes CC (By similarity). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative promoter usage; Named isoforms=2; CC Name=1; Synonyms=M; CC IsoId=Q9DCN2-1; Sequence=Displayed; CC Name=2; Synonyms=S; CC IsoId=Q9DCN2-2; Sequence=VSP_012952; CC -!- SIMILARITY: Belongs to the flavoprotein pyridine nucleotide CC cytochrome reductase family. CC -!- SIMILARITY: Contains 1 FAD-binding FR-type domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF332059; AAK56088.1; -; mRNA. DR EMBL; AF332060; AAK56089.1; -; mRNA. DR EMBL; AK002640; BAB22252.1; -; mRNA. DR EMBL; BC004760; AAH04760.1; -; mRNA. DR EMBL; BC032013; AAH32013.1; -; mRNA. DR EMBL; BC043074; AAH43074.1; -; mRNA. DR RefSeq; NP_084063.1; NM_029787.2. DR RefSeq; XP_006520346.1; XM_006520283.1. DR UniGene; Mm.22560; -. DR ProteinModelPortal; Q9DCN2; -. DR SMR; Q9DCN2; 34-301. DR DIP; DIP-57517N; -. DR IntAct; Q9DCN2; 6. DR MINT; MINT-1867235; -. DR PhosphoSite; Q9DCN2; -. DR PaxDb; Q9DCN2; -. DR PRIDE; Q9DCN2; -. DR Ensembl; ENSMUST00000018186; ENSMUSP00000018186; ENSMUSG00000018042. [Q9DCN2-1] DR GeneID; 109754; -. DR KEGG; mmu:109754; -. DR UCSC; uc007xac.2; mouse. [Q9DCN2-1] DR CTD; 1727; -. DR MGI; MGI:94893; Cyb5r3. DR eggNOG; COG0543; -. DR GeneTree; ENSGT00390000008881; -. DR HOGENOM; HOG000175005; -. DR HOVERGEN; HBG052580; -. DR KO; K00326; -. DR OMA; FKVWYTV; -. DR OrthoDB; EOG7CZK69; -. DR TreeFam; TF314333; -. DR BioCyc; MetaCyc:MONOMER-14527; -. DR ChiTaRS; CYB5R3; mouse. DR NextBio; 362693; -. DR PRO; PR:Q9DCN2; -. DR ArrayExpress; Q9DCN2; -. DR Bgee; Q9DCN2; -. DR CleanEx; MM_CYB5R3; -. DR Genevestigator; Q9DCN2; -. DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005811; C:lipid particle; IEA:Ensembl. DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:MGI. DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell. DR GO; GO:0043531; F:ADP binding; IEA:Ensembl. DR GO; GO:0016208; F:AMP binding; IEA:Ensembl. DR GO; GO:0004128; F:cytochrome-b5 reductase activity, acting on NAD(P)H; IEA:UniProtKB-EC. DR GO; GO:0071949; F:FAD binding; IEA:Ensembl. DR GO; GO:0051287; F:NAD binding; IEA:Ensembl. DR GO; GO:0006695; P:cholesterol biosynthetic process; IEA:UniProtKB-KW. DR InterPro; IPR017927; Fd_Rdtase_FAD-bd. DR InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase. DR InterPro; IPR001834; NADH-Cyt_B5_reductase. DR InterPro; IPR008333; OxRdtase_FAD-bd_dom. DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd. DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl. DR Pfam; PF00970; FAD_binding_6; 1. DR Pfam; PF00175; NAD_binding_1; 1. DR PRINTS; PR00406; CYTB5RDTASE. DR PRINTS; PR00371; FPNCR. DR SUPFAM; SSF63380; SSF63380; 1. DR PROSITE; PS51384; FAD_FR; 1. PE 1: Evidence at protein level; KW Acetylation; Alternative promoter usage; Cholesterol biosynthesis; KW Cholesterol metabolism; Complete proteome; Cytoplasm; KW Direct protein sequencing; Endoplasmic reticulum; FAD; Flavoprotein; KW Lipid biosynthesis; Lipid metabolism; Lipoprotein; Membrane; KW Mitochondrion; Mitochondrion outer membrane; Myristate; NAD; KW Oxidoreductase; Phosphoprotein; Reference proteome; KW Steroid biosynthesis; Steroid metabolism; Sterol biosynthesis; KW Sterol metabolism. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 301 NADH-cytochrome b5 reductase 3 membrane- FT bound form. FT /FTId=PRO_0000019398. FT CHAIN 27 301 NADH-cytochrome b5 reductase 3 soluble FT form. FT /FTId=PRO_0000019400. FT DOMAIN 40 152 FAD-binding FR-type. FT NP_BIND 132 147 FAD (By similarity). FT NP_BIND 171 206 FAD (By similarity). FT MOD_RES 42 42 N6-acetyllysine. FT MOD_RES 43 43 Phosphotyrosine (By similarity). FT MOD_RES 50 50 N6-acetyllysine. FT MOD_RES 120 120 N6-acetyllysine. FT LIPID 2 2 N-myristoyl glycine (By similarity). FT VAR_SEQ 2 23 Missing (in isoform 2). FT /FTId=VSP_012952. SQ SEQUENCE 301 AA; 34128 MW; 984D5B73430F725D CRC64; MGAQLSTLSH VVLSPVWFIY SLFMKLFQRS TPAITLENPD IKYPLRLIDK EVISPDTRRF RFALPSPQHI LGLPIGQHIY LSTRIDGNLV IRPYTPVSSD DDKGFVDLVV KVYFKDTHPK FPAGGKMSQY LENMKIGDTI EFRGPNGLLV YQGKGKFAIR ADKKSNPVVR TVKSVGMIAG GTGITPMLQV IRAVLKDPND HTVCYLLFAN QSEKDILLRP ELEELRNEHS ARFKLWYTVD KAPDAWDYSQ GFVNEEMIRD HLPTPGEEPL ILMCGPPPMI QFACLPNLER VGHPKERCFT F // ID NCPR_MOUSE Reviewed; 678 AA. AC P37040; DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 19-MAR-2014, entry version 122. DE RecName: Full=NADPH--cytochrome P450 reductase; DE Short=CPR; DE Short=P450R; DE EC=1.6.2.4; GN Name=Por; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=ddY; RX PubMed=8011664; DOI=10.1016/0005-2728(94)90146-5; RA Ohgiya S., Ishizaki K., Kamataki T., Shinriki N.; RT "Mouse NADPH-cytochrome P-450 oxidoreductase: molecular cloning and RT functional expression in yeast."; RL Biochim. Biophys. Acta 1186:137-141(1994). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Mammary gland; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: This enzyme is required for electron transfer from NADP CC to cytochrome P450 in microsomes. It can also provide electron CC transfer to heme oxygenase and cytochrome B5. CC -!- CATALYTIC ACTIVITY: NADPH + n oxidized hemoprotein = NADP(+) + n CC reduced hemoprotein. CC -!- COFACTOR: FAD. CC -!- COFACTOR: FMN. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral CC membrane protein. Note=Anchored to the ER membrane by its N- CC terminal hydrophobic region. CC -!- SIMILARITY: In the C-terminal section; belongs to the flavoprotein CC pyridine nucleotide cytochrome reductase family. CC -!- SIMILARITY: Contains 1 FAD-binding FR-type domain. CC -!- SIMILARITY: Contains 1 flavodoxin-like domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; D17571; BAA04496.1; -; mRNA. DR EMBL; BC031463; AAH31463.1; -; mRNA. DR RefSeq; NP_032924.1; NM_008898.1. DR RefSeq; XP_006504461.1; XM_006504398.1. DR RefSeq; XP_006504462.1; XM_006504399.1. DR UniGene; Mm.3863; -. DR ProteinModelPortal; P37040; -. DR SMR; P37040; 63-678. DR BioGrid; 202299; 1. DR IntAct; P37040; 6. DR MINT; MINT-1863828; -. DR STRING; 10090.ENSMUSP00000005651; -. DR PhosphoSite; P37040; -. DR SWISS-2DPAGE; P37040; -. DR PaxDb; P37040; -. DR PRIDE; P37040; -. DR Ensembl; ENSMUST00000005651; ENSMUSP00000005651; ENSMUSG00000005514. DR GeneID; 18984; -. DR KEGG; mmu:18984; -. DR UCSC; uc008zyt.1; mouse. DR CTD; 5447; -. DR MGI; MGI:97744; Por. DR eggNOG; COG0369; -. DR GeneTree; ENSGT00740000115613; -. DR HOGENOM; HOG000282027; -. DR HOVERGEN; HBG000432; -. DR InParanoid; P37040; -. DR KO; K00327; -. DR OMA; YLPHITD; -. DR OrthoDB; EOG7HQN7J; -. DR TreeFam; TF105719; -. DR ChiTaRS; POR; mouse. DR NextBio; 295354; -. DR PRO; PR:P37040; -. DR ArrayExpress; P37040; -. DR Bgee; P37040; -. DR CleanEx; MM_POR; -. DR Genevestigator; P37040; -. DR GO; GO:0005829; C:cytosol; IBA:RefGenome. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl. DR GO; GO:0004128; F:cytochrome-b5 reductase activity, acting on NAD(P)H; IEA:Ensembl. DR GO; GO:0009055; F:electron carrier activity; IEA:Ensembl. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:Ensembl. DR GO; GO:0010181; F:FMN binding; IEA:Ensembl. DR GO; GO:0016787; F:hydrolase activity; IEA:Ensembl. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0047726; F:iron-cytochrome-c reductase activity; IEA:Ensembl. DR GO; GO:0050661; F:NADP binding; IEA:Ensembl. DR GO; GO:0003958; F:NADPH-hemoprotein reductase activity; IBA:RefGenome. DR GO; GO:0008941; F:nitric oxide dioxygenase activity; IEA:Ensembl. DR GO; GO:0016709; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen; IBA:RefGenome. DR GO; GO:0009437; P:carnitine metabolic process; IEA:Ensembl. DR GO; GO:0090346; P:cellular organofluorine metabolic process; IEA:Ensembl. DR GO; GO:0071372; P:cellular response to follicle-stimulating hormone stimulus; IEA:Ensembl. DR GO; GO:0071375; P:cellular response to peptide hormone stimulus; IEA:Ensembl. DR GO; GO:0070988; P:demethylation; IEA:Ensembl. DR GO; GO:0019395; P:fatty acid oxidation; IEA:Ensembl. DR GO; GO:0009812; P:flavonoid metabolic process; IEA:Ensembl. DR GO; GO:0018393; P:internal peptidyl-lysine acetylation; IEA:Ensembl. DR GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl. DR GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IEA:Ensembl. DR GO; GO:0060192; P:negative regulation of lipase activity; IEA:Ensembl. DR GO; GO:0043602; P:nitrate catabolic process; IEA:Ensembl. DR GO; GO:0046210; P:nitric oxide catabolic process; IEA:Ensembl. DR GO; GO:0045542; P:positive regulation of cholesterol biosynthetic process; IEA:Ensembl. DR GO; GO:0032332; P:positive regulation of chondrocyte differentiation; IEA:Ensembl. DR GO; GO:0032770; P:positive regulation of monooxygenase activity; IEA:Ensembl. DR GO; GO:0045880; P:positive regulation of smoothened signaling pathway; IEA:Ensembl. DR GO; GO:0090031; P:positive regulation of steroid hormone biosynthetic process; IEA:Ensembl. DR GO; GO:0003420; P:regulation of growth plate cartilage chondrocyte proliferation; IEA:Ensembl. DR GO; GO:0042493; P:response to drug; IEA:Ensembl. DR GO; GO:0007584; P:response to nutrient; IEA:Ensembl. DR Gene3D; 1.20.990.10; -; 1. DR InterPro; IPR003097; FAD-binding_1. DR InterPro; IPR017927; Fd_Rdtase_FAD-bd. DR InterPro; IPR001094; Flavdoxin. DR InterPro; IPR008254; Flavodoxin/NO_synth. DR InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase. DR InterPro; IPR023173; NADPH_Cyt_P450_Rdtase_dom3. DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd. DR InterPro; IPR023208; P450R. DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl. DR Pfam; PF00667; FAD_binding_1; 1. DR Pfam; PF00258; Flavodoxin_1; 1. DR Pfam; PF00175; NAD_binding_1; 1. DR PIRSF; PIRSF000208; P450R; 1. DR PRINTS; PR00369; FLAVODOXIN. DR PRINTS; PR00371; FPNCR. DR SUPFAM; SSF63380; SSF63380; 1. DR PROSITE; PS51384; FAD_FR; 1. DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1. PE 1: Evidence at protein level; KW Acetylation; Complete proteome; Endoplasmic reticulum; FAD; KW Flavoprotein; FMN; Membrane; NADP; Oxidoreductase; Reference proteome. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 678 NADPH--cytochrome P450 reductase. FT /FTId=PRO_0000167597. FT DOMAIN 80 224 Flavodoxin-like. FT DOMAIN 279 521 FAD-binding FR-type. FT NP_BIND 170 201 FMN (By similarity). FT NP_BIND 314 325 FAD (By similarity). FT NP_BIND 451 461 FAD (By similarity). FT NP_BIND 530 548 NADP (By similarity). FT NP_BIND 625 641 NADP (By similarity). FT MOD_RES 2 2 N-acetylglycine (By similarity). SQ SEQUENCE 678 AA; 77044 MW; 060282A7A55483AF CRC64; MGDSHEDTSA TVPEAVAEEV SLFSTTDIVL FSLIVGVLTY WFIFKKKKEE IPEFSKIQTT APPVKESSFV EKMKKTGRNI IVFYGSQTGT AEEFANRLSK DAHRYGMRGM SADPEEYDLA DLSSLPEIDK SLVVFCMATY GEGDPTDNAQ DFYDWLQETD VDLTGVKFAV FGLGNKTYEH FNAMGKYVDQ RLEQLGAQRI FELGLGDDDG NLEEDFITWR EQFWPAVCEF FGVEATGEES SIRQYELVVH EDMDTAKVYT GEMGRLKSYE NQKPPFDAKN PFLAAVTTNR KLNQGTERHL MHLELDISDS KIRYESGDHV AVYPANDSTL VNQIGEILGA DLDVIMSLNN LDEESNKKHP FPCPTTYRTA LTYYLDITNP PRTNVLYELA QYASEPSEQE HLHKMASSSG EGKELYLSWV VEARRHILAI LQDYPSLRPP IDHLCELLPR LQARYYSIAS SSKVHPNSVH ICAVAVEYEA KSGRVNKGVA TSWLRTKEPA GENGRRALVP MFVRKSQFRL PFKPTTPVIM VGPGTGVAPF MGFIQERAWL REQGKEVGET LLYYGCRRSD EDYLYREELA RFHKDGALTQ LNVAFSREQA HKVYVQHLLK RDKEHLWKLI HEGGAHIYVC GDARNMAKDV QNTFYDIVAE FGPMEHTQAV DYVKKLMTKG RYSLDVWS // ID NDOR1_MOUSE Reviewed; 598 AA. AC A2AI05; Q3TQZ6; Q80WC5; DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 20-FEB-2007, sequence version 1. DT 19-MAR-2014, entry version 60. DE RecName: Full=NADPH-dependent diflavin oxidoreductase 1; DE EC=1.6.-.-; DE AltName: Full=NADPH-dependent FMN and FAD-containing oxidoreductase; GN Name=Ndor1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3). RC STRAIN=C57BL/6J, and NOD; TISSUE=Cerebellum, and Dendritic cell; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Embryo; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: Component of the cytosolic iron-sulfur (Fe-S) protein CC assembly (CIA) machinery. Required for the maturation of CC extramitochondrial Fe-S proteins. Part of an electron transfer CC chain functioning in an early step of cytosolic Fe-S biogenesis. CC Transfers electrons from NADPH to the Fe/S cluster of CIAPIN1 (By CC similarity). CC -!- COFACTOR: FMN (By similarity). CC -!- COFACTOR: FAD (By similarity). CC -!- SUBUNIT: Interacts with CIAPIN1 (By similarity). Interacts with CC DCPS (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region (By CC similarity). Note=Concentrated in perinuclear structure (By CC similarity). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=A2AI05-1; Sequence=Displayed; CC Note=Gene prediction based on EST data; CC Name=2; CC IsoId=A2AI05-2; Sequence=VSP_031489; CC Name=3; CC IsoId=A2AI05-3; Sequence=VSP_031488, VSP_031490, VSP_031491; CC -!- SIMILARITY: Belongs to the NADPH-dependent diflavin oxidoreductase CC NDOR1 family. CC -!- SIMILARITY: In the C-terminal section; belongs to the flavoprotein CC pyridine nucleotide cytochrome reductase family. CC -!- SIMILARITY: Contains 1 FAD-binding FR-type domain. CC -!- SIMILARITY: Contains 1 flavodoxin-like domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK163207; BAE37235.1; -; mRNA. DR EMBL; AK169885; BAE41435.1; -; mRNA. DR EMBL; AL732309; CAM14675.1; -; Genomic_DNA. DR EMBL; BC049789; AAH49789.1; -; mRNA. DR RefSeq; NP_001075945.1; NM_001082476.2. DR RefSeq; NP_001239470.1; NM_001252541.1. DR UniGene; Mm.40020; -. DR ProteinModelPortal; A2AI05; -. DR SMR; A2AI05; 4-598. DR PhosphoSite; A2AI05; -. DR PaxDb; A2AI05; -. DR PRIDE; A2AI05; -. DR Ensembl; ENSMUST00000100329; ENSMUSP00000097903; ENSMUSG00000006471. [A2AI05-2] DR Ensembl; ENSMUST00000114349; ENSMUSP00000109989; ENSMUSG00000006471. [A2AI05-1] DR GeneID; 78797; -. DR KEGG; mmu:78797; -. DR UCSC; uc008iqw.2; mouse. [A2AI05-1] DR UCSC; uc012brw.2; mouse. [A2AI05-2] DR CTD; 27158; -. DR MGI; MGI:1926047; Ndor1. DR eggNOG; COG0369; -. DR GeneTree; ENSGT00620000087711; -. DR HOGENOM; HOG000173033; -. DR HOVERGEN; HBG104950; -. DR InParanoid; A2AI05; -. DR OMA; GPSHFQD; -. DR OrthoDB; EOG7QG44B; -. DR TreeFam; TF105716; -. DR NextBio; 349532; -. DR PRO; PR:A2AI05; -. DR ArrayExpress; A2AI05; -. DR Bgee; A2AI05; -. DR CleanEx; MM_NDOR1; -. DR Genevestigator; A2AI05; -. DR GO; GO:0005829; C:cytosol; ISS:UniProtKB. DR GO; GO:0045111; C:intermediate filament cytoskeleton; IEA:Ensembl. DR GO; GO:0005634; C:nucleus; IEA:Ensembl. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:Ensembl. DR GO; GO:0010181; F:FMN binding; IEA:Ensembl. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0050661; F:NADP binding; IEA:Ensembl. DR GO; GO:0003958; F:NADPH-hemoprotein reductase activity; IBA:RefGenome. DR GO; GO:0016709; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen; IBA:RefGenome. DR GO; GO:0008219; P:cell death; ISS:UniProtKB. DR GO; GO:0036245; P:cellular response to menadione; ISS:UniProtKB. DR Gene3D; 1.20.990.10; -; 1. DR HAMAP; MF_03178; NDOR1; 1. DR InterPro; IPR003097; FAD-binding_1. DR InterPro; IPR017927; Fd_Rdtase_FAD-bd. DR InterPro; IPR001094; Flavdoxin. DR InterPro; IPR008254; Flavodoxin/NO_synth. DR InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase. DR InterPro; IPR023173; NADPH_Cyt_P450_Rdtase_dom3. DR InterPro; IPR028879; NDOR1. DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd. DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl. DR Pfam; PF00667; FAD_binding_1; 1. DR Pfam; PF00258; Flavodoxin_1; 1. DR Pfam; PF00175; NAD_binding_1; 1. DR PRINTS; PR00369; FLAVODOXIN. DR PRINTS; PR00371; FPNCR. DR SUPFAM; SSF63380; SSF63380; 1. DR PROSITE; PS51384; FAD_FR; 1. DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1. PE 2: Evidence at transcript level; KW Alternative splicing; Complete proteome; Cytoplasm; FAD; Flavoprotein; KW FMN; NADP; Oxidoreductase; Reference proteome. FT CHAIN 1 598 NADPH-dependent diflavin oxidoreductase FT 1. FT /FTId=PRO_0000319540. FT DOMAIN 6 150 Flavodoxin-like. FT DOMAIN 206 448 FAD-binding FR-type. FT NP_BIND 12 16 FMN (By similarity). FT NP_BIND 94 125 FMN (By similarity). FT NP_BIND 242 253 FAD (By similarity). FT NP_BIND 379 389 FAD (By similarity). FT NP_BIND 544 560 NADP (By similarity). FT VAR_SEQ 1 45 MQVPQLLVLFGSQTGTAQDEAERLGREARRRRLGCRVQALD FT SYSV -> MRCREGTDQGCQRPYIYLCLVLE (in FT isoform 3). FT /FTId=VSP_031488. FT VAR_SEQ 104 171 KFNFVAKKLHRRLLQLGGSALLPPCLGDDQHELGPDAAIDP FT WVGDLWEKIMVMYPVPLDIPEIPHGVP -> N (in FT isoform 2). FT /FTId=VSP_031489. FT VAR_SEQ 481 488 NFLFFGCR -> EYWSSKAV (in isoform 3). FT /FTId=VSP_031490. FT VAR_SEQ 489 598 Missing (in isoform 3). FT /FTId=VSP_031491. SQ SEQUENCE 598 AA; 67183 MW; 7B621663EEE85FED CRC64; MQVPQLLVLF GSQTGTAQDE AERLGREARR RRLGCRVQAL DSYSVANLIR EPLVIFVCAT TGQGDPPDNM KNFWRFIFRK SLPSSSLCQM DFAVLGLGDS SYAKFNFVAK KLHRRLLQLG GSALLPPCLG DDQHELGPDA AIDPWVGDLW EKIMVMYPVP LDIPEIPHGV PLPSKFIFQF LQEVPSIGAE ELNIASSAPQ TPPSELQPFL APVITNQRVT GPQHFQDVRL IEFDITDSNI SFAAGDVVFI LPSNSEAHTQ QFCQVLCLDP NQFFTLKPRE PGVPDPPGLP QPCTVWNLVS QYLDIASVPR RSFFELLACL SQHALEREKL LELSSARGQE ELWEYCSRPR RTILEVLCDF PHTAGAIPPD YLLDLIPRIR PRAFSIASSL LAHPRRLQIL VAVVKYQTRL KEPRHGLCSS WLASLNPGQA GPVRVPLWVR PGSLVFPKTP DTPIIMVGAG TGVAPFRAAI QERVAHGQTG NFLFFGCRQR DQDFYWQTEW QKLEQKGWLT LVTAFSREQE QKVYVQHRLR ELGPLVWELL DGQGAYFYLA GNAKYLPTDV SEALMSIFQE EGRLSTADAS AYLARLQQTL RFQTETWA // ID NDUS2_MOUSE Reviewed; 463 AA. AC Q91WD5; Q3TNA8; Q3U5Y9; Q3UJX7; Q99L23; DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 19-MAR-2014, entry version 101. DE RecName: Full=NADH dehydrogenase [ubiquinone] iron-sulfur protein 2, mitochondrial; DE EC=1.6.5.3; DE EC=1.6.99.3; DE AltName: Full=Complex I-49kD; DE Short=CI-49kD; DE AltName: Full=NADH-ubiquinone oxidoreductase 49 kDa subunit; DE Flags: Precursor; GN Name=Ndufs2; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=BALB/c, and C57BL/6J; TISSUE=Bone marrow; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Mammary tumor, and Salivary gland; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP PROTEIN SEQUENCE OF 57-73; 76-108; 128-138; 158-166; 172-179; 210-216; RP 255-266; 272-323; 373-421; 424-437 AND 441-463, AND MASS SPECTROMETRY. RC STRAIN=C57BL/6; TISSUE=Brain, and Hippocampus; RA Lubec G., Klug S., Kang S.U.; RL Submitted (APR-2007) to UniProtKB. RN [4] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-62, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23576753; DOI=10.1073/pnas.1302961110; RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., RA Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.; RT "Label-free quantitative proteomics of the lysine acetylome in RT mitochondria identifies substrates of SIRT3 in metabolic pathways."; RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013). CC -!- FUNCTION: Core subunit of the mitochondrial membrane respiratory CC chain NADH dehydrogenase (Complex I) that is believed to belong to CC the minimal assembly required for catalysis. Complex I functions CC in the transfer of electrons from NADH to the respiratory chain. CC The immediate electron acceptor for the enzyme is believed to be CC ubiquinone (By similarity). CC -!- CATALYTIC ACTIVITY: NADH + ubiquinone + 5 H(+)(In) = NAD(+) + CC ubiquinol + 4 H(+)(Out). CC -!- CATALYTIC ACTIVITY: NADH + acceptor = NAD(+) + reduced acceptor. CC -!- COFACTOR: Binds 1 4Fe-4S cluster. CC -!- SUBUNIT: Complex I is composed of 45 different subunits. Component CC of the iron-sulfur (IP) fragment of the enzyme (By similarity). CC Interacts with NDUFAF3 (By similarity). CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral CC membrane protein; Matrix side (By similarity). CC -!- SIMILARITY: Belongs to the complex I 49 kDa subunit family. CC -!- SEQUENCE CAUTION: CC Sequence=AAH03898.1; Type=Erroneous initiation; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK078474; BAC37293.1; -; mRNA. DR EMBL; AK146269; BAE27028.1; -; mRNA. DR EMBL; AK150431; BAE29554.1; -; mRNA. DR EMBL; AK151746; BAE30656.1; -; mRNA. DR EMBL; AK153364; BAE31936.1; -; mRNA. DR EMBL; AK165426; BAE38181.1; -; mRNA. DR EMBL; BC003898; AAH03898.1; ALT_INIT; mRNA. DR EMBL; BC016097; AAH16097.1; -; mRNA. DR RefSeq; NP_694704.1; NM_153064.4. DR UniGene; Mm.21669; -. DR ProteinModelPortal; Q91WD5; -. DR SMR; Q91WD5; 80-463. DR BioGrid; 230541; 1. DR IntAct; Q91WD5; 6. DR MINT; MINT-1860118; -. DR PhosphoSite; Q91WD5; -. DR PaxDb; Q91WD5; -. DR PRIDE; Q91WD5; -. DR Ensembl; ENSMUST00000013737; ENSMUSP00000013737; ENSMUSG00000013593. DR GeneID; 226646; -. DR KEGG; mmu:226646; -. DR UCSC; uc007dnm.1; mouse. DR CTD; 4720; -. DR MGI; MGI:2385112; Ndufs2. DR eggNOG; COG0649; -. DR GeneTree; ENSGT00390000009529; -. DR HOGENOM; HOG000228264; -. DR HOVERGEN; HBG000760; -. DR InParanoid; Q91WD5; -. DR KO; K03935; -. DR OMA; EYRTWTQ; -. DR OrthoDB; EOG7WT411; -. DR TreeFam; TF300370; -. DR NextBio; 378279; -. DR PRO; PR:Q91WD5; -. DR ArrayExpress; Q91WD5; -. DR Bgee; Q91WD5; -. DR CleanEx; MM_NDUFS2; -. DR Genevestigator; Q91WD5; -. DR GO; GO:0005747; C:mitochondrial respiratory chain complex I; ISS:UniProtKB. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:UniProtKB-EC. DR GO; GO:0048038; F:quinone binding; IEA:InterPro. DR GO; GO:0006979; P:response to oxidative stress; ISS:UniProtKB. DR HAMAP; MF_01358; NDH1_NuoD; 1. DR InterPro; IPR001135; NADH_Q_OxRdtase_suD. DR InterPro; IPR014029; NADH_UbQ_OxRdtase_49kDa_CS. DR InterPro; IPR022885; NDH1_su_D/H. DR Pfam; PF00346; Complex1_49kDa; 1. DR TIGRFAMs; TIGR01962; NuoD; 1. DR PROSITE; PS00535; COMPLEX1_49K; 1. PE 1: Evidence at protein level; KW 4Fe-4S; Acetylation; Complete proteome; Direct protein sequencing; KW Electron transport; Iron; Iron-sulfur; Membrane; Metal-binding; KW Methylation; Mitochondrion; Mitochondrion inner membrane; NAD; KW Oxidoreductase; Reference proteome; Respiratory chain; KW Transit peptide; Transport; Ubiquinone. FT TRANSIT 1 33 Mitochondrion (By similarity). FT CHAIN 34 463 NADH dehydrogenase [ubiquinone] iron- FT sulfur protein 2, mitochondrial. FT /FTId=PRO_0000019982. FT METAL 326 326 Iron-sulfur (4Fe-4S) (Potential). FT METAL 332 332 Iron-sulfur (4Fe-4S) (Potential). FT METAL 347 347 Iron-sulfur (4Fe-4S) (Potential). FT MOD_RES 62 62 N6-acetyllysine. FT MOD_RES 118 118 Symmetric dimethylarginine (By FT similarity). FT CONFLICT 1 1 M -> V (in Ref. 2; AAH03898). FT CONFLICT 2 2 A -> R (in Ref. 1; BAE30656/BAE31936). FT CONFLICT 81 81 T -> A (in Ref. 1; BAE27028). FT CONFLICT 186 186 A -> S (in Ref. 1; BAE27028). SQ SEQUENCE 463 AA; 52626 MW; 989934D73F5C8D27 CRC64; MAALRALRCL RGVGAPVLRP GSGIRLPSQP SRGARQWQPD IEWAEQFSGA VMYPSKETAH WKPPPWNDVD ILKEKAVTNM TLNFGPQHPA AHGVLRLVLE LSGEMVRKCD PHIGLLHRGT EKLIEYKTYL QALPYFDRLD YVSMMCNEQA YSIAVEKLLN IQPPPRAQWI RVLFGEITRI LNHIMAVTTH ALDIGAMTPF FWMFEEREKM FEFYERVSGA RMHAAYIRPG GVHQDLPLGL LDDIYEFSKN FSLRIDEVEE MLTNNRIWRN RTVDIGVVTA EDALNYGFSG VMLRGSGIQW DLRKTQPYDV YDQVEFDVPI GSRGDCYDRY LCRVEEMRQS LRIIEQCLNK MPPGEIKVDD AKVSPPKRAE MKTSMESLIH HFKLYTEGYQ VPPGATYTAI EAPKGEFGVY LVSDGSSRPY RCKIKAPGFA HLAGLDKMSK GHMLADVVAI IGTQDIVFGE IDR // ID NDUS1_MOUSE Reviewed; 727 AA. AC Q91VD9; Q3UQ73; Q8BM16; DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 2. DT 19-MAR-2014, entry version 113. DE RecName: Full=NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial; DE EC=1.6.5.3; DE EC=1.6.99.3; DE AltName: Full=Complex I-75kD; DE Short=CI-75kD; DE Flags: Precursor; GN Name=Ndufs1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Embryonic breast, Heart, and Vagina; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Kidney; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP PROTEIN SEQUENCE OF 77-84; 88-108; 185-212; 247-266; 277-289; 292-299; RP 312-325; 361-382; 409-417; 421-441; 451-467; 471-483; 502-511; RP 519-539; 544-557; 608-617; 625-643; 646-655; 674-702 AND 713-727, AND RP MASS SPECTROMETRY. RC STRAIN=C57BL/6; TISSUE=Brain, and Hippocampus; RA Lubec G., Klug S., Kang S.U.; RL Submitted (APR-2007) to UniProtKB. RN [6] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-84; LYS-467; LYS-499 AND RP LYS-709, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Liver; RX PubMed=23576753; DOI=10.1073/pnas.1302961110; RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., RA Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.; RT "Label-free quantitative proteomics of the lysine acetylome in RT mitochondria identifies substrates of SIRT3 in metabolic pathways."; RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013). CC -!- FUNCTION: Core subunit of the mitochondrial membrane respiratory CC chain NADH dehydrogenase (Complex I) that is believed to belong to CC the minimal assembly required for catalysis. Complex I functions CC in the transfer of electrons from NADH to the respiratory chain. CC The immediate electron acceptor for the enzyme is believed to be CC ubiquinone (By similarity). This is the largest subunit of complex CC I and it is a component of the iron-sulfur (IP) fragment of the CC enzyme. It may form part of the active site crevice where NADH is CC oxidized (By similarity). CC -!- CATALYTIC ACTIVITY: NADH + ubiquinone + 5 H(+)(In) = NAD(+) + CC ubiquinol + 4 H(+)(Out). CC -!- CATALYTIC ACTIVITY: NADH + acceptor = NAD(+) + reduced acceptor. CC -!- COFACTOR: Binds 1 2Fe-2S cluster per subunit (By similarity). CC -!- COFACTOR: Binds 2 4Fe-4S clusters per subunit (By similarity). CC -!- SUBUNIT: Complex I is composed of 45 different subunits (By CC similarity). CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane (By CC similarity). Note=Matrix and cytoplasmic side of the mitochondrial CC inner membrane (By similarity). CC -!- PTM: Acetylation of Lys-84 is observed in liver mitochondria from CC fasted mice but not from fed mice. CC -!- SIMILARITY: Belongs to the complex I 75 kDa subunit family. CC -!- SIMILARITY: Contains 1 2Fe-2S ferredoxin-type domain. CC -!- SIMILARITY: Contains 1 4Fe-4S Mo/W bis-MGD-type domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK034597; BAE20494.1; -; mRNA. DR EMBL; AK036926; BAC29641.1; -; mRNA. DR EMBL; AK142711; BAE25170.1; -; mRNA. DR EMBL; AL645950; CAI24120.1; -; Genomic_DNA. DR EMBL; CH466548; EDL00180.1; -; Genomic_DNA. DR EMBL; CH466548; EDL00181.1; -; Genomic_DNA. DR EMBL; CH466548; EDL00182.1; -; Genomic_DNA. DR EMBL; CH466548; EDL00184.1; -; Genomic_DNA. DR EMBL; BC006660; AAH06660.1; -; mRNA. DR EMBL; BC015300; AAH15300.1; -; mRNA. DR RefSeq; NP_001153510.1; NM_001160038.1. DR RefSeq; NP_001153511.1; NM_001160039.1. DR RefSeq; NP_001153512.1; NM_001160040.1. DR RefSeq; NP_663493.2; NM_145518.2. DR RefSeq; XP_006496014.1; XM_006495951.1. DR RefSeq; XP_006496015.1; XM_006495952.1. DR UniGene; Mm.290791; -. DR ProteinModelPortal; Q91VD9; -. DR SMR; Q91VD9; 31-636. DR BioGrid; 230599; 2. DR IntAct; Q91VD9; 5. DR MINT; MINT-1860504; -. DR STRING; 10090.ENSMUSP00000027111; -. DR PhosphoSite; Q91VD9; -. DR REPRODUCTION-2DPAGE; IPI00308882; -. DR REPRODUCTION-2DPAGE; Q91VD9; -. DR PaxDb; Q91VD9; -. DR PRIDE; Q91VD9; -. DR Ensembl; ENSMUST00000027111; ENSMUSP00000027111; ENSMUSG00000025968. DR Ensembl; ENSMUST00000168099; ENSMUSP00000126621; ENSMUSG00000025968. DR GeneID; 227197; -. DR KEGG; mmu:227197; -. DR UCSC; uc007bfu.2; mouse. DR CTD; 4719; -. DR MGI; MGI:2443241; Ndufs1. DR eggNOG; COG1034; -. DR GeneTree; ENSGT00390000018768; -. DR HOGENOM; HOG000031442; -. DR HOVERGEN; HBG003482; -. DR InParanoid; Q3UQ73; -. DR KO; K03934; -. DR OMA; MPVMKGM; -. DR OrthoDB; EOG783MTP; -. DR TreeFam; TF105756; -. DR NextBio; 378510; -. DR PRO; PR:Q91VD9; -. DR ArrayExpress; Q91VD9; -. DR Bgee; Q91VD9; -. DR CleanEx; MM_NDUFS1; -. DR Genevestigator; Q91VD9; -. DR GO; GO:0005758; C:mitochondrial intermembrane space; ISS:UniProtKB. DR GO; GO:0005747; C:mitochondrial respiratory chain complex I; ISS:UniProtKB. DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IBA:RefGenome. DR GO; GO:0008637; P:apoptotic mitochondrial changes; ISS:UniProtKB. DR GO; GO:0046034; P:ATP metabolic process; ISS:UniProtKB. DR GO; GO:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro. DR GO; GO:0045333; P:cellular respiration; ISS:UniProtKB. DR GO; GO:0072593; P:reactive oxygen species metabolic process; ISS:UniProtKB. DR GO; GO:0051881; P:regulation of mitochondrial membrane potential; ISS:UniProtKB. DR Gene3D; 3.10.20.30; -; 1. DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type. DR InterPro; IPR012675; Beta-grasp_dom. DR InterPro; IPR006656; Mopterin_OxRdtase. DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom. DR InterPro; IPR000283; NADH_UbQ_OxRdtase_75kDa_su_CS. DR InterPro; IPR010228; NADH_UbQ_OxRdtase_Gsu. DR InterPro; IPR019574; NADH_UbQ_OxRdtase_Gsu_4Fe4S-bd. DR InterPro; IPR015405; NuoG_C. DR Pfam; PF09326; DUF1982; 1. DR Pfam; PF00384; Molybdopterin; 1. DR Pfam; PF10588; NADH-G_4Fe-4S_3; 1. DR SMART; SM00929; NADH-G_4Fe-4S_3; 1. DR SUPFAM; SSF54292; SSF54292; 1. DR TIGRFAMs; TIGR01973; NuoG; 1. DR PROSITE; PS51085; 2FE2S_FER_2; 1. DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1. DR PROSITE; PS00641; COMPLEX1_75K_1; 1. DR PROSITE; PS00642; COMPLEX1_75K_2; 1. DR PROSITE; PS00643; COMPLEX1_75K_3; 1. PE 1: Evidence at protein level; KW 2Fe-2S; 4Fe-4S; Acetylation; Complete proteome; KW Direct protein sequencing; Electron transport; Iron; Iron-sulfur; KW Membrane; Metal-binding; Mitochondrion; Mitochondrion inner membrane; KW NAD; Oxidoreductase; Reference proteome; Respiratory chain; KW Transit peptide; Transport; Ubiquinone. FT TRANSIT 1 23 Mitochondrion (By similarity). FT CHAIN 24 727 NADH-ubiquinone oxidoreductase 75 kDa FT subunit, mitochondrial. FT /FTId=PRO_0000019969. FT DOMAIN 30 108 2Fe-2S ferredoxin-type. FT DOMAIN 245 301 4Fe-4S Mo/W bis-MGD-type. FT METAL 64 64 Iron-sulfur 1 (2Fe-2S) (By similarity). FT METAL 75 75 Iron-sulfur 1 (2Fe-2S) (By similarity). FT METAL 78 78 Iron-sulfur 1 (2Fe-2S) (By similarity). FT METAL 92 92 Iron-sulfur 1 (2Fe-2S) (By similarity). FT METAL 124 124 Iron-sulfur 2 (4Fe-4S); via pros nitrogen FT (By similarity). FT METAL 128 128 Iron-sulfur 2 (4Fe-4S) (By similarity). FT METAL 131 131 Iron-sulfur 2 (4Fe-4S) (By similarity). FT METAL 137 137 Iron-sulfur 2 (4Fe-4S) (By similarity). FT METAL 176 176 Iron-sulfur 3 (4Fe-4S) (By similarity). FT METAL 179 179 Iron-sulfur 3 (4Fe-4S) (By similarity). FT METAL 182 182 Iron-sulfur 3 (4Fe-4S) (By similarity). FT METAL 226 226 Iron-sulfur 3 (4Fe-4S) (By similarity). FT MOD_RES 84 84 N6-acetyllysine. FT MOD_RES 467 467 N6-acetyllysine. FT MOD_RES 499 499 N6-acetyllysine. FT MOD_RES 709 709 N6-acetyllysine. FT CONFLICT 491 491 V -> A (in Ref. 4; AAH06660/AAH15300). SQ SEQUENCE 727 AA; 79777 MW; 4A4B4BD6C330BB4F CRC64; MLRIPIKRAL IGLSNSPKGY VRTTGTAASN LIEVFVDGQS VMVEPGTTVL QACEKVGMQI PRFCYHERLS VAGNCRMCLV EIEKAPKVVA ACAMPVMKGW NILTNSEKSK KAREGVMEFL LANHPLDCPI CDQGGECDLQ DQSMMFGSDR SRFLEGKRAV EDKNIGPLVK TIMTRCIQCT RCIRFASEIA GVDDLGTTGR GNDMQVGTYI EKMFMSELSG NVIDICPVGA LTSKPYAFTA RPWETRKTES IDVMDAVGSN IVVSTRTGEV MRILPRMHED INEEWISDKT RFAYDGLKRQ RLTEPMVRNE KGLLTYTSWE DALSRVAGML QNFEGNAVAA IAGGLVDAEA LVALKDLLNK VDSDNLCTEE IFPTEGAGTD LRSNYLLNTT IAGVEEADVV LLVGTNPRFE APLFNARIRK SWLHNDLKVA LIGSPVDLTY RYDHLGDSPK ILQDIASGRH SFCEVLKDAK KPMVVLGSSA LQRDDGAAIL VAVSNMVQKI RVTTGVAAEW KVMNILHRIA SQVAALDLGY KPGVEAIRKN PPKMLFLLGA DGGCITRQDL PKDCFIVYQG HHGDVGAPMA DVILPGAAYT EKSATYVNTE GRAQQTKVAV TPPGLAREDW KIIRALSEIA GITLPYDTLD QVRNRLEEVS PNLVRYDDIE ETNYFQQASE LAKLVNQEVL ADPLVPPQLT IKDFYMTDSI SRASQTMAKC VKAVTEGAQA VEEPSIC // ID NDUS3_MOUSE Reviewed; 263 AA. AC Q9DCT2; Q8BTZ3; Q8R073; DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2007, sequence version 2. DT 19-MAR-2014, entry version 115. DE RecName: Full=NADH dehydrogenase [ubiquinone] iron-sulfur protein 3, mitochondrial; DE EC=1.6.5.3; DE EC=1.6.99.3; DE AltName: Full=Complex I-30kD; DE Short=CI-30kD; DE AltName: Full=NADH-ubiquinone oxidoreductase 30 kDa subunit; DE Flags: Precursor; GN Name=Ndufs3; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J, and NOD; TISSUE=Kidney, and Thymus; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP PROTEIN SEQUENCE OF 109-121; 125-135; 186-198; 200-210 AND 218-245, RP AND MASS SPECTROMETRY. RC STRAIN=C57BL/6; TISSUE=Brain, and Hippocampus; RA Lubec G., Klug S., Kang S.U.; RL Submitted (APR-2007) to UniProtKB. CC -!- FUNCTION: Core subunit of the mitochondrial membrane respiratory CC chain NADH dehydrogenase (Complex I) that is believed to belong to CC the minimal assembly required for catalysis. Complex I functions CC in the transfer of electrons from NADH to the respiratory chain. CC The immediate electron acceptor for the enzyme is believed to be CC ubiquinone (By similarity). CC -!- CATALYTIC ACTIVITY: NADH + ubiquinone + 5 H(+)(In) = NAD(+) + CC ubiquinol + 4 H(+)(Out). CC -!- CATALYTIC ACTIVITY: NADH + acceptor = NAD(+) + reduced acceptor. CC -!- SUBUNIT: Complex I is composed of 45 different subunits (By CC similarity). Interacts with NDUFAF3 (By similarity). CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane (By CC similarity). Note=Matrix and cytoplasmic side of the mitochondrial CC inner membrane (By similarity). CC -!- SIMILARITY: Belongs to the complex I 30 kDa subunit family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK002501; BAB22149.1; -; mRNA. DR EMBL; AK088337; BAC40291.1; -; mRNA. DR EMBL; AL672241; CAM15313.1; -; Genomic_DNA. DR EMBL; BC027270; AAH27270.1; -; mRNA. DR EMBL; BC119267; AAI19268.1; -; mRNA. DR EMBL; BC119269; AAI19270.1; -; mRNA. DR RefSeq; NP_080964.1; NM_026688.2. DR UniGene; Mm.30113; -. DR ProteinModelPortal; Q9DCT2; -. DR SMR; Q9DCT2; 47-239. DR BioGrid; 212816; 3. DR DIP; DIP-32378N; -. DR IntAct; Q9DCT2; 6. DR MINT; MINT-4112498; -. DR PhosphoSite; Q9DCT2; -. DR World-2DPAGE; 0004:Q9DCT2; -. DR PaxDb; Q9DCT2; -. DR PRIDE; Q9DCT2; -. DR Ensembl; ENSMUST00000005647; ENSMUSP00000005647; ENSMUSG00000005510. DR GeneID; 68349; -. DR KEGG; mmu:68349; -. DR UCSC; uc008ktr.1; mouse. DR CTD; 4722; -. DR MGI; MGI:1915599; Ndufs3. DR eggNOG; COG0852; -. DR GeneTree; ENSGT00390000017480; -. DR HOGENOM; HOG000009797; -. DR HOVERGEN; HBG000450; -. DR InParanoid; Q9DCT2; -. DR KO; K03936; -. DR OMA; QQVQVTC; -. DR OrthoDB; EOG7R56TC; -. DR TreeFam; TF314794; -. DR NextBio; 327045; -. DR PRO; PR:Q9DCT2; -. DR Bgee; Q9DCT2; -. DR CleanEx; MM_NDUFS3; -. DR Genevestigator; Q9DCT2; -. DR GO; GO:0005747; C:mitochondrial respiratory chain complex I; ISS:UniProtKB. DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:UniProtKB-EC. DR GO; GO:0003954; F:NADH dehydrogenase activity; ISS:UniProtKB. DR GO; GO:0030308; P:negative regulation of cell growth; ISS:UniProtKB. DR GO; GO:2001243; P:negative regulation of intrinsic apoptotic signaling pathway; ISS:UniProtKB. DR GO; GO:0072593; P:reactive oxygen species metabolic process; ISS:UniProtKB. DR HAMAP; MF_01357; NDH1_NuoC; 1. DR InterPro; IPR010218; NADH_DH_suC. DR InterPro; IPR001268; NADH_UbQ_OxRdtase_30kDa_su. DR InterPro; IPR020396; NADH_UbQ_OxRdtase_CS. DR Pfam; PF00329; Complex1_30kDa; 1. DR ProDom; PD001581; NADH_UbQ_OxRdtase_30kDa_su; 1. DR TIGRFAMs; TIGR01961; NuoC_fam; 1. DR PROSITE; PS00542; COMPLEX1_30K; 1. PE 1: Evidence at protein level; KW Complete proteome; Direct protein sequencing; Electron transport; KW Membrane; Mitochondrion; Mitochondrion inner membrane; NAD; KW Oxidoreductase; Reference proteome; Respiratory chain; KW Transit peptide; Transport; Ubiquinone. FT TRANSIT 1 35 Mitochondrion (By similarity). FT CHAIN 36 263 NADH dehydrogenase [ubiquinone] iron- FT sulfur protein 3, mitochondrial. FT /FTId=PRO_0000019999. FT CONFLICT 20 20 G -> D (in Ref. 1; BAB22149). FT CONFLICT 23 23 A -> P (in Ref. 3; AAH27270). FT CONFLICT 49 49 R -> W (in Ref. 3; AAH27270). SQ SEQUENCE 263 AA; 30149 MW; 482F6C4D5E991B7F CRC64; MAAAAARVWC RGLLGAASVG RGAGRPSVLW QHVRRESAAA DKRPTVRPRS DVTHKQLSAF GEYVAEILPK YVQQVQVSCL DELEICIHPD GVIPTLTFLR DHTNAQFKSL ADLTAVDVPT RQNRFEIVYN LLSLRFNSRI RVKTYADELT PIDSIVSVHI AANWYEREVW DMFGVFFFNH PDLRRILTDY GFEGHPFRKD FPLTGYVELR YDDEVKRVVA EPVELAQEFR KFDLNSPWEA FPAYRQPPES LKLEAGDKKP ETK // ID NDUS7_MOUSE Reviewed; 224 AA. AC Q9DC70; DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 19-FEB-2014, entry version 98. DE RecName: Full=NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial; DE EC=1.6.5.3; DE EC=1.6.99.3; DE AltName: Full=Complex I-20kD; DE Short=CI-20kD; DE AltName: Full=NADH-ubiquinone oxidoreductase 20 kDa subunit; DE Flags: Precursor; GN Name=Ndufs7; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Heart; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Colon; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP PROTEIN SEQUENCE OF 78-86; 127-140 AND 157-179, AND MASS SPECTROMETRY. RC STRAIN=C57BL/6; TISSUE=Brain; RA Lubec G., Kang S.U.; RL Submitted (APR-2007) to UniProtKB. RN [4] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain; RX PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200; RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., RA Burlingame A.L.; RT "Comprehensive identification of phosphorylation sites in postsynaptic RT density preparations."; RL Mol. Cell. Proteomics 5:914-922(2006). CC -!- FUNCTION: Core subunit of the mitochondrial membrane respiratory CC chain NADH dehydrogenase (Complex I) that is believed to belong to CC the minimal assembly required for catalysis. Complex I functions CC in the transfer of electrons from NADH to the respiratory chain. CC The immediate electron acceptor for the enzyme is believed to be CC ubiquinone (By similarity). CC -!- CATALYTIC ACTIVITY: NADH + ubiquinone + 5 H(+)(In) = NAD(+) + CC ubiquinol + 4 H(+)(Out). CC -!- CATALYTIC ACTIVITY: NADH + acceptor = NAD(+) + reduced acceptor. CC -!- COFACTOR: Binds 1 4Fe-4S cluster (Potential). CC -!- SUBUNIT: Complex I is composed of 45 different subunits This is a CC component of the iron-sulfur (IP) fragment of the enzyme (By CC similarity). CC -!- SUBCELLULAR LOCATION: Mitochondrion (By similarity). CC -!- SIMILARITY: Belongs to the complex I 20 kDa subunit family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK003132; BAB22592.1; -; mRNA. DR EMBL; BC013503; AAH13503.1; -; mRNA. DR RefSeq; NP_083548.1; NM_029272.3. DR UniGene; Mm.28712; -. DR ProteinModelPortal; Q9DC70; -. DR SMR; Q9DC70; 70-213. DR BioGrid; 217459; 1. DR IntAct; Q9DC70; 1. DR MINT; MINT-1861354; -. DR STRING; 10090.ENSMUSP00000020361; -. DR PhosphoSite; Q9DC70; -. DR PaxDb; Q9DC70; -. DR PRIDE; Q9DC70; -. DR Ensembl; ENSMUST00000020361; ENSMUSP00000020361; ENSMUSG00000020153. DR Ensembl; ENSMUST00000105364; ENSMUSP00000101003; ENSMUSG00000020153. DR GeneID; 75406; -. DR KEGG; mmu:75406; -. DR UCSC; uc007gci.1; mouse. DR CTD; 374291; -. DR MGI; MGI:1922656; Ndufs7. DR eggNOG; COG0377; -. DR GeneTree; ENSGT00390000006565; -. DR HOGENOM; HOG000228249; -. DR HOVERGEN; HBG001576; -. DR InParanoid; Q9DC70; -. DR KO; K03940; -. DR OMA; GVMQYAL; -. DR OrthoDB; EOG7C8GJ9; -. DR TreeFam; TF312859; -. DR NextBio; 342928; -. DR PRO; PR:Q9DC70; -. DR Bgee; Q9DC70; -. DR CleanEx; MM_NDUFS7; -. DR Genevestigator; Q9DC70; -. DR GO; GO:0005747; C:mitochondrial respiratory chain complex I; ISS:UniProtKB. DR GO; GO:0043005; C:neuron projection; IEA:Ensembl. DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl. DR GO; GO:0097060; C:synaptic membrane; IEA:Ensembl. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:UniProtKB-EC. DR GO; GO:0048038; F:quinone binding; IEA:InterPro. DR GO; GO:0032981; P:mitochondrial respiratory chain complex I assembly; ISS:UniProtKB. DR Gene3D; 3.40.50.700; -; 1. DR HAMAP; MF_01356; NDH1_NuoB; 1. DR InterPro; IPR006137; NADH_UbQ_OxRdtase-like_20kDa. DR InterPro; IPR006138; NADH_UQ_OxRdtase_20Kd_su. DR Pfam; PF01058; Oxidored_q6; 1. DR TIGRFAMs; TIGR01957; nuoB_fam; 1. DR PROSITE; PS01150; COMPLEX1_20K; 1. PE 1: Evidence at protein level; KW 4Fe-4S; Complete proteome; Direct protein sequencing; KW Electron transport; Iron; Iron-sulfur; Metal-binding; Mitochondrion; KW NAD; Oxidoreductase; Reference proteome; Respiratory chain; KW Transit peptide; Transport; Ubiquinone. FT TRANSIT 1 35 Mitochondrion (By similarity). FT CHAIN 36 224 NADH dehydrogenase [ubiquinone] iron- FT sulfur protein 7, mitochondrial. FT /FTId=PRO_0000020028. FT METAL 99 99 Iron-sulfur (4Fe-4S) (Potential). FT METAL 100 100 Iron-sulfur (4Fe-4S) (Potential). FT METAL 164 164 Iron-sulfur (4Fe-4S) (Potential). FT METAL 194 194 Iron-sulfur (4Fe-4S) (Potential). SQ SEQUENCE 224 AA; 24683 MW; 234F3FF0ABC36A92 CRC64; MAALAAPGLL SVRILGLRTA QVQLRRVHQS VATEGPSPSP SPSLSSTQSA VSKAGAGAVV PKLSHLPRSR AEYVVTKLDD LINWARRSSL WPMTFGLACC AVEMMHMAAP RYDMDRFGVV FRASPRQADV MIVAGTLTNK MAPALRKVYD QMPEPRYVVS MGSCANGGGY YHYSYSVVRG CDRIVPVDIY VPGCPPTAEA LLYGILQLQR KIKREQKLKI WYRR // ID NDUS8_MOUSE Reviewed; 212 AA. AC Q8K3J1; DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2002, sequence version 1. DT 19-FEB-2014, entry version 97. DE RecName: Full=NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial; DE EC=1.6.5.3; DE EC=1.6.99.3; DE AltName: Full=Complex I-23kD; DE Short=CI-23kD; DE AltName: Full=NADH-ubiquinone oxidoreductase 23 kDa subunit; DE Flags: Precursor; GN Name=Ndufs8; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Lucas-Teixeira V.A., Marques S., Belo J.A.; RT "Genomic organization of the mouse NDUFS8 gene encoding the NADH RT dehydrogenase:ubiquinone Fe-S protein 8."; RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases. RN [2] RP PROTEIN SEQUENCE OF 19-37; 60-90 AND 118-135, AND MASS SPECTROMETRY. RC STRAIN=C57BL/6; TISSUE=Brain; RA Lubec G., Kang S.U.; RL Submitted (APR-2007) to UniProtKB. RN [3] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain; RX PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200; RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., RA Burlingame A.L.; RT "Comprehensive identification of phosphorylation sites in postsynaptic RT density preparations."; RL Mol. Cell. Proteomics 5:914-922(2006). CC -!- FUNCTION: Core subunit of the mitochondrial membrane respiratory CC chain NADH dehydrogenase (Complex I) that is believed to belong to CC the minimal assembly required for catalysis. Complex I functions CC in the transfer of electrons from NADH to the respiratory chain. CC The immediate electron acceptor for the enzyme is believed to be CC ubiquinone (By similarity). CC -!- CATALYTIC ACTIVITY: NADH + ubiquinone + 5 H(+)(In) = NAD(+) + CC ubiquinol + 4 H(+)(Out). CC -!- CATALYTIC ACTIVITY: NADH + acceptor = NAD(+) + reduced acceptor. CC -!- COFACTOR: Binds 2 4Fe-4S clusters per subunit (By similarity). CC -!- SUBUNIT: Complex I is composed of 45 different subunits This is a CC component of the iron-sulfur (IP) fragment of the enzyme (By CC similarity). CC -!- SUBCELLULAR LOCATION: Mitochondrion (By similarity). CC -!- SIMILARITY: Belongs to the complex I 23 kDa subunit family. CC -!- SIMILARITY: Contains 2 4Fe-4S ferredoxin-type domains. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AY096002; AAM34451.1; -; Genomic_DNA. DR PIR; PC7079; PC7079. DR RefSeq; NP_001258372.1; NM_001271443.1. DR RefSeq; NP_001258373.1; NM_001271444.1. DR RefSeq; NP_659119.2; NM_144870.5. DR UniGene; Mm.44227; -. DR ProteinModelPortal; Q8K3J1; -. DR SMR; Q8K3J1; 66-191. DR BioGrid; 230440; 1. DR IntAct; Q8K3J1; 2. DR MINT; MINT-1859976; -. DR PhosphoSite; Q8K3J1; -. DR REPRODUCTION-2DPAGE; Q8K3J1; -. DR PaxDb; Q8K3J1; -. DR PRIDE; Q8K3J1; -. DR Ensembl; ENSMUST00000075092; ENSMUSP00000074600; ENSMUSG00000059734. DR GeneID; 225887; -. DR KEGG; mmu:225887; -. DR UCSC; uc008fxn.1; mouse. DR CTD; 4728; -. DR MGI; MGI:2385079; Ndufs8. DR eggNOG; COG1143; -. DR GeneTree; ENSGT00390000003049; -. DR HOGENOM; HOG000228289; -. DR HOVERGEN; HBG006547; -. DR InParanoid; Q8K3J1; -. DR KO; K03941; -. DR OMA; TYKYVNL; -. DR OrthoDB; EOG7J9VQT; -. DR TreeFam; TF105610; -. DR NextBio; 377849; -. DR PRO; PR:Q8K3J1; -. DR ArrayExpress; Q8K3J1; -. DR Bgee; Q8K3J1; -. DR CleanEx; MM_NDUFS8; -. DR Genevestigator; Q8K3J1; -. DR GO; GO:0005747; C:mitochondrial respiratory chain complex I; IEA:Ensembl. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:UniProtKB-EC. DR GO; GO:0032981; P:mitochondrial respiratory chain complex I assembly; IEA:Ensembl. DR GO; GO:0006979; P:response to oxidative stress; IEA:Ensembl. DR HAMAP; MF_01351; NDH1_NuoI; 1. DR InterPro; IPR001450; 4Fe4S-bd_dom. DR InterPro; IPR017896; 4Fe4S_Fe-S-bd. DR InterPro; IPR017900; 4Fe4S_Fe_S_CS. DR InterPro; IPR010226; NADH_quinone_OxRdtase_chainI. DR Pfam; PF12838; Fer4_7; 1. DR TIGRFAMs; TIGR01971; NuoI; 1. DR PROSITE; PS00198; 4FE4S_FER_1; 2. DR PROSITE; PS51379; 4FE4S_FER_2; 2. PE 1: Evidence at protein level; KW 4Fe-4S; Complete proteome; Direct protein sequencing; KW Electron transport; Iron; Iron-sulfur; Metal-binding; Mitochondrion; KW NAD; Oxidoreductase; Reference proteome; Repeat; Respiratory chain; KW Transit peptide; Transport; Ubiquinone. FT TRANSIT 1 34 Mitochondrion (By similarity). FT CHAIN 35 212 NADH dehydrogenase [ubiquinone] iron- FT sulfur protein 8, mitochondrial. FT /FTId=PRO_0000020014. FT DOMAIN 104 133 4Fe-4S ferredoxin-type 1. FT DOMAIN 143 172 4Fe-4S ferredoxin-type 2. FT METAL 113 113 Iron-sulfur 1 (4Fe-4S) (By similarity). FT METAL 116 116 Iron-sulfur 1 (4Fe-4S) (By similarity). FT METAL 119 119 Iron-sulfur 1 (4Fe-4S) (By similarity). FT METAL 123 123 Iron-sulfur 2 (4Fe-4S) (By similarity). FT METAL 152 152 Iron-sulfur 2 (4Fe-4S) (By similarity). FT METAL 155 155 Iron-sulfur 2 (4Fe-4S) (By similarity). FT METAL 158 158 Iron-sulfur 2 (4Fe-4S) (By similarity). FT METAL 162 162 Iron-sulfur 1 (4Fe-4S) (By similarity). SQ SEQUENCE 212 AA; 24038 MW; 1E06E024EA7829CD CRC64; MYRLSSSMLP RALAQAMRTG HLNGQSLHSS AVAATYKYVN KKEQESEVDM KSATDNAARI LMWTELIRGL GMTLSYLFRE PATINYPFEK GPLSPRFRGE HALRRYPSGE ERCIACKLCE AICPAQAITI EAEPRADGSR RTTRYDIDMT KCIYCGFCQE ACPVDAIVEG PNFEFSTETH EELLYNKEKL LNNGDKWEAE IAANIQADYL YR // ID NDUV1_MOUSE Reviewed; 464 AA. AC Q91YT0; DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 19-MAR-2014, entry version 108. DE RecName: Full=NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial; DE EC=1.6.5.3; DE EC=1.6.99.3; DE AltName: Full=Complex I-51kD; DE Short=CI-51kD; DE AltName: Full=NADH-ubiquinone oxidoreductase 51 kDa subunit; DE Flags: Precursor; GN Name=Ndufv1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Kidney; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP PROTEIN SEQUENCE OF 21-29. RC STRAIN=C57BL/6; TISSUE=Brain; RX PubMed=10870971; RX DOI=10.1002/(SICI)1522-2683(20000501)21:9<1853::AID-ELPS1853>3.3.CO;2-P; RA Tsugita A., Kawakami T., Uchida T., Sakai T., Kamo M., Matsui T., RA Watanabe Y., Morimasa T., Hosokawa K., Toda T.; RT "Proteome analysis of mouse brain: two-dimensional electrophoresis RT profiles of tissue proteins during the course of aging."; RL Electrophoresis 21:1853-1871(2000). RN [4] RP PROTEIN SEQUENCE OF 29-48; 72-81; 89-126; 138-147; 153-219; 258-267; RP 275-297; 303-329; 370-375; 387-394 AND 402-449, AND MASS SPECTROMETRY. RC STRAIN=C57BL/6, and OF1; TISSUE=Brain, and Hippocampus; RA Lubec G., Klug S., Kang S.U., Sunyer B., Chen W.-Q.; RL Submitted (JAN-2009) to UniProtKB. RN [5] RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-81, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., RA Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). RN [6] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-81; LYS-104 AND LYS-375, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23576753; DOI=10.1073/pnas.1302961110; RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., RA Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.; RT "Label-free quantitative proteomics of the lysine acetylome in RT mitochondria identifies substrates of SIRT3 in metabolic pathways."; RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013). CC -!- FUNCTION: Core subunit of the mitochondrial membrane respiratory CC chain NADH dehydrogenase (Complex I) that is believed to belong to CC the minimal assembly required for catalysis. Complex I functions CC in the transfer of electrons from NADH to the respiratory chain. CC The immediate electron acceptor for the enzyme is believed to be CC ubiquinone (By similarity). CC -!- CATALYTIC ACTIVITY: NADH + ubiquinone + 5 H(+)(In) = NAD(+) + CC ubiquinol + 4 H(+)(Out). CC -!- CATALYTIC ACTIVITY: NADH + acceptor = NAD(+) + reduced acceptor. CC -!- COFACTOR: Binds 1 FMN (Potential). CC -!- COFACTOR: Binds 1 4Fe-4S cluster (Potential). CC -!- SUBUNIT: Complex I is composed of 45 different subunits. This is a CC component of the flavoprotein-sulfur (FP) fragment of the enzyme CC (By similarity). CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral CC membrane protein; Matrix side (By similarity). CC -!- SIMILARITY: Belongs to the complex I 51 kDa subunit family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK075692; BAC35893.1; -; mRNA. DR EMBL; BC014818; AAH14818.1; -; mRNA. DR EMBL; BC041682; AAH41682.1; -; mRNA. DR PIR; PC7078; PC7078. DR RefSeq; NP_598427.1; NM_133666.3. DR UniGene; Mm.29842; -. DR ProteinModelPortal; Q91YT0; -. DR SMR; Q91YT0; 38-445. DR BioGrid; 201719; 1. DR IntAct; Q91YT0; 4. DR MINT; MINT-1861002; -. DR STRING; 10090.ENSMUSP00000042967; -. DR PhosphoSite; Q91YT0; -. DR PaxDb; Q91YT0; -. DR PRIDE; Q91YT0; -. DR DNASU; 17995; -. DR Ensembl; ENSMUST00000042497; ENSMUSP00000042967; ENSMUSG00000037916. DR GeneID; 17995; -. DR KEGG; mmu:17995; -. DR UCSC; uc008fye.1; mouse. DR CTD; 4723; -. DR MGI; MGI:107851; Ndufv1. DR eggNOG; COG1894; -. DR GeneTree; ENSGT00390000010641; -. DR HOGENOM; HOG000251534; -. DR HOVERGEN; HBG006542; -. DR InParanoid; Q91YT0; -. DR KO; K03942; -. DR OMA; HFYRHES; -. DR TreeFam; TF300381; -. DR ChiTaRS; NDUFV1; mouse. DR NextBio; 292979; -. DR PRO; PR:Q91YT0; -. DR ArrayExpress; Q91YT0; -. DR Bgee; Q91YT0; -. DR CleanEx; MM_NDUFV1; -. DR Genevestigator; Q91YT0; -. DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:MGI. DR GO; GO:0005747; C:mitochondrial respiratory chain complex I; IEA:Ensembl. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0010181; F:FMN binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:UniProtKB-EC. DR InterPro; IPR001949; NADH-UbQ_OxRdtase_51kDa_CS. DR InterPro; IPR019575; NADH-UbQ_OxRdtase_Fsu_4Fe4S-bd. DR InterPro; IPR011537; NADH-UbQ_OxRdtase_suF. DR InterPro; IPR011538; NADH_UbQ_OxRdtase_51kDa_su. DR InterPro; IPR019554; Soluble_ligand-bd. DR Pfam; PF01512; Complex1_51K; 1. DR Pfam; PF10589; NADH_4Fe-4S; 1. DR Pfam; PF10531; SLBB; 1. DR SMART; SM00928; NADH_4Fe-4S; 1. DR TIGRFAMs; TIGR01959; nuoF_fam; 1. DR PROSITE; PS00644; COMPLEX1_51K_1; 1. DR PROSITE; PS00645; COMPLEX1_51K_2; 1. PE 1: Evidence at protein level; KW 4Fe-4S; Acetylation; Complete proteome; Direct protein sequencing; KW Electron transport; Flavoprotein; FMN; Iron; Iron-sulfur; Membrane; KW Metal-binding; Mitochondrion; Mitochondrion inner membrane; NAD; KW Oxidoreductase; Reference proteome; Respiratory chain; KW Transit peptide; Transport; Ubiquinone. FT TRANSIT 1 20 Mitochondrion. FT CHAIN 21 464 NADH dehydrogenase [ubiquinone] FT flavoprotein 1, mitochondrial. FT /FTId=PRO_0000019978. FT NP_BIND 87 96 NAD(H) (By similarity). FT NP_BIND 199 247 FMN (By similarity). FT METAL 379 379 Iron-sulfur (4Fe-4S) (Potential). FT METAL 382 382 Iron-sulfur (4Fe-4S) (Potential). FT METAL 385 385 Iron-sulfur (4Fe-4S) (Potential). FT METAL 425 425 Iron-sulfur (4Fe-4S) (Potential). FT MOD_RES 81 81 N6-acetyllysine; alternate. FT MOD_RES 81 81 N6-succinyllysine; alternate. FT MOD_RES 104 104 N6-acetyllysine. FT MOD_RES 375 375 N6-acetyllysine. SQ SEQUENCE 464 AA; 50834 MW; 611EAB1546D2A630 CRC64; MLAARHFLGG LVPVRVSVRF SSGTTAPKKT SFGSLKDEDR IFTNLYGRHD WRLKGALRRG DWYKTKEILL KGPDWILGEM KTSGLRGRGG AGFPTGLKWS FMNKPSDGRP KYLVVNADEG EPGTCKDREI MRHDPHKLVE GCLVGGRAMG ARAAYIYIRG EFYNEASNLQ VAIREAYEAG LIGKNACGSD YDFDVFVVRG AGAYICGEET ALIESIEGKQ GKPRLKPPFP ADVGVFGCPT TVANVETVAV SPTICRRGGT WFAGFGRERN SGTKLFNISG HVNHPCTVEE EMSVPLKELI EKHAGGVTGG WDNLLAVIPG GSSTPLIPKS VCETVLMDFD ALVQAQTGLG TAAVIVMDRS TDIVKAIARL IEFYKHESCG QCTPCREGVD WMNKVMARFV KGDARPAEID SLWEISKQIE GHTICALGDG AAWPVQGLIR HFRPELEDRM QRFAQQHRAW QAAS // ID NDUV2_MOUSE Reviewed; 248 AA. AC Q9D6J6; Q3U9L9; Q8BU07; Q8K2L0; DT 16-APR-2002, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2007, sequence version 2. DT 19-MAR-2014, entry version 122. DE RecName: Full=NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial; DE EC=1.6.5.3; DE EC=1.6.99.3; DE AltName: Full=NADH-ubiquinone oxidoreductase 24 kDa subunit; DE Flags: Precursor; GN Name=Ndufv2; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC STRAIN=C57BL/6J, and NOD; RC TISSUE=Bone marrow, Cerebellum, Heart, Hippocampus, and Thymus; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC STRAIN=FVB/N-3; TISSUE=Mammary tumor; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP PROTEIN SEQUENCE OF 42-61; 68-123; 129-153 AND 199-208, AND MASS RP SPECTROMETRY. RC STRAIN=C57BL/6; TISSUE=Brain, and Hippocampus; RA Lubec G., Klug S., Kang S.U.; RL Submitted (APR-2007) to UniProtKB. RN [4] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-60, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23576753; DOI=10.1073/pnas.1302961110; RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., RA Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.; RT "Label-free quantitative proteomics of the lysine acetylome in RT mitochondria identifies substrates of SIRT3 in metabolic pathways."; RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013). CC -!- FUNCTION: Core subunit of the mitochondrial membrane respiratory CC chain NADH dehydrogenase (Complex I) that is believed to belong to CC the minimal assembly required for catalysis. Complex I functions CC in the transfer of electrons from NADH to the respiratory chain. CC The immediate electron acceptor for the enzyme is believed to be CC ubiquinone (By similarity). CC -!- CATALYTIC ACTIVITY: NADH + ubiquinone + 5 H(+)(In) = NAD(+) + CC ubiquinol + 4 H(+)(Out). CC -!- CATALYTIC ACTIVITY: NADH + acceptor = NAD(+) + reduced acceptor. CC -!- COFACTOR: Binds 1 2Fe-2S cluster (Potential). CC -!- SUBUNIT: Complex I is composed of 45 different subunits. This is a CC component of the flavoprotein-sulfur (FP) fragment of the enzyme CC (By similarity). CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane (By CC similarity). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9D6J6-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9D6J6-2; Sequence=VSP_025017; CC -!- SIMILARITY: Belongs to the complex I 24 kDa subunit family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK013511; BAB28888.1; -; mRNA. DR EMBL; AK078351; BAC37233.1; -; mRNA. DR EMBL; AK088193; BAC40201.1; -; mRNA. DR EMBL; AK146998; BAE27595.1; -; mRNA. DR EMBL; AK150404; BAE29530.1; -; mRNA. DR EMBL; AK151729; BAE30647.1; -; mRNA. DR EMBL; AK159460; BAE35102.1; -; mRNA. DR EMBL; AK166539; BAE38841.1; -; mRNA. DR EMBL; AK169143; BAE40922.1; -; mRNA. DR EMBL; BC030946; AAH30946.1; -; mRNA. DR RefSeq; NP_001265344.1; NM_001278415.1. DR RefSeq; NP_082664.1; NM_028388.3. DR UniGene; Mm.2206; -. DR ProteinModelPortal; Q9D6J6; -. DR SMR; Q9D6J6; 62-211. DR BioGrid; 215635; 3. DR IntAct; Q9D6J6; 6. DR MINT; MINT-5107881; -. DR PhosphoSite; Q9D6J6; -. DR REPRODUCTION-2DPAGE; Q9D6J6; -. DR PaxDb; Q9D6J6; -. DR PRIDE; Q9D6J6; -. DR Ensembl; ENSMUST00000024909; ENSMUSP00000024909; ENSMUSG00000024099. [Q9D6J6-2] DR Ensembl; ENSMUST00000143987; ENSMUSP00000121557; ENSMUSG00000024099. [Q9D6J6-1] DR GeneID; 72900; -. DR KEGG; mmu:72900; -. DR UCSC; uc008dgw.1; mouse. [Q9D6J6-1] DR CTD; 4729; -. DR MGI; MGI:1920150; Ndufv2. DR eggNOG; COG1905; -. DR GeneTree; ENSGT00390000017580; -. DR HOVERGEN; HBG029601; -. DR InParanoid; Q9D6J6; -. DR KO; K03943; -. DR OMA; VHRDTPY; -. DR OrthoDB; EOG73JKW9; -. DR TreeFam; TF300004; -. DR ChiTaRS; NDUFV2; mouse. DR NextBio; 337117; -. DR PRO; PR:Q9D6J6; -. DR ArrayExpress; Q9D6J6; -. DR Bgee; Q9D6J6; -. DR CleanEx; MM_NDUFV2; -. DR Genevestigator; Q9D6J6; -. DR GO; GO:0005747; C:mitochondrial respiratory chain complex I; IBA:RefGenome. DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0009055; F:electron carrier activity; IBA:RefGenome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IBA:RefGenome. DR GO; GO:0048738; P:cardiac muscle tissue development; IEA:Ensembl. DR GO; GO:0006120; P:mitochondrial electron transport, NADH to ubiquinone; IBA:RefGenome. DR GO; GO:0007399; P:nervous system development; IEA:Ensembl. DR Gene3D; 3.40.30.10; -; 1. DR InterPro; IPR002023; NuoE-like. DR InterPro; IPR012336; Thioredoxin-like_fold. DR PANTHER; PTHR10371; PTHR10371; 1. DR Pfam; PF01257; 2Fe-2S_thioredx; 1. DR PIRSF; PIRSF000216; NADH_DH_24kDa; 1. DR SUPFAM; SSF52833; SSF52833; 1. DR TIGRFAMs; TIGR01958; nuoE_fam; 1. DR PROSITE; PS01099; COMPLEX1_24K; 1. PE 1: Evidence at protein level; KW 2Fe-2S; Acetylation; Alternative splicing; Complete proteome; KW Direct protein sequencing; Electron transport; Iron; Iron-sulfur; KW Membrane; Metal-binding; Mitochondrion; Mitochondrion inner membrane; KW NAD; Oxidoreductase; Phosphoprotein; Reference proteome; KW Respiratory chain; Transit peptide; Transport; Ubiquinone. FT TRANSIT 1 31 Mitochondrion. FT CHAIN 32 248 NADH dehydrogenase [ubiquinone] FT flavoprotein 2, mitochondrial. FT /FTId=PRO_0000020004. FT METAL 134 134 Iron-sulfur (2Fe-2S) (Potential). FT METAL 139 139 Iron-sulfur (2Fe-2S) (Potential). FT METAL 175 175 Iron-sulfur (2Fe-2S) (Potential). FT METAL 179 179 Iron-sulfur (2Fe-2S) (Potential). FT MOD_RES 60 60 N6-acetyllysine. FT MOD_RES 192 192 Phosphotyrosine; by SRC (By similarity). FT VAR_SEQ 1 96 Missing (in isoform 2). FT /FTId=VSP_025017. FT CONFLICT 64 64 A -> T (in Ref. 1; BAB28888). SQ SEQUENCE 248 AA; 27285 MW; DE0111BE49A1867E CRC64; MFSLALRARA TGLAAQWGRH ARNLHKTAVH NGAGGALFVH RDTPENNPDT PFDFTPENYK RIEAIVKNYP EGHQAAAVLP VLDLAQRQNG WLPISAMNKV AEVLQVPPMR VYEVATFYTM YNRKPVGKYH IQVCTTTPCM LRDSDSILET LQRKLGIKVG ETTPDKLFTL IEVECLGACV NAPMVQINDN YYEDLTPKDI EEIIDELKAG KVPKPGPRSG RFCCEPAGGL TSLTEPPKGP GFGVQAGL // ID NNTM_MOUSE Reviewed; 1086 AA. AC Q61941; Q9JK70; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 16-AUG-2004, sequence version 2. DT 19-MAR-2014, entry version 109. DE RecName: Full=NAD(P) transhydrogenase, mitochondrial; DE EC=1.6.1.2; DE AltName: Full=Nicotinamide nucleotide transhydrogenase; DE AltName: Full=Pyridine nucleotide transhydrogenase; DE Flags: Precursor; GN Name=Nnt; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=C57BL/6 X CBA; TISSUE=Liver; RX PubMed=8616157; DOI=10.1016/0005-2728(95)00159-X; RA Lagberg E.M., Betsholtz C., Rydstrom J.; RT "The cDNA sequence of proton-pumping nicotinamide nucleotide RT transhydrogenase from man and mouse."; RL Biochim. Biophys. Acta 1273:203-205(1996). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=129/SvJ; RX PubMed=11513952; DOI=10.1016/S0167-4781(01)00257-3; RA Arkblad E.L., Betsholtz C., Mandoli D., Rydstrom J.; RT "Characterization of a nicotinamide nucleotide transhydrogenase gene RT from the green alga Acetabularia acetabulum and comparison of its RT structure with those of the corresponding genes in mouse and RT Caenorhabditis elegans."; RL Biochim. Biophys. Acta 1520:115-123(2001). RN [3] RP PROTEIN SEQUENCE OF 72-84; 214-224; 268-279; 367-379; 434-442; 769-777 RP AND 940-949, AND MASS SPECTROMETRY. RC STRAIN=C57BL/6; TISSUE=Brain; RA Lubec G., Kang S.U.; RL Submitted (APR-2007) to UniProtKB. RN [4] RP DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY. RX PubMed=22634753; DOI=10.1038/ng.2299; RA Meimaridou E., Kowalczyk J., Guasti L., Hughes C.R., Wagner F., RA Frommolt P., Nurnberg P., Mann N.P., Banerjee R., Saka H.N., RA Chapple J.P., King P.J., Clark A.J., Metherell L.A.; RT "Mutations in NNT encoding nicotinamide nucleotide transhydrogenase RT cause familial glucocorticoid deficiency."; RL Nat. Genet. 44:740-742(2012). RN [5] RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-117; LYS-224; LYS-294; RP LYS-331 AND LYS-1079, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE RP SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., RA Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). CC -!- FUNCTION: The transhydrogenation between NADH and NADP is coupled CC to respiration and ATP hydrolysis and functions as a proton pump CC across the membrane. May play a role in reactive oxygen species CC (ROS) detoxification in the adrenal gland (By similarity). CC -!- CATALYTIC ACTIVITY: NADPH + NAD(+) = NADP(+) + NADH. CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass CC membrane protein; Matrix side (Potential). CC -!- TISSUE SPECIFICITY: Widely expressed with expression most readily CC detectable in adrenal, heart, kidney, thyroid and adipose tissues. CC -!- DISRUPTION PHENOTYPE: Higher levels of adrenocortical cell CC apoptosis and impaired glucocorticoid production are observed. CC -!- SIMILARITY: In the N-terminal section; belongs to the AlaDH/PNT CC family. CC -!- SIMILARITY: In the C-terminal section; belongs to the PNT beta CC subunit family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; Z49204; CAA89065.1; -; mRNA. DR EMBL; AF257157; AAF72982.2; -; Genomic_DNA. DR EMBL; AF257137; AAF72982.2; JOINED; Genomic_DNA. DR EMBL; AF257138; AAF72982.2; JOINED; Genomic_DNA. DR EMBL; AF257139; AAF72982.2; JOINED; Genomic_DNA. DR EMBL; AF257140; AAF72982.2; JOINED; Genomic_DNA. DR EMBL; AF257141; AAF72982.2; JOINED; Genomic_DNA. DR EMBL; AF257142; AAF72982.2; JOINED; Genomic_DNA. DR EMBL; AF257143; AAF72982.2; JOINED; Genomic_DNA. DR EMBL; AF257144; AAF72982.2; JOINED; Genomic_DNA. DR EMBL; AF257145; AAF72982.2; JOINED; Genomic_DNA. DR EMBL; AF257146; AAF72982.2; JOINED; Genomic_DNA. DR EMBL; AF257147; AAF72982.2; JOINED; Genomic_DNA. DR EMBL; AF257148; AAF72982.2; JOINED; Genomic_DNA. DR EMBL; AF257149; AAF72982.2; JOINED; Genomic_DNA. DR EMBL; AF257150; AAF72982.2; JOINED; Genomic_DNA. DR EMBL; AF257151; AAF72982.2; JOINED; Genomic_DNA. DR EMBL; AF257152; AAF72982.2; JOINED; Genomic_DNA. DR EMBL; AF257153; AAF72982.2; JOINED; Genomic_DNA. DR EMBL; AF257154; AAF72982.2; JOINED; Genomic_DNA. DR EMBL; AF257155; AAF72982.2; JOINED; Genomic_DNA. DR EMBL; AF257156; AAF72982.2; JOINED; Genomic_DNA. DR PIR; S54876; S54876. DR UniGene; Mm.132584; -. DR ProteinModelPortal; Q61941; -. DR SMR; Q61941; 59-439, 902-1083. DR MINT; MINT-1841613; -. DR PhosphoSite; Q61941; -. DR PRIDE; Q61941; -. DR MGI; MGI:109279; Nnt. DR HOVERGEN; HBG006511; -. DR ChiTaRS; NNT; mouse. DR PRO; PR:Q61941; -. DR CleanEx; MM_NNT; -. DR Genevestigator; Q61941; -. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:MGI. DR GO; GO:0008750; F:NAD(P)+ transhydrogenase (AB-specific) activity; IEA:UniProtKB-EC. DR GO; GO:0050661; F:NADP binding; IEA:InterPro. DR GO; GO:0015992; P:proton transport; IEA:InterPro. DR GO; GO:0072593; P:reactive oxygen species metabolic process; ISS:UniProtKB. DR InterPro; IPR008142; Ala_DH/PNT_CS1. DR InterPro; IPR008143; Ala_DH/PNT_CS2. DR InterPro; IPR007886; AlaDH/PNT_N. DR InterPro; IPR007698; AlaDH/PNT_NAD(H)-bd. DR InterPro; IPR012136; NADH_DH_b. DR InterPro; IPR026255; NADP_transhyd_a. DR InterPro; IPR024605; NADP_transhyd_a_C. DR Pfam; PF01262; AlaDh_PNT_C; 1. DR Pfam; PF05222; AlaDh_PNT_N; 1. DR Pfam; PF12769; DUF3814; 1. DR Pfam; PF02233; PNTB; 1. DR SMART; SM01002; AlaDh_PNT_C; 1. DR SMART; SM01003; AlaDh_PNT_N; 1. DR TIGRFAMs; TIGR00561; pntA; 1. DR PROSITE; PS00836; ALADH_PNT_1; 1. DR PROSITE; PS00837; ALADH_PNT_2; 1. PE 1: Evidence at protein level; KW Acetylation; Complete proteome; Direct protein sequencing; Membrane; KW Mitochondrion; Mitochondrion inner membrane; NAD; NADP; KW Oxidoreductase; Reference proteome; Transit peptide; Transmembrane; KW Transmembrane helix. FT TRANSIT 1 43 Mitochondrion (By similarity). FT CHAIN 44 1086 NAD(P) transhydrogenase, mitochondrial. FT /FTId=PRO_0000001056. FT TOPO_DOM 44 474 Mitochondrial matrix. FT TRANSMEM 475 493 Helical; (Potential). FT TRANSMEM 501 521 Helical; (Potential). FT TRANSMEM 527 546 Helical; (Potential). FT TRANSMEM 558 578 Helical; (Potential). FT TOPO_DOM 579 595 Mitochondrial matrix. FT TRANSMEM 596 616 Helical; (Potential). FT TRANSMEM 622 642 Helical; (Potential). FT TRANSMEM 646 666 Helical; (Potential). FT TRANSMEM 672 691 Helical; (Potential). FT TRANSMEM 702 722 Helical; (Potential). FT TOPO_DOM 723 739 Cytoplasmic. FT TRANSMEM 740 760 Helical; (Potential). FT TRANSMEM 778 797 Helical; (Potential). FT TRANSMEM 801 819 Helical; (Potential). FT TRANSMEM 833 853 Helical; (Potential). FT TRANSMEM 857 879 Helical; (Potential). FT TOPO_DOM 880 1086 Mitochondrial matrix. FT NP_BIND 229 259 NAD (By similarity). FT NP_BIND 965 970 NADP (By similarity). FT NP_BIND 1007 1011 NADP (By similarity). FT NP_BIND 1042 1049 NADP (By similarity). FT NP_BIND 1068 1069 NADP (By similarity). FT MOD_RES 70 70 N6-acetyllysine (By similarity). FT MOD_RES 117 117 N6-succinyllysine. FT MOD_RES 224 224 N6-succinyllysine. FT MOD_RES 294 294 N6-succinyllysine. FT MOD_RES 331 331 N6-succinyllysine. FT MOD_RES 397 397 N6-acetyllysine (By similarity). FT MOD_RES 1079 1079 N6-succinyllysine. FT CONFLICT 35 35 T -> M (in Ref. 1; CAA89065). FT CONFLICT 775 775 P -> L (in Ref. 1; CAA89065). FT CONFLICT 813 813 G -> A (in Ref. 1; CAA89065). SQ SEQUENCE 1086 AA; 113838 MW; A023285169834D07 CRC64; MAHLLKTVVA GCSCPFLSNL GSSKVLPGKR DFVRTLRTHQ ALWCKSPVKP GIPYKQLTVG VPKEIFQNEK RVALSPAGVQ ALVKQGFNVV VESGAGEASK FPDDLYRAAG AQIQGMKEVL ASDLVVKVRA PMVNPTLGAH EADFLKPSGT LISFIYPAQN PDLLNKLSER KTTVLAMDQV PRVTIAQGYD ALSSMANISG YKAVVLAANH FGRFFTGQIT AAGKVPPAKI LIVGGGVAGL ASAGAAKSMG AVVRGFDTRA AALEQFKSLG AEPLEVDLKE SGEGQGGYAK EMSKEFIEAE MKLFAQQCKE VDILISTALI PGKKAPVLFS KEMIESMKEG SVVVDLAAEA GGNFETTKPG ELYVHKGITH IGYTDLPSRM ATQASTLYSN NITKLLKAIS PDKDNFHFEV KDDFDFGTMS HVIRGTVVMK DGKVIFPAPT PKNIPEEAPV KPKTVAELEA EKAGTVSMYT KTLTTASVYS AGLTGMLGLG IVAPNVAFSQ MVTTFGLAGI IGYHTVWGVT PALHSPLMSV TNAISGLTAV GGLALMGGHF YPSTTSQSLA ALATFISSVN IAGGFLVTQR MLDMFKRPTD PPEYNYLYLL PGGTFVGGYL AALYGGYNIE EIMYLGSGLC CVGALGGLST QGTARLGNAL GMIGVAGGLA ATLGGLKPDP QLLAQMSGAM AMGGTIGLTI AKRIQISDLP QLVAAFHSLV GLAAVLTCMA EYIVEYPHFA MDATSNFTKI VAYLGTYIGG VTFSGSLVAY GKLQGILKSA PLLLPGRHAL NAGLLAASVG GIIPFMADPS FTTGITCLGS VSGLSTLMGV TLTAAIGGAD MPVVITVLNS YSGWALCAEG FLLNNNLLTI VGALIGSSGA ILSYIMCVAM NRSLANVILG GYGTTSTAGG KPMEISGTHT EINLDNAVEM IREANSIVIT PGYGLCAAKA QYPIADLVKM LTEQGKKVRF GIHPVAGRMP GQLNVLLAEA GVPYDIVLEM DEINSDFPDT DLVLVIGAND TVNSAAQEDP NSIIAGMPVL EVWKSKQVIV MKRSLGVGYA AVDNPIFYKP NTAMLLGDAK KTCDALQAKV RESYQK // ID NO66_MOUSE Reviewed; 603 AA. AC Q9JJF3; B2RQV2; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 19-JAN-2010, sequence version 2. DT 19-FEB-2014, entry version 87. DE RecName: Full=Bifunctional lysine-specific demethylase and histidyl-hydroxylase NO66; DE EC=1.14.11.-; DE EC=1.14.11.27; DE AltName: Full=Histone lysine demethylase NO66; GN Name=No66; Synonyms=Mapjd; ORFNames=MNCb-7109; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6; TISSUE=Brain; RA Osada N., Kusuda J., Tanuma R., Ito A., Hirata M., Sugano S., RA Hashimoto K.; RT "Isolation of full-length cDNA clones from mouse brain cDNA library RT made by oligo-capping method."; RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP SUBCELLULAR LOCATION. RX PubMed=14742713; DOI=10.1091/mbc.E03-08-0623; RA Eilbracht J., Reichenzeller M., Hergt M., Schnoelzer M., Heid H., RA Stoehr M., Franke W.W., Schmidt-Zachmann M.S.; RT "NO66, a highly conserved dual location protein in the nucleolus and RT in a special type of synchronously replicating chromatin."; RL Mol. Biol. Cell 15:1816-1832(2004). RN [5] RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, CATALYTIC ACTIVITY, RP COFACTOR, SUBCELLULAR LOCATION, INTERACTION WITH SP7, AND MUTAGENESIS RP OF HIS-302 AND HIS-367. RX PubMed=19927124; DOI=10.1038/emboj.2009.332; RA Sinha K.M., Yasuda H., Coombes M.M., Dent S.Y., de Crombrugghe B.; RT "Regulation of the osteoblast-specific transcription factor Osterix by RT NO66, a Jumonji family histone demethylase."; RL EMBO J. 29:68-79(2010). CC -!- FUNCTION: Oxygenase that can act as both a histone lysine CC demethylase and a ribosomal histidine hydroxylase Also catalyzes CC the hydroxylation of 60S ribosomal protein L8 on 'His-216'. Acts CC as a regulator of osteoblast differentiation via its interaction CC with SP7/OSX by demethylating H3K4me and H3K36me, thereby CC inhibiting SP7/OSX-mediated promoter activation. May also play a CC role in ribosome biogenesis and in the replication or remodeling CC of certain heterochromatic region. Participates in MYC-induced CC transcriptional activation (By similarity). Specifically CC demethylates 'Lys-4' (H3K4me) and 'Lys-36' (H3K36me) of histone CC H3, thereby playing a central role in histone code. Preferentially CC demethylates trimethylated H3 'Lys-4' (H3K4me3) and monomethylated CC H3 'Lys-4' (H3K4me1) residues, while it has weaker activity for CC dimethylated H3 'Lys-36' (H3K36me2). CC -!- CATALYTIC ACTIVITY: L-histidine-[60S ribosomal protein L8] + 2- CC oxoglutarate + O(2) = (3S)-3-hydroxy-L-histidine-[60S ribosomal CC protein L8] + succinate + CO(2). CC -!- CATALYTIC ACTIVITY: Protein N(6),N(6)-dimethyl-L-lysine + 2- CC oxoglutarate + O(2) = protein N(6)-methyl-L-lysine + succinate + CC formaldehyde + CO(2). CC -!- CATALYTIC ACTIVITY: Protein N(6)-methyl-L-lysine + 2-oxoglutarate CC + O(2) = protein L-lysine + succinate + formaldehyde + CO(2). CC -!- COFACTOR: Binds 1 Fe(2+) ion per subunit. CC -!- SUBUNIT: Interacts with SP7/OSX; the interaction is direct. CC Interacts with PHF19; leading to its recruitment to H3K36me3 CC sites. Interacts with MYC (By similarity). CC -!- INTERACTION: CC Q8VI67:Sp7; NbExp=3; IntAct=EBI-7608809, EBI-7608836; CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus (By similarity). Nucleus, CC nucleoplasm. CC -!- TISSUE SPECIFICITY: Present in developing bones (at protein CC level). Widely but not ubiquitously expressed. CC -!- SIMILARITY: Belongs to the MINA53/NO66 family. NO66 subfamily. CC -!- SIMILARITY: Contains 1 JmjC domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AB041553; BAA95038.1; -; mRNA. DR EMBL; CH466590; EDL02754.1; -; Genomic_DNA. DR EMBL; BC138094; AAI38095.1; -; mRNA. DR RefSeq; NP_076122.2; NM_023633.3. DR UniGene; Mm.251483; -. DR ProteinModelPortal; Q9JJF3; -. DR SMR; Q9JJF3; 144-600. DR IntAct; Q9JJF3; 3. DR MINT; MINT-4130008; -. DR STRING; 10090.ENSMUSP00000057984; -. DR PhosphoSite; Q9JJF3; -. DR PaxDb; Q9JJF3; -. DR PRIDE; Q9JJF3; -. DR Ensembl; ENSMUST00000053744; ENSMUSP00000057984; ENSMUSG00000046791. DR GeneID; 71952; -. DR KEGG; mmu:71952; -. DR UCSC; uc007odz.2; mouse. DR MGI; MGI:1919202; 2410016O06Rik. DR eggNOG; NOG83808; -. DR GeneTree; ENSGT00390000000083; -. DR HOGENOM; HOG000030688; -. DR HOVERGEN; HBG060021; -. DR InParanoid; B2RQV2; -. DR KO; K16914; -. DR OMA; TVENSRV; -. DR OrthoDB; EOG74FF0N; -. DR TreeFam; TF318659; -. DR NextBio; 335036; -. DR PRO; PR:Q9JJF3; -. DR Bgee; Q9JJF3; -. DR CleanEx; MM_2410016O06RIK; -. DR Genevestigator; Q9JJF3; -. DR GO; GO:0005730; C:nucleolus; IDA:MGI. DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0051864; F:histone demethylase activity (H3-K36 specific); IDA:UniProtKB. DR GO; GO:0032453; F:histone demethylase activity (H3-K4 specific); IDA:UniProtKB. DR GO; GO:0005506; F:iron ion binding; IMP:UniProtKB. DR GO; GO:0006338; P:chromatin remodeling; TAS:MGI. DR GO; GO:0045668; P:negative regulation of osteoblast differentiation; IMP:UniProtKB. DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB. DR GO; GO:0042254; P:ribosome biogenesis; TAS:MGI. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR InterPro; IPR003347; JmjC_dom. DR InterPro; IPR013109; NO66/MINA. DR PANTHER; PTHR13096:SF0; PTHR13096:SF0; 1. DR Pfam; PF08007; Cupin_4; 1. DR SMART; SM00558; JmjC; 1. DR PROSITE; PS51184; JMJC; 1. PE 1: Evidence at protein level; KW Acetylation; Chromatin regulator; Complete proteome; Dioxygenase; KW Iron; Metal-binding; Nucleus; Oxidoreductase; Phosphoprotein; KW Reference proteome; Repressor; Transcription; KW Transcription regulation. FT CHAIN 1 603 Bifunctional lysine-specific demethylase FT and histidyl-hydroxylase NO66. FT /FTId=PRO_0000264614. FT DOMAIN 256 401 JmjC. FT METAL 302 302 Iron; catalytic (Probable). FT METAL 304 304 Iron; catalytic (By similarity). FT METAL 367 367 Iron; catalytic (Probable). FT MOD_RES 1 1 N-acetylmethionine (By similarity). FT MOD_RES 91 91 Phosphoserine (By similarity). FT MUTAGEN 302 302 H->A: Loss of demethylase activity. FT MUTAGEN 367 367 H->A: Loss of demethylase activity. FT CONFLICT 410 410 V -> E (in Ref. 1; BAA95038). SQ SEQUENCE 603 AA; 67557 MW; DAB901939874D538 CRC64; MDELPNGNGA ALLKRGRGRR RRHPQSQPRG ASVLALPLRP RKIRRHRKSA AASRVAALRA RALRSEDSDS KVAVASVRGK RKRPAELLEA SRSAEPRPVS ARPRSASATL PSRVEGWAAL SRNLGTAAPP PPGSHADEPG RPRASPLQQV LTELNGIPSS RRRAARLFEW LLAPLPPDHF YRRLWEREAV LVRRQDRSYY EGLFSTADLD SMLRYEDVQF GQHLDAARYV DGRRETLNPP GRALPAAAWS LYRAGCSLRL LCPQAFSPTV WQFLAVLQEQ FGSMAGSNVY LTPPDSQGFA PHYDDIEAFV LQLEGRKLWR VYRPRDPSEE LALTSSPNFS QEDLGEPVLQ TVLEPGDLLY FPRGFIHQAE CQDGVHSLHL TLSTYQRNTW GDFLEAVLPL AVQAAIEENV EFRRGLPRDF MDYMGAQHSD SKDPRRTAFM EKVRVLVARL GHFAPVDAVA DQRAKDFIHD SLPPVLTDRE RALSVHGLPV RWEAGEPVNV GAQLTTETQV HMLQDGVARL VGEGGRLFLY HTVENSRVYH LEEPKCLEIH PQQADAMELL LRSYPEFVRV GDLPCDSVED QLSLATMLYD KGLLLTKTPL VPS // ID NOS1_MOUSE Reviewed; 1429 AA. AC Q9Z0J4; Q3UR10; Q64208; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1999, sequence version 1. DT 19-MAR-2014, entry version 142. DE RecName: Full=Nitric oxide synthase, brain; DE EC=1.14.13.39; DE AltName: Full=Constitutive NOS; DE AltName: Full=NC-NOS; DE AltName: Full=NOS type I; DE AltName: Full=Neuronal NOS; DE Short=N-NOS; DE Short=nNOS; DE AltName: Full=Peptidyl-cysteine S-nitrosylase NOS1; DE AltName: Full=bNOS; GN Name=Nos1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS N-NOS-1 AND N-NOS-2). RC STRAIN=BALB/c; TISSUE=Brain; RX PubMed=7686743; DOI=10.1006/bbrc.1993.1726; RA Ogura T., Yokoyama T., Fujisawa H., Kurashima Y., Esumi H.; RT "Structural diversity of neuronal oxide synthase mRNA in the nervous RT system."; RL Biochem. Biophys. Res. Commun. 193:1014-1022(1993). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM NNOS MU). RC TISSUE=Skeletal muscle; RX PubMed=8626668; DOI=10.1074/jbc.271.19.11204; RA Silvagno F., Xia H., Bredt D.S.; RT "Neuronal nitric-oxide synthase-mu, an alternatively spliced isoform RT expressed in differentiated skeletal muscle."; RL J. Biol. Chem. 271:11204-11208(1996). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1320-1429. RC STRAIN=C57BL/6J; TISSUE=Spinal ganglion; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [4] RP ALTERNATIVE SPLICING (ISOFORMS NNOS BETA; NNOS GAMMA AND NNOS MU). RX PubMed=9208206; RA Brenman J.E., Xia H., Chao D.S., Black S.M., Bredt D.S.; RT "Regulation of neuronal nitric oxide synthase through alternative RT transcripts."; RL Dev. Neurosci. 19:224-231(1997). RN [5] RP INTERACTION WITH DLG4. RX PubMed=10623522; DOI=10.1006/jmbi.1999.3350; RA Tochio H., Hung F., Li M., Bredt D.S., Zhang M.; RT "Solution structure and backbone dynamics of the second PDZ domain of RT postsynaptic density-95."; RL J. Mol. Biol. 295:225-237(2000). RN [6] RP INTERACTION WITH RASD1 AND CAPON. RX PubMed=11086993; DOI=10.1016/S0896-6273(00)00095-7; RA Fang M., Jaffrey S.R., Sawa A., Ye K., Luo X., Snyder S.H.; RT "Dexras1: a G protein specifically coupled to neuronal nitric oxide RT synthase via CAPON."; RL Neuron 28:183-193(2000). RN [7] RP INTERACTION WITH HTR4. RX PubMed=15466885; DOI=10.1242/jcs.01379; RA Joubert L., Hanson B., Barthet G., Sebben M., Claeysen S., Hong W., RA Marin P., Dumuis A., Bockaert J.; RT "New sorting nexin (SNX27) and NHERF specifically interact with the 5- RT HT4a receptor splice variant: roles in receptor targeting."; RL J. Cell Sci. 117:5367-5379(2004). RN [8] RP FUNCTION AS NITROSYLASE. RX PubMed=17293453; DOI=10.1073/pnas.0611620104; RA Mustafa A.K., Kumar M., Selvakumar B., Ho G.P., Ehmsen J.T., RA Barrow R.K., Amzel L.M., Snyder S.H.; RT "Nitric oxide S-nitrosylates serine racemase, mediating feedback RT inhibition of D-serine formation."; RL Proc. Natl. Acad. Sci. U.S.A. 104:2950-2955(2007). RN [9] RP INTERACTION WITH SLC6A4. RX PubMed=17452640; DOI=10.1073/pnas.0610964104; RA Chanrion B., Mannoury la Cour C., Bertaso F., Lerner-Natoli M., RA Freissmuth M., Millan M.J., Bockaert J., Marin P.; RT "Physical interaction between the serotonin transporter and neuronal RT nitric oxide synthase underlies reciprocal modulation of their RT activity."; RL Proc. Natl. Acad. Sci. U.S.A. 104:8119-8124(2007). RN [10] RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 725-747 IN COMPLEX WITH RP CALMODULIN. RA Valentine K.G., Ng H.L., Schneeweis L., Kranz J.K., Frederick K.K., RA Alber T., Wand A.J.; RT "Crystal structure of calmodulin-neuronal nitric oxide synthase RT complex."; RL Submitted (DEC-2006) to the PDB data bank. CC -!- FUNCTION: Produces nitric oxide (NO) which is a messenger molecule CC with diverse functions throughout the body. In the brain and CC peripheral nervous system, NO displays many properties of a CC neurotransmitter. Probably has nitrosylase activity and mediates CC cysteine S-nitrosylation of cytoplasmic target proteins such SRR. CC Isoform NNOS Mu may be an effector enzyme for the dystrophin CC complex. CC -!- CATALYTIC ACTIVITY: 2 L-arginine + 3 NADPH + 4 O(2) = 2 L- CC citrulline + 2 nitric oxide + 3 NADP(+) + 4 H(2)O. CC -!- COFACTOR: Heme group (By similarity). CC -!- COFACTOR: Binds 1 FAD (By similarity). CC -!- COFACTOR: Binds 1 FMN (By similarity). CC -!- COFACTOR: Tetrahydrobiopterin (BH4). May stabilize the dimeric CC form of the enzyme (By similarity). CC -!- ENZYME REGULATION: Stimulated by calcium/calmodulin. Inhibited by CC n-Nos-inhibiting protein (PIN) which may prevent the dimerization CC of the protein. Inhibited by NOSIP (By similarity). CC -!- SUBUNIT: Homodimer. Forms a ternary complex with CAPON and SYN1. CC Interacts with ZDHHC23. Interacts with NOSIP; which may impair its CC synaptic location (By similarity). Interacts with DLG4; the CC interaction possibly being prevented by the association between CC NOS1 and CAPON. Interacts with HTR4. Forms a ternary complex with CC CAPON and RASD1. Interacts with VAC14 (By similarity). Interacts CC (via N-terminus domain) with DLG4 (via N-terminus tandem pair of CC PDZ domains) (By similarity). Interacts with SLC6A4. CC -!- SUBCELLULAR LOCATION: Cell membrane, sarcolemma; Peripheral CC membrane protein. Cell projection, dendritic spine (By CC similarity). Note=In skeletal muscle, it is localized beneath the CC sarcolemma of fast-twitch muscle fiber by associating with the CC dystrophin glycoprotein complex. In neurons, enriched in dendritic CC spines (By similarity). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=5; CC Name=N-NOS-1; CC IsoId=Q9Z0J4-1; Sequence=Displayed; CC Name=N-NOS-2; CC IsoId=Q9Z0J4-2; Sequence=VSP_003578; CC Name=NNOS beta; CC IsoId=Q9Z0J4-3; Sequence=VSP_003575, VSP_003576; CC Name=NNOS gamma; CC IsoId=Q9Z0J4-4; Sequence=VSP_003577; CC Name=NNOS Mu; Synonyms=Muscle-specific; CC IsoId=Q9Z0J4-5; Sequence=VSP_003579; CC -!- TISSUE SPECIFICITY: Widely expressed in the nervous system: CC expressed in cerebrum, olfactory bulb, hippocampus, midbrain, CC cerebellum, pons, medulla oblongata, and spinal cord. Also found CC in skeletal muscle, where it is localized beneath the sarcolemma CC of fast twitch muscle fibers, and in spleen, heart, kidney, and CC liver. N-NOS-1 and N-NOS-2 are found in all parts of the nervous CC system. NNOS beta and gamma occur in a region-specific manner in CC the brain and NNOS beta expression is developmentally regulated. CC NNOS Mu is only found in mature skeletal and cardiac muscles. CC -!- INDUCTION: By cholinergic agonists acting at inositol phosphate- CC linked muscarinic receptors in cardiac myocytes. CC -!- DOMAIN: The PDZ domain in the N-terminal part of the neuronal CC isoform participates in protein-protein interaction, and is CC responsible for targeting nNos to synaptic membranes in muscles. CC Mediates interaction with VAC14 (By similarity). CC -!- PTM: Ubiquitinated; mediated by STUB1/CHIP in the presence of CC Hsp70 and Hsp40 (in vitro) (By similarity). CC -!- DISEASE: Note=In MDX mice (mouse model of dystrophinopathy) the CC dystrophin complex is disrupted and nNOS is displaced from CC sarcolemma and accumulates in the cytosol. CC -!- SIMILARITY: Belongs to the NOS family. CC -!- SIMILARITY: Contains 1 FAD-binding FR-type domain. CC -!- SIMILARITY: Contains 1 flavodoxin-like domain. CC -!- SIMILARITY: Contains 1 PDZ (DHR) domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; D14552; BAA03415.1; -; mRNA. DR EMBL; S81982; AAB36469.1; -; mRNA. DR EMBL; AK141904; BAE24878.1; -; mRNA. DR PIR; JN0609; JN0609. DR RefSeq; NP_032738.1; NM_008712.2. DR RefSeq; XP_006530256.1; XM_006530193.1. DR UniGene; Mm.442195; -. DR UniGene; Mm.44249; -. DR PDB; 2O60; X-ray; 1.55 A; B=725-747. DR PDBsum; 2O60; -. DR ProteinModelPortal; Q9Z0J4; -. DR SMR; Q9Z0J4; 12-126, 298-716, 750-1413. DR BioGrid; 201805; 5. DR DIP; DIP-31556N; -. DR IntAct; Q9Z0J4; 3. DR BindingDB; Q9Z0J4; -. DR ChEMBL; CHEMBL4719; -. DR PhosphoSite; Q9Z0J4; -. DR PaxDb; Q9Z0J4; -. DR PRIDE; Q9Z0J4; -. DR DNASU; 18125; -. DR Ensembl; ENSMUST00000142742; ENSMUSP00000120421; ENSMUSG00000029361. [Q9Z0J4-1] DR Ensembl; ENSMUST00000171055; ENSMUSP00000127432; ENSMUSG00000029361. [Q9Z0J4-1] DR GeneID; 18125; -. DR KEGG; mmu:18125; -. DR UCSC; uc008zfy.2; mouse. [Q9Z0J4-1] DR CTD; 4842; -. DR MGI; MGI:97360; Nos1. DR eggNOG; COG4362; -. DR GeneTree; ENSGT00620000087711; -. DR HOGENOM; HOG000220884; -. DR HOVERGEN; HBG000159; -. DR InParanoid; Q3UR10; -. DR KO; K13240; -. DR OrthoDB; EOG79SDW7; -. DR EvolutionaryTrace; Q9Z0J4; -. DR NextBio; 293344; -. DR PRO; PR:Q9Z0J4; -. DR ArrayExpress; Q9Z0J4; -. DR Bgee; Q9Z0J4; -. DR CleanEx; MM_NOS1; -. DR Genevestigator; Q9Z0J4; -. DR GO; GO:0005856; C:cytoskeleton; IDA:BHF-UCL. DR GO; GO:0005829; C:cytosol; IBA:RefGenome. DR GO; GO:0043197; C:dendritic spine; IEA:UniProtKB-SubCell. DR GO; GO:0045121; C:membrane raft; IDA:MGI. DR GO; GO:0005739; C:mitochondrion; ISO:MGI. DR GO; GO:0042383; C:sarcolemma; IDA:BHF-UCL. DR GO; GO:0016529; C:sarcoplasmic reticulum; IEA:Ensembl. DR GO; GO:0045202; C:synapse; IDA:MGI. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. DR GO; GO:0010181; F:FMN binding; IEA:InterPro. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0050661; F:NADP binding; IEA:InterPro. DR GO; GO:0003958; F:NADPH-hemoprotein reductase activity; IBA:RefGenome. DR GO; GO:0004517; F:nitric-oxide synthase activity; IDA:BHF-UCL. DR GO; GO:0071363; P:cellular response to growth factor stimulus; IMP:BHF-UCL. DR GO; GO:0042738; P:exogenous drug catabolic process; IMP:MGI. DR GO; GO:0033555; P:multicellular organismal response to stress; IEA:Ensembl. DR GO; GO:0045776; P:negative regulation of blood pressure; IBA:RefGenome. DR GO; GO:0051926; P:negative regulation of calcium ion transport; IMP:MGI. DR GO; GO:0051346; P:negative regulation of hydrolase activity; IMP:MGI. DR GO; GO:0043267; P:negative regulation of potassium ion transport; IMP:MGI. DR GO; GO:0051612; P:negative regulation of serotonin uptake; IDA:UniProtKB. DR GO; GO:0006809; P:nitric oxide biosynthetic process; IDA:BHF-UCL. DR GO; GO:0007263; P:nitric oxide mediated signal transduction; IBA:RefGenome. DR GO; GO:0018119; P:peptidyl-cysteine S-nitrosylation; IDA:MGI. DR GO; GO:0031284; P:positive regulation of guanylate cyclase activity; IBA:RefGenome. DR GO; GO:0035066; P:positive regulation of histone acetylation; IMP:BHF-UCL. DR GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IMP:MGI. DR GO; GO:0045909; P:positive regulation of vasodilation; IBA:RefGenome. DR GO; GO:0002028; P:regulation of sodium ion transport; IMP:MGI. DR GO; GO:0009408; P:response to heat; IEA:Ensembl. DR GO; GO:0001666; P:response to hypoxia; IEA:Ensembl. DR GO; GO:0006941; P:striated muscle contraction; IMP:MGI. DR Gene3D; 1.20.990.10; -; 1. DR Gene3D; 3.90.340.10; -; 1. DR InterPro; IPR003097; FAD-binding_1. DR InterPro; IPR017927; Fd_Rdtase_FAD-bd. DR InterPro; IPR001094; Flavdoxin. DR InterPro; IPR008254; Flavodoxin/NO_synth. DR InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase. DR InterPro; IPR023173; NADPH_Cyt_P450_Rdtase_dom3. DR InterPro; IPR004030; NO_synthase_oxygenase_dom. DR InterPro; IPR012144; NOS_euk. DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd. DR InterPro; IPR001478; PDZ. DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl. DR Pfam; PF00667; FAD_binding_1; 1. DR Pfam; PF00258; Flavodoxin_1; 1. DR Pfam; PF00175; NAD_binding_1; 1. DR Pfam; PF02898; NO_synthase; 1. DR Pfam; PF00595; PDZ; 1. DR PIRSF; PIRSF000333; NOS; 1. DR PRINTS; PR00369; FLAVODOXIN. DR PRINTS; PR00371; FPNCR. DR SMART; SM00228; PDZ; 1. DR SUPFAM; SSF50156; SSF50156; 1. DR SUPFAM; SSF56512; SSF56512; 1. DR SUPFAM; SSF63380; SSF63380; 1. DR PROSITE; PS51384; FAD_FR; 1. DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1. DR PROSITE; PS60001; NOS; 1. DR PROSITE; PS50106; PDZ; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Calmodulin-binding; Cell membrane; KW Cell projection; Complete proteome; FAD; Flavoprotein; FMN; Heme; KW Iron; Membrane; Metal-binding; NADP; Oxidoreductase; KW Reference proteome; Ubl conjugation. FT CHAIN 1 1429 Nitric oxide synthase, brain. FT /FTId=PRO_0000170922. FT DOMAIN 17 99 PDZ. FT DOMAIN 755 935 Flavodoxin-like. FT DOMAIN 990 1237 FAD-binding FR-type. FT NP_BIND 881 912 FMN (By similarity). FT NP_BIND 1027 1038 FAD (By similarity). FT NP_BIND 1170 1180 FAD (By similarity). FT NP_BIND 1245 1263 NADP (By similarity). FT NP_BIND 1343 1358 NADP (By similarity). FT REGION 1 200 Interaction with NOSIP (By similarity). FT REGION 163 240 PIN (nNOS-inhibiting protein) binding (By FT similarity). FT REGION 725 745 Calmodulin-binding. FT REGION 750 769 Tetrahydrobiopterin-binding (By FT similarity). FT METAL 415 415 Iron (heme axial ligand) (By similarity). FT VAR_SEQ 1 331 Missing (in isoform NNOS gamma). FT /FTId=VSP_003577. FT VAR_SEQ 1 230 Missing (in isoform NNOS beta). FT /FTId=VSP_003575. FT VAR_SEQ 231 236 TGIQVD -> MRGLGS (in isoform NNOS beta). FT /FTId=VSP_003576. FT VAR_SEQ 504 608 Missing (in isoform N-NOS-2). FT /FTId=VSP_003578. FT VAR_SEQ 839 839 K -> KYPEPLRFFPRKGPSLSHVDSEAHSLVAARDSQHR FT (in isoform NNOS Mu). FT /FTId=VSP_003579. FT CONFLICT 1320 1320 K -> Q (in Ref. 3; BAE24878). FT HELIX 731 744 SQ SEQUENCE 1429 AA; 160472 MW; 3782848D65B41BFC CRC64; MEEHTFGVQQ IQPNVISVRL FKRKVGGLGF LVKERVSKPP VIISDLIRGG AAEQSGLIQA GDIILAVNDR PLVDLSYDSA LEVLRGIASE THVVLILRGP EGFTTHLETT FTGDGTPKTI RVTQPLGTPT KAVDLSRQPS ASKDQPLAVD RVPGPSNGPQ HAQGRGQGAG SVSQANGVAI DPTMKNTKAN LQDSGEQDEL LKEIEPVLSI LTGGGKAVNR GGPAKAEMKD TGIQVDRDLD GKLHKAPPLG GENDRVFNDL WGKGNVPVVL NNPYSENEQS PASGKQSPTK NGSPSRCPRF LKVKNWETDV VLTDTLHLKS TLETGCTEQI CMGSIMLPSH HIRKSEDVRT KDQLFPLAKE FLDQYYSSIK RFGSKAHMDR LEEVNKEIES TSTYQLKDTE LIYGAKHAWR NASRCVGRIQ WSKLQVFDAR DCTTAHGMFN YICNHVKYAT NKGNLRSAIT IFPQRTDGKH DFRVWNSQLI RYAGYKQPDG STLGDPANVE FTEICIQQGW KPPRGRFDVL PLLLQANGND PELFQIPPEL VLEVPIRHPK FDWFKDLGLK WYGLPAVSNM LLEIGGLEFS ACPFSGWYMG TEIGVRDYCD NSRYNILEEV AKKMDLDMRK TSSLWKDQAL VEINIAVLYS FQSDKVTIVD HHSATESFIK HMENEYRCRG GCPADWVWIV PPMSGSITPV FHQEMLNYRL TPSFEYQPDP WNTHVWKGTN GTPTKRRAIG FKKLAEAVKF SAKLMGQAMA KRVKATILYA TETGKSQAYA KTLCEIFKHA FDAKAMSMEE YDIVHLEHEA LVLVVTSTFG NGDPPENGEK FGCALMEMRH PNSVQEERKS YKVRFNSVSS YSDSRKSSGD GPDLRDNFES TGPLANVRFS VFGLGSRAYP HFCAFGHAVD TLLEELGGER ILKMREGDEL CGQEEAFRTW AKKVFKAACD VFCVGDDVNI EKANNSLISN DRSWKRNKFR LTYVAEAPEL TQGLSNVHKK RVSAARLLSR QNLQSPKSSR STIFVRLHTN GNQELQYQPG DHLGVFPGNH EDLVNALIER LEDAPPANHV VKVEMLEERN TALGVISNWK DESRLPPCTI FQAFKYYLDI TTPPTPLQLQ QFASLATNEK EKQRLLVLSK GLQEYEEWKW GKNPTMVEVL EEFPSIQMPA TLLLTQLSLL QPRYYSISSS PDMYPDEVHL TVAIVSYHTR DGEGPVHHGV CSSWLNRIQA DDVVPCFVRG APSFHLPRNP QVPCILVGPG TGIAPFRSFW QQRQFDIQHK GMNPCPMVLV FGCRQSKIDH IYREETLQAK NKGVFRELYT AYSREPDRPK KYVQDVLQEQ LAESVYRALK EQGGHIYVCG DVTMAADVLK AIQRIMTQQG KLSEEDAGVF ISRLRDDNRY HEDIFGVTLR TYEVTNRLRS ESIAFIEESK KDTDEVFSS // ID NOS2_MOUSE Reviewed; 1144 AA. AC P29477; O70515; O70516; Q5SXT3; Q6P6A0; Q8R410; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1993, sequence version 1. DT 19-FEB-2014, entry version 155. DE RecName: Full=Nitric oxide synthase, inducible; DE EC=1.14.13.39; DE AltName: Full=Inducible NO synthase; DE Short=Inducible NOS; DE Short=iNOS; DE AltName: Full=Macrophage NOS; DE Short=MAC-NOS; DE AltName: Full=NOS type II; DE AltName: Full=Peptidyl-cysteine S-nitrosylase NOS2; GN Name=Nos2; Synonyms=Inosl; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=1373522; DOI=10.1126/science.1373522; RA Xie Q.-W., Cho H.J., Calaycay J., Mumford R.A., Swiderek K.M., RA Lee T.D., Ding A., Troso T., Nathan C.; RT "Cloning and characterization of inducible nitric oxide synthase from RT mouse macrophages."; RL Science 256:225-228(1992). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=1379716; DOI=10.1073/pnas.89.15.6711; RA Lowenstein C.J., Glatt C.S., Bredt D.S., Snyder S.H.; RT "Cloned and expressed macrophage nitric oxide synthase contrasts with RT the brain enzyme."; RL Proc. Natl. Acad. Sci. U.S.A. 89:6711-6715(1992). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=1372907; RA Lyons C.R., Orloff G.J., Cunningham J.M.; RT "Molecular cloning and functional expression of an inducible nitric RT oxide synthase from a murine macrophage cell line."; RL J. Biol. Chem. 267:6370-6374(1992). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=7503239; RA Kone B.C., Schwoebel J., Turner P., Mohaupt M.G., Cangro C.B.; RT "Role of NF-kappa B in the regulation of inducible nitric oxide RT synthase in an MTAL cell line."; RL Am. J. Physiol. 269:F718-F729(1995). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS ARG-211; LEU-967 AND PHE-968. RC STRAIN=B10.S/J, BALB/cByJ, DBA/2J, NOD/LtJ, and SJL/J; TISSUE=Spleen; RX PubMed=10438970; RA Teuscher C., Butterfield R.J., Ma R.Z., Zachary J.F., Doerge R.W., RA Blankenhorn E.P.; RT "Sequence polymorphisms in the chemokines Scya1 (TCA-3), Scya2 RT (monocyte chemoattractant protein (MCP)-1), and Scya12 (MCP-5) are RT candidates for eae7, a locus controlling susceptibility to monophasic RT remitting/nonrelapsing experimental allergic encephalomyelitis."; RL J. Immunol. 163:2262-2266(1999). RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=CD-1; RA Coge F., Levacher B., Rique H., Leopold O., Boutin J.A., RA Galizzi J.-P.; RT "Genomic structure of the murine inducible nitric oxide synthase (i- RT NOS) gene."; RL Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=ICR; RA Hagiwara K., Endo Y., Xin H., Takahashi M., Huqun X., Nukiwa T.; RT "Mouse inducible nitric oxide synthase mRNA."; RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=NMRI; TISSUE=Mammary tumor; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [10] RP PROTEIN SEQUENCE OF 733-744, AND MASS SPECTROMETRY. RC STRAIN=OF1; TISSUE=Hippocampus; RA Lubec G., Sunyer B., Chen W.-Q.; RL Submitted (JAN-2009) to UniProtKB. RN [11] RP EFFECT OF ASPIRIN. RC TISSUE=Macrophage; RX PubMed=7544010; DOI=10.1073/pnas.92.17.7926; RA Amin A.R., Vyas P., Attur M., Leszczynska-Piziak J., Patel I.R., RA Weissmann G., Abramson S.B.; RT "The mode of action of aspirin-like drugs: effect on inducible nitric RT oxide synthase."; RL Proc. Natl. Acad. Sci. U.S.A. 92:7926-7930(1995). RN [12] RP FUNCTION AS NITROSYLASE. RX PubMed=16373578; DOI=10.1126/science.1119407; RA Kim S.F., Huri D.A., Snyder S.H.; RT "Inducible nitric oxide synthase binds, S-nitrosylates, and activates RT cyclooxygenase-2."; RL Science 310:1966-1970(2005). RN [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006; RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M., RA Thibault P.; RT "The phagosomal proteome in interferon-gamma-activated macrophages."; RL Immunity 30:143-154(2009). RN [14] RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 116-496. RX PubMed=9334294; DOI=10.1126/science.278.5337.425; RA Crane B.R., Arvai A.S., Gachhui R., Wu C., Ghosh D.K., Getzoff E.D., RA Stuehr D.J., Tainer J.A.; RT "The structure of nitric oxide synthase oxygenase domain and inhibitor RT complexes."; RL Science 278:425-431(1997). RN [15] RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 77-496. RX PubMed=9516116; DOI=10.1126/science.279.5359.2121; RA Crane B.R., Arvai A.S., Ghosh D.K., Wu C., Getzoff E.D., Stuehr D.J., RA Tainer J.A.; RT "Structure of nitric oxide synthase oxygenase dimer with pterin and RT substrate."; RL Science 279:2121-2126(1998). RN [16] RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 77-496. RX PubMed=10562538; DOI=10.1093/emboj/18.22.6260; RA Ghosh D.K., Crane B.R., Ghosh S., Wolan D., Gachhui R., Crooks C., RA Presta A., Tainer J.A., Getzoff E.D., Stuehr D.J.; RT "Inducible nitric oxide synthase: role of the N-terminal beta-hairpin RT hook and pterin-binding segment in dimerization and RT tetrahydrobiopterin interaction."; RL EMBO J. 18:6260-6270(1999). RN [17] RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 77-499. RX PubMed=10562539; DOI=10.1093/emboj/18.22.6271; RA Crane B.R., Rosenfeld R.J., Arvai A.S., Ghosh D.K., Ghosh S., RA Tainer J.A., Stuehr D.J., Getzoff E.D.; RT "N-terminal domain swapping and metal ion binding in nitric oxide RT synthase dimerization."; RL EMBO J. 18:6271-6281(1999). RN [18] RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 77-496. RX PubMed=10769116; DOI=10.1021/bi992409a; RA Crane B.R., Arvai A.S., Ghosh S., Getzoff E.D., Stuehr D.J., RA Tainer J.A.; RT "Structures of the N(omega)-hydroxy-L-arginine complex of inducible RT nitric oxide synthase oxygenase dimer with active and inactive RT pterins."; RL Biochemistry 39:4608-4621(2000). RN [19] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF TRP-457 MUTANTS. RX PubMed=11669619; DOI=10.1021/bi011183k; RA Aoyagi M., Arvai A.S., Ghosh S., Stuehr D.J., Tainer J.A., RA Getzoff E.D.; RT "Structures of tetrahydrobiopterin binding-site mutants of inducible RT nitric oxide synthase oxygenase dimer and implicated roles of RT Trp457."; RL Biochemistry 40:12826-12832(2001). RN [20] RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 77-496. RX PubMed=12437348; DOI=10.1021/bi026313j; RA Rosenfeld R.J., Garcin E.D., Panda K., Andersson G., Aberg A., RA Wallace A.V., Morris G.M., Olson A.J., Stuehr D.J., Tainer J.A., RA Getzoff E.D.; RT "Conformational changes in nitric oxide synthases induced by RT chlorzoxazone and nitroindazoles: crystallographic and computational RT analyses of inhibitor potency."; RL Biochemistry 41:13915-13925(2002). RN [21] RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 77-495. RX PubMed=12464241; DOI=10.1016/S0003-9861(02)00555-6; RA Fedorov R., Ghosh D.K., Schlichting I.; RT "Crystal structures of cyanide complexes of P450cam and the oxygenase RT domain of inducible nitric oxide synthase -- structural models of the RT short-lived oxygen complexes."; RL Arch. Biochem. Biophys. 409:25-31(2003). CC -!- FUNCTION: Produces nitric oxide (NO) which is a messenger molecule CC with diverse functions throughout the body. In macrophages, NO CC mediates tumoricidal and bactericidal actions. Also has CC nitrosylase activity and mediates cysteine S-nitrosylation of CC cytoplasmic target proteins such COX2. CC -!- CATALYTIC ACTIVITY: 2 L-arginine + 3 NADPH + 4 O(2) = 2 L- CC citrulline + 2 nitric oxide + 3 NADP(+) + 4 H(2)O. CC -!- COFACTOR: Heme group. CC -!- COFACTOR: Binds 1 FAD. CC -!- COFACTOR: Binds 1 FMN. CC -!- COFACTOR: Tetrahydrobiopterin (BH4). May stabilize the dimeric CC form of the enzyme. CC -!- ENZYME REGULATION: Not stimulated by calcium/calmodulin. Aspirin CC inhibits expression and function of this enzyme and effects may be CC exerted at the level of translational/post-translational CC modification and directly on the catalytic activity. CC -!- SUBUNIT: Homodimer. Binds SLC9A3R1 (By similarity). CC -!- TISSUE SPECIFICITY: Macrophages. CC -!- INDUCTION: By treatment with endotoxins or cytokines. CC -!- SIMILARITY: Belongs to the NOS family. CC -!- SIMILARITY: Contains 1 FAD-binding FR-type domain. CC -!- SIMILARITY: Contains 1 flavodoxin-like domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M87039; AAA39315.1; -; mRNA. DR EMBL; M92649; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; M84373; AAA39834.1; -; mRNA. DR EMBL; U43428; AAC52356.1; -; mRNA. DR EMBL; AF065919; AAC17914.1; -; mRNA. DR EMBL; AF065920; AAC17915.1; -; mRNA. DR EMBL; AF065921; AAC17916.2; -; mRNA. DR EMBL; AF065922; AAC17917.2; -; mRNA. DR EMBL; AF065923; AAC17918.2; -; mRNA. DR EMBL; AF427516; AAL24076.1; -; Genomic_DNA. DR EMBL; AY090567; AAM11887.1; -; mRNA. DR EMBL; AL592185; CAI25275.1; -; Genomic_DNA. DR EMBL; BC062378; AAH62378.1; -; mRNA. DR PIR; A43271; A43271. DR RefSeq; NP_035057.1; NM_010927.3. DR UniGene; Mm.2893; -. DR PDB; 1DD7; X-ray; 2.25 A; A=114-498. DR PDB; 1DF1; X-ray; 2.35 A; A/B=77-499. DR PDB; 1DWV; X-ray; 2.35 A; A/B=77-496. DR PDB; 1DWW; X-ray; 2.35 A; A/B=77-496. DR PDB; 1DWX; X-ray; 2.60 A; A/B=77-496. DR PDB; 1JWJ; X-ray; 2.60 A; A/B=66-498. DR PDB; 1JWK; X-ray; 2.30 A; A/B=66-498. DR PDB; 1M8D; X-ray; 2.35 A; A/B=65-498. DR PDB; 1M8E; X-ray; 2.90 A; A/B=65-498. DR PDB; 1M8H; X-ray; 2.85 A; A/B=65-498. DR PDB; 1M8I; X-ray; 2.70 A; A/B=65-498. DR PDB; 1M9T; X-ray; 2.40 A; A/B=65-498. DR PDB; 1N2N; X-ray; 2.40 A; A/B=77-495. DR PDB; 1NOC; X-ray; 2.60 A; A=115-498. DR PDB; 1NOD; X-ray; 2.60 A; A/B=77-499. DR PDB; 1NOS; X-ray; 2.10 A; A=115-498. DR PDB; 1QOM; X-ray; 2.70 A; A/B=65-498. DR PDB; 1QW4; X-ray; 2.40 A; A/B=77-495. DR PDB; 1QW5; X-ray; 2.70 A; A/B=77-495. DR PDB; 1R35; X-ray; 2.30 A; A/B=66-498. DR PDB; 1VAF; X-ray; 2.90 A; A/B=77-495. DR PDB; 2BHJ; X-ray; 3.20 A; A=77-498. DR PDB; 2NOD; X-ray; 2.60 A; A/B=77-499. DR PDB; 2NOS; X-ray; 2.30 A; A=115-498. DR PDB; 2ORO; X-ray; 2.00 A; A=114-498. DR PDB; 2ORP; X-ray; 1.97 A; A=114-498. DR PDB; 2ORQ; X-ray; 2.10 A; A=114-498. DR PDB; 2ORR; X-ray; 2.00 A; A=114-498. DR PDB; 2ORS; X-ray; 2.00 A; A=114-498. DR PDB; 2ORT; X-ray; 1.87 A; A=114-498. DR PDB; 2Y37; X-ray; 2.60 A; A/B=66-498. DR PDB; 3DWJ; X-ray; 2.75 A; A/B=66-496. DR PDB; 3E65; X-ray; 2.05 A; A/B=66-498. DR PDB; 3E67; X-ray; 2.60 A; A/B=66-498. DR PDB; 3E68; X-ray; 2.20 A; A/B=66-498. DR PDB; 3E6L; X-ray; 2.30 A; A/B=66-498. DR PDB; 3E6N; X-ray; 2.40 A; A/B=66-498. DR PDB; 3E6O; X-ray; 2.60 A; A/B=66-498. DR PDB; 3E6T; X-ray; 2.50 A; A/B=66-498. DR PDB; 3E7I; X-ray; 2.90 A; A/B=66-498. DR PDB; 3E7M; X-ray; 2.00 A; A/B=66-498. DR PDB; 3E7T; X-ray; 2.60 A; A/B=66-498. DR PDB; 3EAI; X-ray; 2.20 A; A/B=66-498. DR PDB; 3EBD; X-ray; 2.40 A; A/B=66-498. DR PDB; 3EBF; X-ray; 2.29 A; A/B=66-498. DR PDB; 3GOF; X-ray; 1.45 A; C/D=503-518. DR PDB; 3NOD; X-ray; 2.70 A; A/B=77-499. DR PDB; 3NQS; X-ray; 2.20 A; A/B=66-498. DR PDB; 3NW2; X-ray; 2.80 A; A/B=77-499. DR PDBsum; 1DD7; -. DR PDBsum; 1DF1; -. DR PDBsum; 1DWV; -. DR PDBsum; 1DWW; -. DR PDBsum; 1DWX; -. DR PDBsum; 1JWJ; -. DR PDBsum; 1JWK; -. DR PDBsum; 1M8D; -. DR PDBsum; 1M8E; -. DR PDBsum; 1M8H; -. DR PDBsum; 1M8I; -. DR PDBsum; 1M9T; -. DR PDBsum; 1N2N; -. DR PDBsum; 1NOC; -. DR PDBsum; 1NOD; -. DR PDBsum; 1NOS; -. DR PDBsum; 1QOM; -. DR PDBsum; 1QW4; -. DR PDBsum; 1QW5; -. DR PDBsum; 1R35; -. DR PDBsum; 1VAF; -. DR PDBsum; 2BHJ; -. DR PDBsum; 2NOD; -. DR PDBsum; 2NOS; -. DR PDBsum; 2ORO; -. DR PDBsum; 2ORP; -. DR PDBsum; 2ORQ; -. DR PDBsum; 2ORR; -. DR PDBsum; 2ORS; -. DR PDBsum; 2ORT; -. DR PDBsum; 2Y37; -. DR PDBsum; 3DWJ; -. DR PDBsum; 3E65; -. DR PDBsum; 3E67; -. DR PDBsum; 3E68; -. DR PDBsum; 3E6L; -. DR PDBsum; 3E6N; -. DR PDBsum; 3E6O; -. DR PDBsum; 3E6T; -. DR PDBsum; 3E7I; -. DR PDBsum; 3E7M; -. DR PDBsum; 3E7T; -. DR PDBsum; 3EAI; -. DR PDBsum; 3EBD; -. DR PDBsum; 3EBF; -. DR PDBsum; 3GOF; -. DR PDBsum; 3NOD; -. DR PDBsum; 3NQS; -. DR PDBsum; 3NW2; -. DR ProteinModelPortal; P29477; -. DR SMR; P29477; 77-497, 505-1126. DR BioGrid; 201806; 6. DR DIP; DIP-31080N; -. DR IntAct; P29477; 1. DR MINT; MINT-202500; -. DR BindingDB; P29477; -. DR ChEMBL; CHEMBL3464; -. DR PhosphoSite; P29477; -. DR PRIDE; P29477; -. DR Ensembl; ENSMUST00000018610; ENSMUSP00000018610; ENSMUSG00000020826. DR GeneID; 18126; -. DR KEGG; mmu:18126; -. DR UCSC; uc007kkc.1; mouse. DR CTD; 4843; -. DR MGI; MGI:97361; Nos2. DR eggNOG; COG4362; -. DR GeneTree; ENSGT00620000087711; -. DR HOGENOM; HOG000220884; -. DR HOVERGEN; HBG000159; -. DR InParanoid; P29477; -. DR KO; K13241; -. DR OMA; KFTNSPT; -. DR OrthoDB; EOG79SDW7; -. DR TreeFam; TF324410; -. DR EvolutionaryTrace; P29477; -. DR NextBio; 293348; -. DR PRO; PR:P29477; -. DR Bgee; P29477; -. DR CleanEx; MM_NOS2; -. DR Genevestigator; P29477; -. DR GO; GO:0030863; C:cortical cytoskeleton; IDA:MGI. DR GO; GO:0005829; C:cytosol; TAS:UniProtKB. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:MGI. DR GO; GO:0005777; C:peroxisome; IEA:Ensembl. DR GO; GO:0034618; F:arginine binding; IDA:BHF-UCL. DR GO; GO:0005516; F:calmodulin binding; TAS:UniProtKB. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IDA:BHF-UCL. DR GO; GO:0010181; F:FMN binding; IDA:BHF-UCL. DR GO; GO:0020037; F:heme binding; IDA:BHF-UCL. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0050661; F:NADP binding; IEA:InterPro. DR GO; GO:0003958; F:NADPH-hemoprotein reductase activity; IBA:RefGenome. DR GO; GO:0004517; F:nitric-oxide synthase activity; IDA:BHF-UCL. DR GO; GO:0042803; F:protein homodimerization activity; IDA:BHF-UCL. DR GO; GO:0034617; F:tetrahydrobiopterin binding; IDA:BHF-UCL. DR GO; GO:0006527; P:arginine catabolic process; IDA:BHF-UCL. DR GO; GO:0071346; P:cellular response to interferon-gamma; IDA:MGI. DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IDA:MGI. DR GO; GO:0042742; P:defense response to bacterium; IMP:MGI. DR GO; GO:0006954; P:inflammatory response; TAS:UniProtKB. DR GO; GO:0045776; P:negative regulation of blood pressure; IBA:RefGenome. DR GO; GO:0010629; P:negative regulation of gene expression; IGI:UniProtKB. DR GO; GO:0042177; P:negative regulation of protein catabolic process; IDA:BHF-UCL. DR GO; GO:0006809; P:nitric oxide biosynthetic process; IDA:BHF-UCL. DR GO; GO:0007263; P:nitric oxide mediated signal transduction; IBA:RefGenome. DR GO; GO:0018119; P:peptidyl-cysteine S-nitrosylation; IDA:UniProtKB. DR GO; GO:0031284; P:positive regulation of guanylate cyclase activity; IBA:RefGenome. DR GO; GO:0051712; P:positive regulation of killing of cells of other organism; IEA:Ensembl. DR GO; GO:0045909; P:positive regulation of vasodilation; IBA:RefGenome. DR GO; GO:0042127; P:regulation of cell proliferation; IGI:MGI. DR GO; GO:0050796; P:regulation of insulin secretion; IEA:Ensembl. DR GO; GO:0001666; P:response to hypoxia; IDA:MGI. DR GO; GO:0006801; P:superoxide metabolic process; IMP:MGI. DR Gene3D; 1.20.990.10; -; 1. DR Gene3D; 3.90.340.10; -; 1. DR InterPro; IPR003097; FAD-binding_1. DR InterPro; IPR017927; Fd_Rdtase_FAD-bd. DR InterPro; IPR001094; Flavdoxin. DR InterPro; IPR008254; Flavodoxin/NO_synth. DR InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase. DR InterPro; IPR023173; NADPH_Cyt_P450_Rdtase_dom3. DR InterPro; IPR004030; NO_synthase_oxygenase_dom. DR InterPro; IPR012144; NOS_euk. DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd. DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl. DR PANTHER; PTHR19384:SF5; PTHR19384:SF5; 1. DR Pfam; PF00667; FAD_binding_1; 1. DR Pfam; PF00258; Flavodoxin_1; 1. DR Pfam; PF00175; NAD_binding_1; 1. DR Pfam; PF02898; NO_synthase; 1. DR PIRSF; PIRSF000333; NOS; 1. DR PRINTS; PR00369; FLAVODOXIN. DR PRINTS; PR00371; FPNCR. DR SUPFAM; SSF56512; SSF56512; 1. DR SUPFAM; SSF63380; SSF63380; 1. DR PROSITE; PS51384; FAD_FR; 1. DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1. DR PROSITE; PS60001; NOS; 1. PE 1: Evidence at protein level; KW 3D-structure; Calmodulin-binding; Complete proteome; KW Direct protein sequencing; FAD; Flavoprotein; FMN; Heme; Iron; KW Metal-binding; NADP; Oxidoreductase; Polymorphism; Reference proteome; KW Zinc. FT CHAIN 1 1144 Nitric oxide synthase, inducible. FT /FTId=PRO_0000170934. FT DOMAIN 533 671 Flavodoxin-like. FT DOMAIN 724 964 FAD-binding FR-type. FT NP_BIND 617 648 FMN (By similarity). FT NP_BIND 761 772 FAD (By similarity). FT NP_BIND 897 907 FAD (By similarity). FT NP_BIND 972 990 NADP (By similarity). FT NP_BIND 1070 1085 NADP (By similarity). FT REGION 503 523 Calmodulin-binding (Potential). FT METAL 104 104 Zinc. FT METAL 109 109 Zinc. FT METAL 194 194 Iron (heme axial ligand). FT VARIANT 211 211 C -> R (in strain: NOD/LtJ). FT VARIANT 967 967 P -> L (in strain: SJL/J). FT VARIANT 968 968 S -> F (in strain: BALB/CBYJ). FT CONFLICT 19 19 K -> T (in Ref. 4; AAC52356). FT CONFLICT 72 72 T -> TP (in Ref. 7; AAM11887 and 9; FT AAH62378). FT CONFLICT 191 191 A -> V (in Ref. 2; M92649). FT CONFLICT 245 245 S -> T (in Ref. 7; AAM11887 and 9; FT AAH62378). FT CONFLICT 844 844 A -> G (in Ref. 2; M92649). FT CONFLICT 1075 1075 I -> V (in Ref. 9; AAH62378). FT STRAND 79 83 FT TURN 84 86 FT STRAND 89 92 FT HELIX 94 97 FT STRAND 103 107 FT HELIX 117 119 FT HELIX 130 146 FT TURN 147 150 FT HELIX 153 170 FT HELIX 177 189 FT HELIX 195 199 FT STRAND 204 207 FT HELIX 208 210 FT HELIX 214 229 FT HELIX 230 232 FT STRAND 237 240 FT STRAND 245 249 FT STRAND 255 259 FT STRAND 263 265 FT STRAND 267 269 FT STRAND 271 273 FT HELIX 275 277 FT HELIX 278 286 FT STRAND 294 296 FT STRAND 301 304 FT STRAND 311 313 FT HELIX 317 319 FT STRAND 322 324 FT HELIX 332 334 FT TURN 335 337 FT STRAND 339 342 FT STRAND 350 353 FT STRAND 356 359 FT HELIX 369 373 FT HELIX 375 378 FT TURN 380 383 FT HELIX 386 392 FT HELIX 400 402 FT HELIX 415 422 FT HELIX 430 442 FT HELIX 455 458 FT STRAND 461 463 FT HELIX 464 466 FT HELIX 468 471 FT STRAND 480 485 FT HELIX 489 492 FT HELIX 509 517 SQ SEQUENCE 1144 AA; 130575 MW; 0735BE676113457F CRC64; MACPWKFLFK VKSYQSDLKE EKDINNNVKK TPCAVLSPTI QDDPKSHQNG SPQLLTGTAQ NVPESLDKLH VTSTRPQYVR IKNWGSGEIL HDTLHHKATS DFTCKSKSCL GSIMNPKSLT RGPRDKPTPL EELLPHAIEF INQYYGSFKE AKIEEHLARL EAVTKEIETT GTYQLTLDEL IFATKMAWRN APRCIGRIQW SNLQVFDARN CSTAQEMFQH ICRHILYATN NGNIRSAITV FPQRSDGKHD FRLWNSQLIR YAGYQMPDGT IRGDAATLEF TQLCIDLGWK PRYGRFDVLP LVLQADGQDP EVFEIPPDLV LEVTMEHPKY EWFQELGLKW YALPAVANML LEVGGLEFPA CPFNGWYMGT EIGVRDFCDT QRYNILEEVG RRMGLETHTL ASLWKDRAVT EINVAVLHSF QKQNVTIMDH HTASESFMKH MQNEYRARGG CPADWIWLVP PVSGSITPVF HQEMLNYVLS PFYYYQIEPW KTHIWQNEKL RPRRREIRFR VLVKVVFFAS MLMRKVMASR VRATVLFATE TGKSEALARD LATLFSYAFN TKVVCMDQYK ASTLEEEQLL LVVTSTFGNG DCPSNGQTLK KSLFMLRELN HTFRYAVFGL GSSMYPQFCA FAHDIDQKLS HLGASQLAPT GEGDELSGQE DAFRSWAVQT FRAACETFDV RSKHHIQIPK RFTSNATWEP QQYRLIQSPE PLDLNRALSS IHAKNVFTMR LKSQQNLQSE KSSRTTLLVQ LTFEGSRGPS YLPGEHLGIF PGNQTALVQG ILERVVDCPT PHQTVCLEVL DESGSYWVKD KRLPPCSLSQ ALTYFLDITT PPTQLQLHKL ARFATDETDR QRLEALCQPS EYNDWKFSNN PTFLEVLEEF PSLHVPAAFL LSQLPILKPR YYSISSSQDH TPSEVHLTVA VVTYRTRDGQ GPLHHGVCST WIRNLKPQDP VPCFVRSVSG FQLPEDPSQP CILIGPGTGI APFRSFWQQR LHDSQHKGLK GGRMSLVFGC RHPEEDHLYQ EEMQEMVRKR VLFQVHTGYS RLPGKPKVYV QDILQKQLAN EVLSVLHGEQ GHLYICGDVR MARDVATTLK KLVATKLNLS EEQVEDYFFQ LKSQKRYHED IFGAVFSYGA KKGSALEEPK ATRL // ID NOS3_MOUSE Reviewed; 1202 AA. AC P70313; O55056; Q7TSV7; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 4. DT 19-MAR-2014, entry version 145. DE RecName: Full=Nitric oxide synthase, endothelial; DE EC=1.14.13.39; DE AltName: Full=Constitutive NOS; DE Short=cNOS; DE AltName: Full=EC-NOS; DE AltName: Full=Endothelial NOS; DE Short=eNOS; DE AltName: Full=NOS type III; DE Short=NOSIII; GN Name=Nos3; Synonyms=Ecnos; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Fetal heart; RX PubMed=8764825; DOI=10.1016/0167-4781(96)00098-X; RA Gnanapandithen K., Chen Z., Kau C.-L., Gorczynski R.M., Marsden P.A.; RT "Cloning and characterization of murine endothelial constitutive RT nitric oxide synthase."; RL Biochim. Biophys. Acta 1308:103-106(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Colon; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-54, AND FUNCTION. RX PubMed=9843834; RA Gregg A.R., Schauer A., Shi O., Liu Z., Lee C.G.L., O'Brien W.E.; RT "Limb reduction defects in endothelial nitric oxide synthase-deficient RT mice."; RL Am. J. Physiol. 275:H2319-H2324(1998). RN [4] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1174, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=17242355; DOI=10.1073/pnas.0609836104; RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; RT "Large-scale phosphorylation analysis of mouse liver."; RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). CC -!- FUNCTION: Produces nitric oxide (NO) which is implicated in CC vascular smooth muscle relaxation through a cGMP-mediated signal CC transduction pathway. NO mediates vascular endothelial growth CC factor (VEGF)-induced angiogenesis in coronary vessels and CC promotes blood clotting through the activation of platelets. May CC play a significant role in normal and abnormal limb development. CC -!- CATALYTIC ACTIVITY: 2 L-arginine + 3 NADPH + 4 O(2) = 2 L- CC citrulline + 2 nitric oxide + 3 NADP(+) + 4 H(2)O. CC -!- COFACTOR: Heme group. CC -!- COFACTOR: Binds 1 FAD. CC -!- COFACTOR: Binds 1 FMN. CC -!- COFACTOR: Tetrahydrobiopterin (BH4). May stabilize the dimeric CC form of the enzyme. CC -!- ENZYME REGULATION: Stimulated by calcium/calmodulin. Inhibited by CC NOSIP and NOSTRIN (By similarity). CC -!- SUBUNIT: Homodimer. Interacts with NOSIP and NOSTRIN (By CC similarity). CC -!- SUBCELLULAR LOCATION: Membrane, caveola (By similarity). CC Cytoplasm, cytoskeleton (By similarity). Golgi apparatus (By CC similarity). Cell membrane (By similarity). Note=Specifically CC associates with actin cytoskeleton in the G2 phase of the cell CC cycle, which is favored by interaction with NOSIP and results in a CC reduced enzymatic activity (By similarity). CC -!- PTM: Phosphorylation by AMPK at Ser-1176 in the presence of CC Ca(2+)-calmodulin (CaM) activates activity. In absence of Ca(2+)- CC calmodulin, AMPK also phosphorylates Thr-494, resulting in CC inhibition of activity (By similarity). CC -!- SIMILARITY: Belongs to the NOS family. CC -!- SIMILARITY: Contains 1 FAD-binding FR-type domain. CC -!- SIMILARITY: Contains 1 flavodoxin-like domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U53142; AAC52766.1; -; mRNA. DR EMBL; BC052636; AAH52636.1; -; mRNA. DR EMBL; AF045940; AAC02553.1; -; Genomic_DNA. DR PIR; S71424; S71424. DR RefSeq; NP_032739.3; NM_008713.4. DR UniGene; Mm.258415; -. DR ProteinModelPortal; P70313; -. DR SMR; P70313; 66-480, 491-1176. DR BioGrid; 201807; 1. DR DIP; DIP-31086N; -. DR IntAct; P70313; 1. DR STRING; 10090.ENSMUSP00000030834; -. DR BindingDB; P70313; -. DR ChEMBL; CHEMBL2643; -. DR PhosphoSite; P70313; -. DR PaxDb; P70313; -. DR PRIDE; P70313; -. DR Ensembl; ENSMUST00000030834; ENSMUSP00000030834; ENSMUSG00000028978. DR GeneID; 18127; -. DR KEGG; mmu:18127; -. DR UCSC; uc008wrd.2; mouse. DR CTD; 4846; -. DR MGI; MGI:97362; Nos3. DR eggNOG; COG4362; -. DR GeneTree; ENSGT00620000087711; -. DR HOGENOM; HOG000220884; -. DR HOVERGEN; HBG000159; -. DR InParanoid; Q7TSV7; -. DR KO; K13242; -. DR OMA; WGKLQVF; -. DR OrthoDB; EOG79SDW7; -. DR TreeFam; TF324410; -. DR NextBio; 293352; -. DR PRO; PR:P70313; -. DR ArrayExpress; P70313; -. DR Bgee; P70313; -. DR CleanEx; MM_NOS3; -. DR Genevestigator; P70313; -. DR GO; GO:0005901; C:caveola; IEA:UniProtKB-SubCell. DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell. DR GO; GO:0005829; C:cytosol; IBA:RefGenome. DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell. DR GO; GO:0005634; C:nucleus; IDA:MGI. DR GO; GO:0034618; F:arginine binding; IEA:Ensembl. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. DR GO; GO:0010181; F:FMN binding; IEA:InterPro. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0050661; F:NADP binding; IEA:InterPro. DR GO; GO:0003958; F:NADPH-hemoprotein reductase activity; IBA:RefGenome. DR GO; GO:0004517; F:nitric-oxide synthase activity; IMP:MGI. DR GO; GO:0034617; F:tetrahydrobiopterin binding; IEA:Ensembl. DR GO; GO:0001525; P:angiogenesis; IMP:MGI. DR GO; GO:0006527; P:arginine catabolic process; IEA:Ensembl. DR GO; GO:0001974; P:blood vessel remodeling; IMP:BHF-UCL. DR GO; GO:0043542; P:endothelial cell migration; IEA:Ensembl. DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI. DR GO; GO:0031663; P:lipopolysaccharide-mediated signaling pathway; IMP:MGI. DR GO; GO:0030324; P:lung development; IMP:MGI. DR GO; GO:0045776; P:negative regulation of blood pressure; IBA:RefGenome. DR GO; GO:0051926; P:negative regulation of calcium ion transport; IMP:MGI. DR GO; GO:0008285; P:negative regulation of cell proliferation; IMP:BHF-UCL. DR GO; GO:0051346; P:negative regulation of hydrolase activity; IMP:MGI. DR GO; GO:0014740; P:negative regulation of muscle hyperplasia; IMP:BHF-UCL. DR GO; GO:0043267; P:negative regulation of potassium ion transport; IMP:MGI. DR GO; GO:0006809; P:nitric oxide biosynthetic process; IMP:MGI. DR GO; GO:0007263; P:nitric oxide mediated signal transduction; IBA:RefGenome. DR GO; GO:0001542; P:ovulation from ovarian follicle; IMP:MGI. DR GO; GO:0045766; P:positive regulation of angiogenesis; IMP:BHF-UCL. DR GO; GO:0031284; P:positive regulation of guanylate cyclase activity; IBA:RefGenome. DR GO; GO:0045909; P:positive regulation of vasodilation; IBA:RefGenome. DR GO; GO:0050880; P:regulation of blood vessel size; IMP:BHF-UCL. DR GO; GO:0002028; P:regulation of sodium ion transport; IMP:MGI. DR GO; GO:0003100; P:regulation of systemic arterial blood pressure by endothelin; IEA:Ensembl. DR GO; GO:0003057; P:regulation of the force of heart contraction by chemical signal; IGI:MGI. DR GO; GO:0034405; P:response to fluid shear stress; IEA:Ensembl. DR GO; GO:0014806; P:smooth muscle hyperplasia; IMP:BHF-UCL. DR Gene3D; 1.20.990.10; -; 1. DR Gene3D; 3.90.340.10; -; 1. DR InterPro; IPR003097; FAD-binding_1. DR InterPro; IPR017927; Fd_Rdtase_FAD-bd. DR InterPro; IPR001094; Flavdoxin. DR InterPro; IPR008254; Flavodoxin/NO_synth. DR InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase. DR InterPro; IPR023173; NADPH_Cyt_P450_Rdtase_dom3. DR InterPro; IPR004030; NO_synthase_oxygenase_dom. DR InterPro; IPR012144; NOS_euk. DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd. DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl. DR PANTHER; PTHR19384:SF5; PTHR19384:SF5; 1. DR Pfam; PF00667; FAD_binding_1; 1. DR Pfam; PF00258; Flavodoxin_1; 1. DR Pfam; PF00175; NAD_binding_1; 1. DR Pfam; PF02898; NO_synthase; 1. DR PIRSF; PIRSF000333; NOS; 1. DR PRINTS; PR00369; FLAVODOXIN. DR PRINTS; PR00371; FPNCR. DR SUPFAM; SSF56512; SSF56512; 1. DR SUPFAM; SSF63380; SSF63380; 1. DR PROSITE; PS51384; FAD_FR; 1. DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1. DR PROSITE; PS60001; NOS; 1. PE 1: Evidence at protein level; KW Calcium; Calmodulin-binding; Cell membrane; Complete proteome; KW Cytoplasm; Cytoskeleton; FAD; Flavoprotein; FMN; Golgi apparatus; KW Heme; Iron; Lipoprotein; Membrane; Metal-binding; Myristate; NADP; KW Oxidoreductase; Palmitate; Phosphoprotein; Reference proteome; Zinc. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 1202 Nitric oxide synthase, endothelial. FT /FTId=PRO_0000170944. FT DOMAIN 519 702 Flavodoxin-like. FT DOMAIN 755 1001 FAD-binding FR-type. FT NP_BIND 648 679 FMN (By similarity). FT NP_BIND 792 803 FAD (By similarity). FT NP_BIND 934 944 FAD (By similarity). FT NP_BIND 1009 1027 NADP (By similarity). FT NP_BIND 1107 1122 NADP (By similarity). FT REGION 97 485 Interaction with NOSIP (By similarity). FT REGION 490 509 Calmodulin-binding (Potential). FT COMPBIAS 31 68 Pro-rich. FT METAL 93 93 Zinc (By similarity). FT METAL 98 98 Zinc (By similarity). FT METAL 183 183 Iron (heme axial ligand) (By similarity). FT MOD_RES 140 140 Phosphoserine (By similarity). FT MOD_RES 494 494 Phosphothreonine; by AMPK (By FT similarity). FT MOD_RES 632 632 Phosphoserine (By similarity). FT MOD_RES 1174 1174 Phosphothreonine. FT MOD_RES 1176 1176 Phosphoserine; by AMPK (Probable). FT LIPID 2 2 N-myristoyl glycine (By similarity). FT LIPID 15 15 S-palmitoyl cysteine (By similarity). FT LIPID 26 26 S-palmitoyl cysteine (By similarity). FT CONFLICT 50 50 P -> A (in Ref. 1; AAC52766). FT CONFLICT 298 298 P -> S (in Ref. 1; AAC52766). SQ SEQUENCE 1202 AA; 132916 MW; E1F65C43601F0937 CRC64; MGNLKSVGQE PGPPCGLGLG LGLGLCGKQG PASPAPEPSQ APAPPSPTRP APDHSPPLTR PPDGPRFPRV KNWEVGSITY DTLSAQAQQD GPCTSRRCLG SLVFPRKLQS RPTQGPSPTE QLLGQARDFI NQYYNSIKRS GSQAHEQRLQ EVEAEVAATG TYQLRESELV FGAKQAWRNA PRCVGRIQWG KLQVFDARDC RTAQEMFTYI CNHIKYATNR GNLRSAITVF PQRCPGRGDF RIWNSQLIRY AGYRQQDGSV RGDPANVEIT ELCIQHGWTP GNGRFDVLPL LLQAPDEPPE LFTLPPEMVL EVPLEHPTLE WFAALGLRWY ALPAVSNMLL EIGGLEFPAA PFSGWYMSSE IGMRDLCDPH RYNILEDVAV CMDLDTRTTS SLWKDKAAVE INVAVLHSYQ LAKVTIVDHH AATASFMKHL ENEQKARGGC PADWAWIVPP ISGSLTPVFH QEMVNYFLSP AFRYQPDPWK GSAAKGAGIT RKKTFKEVAN AVKISASLMG TVMAKRVKAT ILYGSETGRA QSYAQQLGRL FRKAFDPRVL CMDEYDVVSL EHEALVLVVT STFGNGDPPE NGESFAAALM EMSGPYNSSP RPEQHKSYKI RFNSVSCSDP LVSSWRRKRK ESSNTDSAGA LGTLRFCVFG LGSRAYPHFC AFARAVDTRL EELGGERLLQ LGQGDELCGQ EEAFRGWAQA AFQAACETFC VGEDAKAAAR DIFSPKRSWK RQRYRLSTQA ESLQLLPGLT HVHRRKMFQA TILSVENLQS SKSTRATILV RLDTGGQEGL QYQPGDHIGV CPPNRPGLVE ALLSRVEDPP PSTEPVAVEQ LEKGSPGGPP PGWVRDPRLP PCTLRQALTY FLDITSPPSP RLLRLLSTLA EESSEQQELE ALSQDPRRYE EWKWFSCPTL LEVLEQFPSV ALPAPLILTQ LPLLQPRYYS VSSAPSAHPG EIHLTIAVLA YRTQDGLGPL HYGVCSTWMS QLKAGDPVPC FIRGAPSFRL PPDPNLPCIL VGPGTGIAPF RGFWQDRLHD IEIKGLQPAP MTLVFGCRCS QLDHLYRDEV LDAQQRGVFG QVLTAFSRDP GSPKTYVQDL LRTELAAEVH RVLCLEQGHM FVCGDVTMAT SVLQTVQRIL ATEGGMELDE AGDVIGVLRD QQRYHEDIFG LTLRTQEVTS RIRTQSFSLQ ERQLRGAVPW SFDPPGPEIP GS // ID NOX3_MOUSE Reviewed; 568 AA. AC Q672J9; Q6Y4Q8; DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot. DT 21-MAR-2006, sequence version 2. DT 19-FEB-2014, entry version 67. DE RecName: Full=NADPH oxidase 3; DE EC=1.6.3.-; GN Name=Nox3; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, MUTAGENESIS OF GLY-408 AND RP LYS-542, AND DISRUPTION PHENOTYPE. RC STRAIN=C3Heb/FeJ; RX PubMed=15014044; DOI=10.1101/gad.1172504; RA Paffenholz R., Bergstrom R.A., Pasutto F., Wabnitz P., Munroe R.J., RA Jagla W., Heinzmann U., Marquardt A., Bareiss A., Laufs J., Russ A., RA Stumm G., Schimenti J.C., Bergstrom D.E.; RT "Vestibular defects in head-tilt mice result from mutations in Nox3, RT encoding an NADPH oxidase."; RL Genes Dev. 18:486-491(2004). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DEVELOPMENTAL STAGE, TISSUE RP SPECIFICITY, AND ENZYME REGULATION. RC STRAIN=C57BL/6; TISSUE=Inner ear; RX PubMed=15326186; DOI=10.1074/jbc.M403046200; RA Banfi B., Malgrange B., Knisz J., Steger K., Dubois-Dauphin M., RA Krause K.-H.; RT "NOX3, a superoxide-generating NADPH oxidase of the inner ear."; RL J. Biol. Chem. 279:46065-46072(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: NADPH oxidase which constitutively produces superoxide CC upon formation of a complex with CYBA/p22phox. Plays a role in the CC biogenesis of otoconia/otolith, which are crystalline structures CC of the inner ear involved in the perception of gravity. CC -!- ENZYME REGULATION: Activated by the ototoxic drug cisplatin. CC Activated by NOXO1. Cooperatively activated by NCF1 and NCF2 or CC NOXA1 in a phorbol 12-myristate 13-acetate (PMA)-dependent manner. CC Inhibited by diphenyleneiodonium chloride. CC -!- SUBUNIT: Interacts with and stabilizes CYBA/p22phox. CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein CC (Potential). CC -!- TISSUE SPECIFICITY: Specifically expressed in inner ear by the CC spiral glanglion neurons, the vestibular system and the sensory CC epithelial cell layer of the saccule. Weakly expressed in skull CC and brain. CC -!- DEVELOPMENTAL STAGE: Expressed in fetal kidney. CC -!- DISRUPTION PHENOTYPE: Mice display balance defects, a tilted CC position of the head and abnormal performances in motor CC coordination tests. This is associated with the absence of CC otoconia in both the utricle and saccule of the inner ear. CC -!- SIMILARITY: Contains 1 FAD-binding FR-type domain. CC -!- SIMILARITY: Contains 1 ferric oxidoreductase domain. CC -!- SEQUENCE CAUTION: CC Sequence=AAI06863.1; Type=Erroneous initiation; CC Sequence=AAO65981.1; Type=Erroneous initiation; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AY182377; AAO65981.1; ALT_INIT; mRNA. DR EMBL; AY573240; AAT80344.1; -; mRNA. DR EMBL; BC106862; AAI06863.1; ALT_INIT; mRNA. DR RefSeq; NP_945196.2; NM_198958.2. DR UniGene; Mm.328756; -. DR ProteinModelPortal; Q672J9; -. DR SMR; Q672J9; 383-568. DR STRING; 10090.ENSMUSP00000024565; -. DR PeroxiBase; 5959; MmNOx03. DR PhosphoSite; Q672J9; -. DR PRIDE; Q672J9; -. DR Ensembl; ENSMUST00000024565; ENSMUSP00000024565; ENSMUSG00000023802. DR Ensembl; ENSMUST00000115800; ENSMUSP00000111466; ENSMUSG00000023802. DR GeneID; 224480; -. DR KEGG; mmu:224480; -. DR UCSC; uc008aev.1; mouse. DR CTD; 50508; -. DR MGI; MGI:2681162; Nox3. DR eggNOG; NOG287712; -. DR GeneTree; ENSGT00550000074350; -. DR HOGENOM; HOG000216669; -. DR HOVERGEN; HBG003760; -. DR InParanoid; Q672J9; -. DR KO; K08008; -. DR OrthoDB; EOG71P299; -. DR TreeFam; TF105354; -. DR BRENDA; 1.6.3.1; 3474. DR NextBio; 377195; -. DR PRO; PR:Q672J9; -. DR Bgee; Q672J9; -. DR CleanEx; MM_NOX3; -. DR Genevestigator; Q672J9; -. DR GO; GO:0005737; C:cytoplasm; IDA:MGI. DR GO; GO:0043020; C:NADPH oxidase complex; IDA:MGI. DR GO; GO:0016175; F:superoxide-generating NADPH oxidase activity; IDA:MGI. DR GO; GO:0009590; P:detection of gravity; IMP:MGI. DR GO; GO:0048840; P:otolith development; IMP:MGI. DR GO; GO:0042554; P:superoxide anion generation; IDA:MGI. DR GO; GO:0001659; P:temperature homeostasis; IMP:MGI. DR InterPro; IPR000778; Cyt_b245_heavy_chain. DR InterPro; IPR013112; FAD-bd_8. DR InterPro; IPR017927; Fd_Rdtase_FAD-bd. DR InterPro; IPR013130; Fe3_Rdtase_TM_dom. DR InterPro; IPR013121; Fe_red_NAD-bd_6. DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl. DR Pfam; PF08022; FAD_binding_8; 1. DR Pfam; PF01794; Ferric_reduct; 1. DR Pfam; PF08030; NAD_binding_6; 1. DR PRINTS; PR00466; GP91PHOX. DR SUPFAM; SSF63380; SSF63380; 1. DR PROSITE; PS51384; FAD_FR; 1. PE 1: Evidence at protein level; KW Complete proteome; Glycoprotein; Membrane; Oxidoreductase; KW Reference proteome; Transmembrane; Transmembrane helix. FT CHAIN 1 568 NADPH oxidase 3. FT /FTId=PRO_0000227597. FT TOPO_DOM 1 12 Cytoplasmic (Potential). FT TRANSMEM 13 33 Helical; (Potential). FT TOPO_DOM 34 49 Extracellular (Potential). FT TRANSMEM 50 70 Helical; (Potential). FT TOPO_DOM 71 103 Cytoplasmic (Potential). FT TRANSMEM 104 124 Helical; (Potential). FT TOPO_DOM 125 167 Extracellular (Potential). FT TRANSMEM 168 188 Helical; (Potential). FT TOPO_DOM 189 201 Cytoplasmic (Potential). FT TRANSMEM 202 222 Helical; (Potential). FT TOPO_DOM 223 395 Extracellular (Potential). FT TRANSMEM 396 416 Helical; (Potential). FT TOPO_DOM 417 568 Cytoplasmic (Potential). FT DOMAIN 55 284 Ferric oxidoreductase. FT DOMAIN 285 395 FAD-binding FR-type. FT CARBOHYD 238 238 N-linked (GlcNAc...) (Potential). FT MUTAGEN 408 408 G->R: Defects in otoconia biogenesis. FT MUTAGEN 542 542 K->E: Defects in otoconia biogenesis. FT CONFLICT 161 161 D -> Y (in Ref. 2; AAT80344). SQ SEQUENCE 568 AA; 64495 MW; 345FD67494ADB8F2 CRC64; MPVCWILNES GSFVVALLWL AVNAYLFIDT FFWYTEEEAF FYTRVILGSA LAWARASAVC LNFNCMLILL PVSRNFISLV RGTSVCCRGP WRRQLDKNLN FHKLVAYGIA VNSVIHIVAH LFNLERYHLG QAKDAEGLLA ALSKLGDAPN ESYLNPVRTF DMGTTTELLM TVSGITGLGI SLALVFIMTS STEFIRRSSY ELFWYTHHIF VFFFISLAIH GGGRIIRGQT PESLRLHNVT YCRDHYAEWQ AAALCPVPQF SGKEPSAWKW ALGPVVLYAC ERIIRFWRSH QEVVITKVVS HPSAVLELHM KKRDFKMAPG QYIFIQCPSV SPLEWHPFTL TSAPQEDFFS VHIRASGDWT EALLKAFRVE GQAPSELCSM PRLAVDGPFG GSLADVFHYP VSVCIATGIG VTPFASLLKS VWYKCCESQS LPELSKVYFY WICRDAGAFE WFADLLLSLE TRMSEQGKAH LLSYHIYLTG WDENQAIHIA LHWDESLDVI TGLKQKAFYG RPNWNDEFKQ IAYNHPSSSI GVFFCGSKAM SKTLQKMCRL YSSVDPRGVH FYYNKENF // ID NOX4_MOUSE Reviewed; 578 AA. AC Q9JHI8; Q3TF39; Q8C3M1; Q8VCA3; DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 19-MAR-2014, entry version 92. DE RecName: Full=NADPH oxidase 4; DE EC=1.6.3.-; DE AltName: Full=Kidney oxidase-1; DE Short=KOX-1; DE AltName: Full=Kidney superoxide-producing NADPH oxidase; DE AltName: Full=Renal NAD(P)H-oxidase; DE AltName: Full=Superoxide-generating NADPH oxidase 4; GN Name=Nox4; Synonyms=Renox; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, RP AND ENZYME REGULATION. RC TISSUE=Kidney; RX PubMed=10869423; DOI=10.1073/pnas.130135897; RA Geiszt M., Kopp J.B., Varnai P., Leto T.L.; RT "Identification of renox, an NAD(P)H oxidase in kidney."; RL Proc. Natl. Acad. Sci. U.S.A. 97:8010-8014(2000). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=11032835; DOI=10.1074/jbc.M007597200; RA Shiose A., Kuroda J., Tsuruya K., Hirai M., Hirakata H., Naito S., RA Hattori M., Sakaki Y., Sumimoto H.; RT "A novel superoxide-producing NAD(P)H oxidase in kidney."; RL J. Biol. Chem. 276:1417-1423(2001). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND TISSUE RP SPECIFICITY. RX PubMed=11098048; DOI=10.1074/jbc.M001004200; RA Yang S., Madyastha P., Bingel S., Ries W., Key L.; RT "A new superoxide-generating oxidase in murine osteoclasts."; RL J. Biol. Chem. 276:5452-5458(2001). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RA Banfi B., Maturana A., Demaurex N., Krause K.-H.; RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3). RC STRAIN=C57BL/6J; TISSUE=Heart, and Liver; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4). RC STRAIN=FVB/N; TISSUE=Kidney; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [7] RP INDUCTION. RX PubMed=15016652; DOI=10.1182/blood-2003-07-2240; RA Suliman H.B., Ali M., Piantadosi C.A.; RT "Superoxide dismutase-3 promotes full expression of the EPO response RT to hypoxia."; RL Blood 104:43-50(2004). RN [8] RP ENZYME REGULATION. RX PubMed=15638999; DOI=10.1211/0022357055119; RA Ding Y., Chen Z.-J., Liu S., Che D., Vetter M., Chang C.-H.; RT "Inhibition of Nox-4 activity by plumbagin, a plant-derived bioactive RT naphthoquinone."; RL J. Pharm. Pharmacol. 57:111-116(2005). RN [9] RP TISSUE SPECIFICITY, AND INDUCTION. RX PubMed=15802177; DOI=10.1016/j.neuroscience.2004.12.038; RA Vallet P., Charnay Y., Steger K., Ogier-Denis E., Kovari E., RA Herrmann F., Michel J.-P., Szanto I.; RT "Neuronal expression of the NADPH oxidase NOX4, and its regulation in RT mouse experimental brain ischemia."; RL Neuroscience 132:233-238(2005). CC -!- FUNCTION: Constitutive NADPH oxidase which generates superoxide CC intracellularly upon formation of a complex with CYBA/p22phox. CC Regulates signaling cascades probably through phosphatases CC inhibition. May function as an oxygen sensor regulating the CC KCNK3/TASK-1 potassium channel and HIF1A activity. May regulate CC insulin signaling cascade. May play a role in apoptosis, bone CC resorption and lipolysaccharide-mediated activation of NFKB. CC -!- ENZYME REGULATION: Activated by insulin. Inhibited by diphenylene CC iodonium (By similarity). Inhibited by plumbagin. Activated by CC phorbol 12-myristate 13-acetate (PMA). CC -!- SUBUNIT: Interacts with, relocalizes and stabilizes CYBA/p22phox. CC Interacts with TLR4. Interacts with protein disulfide isomerase CC (By similarity). CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass CC membrane protein (By similarity). Cell junction, focal adhesion CC (By similarity). Cell membrane (By similarity). Note=May localize CC to plasma membrane and focal adhesions (By similarity). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; CC IsoId=Q9JHI8-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9JHI8-2; Sequence=VSP_019060, VSP_019061; CC Note=No experimental confirmation available; CC Name=3; CC IsoId=Q9JHI8-3; Sequence=VSP_019063, VSP_019064; CC Note=No experimental confirmation available; CC Name=4; CC IsoId=Q9JHI8-4; Sequence=VSP_019062; CC Note=No experimental confirmation available; CC -!- TISSUE SPECIFICITY: EXpressed in brain, in all layers of the CC cerebellum, in pyramidal cells of the Ammon horn and in Purkinje CC cells (at protein level). Expressed in osteoclasts, leukocytes, CC kidney, liver and lung. CC -!- INDUCTION: Upon brain ischemia it is up-regulated in ischemic CC tissues and more specially in neocapillaries (at protein level). CC Up-regulated upon hypoxia. CC -!- PTM: N-glycosylation is required for the function (By similarity). CC -!- SIMILARITY: Contains 1 FAD-binding FR-type domain. CC -!- SIMILARITY: Contains 1 ferric oxidoreductase domain. CC -!- SEQUENCE CAUTION: CC Sequence=BC021378; Type=Frameshift; Positions=52; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF261944; AAF87573.1; -; mRNA. DR EMBL; AB041034; BAA95682.1; -; mRNA. DR EMBL; AB042745; BAB18134.1; -; mRNA. DR EMBL; AF218723; AAF43142.1; -; mRNA. DR EMBL; AF276957; AAK69443.1; -; mRNA. DR EMBL; AK050371; BAC34215.1; -; mRNA. DR EMBL; AK085509; BAC39460.1; -; mRNA. DR EMBL; AK169304; BAE41059.1; -; mRNA. DR EMBL; BC021378; -; NOT_ANNOTATED_CDS; mRNA. DR RefSeq; NP_056575.1; NM_015760.5. DR RefSeq; XP_006508075.1; XM_006508012.1. DR UniGene; Mm.31748; -. DR ProteinModelPortal; Q9JHI8; -. DR SMR; Q9JHI8; 409-577. DR PeroxiBase; 5966; MmNOx04. DR PhosphoSite; Q9JHI8; -. DR PRIDE; Q9JHI8; -. DR DNASU; 50490; -. DR Ensembl; ENSMUST00000032781; ENSMUSP00000032781; ENSMUSG00000030562. [Q9JHI8-1] DR Ensembl; ENSMUST00000068829; ENSMUSP00000070039; ENSMUSG00000030562. [Q9JHI8-3] DR GeneID; 50490; -. DR KEGG; mmu:50490; -. DR UCSC; uc009ifj.1; mouse. [Q9JHI8-2] DR UCSC; uc009ifk.1; mouse. [Q9JHI8-3] DR UCSC; uc009ifl.1; mouse. [Q9JHI8-1] DR UCSC; uc009ifm.1; mouse. [Q9JHI8-4] DR CTD; 50507; -. DR MGI; MGI:1354184; Nox4. DR eggNOG; NOG265816; -. DR GeneTree; ENSGT00550000074350; -. DR HOGENOM; HOG000216669; -. DR HOVERGEN; HBG003760; -. DR OMA; FCCGPNS; -. DR OrthoDB; EOG7RZ5PZ; -. DR TreeFam; TF105354; -. DR NextBio; 307468; -. DR PRO; PR:Q9JHI8; -. DR ArrayExpress; Q9JHI8; -. DR Bgee; Q9JHI8; -. DR CleanEx; MM_NOX4; -. DR Genevestigator; Q9JHI8; -. DR GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl. DR GO; GO:0071944; C:cell periphery; IDA:UniProtKB. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell. DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl. DR GO; GO:0043020; C:NADPH oxidase complex; IEA:Ensembl. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB. DR GO; GO:0072341; F:modified amino acid binding; IEA:Ensembl. DR GO; GO:0016174; F:NAD(P)H oxidase activity; IEA:Ensembl. DR GO; GO:0016175; F:superoxide-generating NADPH oxidase activity; IMP:UniProtKB. DR GO; GO:0045453; P:bone resorption; IMP:MGI. DR GO; GO:0055007; P:cardiac muscle cell differentiation; IMP:MGI. DR GO; GO:0007569; P:cell aging; IMP:UniProtKB. DR GO; GO:0000902; P:cell morphogenesis; IMP:UniProtKB. DR GO; GO:0071320; P:cellular response to cAMP; IEA:Ensembl. DR GO; GO:0071480; P:cellular response to gamma radiation; IEA:Ensembl. DR GO; GO:0071333; P:cellular response to glucose stimulus; IEP:UniProtKB. DR GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IEA:Ensembl. DR GO; GO:0050667; P:homocysteine metabolic process; IEA:Ensembl. DR GO; GO:0008285; P:negative regulation of cell proliferation; IMP:UniProtKB. DR GO; GO:0043065; P:positive regulation of apoptotic process; IEA:Ensembl. DR GO; GO:2000573; P:positive regulation of DNA biosynthetic process; IMP:UniProtKB. DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IMP:UniProtKB. DR GO; GO:0043406; P:positive regulation of MAP kinase activity; IMP:UniProtKB. DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; IMP:UniProtKB. DR GO; GO:2000379; P:positive regulation of reactive oxygen species metabolic process; IEA:Ensembl. DR GO; GO:0014911; P:positive regulation of smooth muscle cell migration; IEA:Ensembl. DR GO; GO:0051496; P:positive regulation of stress fiber assembly; IEA:Ensembl. DR GO; GO:0001666; P:response to hypoxia; IEA:Ensembl. DR GO; GO:0042554; P:superoxide anion generation; IDA:UniProtKB. DR InterPro; IPR000778; Cyt_b245_heavy_chain. DR InterPro; IPR013112; FAD-bd_8. DR InterPro; IPR017927; Fd_Rdtase_FAD-bd. DR InterPro; IPR013130; Fe3_Rdtase_TM_dom. DR InterPro; IPR013121; Fe_red_NAD-bd_6. DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl. DR Pfam; PF08022; FAD_binding_8; 1. DR Pfam; PF01794; Ferric_reduct; 1. DR Pfam; PF08030; NAD_binding_6; 1. DR PRINTS; PR00466; GP91PHOX. DR SUPFAM; SSF63380; SSF63380; 1. DR PROSITE; PS51384; FAD_FR; 1. PE 1: Evidence at protein level; KW Alternative splicing; Cell junction; Cell membrane; Complete proteome; KW Disulfide bond; Endoplasmic reticulum; Glycoprotein; Membrane; NADP; KW Oxidoreductase; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 578 NADPH oxidase 4. FT /FTId=PRO_0000238981. FT TOPO_DOM 1 16 Cytoplasmic (Potential). FT TRANSMEM 17 37 Helical; (Potential). FT TOPO_DOM 38 62 Extracellular (Potential). FT TRANSMEM 63 83 Helical; (Potential). FT TOPO_DOM 84 104 Cytoplasmic (Potential). FT TRANSMEM 105 125 Helical; (Potential). FT TOPO_DOM 126 154 Extracellular (Potential). FT TRANSMEM 155 175 Helical; (Potential). FT TOPO_DOM 176 188 Cytoplasmic (Potential). FT TRANSMEM 189 209 Helical; (Potential). FT TOPO_DOM 210 424 Extracellular (Potential). FT TRANSMEM 425 445 Helical; (Potential). FT TOPO_DOM 446 578 Cytoplasmic (Potential). FT DOMAIN 58 303 Ferric oxidoreductase. FT DOMAIN 304 419 FAD-binding FR-type. FT REGION 248 575 Mediates interaction with TLR4 (By FT similarity). FT CARBOHYD 133 133 N-linked (GlcNAc...) (Potential). FT CARBOHYD 230 230 N-linked (GlcNAc...) (Potential). FT VAR_SEQ 150 164 DPRKLLFTTIPGLTG -> VGGVCFSIFCSLVIR (in FT isoform 2). FT /FTId=VSP_019060. FT VAR_SEQ 165 578 Missing (in isoform 2). FT /FTId=VSP_019061. FT VAR_SEQ 358 358 M -> MLCQKRWQPWHSRVWIYSFFVCSDAACHEDTSKMNH FT AFLL (in isoform 4). FT /FTId=VSP_019062. FT VAR_SEQ 540 540 K -> FEDQGQDFVPARKQHLHRGAPKALSFFSNGKGYLHF FT TIMTLKKCCFHGSPLIF (in isoform 3). FT /FTId=VSP_019063. FT VAR_SEQ 541 578 Missing (in isoform 3). FT /FTId=VSP_019064. FT CONFLICT 298 298 R -> G (in Ref. 5; BAC39460). SQ SEQUENCE 578 AA; 66519 MW; 7887ADD40599A3D1 CRC64; MAVSWRSWLA NEGVKHLCLL IWLSLNVLLF WKTFLLYNQG PEYYYIHQML GLGLCLSRAS ASVLNLNCSL ILLPMCRTVL AYLRGSQKVP SRRTRRLLDK SKTLHITCGV TICIFSGVHV AAHLVNALNF SVNYSEDFLE LNAARYQNED PRKLLFTTIP GLTGVCMVVV LFLMVTASTY AIRVSNYDIF WYTHNLFFVF YMLLLLHVSG GLLKYQTNVD THPPGCISLN QTSSQNMSIP DYVSEHFHGS LPRGFSKLED RYQKTLVKIC LEEPKFQAHF PQTWIWISGP LCLYCAERLY RCIRSNKPVT IISVINHPSD VMELRMIKEN FKARPGQYII LHCPSVSALE NHPFTLTMCP TETKATFGVH FKVVGDWTER FRDLLLPPSS QDSEILPFIH SRNYPKLYID GPFGSPFEES LNYEVSLCVA GGIGVTPFAS ILNTLLDDWK PYKLRRLYFI WVCRDIQSFQ WFADLLCVLH NKFWQENRPD FVNIQLYLSQ TDGIQKIIGE KYHTLNSRLF IGRPRWKLLF DEIAKCNRGK TVGVFCCGPS SISKTLHSLS NRNNSYGTKF EYNKESFS // ID NOX1_MOUSE Reviewed; 591 AA. AC Q8CIZ9; A2AEK5; Q0KKX3; Q0KKX5; Q811U2; DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot. DT 19-JAN-2010, sequence version 2. DT 19-MAR-2014, entry version 89. DE RecName: Full=NADPH oxidase 1; DE Short=NOX-1; DE EC=1.-.-.-; GN Name=Nox1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INTERACTION WITH NOXO1, AND RP ENZYME REGULATION. RC STRAIN=BALB/c; RX PubMed=12473664; DOI=10.1074/jbc.C200613200; RA Banfi B., Clark R.A., Steger K., Krause K.-H.; RT "Two novel proteins activate superoxide generation by the NADPH RT oxidase NOX1."; RL J. Biol. Chem. 278:3510-3513(2003). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC STRAIN=C57BL/6J; TISSUE=Colon; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-75 (ISOFORM 1), NUCLEOTIDE SEQUENCE RP [MRNA] OF 29-75 (ISOFORM 2), FUNCTION, ALTERNATIVE SPLICING, TISSUE RP SPECIFICITY, AND INDUCTION. RC TISSUE=Colon, and Vascular smooth muscle; RX PubMed=16724959; DOI=10.1042/BJ20060300; RA Arakawa N., Katsuyama M., Matsuno K., Urao N., Tabuchi Y., Okigaki M., RA Matsubara H., Yabe-Nishimura C.; RT "Novel transcripts of Nox1 are regulated by alternative promoters and RT expressed under phenotypic modulation of vascular smooth muscle RT cells."; RL Biochem. J. 398:303-310(2006). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 116-565 (ISOFORMS 1/2). RC STRAIN=C57BL/6; RA Matsumoto Y., Blanchard T.G.; RT "Nox1 expression in the gastric mucosa of Helicobacter-infected RT gp91phox-/- mice."; RL Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Pyridine nucleotide-dependent oxidoreductase that CC generates superoxide and might conduct H(+) ions as part of its CC electron transport mechanism. CC -!- COFACTOR: NADP (Potential). CC -!- COFACTOR: FAD (Potential). CC -!- ENZYME REGULATION: The oxidase activity is potentiated by NOXA1 CC and NOXO1. CC -!- SUBUNIT: NOX1, NOXA1, NOXO1, RAC1 and CYBA forms a functional CC multimeric complex supporting ROS production. Interacts with NOXA1 CC and NOXO1. CC -!- SUBCELLULAR LOCATION: Cell projection, invadopodium membrane; CC Multi-pass membrane protein (By similarity). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; Synonyms=f-type, c-type; CC IsoId=Q8CIZ9-1; Sequence=Displayed; CC Note=Product of f-type and c-type mRNA, which differ only in CC 5'-UTR; CC Name=2; Synonyms=a-type; CC IsoId=Q8CIZ9-2; Sequence=VSP_038574; CC Name=3; CC IsoId=Q8CIZ9-3; Sequence=VSP_038574, VSP_038575; CC Note=Gene prediction based on human ortholog; CC -!- TISSUE SPECIFICITY: Isoform 2 expressed in colon and vascular CC smooth muscle cells (VSMC). CC -!- INDUCTION: Isoform 1 (c-type) induced in VSMC by angiotensin II CC and injury to the artery. CC -!- SIMILARITY: Contains 1 FAD-binding FR-type domain. CC -!- SIMILARITY: Contains 1 ferric oxidoreductase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF539799; AAN75144.1; -; mRNA. DR EMBL; AK136432; BAE22974.1; -; mRNA. DR EMBL; AL671915; CAM16733.1; -; Genomic_DNA. DR EMBL; AL671915; CAM16734.1; -; Genomic_DNA. DR EMBL; AB206383; BAF03561.1; -; mRNA. DR EMBL; AB206384; BAF03562.1; -; mRNA. DR EMBL; AB206385; BAF03563.1; -; mRNA. DR EMBL; AY174116; AAO20852.1; -; mRNA. DR RefSeq; NP_757340.1; NM_172203.2. DR RefSeq; XP_006528578.1; XM_006528515.1. DR UniGene; Mm.233865; -. DR UniGene; Mm.455133; -. DR UniGene; Mm.67938; -. DR ProteinModelPortal; Q8CIZ9; -. DR SMR; Q8CIZ9; 406-591. DR STRING; 10090.ENSMUSP00000033610; -. DR PeroxiBase; 5963; MmNOx01. DR PhosphoSite; Q8CIZ9; -. DR PaxDb; Q8CIZ9; -. DR PRIDE; Q8CIZ9; -. DR DNASU; 237038; -. DR Ensembl; ENSMUST00000033610; ENSMUSP00000033610; ENSMUSG00000031257. [Q8CIZ9-2] DR Ensembl; ENSMUST00000113275; ENSMUSP00000108900; ENSMUSG00000031257. [Q8CIZ9-3] DR Ensembl; ENSMUST00000159231; ENSMUSP00000124225; ENSMUSG00000031257. DR Ensembl; ENSMUST00000162833; ENSMUSP00000123841; ENSMUSG00000031257. DR GeneID; 237038; -. DR KEGG; mmu:237038; -. DR UCSC; uc009ufl.1; mouse. [Q8CIZ9-1] DR CTD; 27035; -. DR MGI; MGI:2450016; Nox1. DR eggNOG; COG4097; -. DR GeneTree; ENSGT00550000074350; -. DR HOGENOM; HOG000216669; -. DR HOVERGEN; HBG003760; -. DR InParanoid; Q811U2; -. DR KO; K08008; -. DR OMA; KEFWEQI; -. DR OrthoDB; EOG71P299; -. DR TreeFam; TF105354; -. DR BRENDA; 1.6.3.1; 3474. DR NextBio; 383203; -. DR PRO; PR:Q8CIZ9; -. DR ArrayExpress; Q8CIZ9; -. DR Bgee; Q8CIZ9; -. DR CleanEx; MM_NOX1; -. DR Genevestigator; Q8CIZ9; -. DR GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW. DR GO; GO:0005769; C:early endosome; IEA:Ensembl. DR GO; GO:0005768; C:endosome; IMP:MGI. DR GO; GO:0071438; C:invadopodium membrane; ISS:UniProtKB. DR GO; GO:0043020; C:NADPH oxidase complex; IEA:Ensembl. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW. DR GO; GO:0016175; F:superoxide-generating NADPH oxidase activity; IDA:MGI. DR GO; GO:0030171; F:voltage-gated proton channel activity; IEA:Ensembl. DR GO; GO:0001525; P:angiogenesis; IEA:Ensembl. DR GO; GO:0016477; P:cell migration; IEA:Ensembl. DR GO; GO:0071455; P:cellular response to hyperoxia; IMP:MGI. DR GO; GO:0030198; P:extracellular matrix organization; IMP:MGI. DR GO; GO:0042743; P:hydrogen peroxide metabolic process; IEA:Ensembl. DR GO; GO:0051454; P:intracellular pH elevation; IEA:Ensembl. DR GO; GO:0034220; P:ion transmembrane transport; IEA:GOC. DR GO; GO:0072592; P:oxygen metabolic process; IMP:MGI. DR GO; GO:0008284; P:positive regulation of cell proliferation; IEA:Ensembl. DR GO; GO:0045726; P:positive regulation of integrin biosynthetic process; IEA:Ensembl. DR GO; GO:1902177; P:positive regulation of intrinsic apoptotic signaling pathway in response to oxidative stress; IMP:MGI. DR GO; GO:0046330; P:positive regulation of JNK cascade; IMP:MGI. DR GO; GO:0010575; P:positive regulation vascular endothelial growth factor production; IEA:Ensembl. DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:GOC. DR GO; GO:0003081; P:regulation of systemic arterial blood pressure by renin-angiotensin; IMP:MGI. DR GO; GO:0009268; P:response to pH; IEA:Ensembl. DR GO; GO:0006950; P:response to stress; IEA:Ensembl. DR GO; GO:0042554; P:superoxide anion generation; IDA:MGI. DR InterPro; IPR000778; Cyt_b245_heavy_chain. DR InterPro; IPR013112; FAD-bd_8. DR InterPro; IPR017927; Fd_Rdtase_FAD-bd. DR InterPro; IPR013130; Fe3_Rdtase_TM_dom. DR InterPro; IPR013121; Fe_red_NAD-bd_6. DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl. DR Pfam; PF08022; FAD_binding_8; 1. DR Pfam; PF01794; Ferric_reduct; 1. DR Pfam; PF08030; NAD_binding_6; 1. DR PRINTS; PR00466; GP91PHOX. DR SUPFAM; SSF63380; SSF63380; 1. DR PROSITE; PS51384; FAD_FR; 1. PE 1: Evidence at protein level; KW Alternative splicing; Cell junction; Cell membrane; Cell projection; KW Complete proteome; Electron transport; FAD; Flavoprotein; KW Glycoprotein; Heme; Iron; Membrane; Metal-binding; NADP; KW Oxidoreductase; Reference proteome; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1 591 NADPH oxidase 1. FT /FTId=PRO_0000322982. FT TOPO_DOM 1 36 Cytoplasmic (Potential). FT TRANSMEM 37 59 Helical; Name=1; (Potential). FT TOPO_DOM 60 72 Extracellular (Potential). FT TRANSMEM 73 97 Helical; Name=2; (Potential). FT TOPO_DOM 98 130 Cytoplasmic (Potential). FT TRANSMEM 131 151 Helical; Name=3; (Potential). FT TOPO_DOM 152 195 Extracellular (Potential). FT TRANSMEM 196 216 Helical; Name=4; (Potential). FT TOPO_DOM 217 234 Cytoplasmic (Potential). FT TRANSMEM 235 255 Helical; Name=5; (Potential). FT TOPO_DOM 256 423 Extracellular (Potential). FT TRANSMEM 424 444 Helical; Name=6; (Potential). FT TOPO_DOM 445 591 Cytoplasmic (Potential). FT DOMAIN 82 316 Ferric oxidoreductase. FT DOMAIN 317 418 FAD-binding FR-type. FT NP_BIND 365 371 FAD (Potential). FT REGION 424 563 Interaction with NOXO1 (By similarity). FT METAL 129 129 Iron (heme axial ligand) (Probable). FT METAL 143 143 Iron (heme axial ligand) (Probable). FT METAL 236 236 Iron (heme axial ligand) (Probable). FT METAL 248 248 Iron (heme axial ligand) (Probable). FT CARBOHYD 189 189 N-linked (GlcNAc...) (Potential). FT CARBOHYD 269 269 N-linked (GlcNAc...) (Potential). FT VAR_SEQ 1 28 Missing (in isoform 2 and isoform 3). FT /FTId=VSP_038574. FT VAR_SEQ 460 508 Missing (in isoform 3). FT /FTId=VSP_038575. SQ SEQUENCE 591 AA; 68193 MW; B2D4AE54186A066B CRC64; MAGELRGSRG PLQRIQIAPR EAPNLHLTMG NWLVNHWLSV LFLVSWLGLN IFLFVYAFLN YEKSDKYYYT REILGTALAL ARASALCLNF NSMMILIPVC RNLLSFLRGT CSFCNRTLRK PLDHNLTFHK LVAYMICIFT VIHIIAHLFN FERYRRSQQA MDGSLASVLS SLSHPEKEDS WLNPIQSPNM TVMYAAFTSI AGLTGVIATV ALVLMVTSAM EFIRRNYFEL FWYTHHLFIV YIICLGIHGL GGIVRGQTEE SLGESHPHNC SHSFHEWDDH KGSCRHPHFA GHPPESWKWI LAPIAFYIFE RILRFYRSQQ KVVITKVVMH PSNVLELQMR KRGFSMEVGQ YIFVNCPSIS FLEWHPFTLT SAPEEEFFSV HIRAAGDWTR NLIRTFEQQH SPMPRIEVDG PFGTVSEDVF QYEVAVLVGA GIGVTPFASI LKSIWYKFQR ADNKLKTQKI YFYWICRETG AFAWFNNLLN SLEQEMEELG KMDFLNYRLF LTGWDSNIAG HAALNFDRAT DILTGLKQKT SFGRPMWDNE FSRIATAHPK SAVGVFLCGP RTLAKSLRKR CQRYSSLDPR KVQFYFNKET F // ID NQO1_MOUSE Reviewed; 274 AA. AC Q64669; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 19-FEB-2014, entry version 120. DE RecName: Full=NAD(P)H dehydrogenase [quinone] 1; DE EC=1.6.5.2; DE AltName: Full=Azoreductase; DE AltName: Full=DT-diaphorase; DE Short=DTD; DE AltName: Full=Menadione reductase; DE AltName: Full=NAD(P)H:quinone oxidoreductase 1; DE AltName: Full=Phylloquinone reductase; DE AltName: Full=Quinone reductase 1; DE Short=QR1; GN Name=Nqo1; Synonyms=Dia4, Nmo1, Nmor1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=C57BL/6 X CBA; TISSUE=Liver; RX PubMed=7704040; RA Vasiliou V., Theurer M.J., Puga A., Reuter S.F., Nebert D.W.; RT "Mouse dioxin-inducible NAD(P)H: menadione oxidoreductase: NMO1 cDNA RT sequence and genetic differences in mRNA levels."; RL Pharmacogenetics 4:341-348(1994). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE. RC TISSUE=Liver; RX PubMed=7527260; RA Chen S., Clarke P.E., Martino P.A., Deng P.S., Yeh C.H., Lee T.D., RA Prochaska H.J., Talalay P.; RT "Mouse liver NAD(P)H:quinone acceptor oxidoreductase: protein sequence RT analysis by tandem mass spectrometry, cDNA cloning, expression in RT Escherichia coli, and enzyme activity analysis."; RL Protein Sci. 3:1296-1304(1994). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH FAD, AND RP SUBUNIT. RX PubMed=10706635; DOI=10.1073/pnas.050585797; RA Faig M., Bianchet M.A., Talalay P., Chen S., Winski S., Ross D., RA Amzel L.M.; RT "Structures of recombinant human and mouse NAD(P)H:quinone RT oxidoreductases: species comparison and structural changes with RT substrate binding and release."; RL Proc. Natl. Acad. Sci. U.S.A. 97:3177-3182(2000). CC -!- FUNCTION: The enzyme apparently serves as a quinone reductase in CC connection with conjugation reactions of hydroquinons involved in CC detoxification pathways as well as in biosynthetic processes such CC as the vitamin K-dependent gamma-carboxylation of glutamate CC residues in prothrombin synthesis (By similarity). CC -!- CATALYTIC ACTIVITY: NAD(P)H + a quinone = NAD(P)(+) + a CC hydroquinone. CC -!- COFACTOR: FAD. CC -!- SUBUNIT: Homodimer. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- INDUCTION: By polycyclic hydrocarbons such as dioxin (Governed by CC the aromatic hydrocarbon-responsive (AH) locus). CC -!- SIMILARITY: Belongs to the NAD(P)H dehydrogenase (quinone) family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U12961; AAA80184.1; -; mRNA. DR EMBL; S75951; AAB32718.1; -; mRNA. DR PIR; A57691; A57691. DR RefSeq; NP_032732.3; NM_008706.5. DR UniGene; Mm.252; -. DR PDB; 1DXQ; X-ray; 2.80 A; A/B/C/D=2-274. DR PDBsum; 1DXQ; -. DR ProteinModelPortal; Q64669; -. DR SMR; Q64669; 2-274. DR BioGrid; 201790; 1. DR ChEMBL; CHEMBL5611; -. DR PhosphoSite; Q64669; -. DR PaxDb; Q64669; -. DR PRIDE; Q64669; -. DR Ensembl; ENSMUST00000003947; ENSMUSP00000003947; ENSMUSG00000003849. DR GeneID; 18104; -. DR KEGG; mmu:18104; -. DR UCSC; uc009nhq.1; mouse. DR CTD; 1728; -. DR MGI; MGI:103187; Nqo1. DR eggNOG; COG2249; -. DR GeneTree; ENSGT00440000033410; -. DR HOGENOM; HOG000149970; -. DR HOVERGEN; HBG029104; -. DR InParanoid; Q64669; -. DR KO; K00355; -. DR OMA; YDVLPPF; -. DR OrthoDB; EOG7CZK6F; -. DR TreeFam; TF300296; -. DR EvolutionaryTrace; Q64669; -. DR NextBio; 293281; -. DR PRO; PR:Q64669; -. DR ArrayExpress; Q64669; -. DR Bgee; Q64669; -. DR CleanEx; MM_NQO1; -. DR Genevestigator; Q64669; -. DR GO; GO:0005829; C:cytosol; IEA:Ensembl. DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl. DR GO; GO:0003955; F:NAD(P)H dehydrogenase (quinone) activity; IDA:MGI. DR GO; GO:0004784; F:superoxide dismutase activity; IEA:Ensembl. DR GO; GO:0007568; P:aging; IEA:Ensembl. DR GO; GO:0043086; P:negative regulation of catalytic activity; IDA:MGI. DR GO; GO:0043525; P:positive regulation of neuron apoptotic process; IEA:Ensembl. DR GO; GO:0032355; P:response to estradiol; IEA:Ensembl. DR GO; GO:0045471; P:response to ethanol; IEA:Ensembl. DR GO; GO:0007584; P:response to nutrient; IEA:Ensembl. DR GO; GO:0006979; P:response to oxidative stress; IMP:MGI. DR GO; GO:0006801; P:superoxide metabolic process; IEA:Ensembl. DR InterPro; IPR003680; Flavodoxin_fold. DR Pfam; PF02525; Flavodoxin_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Complete proteome; Cytoplasm; KW Direct protein sequencing; FAD; Flavoprotein; NAD; NADP; KW Oxidoreductase; Reference proteome. FT INIT_MET 1 1 Removed. FT CHAIN 2 274 NAD(P)H dehydrogenase [quinone] 1. FT /FTId=PRO_0000071623. FT NP_BIND 18 19 FAD. FT NP_BIND 104 107 FAD. FT NP_BIND 148 151 FAD. FT REGION 126 128 Substrate binding (By similarity). FT BINDING 12 12 FAD. FT BINDING 67 67 FAD. FT BINDING 156 156 FAD. FT BINDING 201 201 FAD. FT MOD_RES 2 2 N-acetylalanine. FT STRAND 5 10 FT HELIX 18 32 FT STRAND 36 41 FT HELIX 42 45 FT HELIX 68 77 FT HELIX 83 94 FT STRAND 96 103 FT HELIX 111 120 FT TURN 123 125 FT STRAND 129 131 FT HELIX 133 135 FT TURN 137 140 FT STRAND 141 151 FT HELIX 153 156 FT STRAND 160 162 FT HELIX 165 173 FT TURN 174 176 FT HELIX 177 180 FT STRAND 188 191 FT TURN 193 195 FT HELIX 198 212 FT HELIX 213 217 FT HELIX 226 228 FT TURN 233 236 FT STRAND 237 239 FT HELIX 241 247 FT STRAND 254 256 FT TURN 268 270 SQ SEQUENCE 274 AA; 30960 MW; 68F380922FD72965 CRC64; MAARRALIVL AHSEKTSFNY AMKEAAVEAL KKRGWEVLES DLYAMNFNPI ISRNDITGEL KDSKNFQYPS ESSLAYKEGR LSPDIVAEHK KLEAADLVIF QFPLQWFGVP AILKGWFERV LVAGFAYTYA AMYDNGPFQN KKTLLSITTG GSGSMYSLQG VHGDMNVILW PIQSGILRFC GFQVLEPQLV YSIGHTPPDA RMQILEGWKK RLETVWEETP LYFAPSSLFD LNFQAGFLMK KEVQEEQKKN KFGLSVGHHL GKSIPADNQI KARK // ID NQO2_MOUSE Reviewed; 231 AA. AC Q9JI75; DT 25-NOV-2002, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 19-MAR-2014, entry version 94. DE RecName: Full=Ribosyldihydronicotinamide dehydrogenase [quinone]; DE EC=1.10.99.2; DE AltName: Full=NRH dehydrogenase [quinone] 2; DE AltName: Full=NRH:quinone oxidoreductase 2; DE AltName: Full=Quinone reductase 2; DE Short=QR2; GN Name=Nqo2; Synonyms=Nmor2; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. RC TISSUE=Kidney; RX PubMed=10903442; DOI=10.1016/S0378-1119(00)00221-3; RA Long D.J. II, Jaiswal A.K.; RT "Mouse NRH:quinone oxidoreductase (NQO2): cloning of cDNA and gene- RT and tissue-specific expression."; RL Gene 252:107-117(2000). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Embryonic liver; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Thymus; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: The enzyme apparently serves as a quinone reductase in CC connection with conjugation reactions of hydroquinones involved in CC detoxification pathways as well as in biosynthetic processes such CC as the vitamin K-dependent gamma-carboxylation of glutamate CC residues in prothrombin synthesis. CC -!- CATALYTIC ACTIVITY: 1-(beta-D-ribofuranosyl)-1,4- CC dihydronicotinamide + a quinone = 1-(beta-D- CC ribofuranosyl)nicotinamide + a hydroquinone. CC -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity). CC -!- COFACTOR: FAD (By similarity). CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- MISCELLANEOUS: Uses dihydronicotinamide riboside (NRH) rather than CC NAD(P)H as an electron donor. CC -!- SIMILARITY: Belongs to the NAD(P)H dehydrogenase (quinone) family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF252260; AAF97785.1; -; mRNA. DR EMBL; AF254081; AAF97789.1; -; Genomic_DNA. DR EMBL; AF254076; AAF97789.1; JOINED; Genomic_DNA. DR EMBL; AF254077; AAF97789.1; JOINED; Genomic_DNA. DR EMBL; AF254078; AAF97789.1; JOINED; Genomic_DNA. DR EMBL; AF254079; AAF97789.1; JOINED; Genomic_DNA. DR EMBL; AF254080; AAF97789.1; JOINED; Genomic_DNA. DR EMBL; AK010842; BAB27217.1; -; mRNA. DR EMBL; BC027629; AAH27629.1; -; mRNA. DR RefSeq; NP_001156713.1; NM_001163241.1. DR RefSeq; NP_001156714.1; NM_001163242.1. DR RefSeq; NP_064678.1; NM_020282.3. DR RefSeq; XP_006516637.1; XM_006516574.1. DR UniGene; Mm.264036; -. DR ProteinModelPortal; Q9JI75; -. DR SMR; Q9JI75; 3-229. DR PhosphoSite; Q9JI75; -. DR PaxDb; Q9JI75; -. DR PRIDE; Q9JI75; -. DR Ensembl; ENSMUST00000021843; ENSMUSP00000021843; ENSMUSG00000046949. DR Ensembl; ENSMUST00000058978; ENSMUSP00000053809; ENSMUSG00000046949. DR GeneID; 18105; -. DR KEGG; mmu:18105; -. DR UCSC; uc007qas.2; mouse. DR CTD; 4835; -. DR MGI; MGI:104513; Nqo2. DR eggNOG; COG2249; -. DR GeneTree; ENSGT00440000033410; -. DR HOGENOM; HOG000149970; -. DR HOVERGEN; HBG029104; -. DR KO; K08071; -. DR OMA; EPKSFNG; -. DR OrthoDB; EOG7CZK6F; -. DR TreeFam; TF300296; -. DR BRENDA; 1.10.99.2; 3474. DR NextBio; 293285; -. DR PRO; PR:Q9JI75; -. DR Bgee; Q9JI75; -. DR CleanEx; MM_NQO2; -. DR Genevestigator; Q9JI75; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005634; C:nucleus; IEA:Ensembl. DR GO; GO:0001512; F:dihydronicotinamide riboside quinone reductase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0007613; P:memory; IEA:Ensembl. DR InterPro; IPR003680; Flavodoxin_fold. DR Pfam; PF02525; Flavodoxin_2; 1. PE 2: Evidence at transcript level; KW Complete proteome; Cytoplasm; FAD; Flavoprotein; Metal-binding; KW Oxidoreductase; Phosphoprotein; Reference proteome; Zinc. FT CHAIN 1 231 Ribosyldihydronicotinamide dehydrogenase FT [quinone]. FT /FTId=PRO_0000071627. FT NP_BIND 18 21 FAD (By similarity). FT NP_BIND 104 107 FAD (By similarity). FT NP_BIND 148 151 FAD (By similarity). FT REGION 127 129 Substrate binding (By similarity). FT METAL 174 174 Zinc (By similarity). FT METAL 178 178 Zinc (By similarity). FT METAL 223 223 Zinc (By similarity). FT BINDING 12 12 FAD (By similarity). FT BINDING 156 156 FAD (By similarity). FT BINDING 194 194 FAD (By similarity). FT BINDING 201 201 FAD (By similarity). FT MOD_RES 197 197 Phosphoserine (By similarity). SQ SEQUENCE 231 AA; 26248 MW; D5D9AB805C4AD9F5 CRC64; MAGKKVLIVY AHQEPKSFNG SLKKVAVEEL SKQGCTVTVS DLYSMNFEPR ATRNDITGAP SNPDVFSYGI ETHEAYKKKA LTSDIFEEQR KVQEADLVIF QFPLYWFSVP AILKGWMDRV LCRGFAFDIP GFYDSGFLKG KLALLSLTTG GTAEMYTKDG VSGDFRYFLW PLQHGTLHFC GFKVLAPQIS FGLDVSSEEE RKVMLASWAQ RLKSIWKEEP IHCTPPWYFQ E // ID NSDHL_MOUSE Reviewed; 362 AA. AC Q9R1J0; O55109; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 19-FEB-2014, entry version 100. DE RecName: Full=Sterol-4-alpha-carboxylate 3-dehydrogenase, decarboxylating; DE EC=1.1.1.170; GN Name=Nsdhl; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=10369263; DOI=10.1038/9700; RA Liu X.Y., Dangel A.W., Kelley R.I., Zhao W., Denny P., Botcherby M., RA Cattanach B., Peters J., Hunsicker P.R., Mallon A.-M., Strivens M.A., RA Bate R., Miller W., Rhodes M., Brown S.D.M., Herman G.E.; RT "The gene mutated in bare patches and striated mice encodes a novel RT 3beta-hydroxysteroid dehydrogenase."; RL Nat. Genet. 22:182-187(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6; RX PubMed=10854409; DOI=10.1101/gr.10.6.758; RA Mallon A.-M., Platzer M., Bate R., Gloeckner G., Botcherby M.R.M., RA Nordsiek G., Strivens M.A., Kioschis P., Dangel A., Cunningham D., RA Straw R.N.A., Weston P., Gilbert M., Fernando S., Goodall K., RA Hunter G., Greystrong J.S., Clarke D., Kimberley C., Goerdes M., RA Blechschmidt K., Rump A., Hinzmann B., Mundy C.R., Miller W., RA Poustka A., Herman G.E., Rhodes M., Denny P., Rosenthal A., RA Brown S.D.M.; RT "Comparative genome sequence analysis of the Bpa/Str region in mouse RT and man."; RL Genome Res. 10:758-775(2000). CC -!- CATALYTIC ACTIVITY: A 3-beta-hydroxysteroid-4-alpha-carboxylate + CC NAD(P)(+) = a 3-oxosteroid + CO(2) + NAD(P)H. CC -!- PATHWAY: Steroid biosynthesis; zymosterol biosynthesis; zymosterol CC from lanosterol: step 4/6. CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein CC (Potential). CC -!- SIMILARITY: Belongs to the 3-beta-HSD family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF100198; AAD38448.1; -; mRNA. DR EMBL; AL021127; CAA15948.2; -; Genomic_DNA. DR RefSeq; NP_035071.3; NM_010941.3. DR UniGene; Mm.38792; -. DR ProteinModelPortal; Q9R1J0; -. DR SMR; Q9R1J0; 26-355. DR IntAct; Q9R1J0; 3. DR MINT; MINT-1837653; -. DR STRING; 10090.ENSMUSP00000033715; -. DR PhosphoSite; Q9R1J0; -. DR PaxDb; Q9R1J0; -. DR PRIDE; Q9R1J0; -. DR Ensembl; ENSMUST00000033715; ENSMUSP00000033715; ENSMUSG00000031349. DR GeneID; 18194; -. DR KEGG; mmu:18194; -. DR UCSC; uc009tkv.1; mouse. DR CTD; 50814; -. DR MGI; MGI:1099438; Nsdhl. DR eggNOG; COG0451; -. DR GeneTree; ENSGT00550000074557; -. DR HOGENOM; HOG000167989; -. DR HOVERGEN; HBG054675; -. DR InParanoid; Q9R1J0; -. DR KO; K07748; -. DR OMA; EPMRDQV; -. DR OrthoDB; EOG77M8NP; -. DR TreeFam; TF354279; -. DR UniPathway; UPA00770; UER00757. DR ChiTaRS; NSDHL; mouse. DR NextBio; 293544; -. DR PRO; PR:Q9R1J0; -. DR ArrayExpress; Q9R1J0; -. DR Bgee; Q9R1J0; -. DR CleanEx; MM_NSDHL; -. DR Genevestigator; Q9R1J0; -. DR GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005811; C:lipid particle; IEA:Ensembl. DR GO; GO:0003854; F:3-beta-hydroxy-delta5-steroid dehydrogenase activity; IEA:InterPro. DR GO; GO:0047012; F:sterol-4-alpha-carboxylate 3-dehydrogenase (decarboxylating) activity; IEA:UniProtKB-EC. DR GO; GO:0006695; P:cholesterol biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0008203; P:cholesterol metabolic process; IMP:MGI. DR GO; GO:0001942; P:hair follicle development; IMP:MGI. DR GO; GO:0060716; P:labyrinthine layer blood vessel development; IMP:MGI. DR GO; GO:0007224; P:smoothened signaling pathway; IGI:MGI. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR002225; 3Beta_OHSteriod_DH/Estase. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Pfam; PF01073; 3Beta_HSD; 1. PE 2: Evidence at transcript level; KW Acetylation; Cholesterol biosynthesis; Cholesterol metabolism; KW Complete proteome; Lipid biosynthesis; Lipid metabolism; Membrane; KW NAD; Oxidoreductase; Reference proteome; Steroid biosynthesis; KW Steroid metabolism; Sterol biosynthesis; Sterol metabolism; KW Transmembrane; Transmembrane helix. FT CHAIN 1 362 Sterol-4-alpha-carboxylate 3- FT dehydrogenase, decarboxylating. FT /FTId=PRO_0000087800. FT TRANSMEM 287 307 Helical; (Potential). FT ACT_SITE 161 161 Proton acceptor (By similarity). FT BINDING 165 165 NAD (By similarity). FT MOD_RES 1 1 N-acetylmethionine (By similarity). SQ SEQUENCE 362 AA; 40686 MW; 4DB53EC0314885C3 CRC64; MEQAVHGESK RGQVTGTHLT NDISKAKKCT VIGGSGFLGQ HMVEQLLERG YTVNVFDIHQ GFDNPRVQFF IGDLCNQQDL YPALKGVSTV FHCASPPPYS NNKELFYRVN FIGTKTVIET CREAGVQKLI LTSSASVVFE GVDIKNGTED LPYAMKPIDY YTETKILQER AVLDANDPKK NFLTAAIRPH GIFGPRDPQL VPILIDAARK GKMKFMIGNG ENLVDFTFVE NVVHGHILAA EHLSQDAALG GKAFHITNDE PIPFWTFLSR ILTGLNYEAP KYHIPYWMAY YLAFLLSLLV MVVSPLIQIQ PTFTPIRVAL AGTFHYYSCE KAKKLFGYRP LVTMDEAVER TVQSFHHLRK DK // ID NU1M_MOUSE Reviewed; 318 AA. AC P03888; Q9G0S6; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 04-JAN-2005, sequence version 3. DT 19-MAR-2014, entry version 101. DE RecName: Full=NADH-ubiquinone oxidoreductase chain 1; DE EC=1.6.5.3; DE AltName: Full=NADH dehydrogenase subunit 1; GN Name=Mtnd1; Synonyms=mt-Nd1, Nd1; OS Mus musculus (Mouse). OG Mitochondrion. OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=7332926; DOI=10.1016/0092-8674(81)90300-7; RA Bibb M.J., van Etten R.A., Wright C.T., Walberg M.W., Clayton D.A.; RT "Sequence and gene organization of mouse mitochondrial DNA."; RL Cell 26:167-180(1981). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=C3H/He, SAMP1, SAMP8, and SAMR1; TISSUE=Liver; RX PubMed=11535650; DOI=10.1093/jhered/92.4.352; RA Mizutani J., Chiba T., Tanaka M., Higuchi K., Mori M.; RT "Unique mutations in mitochondrial DNA of senescence-accelerated mouse RT (SAM) strains."; RL J. Hered. 92:352-355(2001). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ALR/Lt, ALS/Lt, NOD/LtJ, and NON/Lt; RA Mathews C.E., Leiter E.H., Spirina O., Bykhovskaya Y., RA Fischel-Ghodsian N.; RT "The ALR/Lt mouse: contribution of the mitochondrial genome in RT resistance against both chemically-induced and autoimmune diabetes."; RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BALB/cJ, C3H/An, and C57BL/6J; TISSUE=Fibroblast, and Platelet; RX PubMed=12954771; DOI=10.1093/nar/gkg739; RA Bayona-Bafaluy M.P., Acin-Perez R., Mullikin J.C., Park J.S., RA Moreno-Loshuertos R., Hu P., Perez-Martos A., Fernandez-Silva P., RA Bai Y., Enriquez J.A.; RT "Revisiting the mouse mitochondrial DNA sequence."; RL Nucleic Acids Res. 31:5349-5355(2003). RN [5] RP PROTEIN SEQUENCE OF 27-54 AND 127-134, AND MASS SPECTROMETRY. RC STRAIN=C57BL/6; TISSUE=Brain; RA Lubec G., Kang S.U.; RL Submitted (APR-2007) to UniProtKB. CC -!- FUNCTION: Core subunit of the mitochondrial membrane respiratory CC chain NADH dehydrogenase (Complex I) that is believed to belong to CC the minimal assembly required for catalysis. Complex I functions CC in the transfer of electrons from NADH to the respiratory chain. CC The immediate electron acceptor for the enzyme is believed to be CC ubiquinone (By similarity). CC -!- CATALYTIC ACTIVITY: NADH + ubiquinone + 5 H(+)(In) = NAD(+) + CC ubiquinol + 4 H(+)(Out). CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass CC membrane protein (By similarity). CC -!- SIMILARITY: Belongs to the complex I subunit 1 family. CC -!- SEQUENCE CAUTION: CC Sequence=AAB48644.1; Type=Erroneous initiation; CC Sequence=CAA24080.1; Type=Erroneous initiation; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; V00711; CAA24080.1; ALT_INIT; Genomic_DNA. DR EMBL; J01420; AAB48644.1; ALT_INIT; Genomic_DNA. DR EMBL; AB042523; BAA95653.2; -; Genomic_DNA. DR EMBL; AB042524; BAA95640.2; -; Genomic_DNA. DR EMBL; AB042809; BAA95795.2; -; Genomic_DNA. DR EMBL; AB049357; BAB13801.2; -; Genomic_DNA. DR EMBL; AJ512208; CAD54432.1; -; Genomic_DNA. DR EMBL; AY172335; AAN85122.1; -; Genomic_DNA. DR EMBL; AY339599; AAP89023.2; -; Genomic_DNA. DR EMBL; AJ489607; CAD33907.1; -; Genomic_DNA. DR EMBL; AY533105; AAS01439.1; -; Genomic_DNA. DR EMBL; AY533106; AAS01452.1; -; Genomic_DNA. DR EMBL; AY533107; AAS01465.1; -; Genomic_DNA. DR EMBL; AY533108; AAS01478.1; -; Genomic_DNA. DR PIR; A00409; QXMS1M. DR RefSeq; NP_904328.1; NC_005089.1. DR RefSeq; YP_220550.1; NC_006914.1. DR ProteinModelPortal; P03888; -. DR SMR; P03888; 1-298. DR BioGrid; 201547; 1. DR IntAct; P03888; 1. DR PaxDb; P03888; -. DR PRIDE; P03888; -. DR Ensembl; ENSMUST00000082392; ENSMUSP00000080991; ENSMUSG00000064341. DR GeneID; 17716; -. DR GeneID; 3338902; -. DR KEGG; mmu:17716; -. DR CTD; 4535; -. DR MGI; MGI:101787; mt-Nd1. DR eggNOG; COG1005; -. DR HOGENOM; HOG000228276; -. DR HOVERGEN; HBG016682; -. DR InParanoid; P03888; -. DR KO; K03878; -. DR OMA; LDLGWKF; -. DR OrthoDB; EOG77WWCV; -. DR ProtClustDB; MTH00104; -. DR NextBio; 292332; -. DR Genevestigator; P03888; -. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005747; C:mitochondrial respiratory chain complex I; IEA:Ensembl. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:UniProtKB-EC. DR HAMAP; MF_01350; NDH1_NuoH; 1. DR InterPro; IPR001694; NADH_UbQ_OxRdtase_su1/FPO. DR InterPro; IPR018086; NADH_UbQ_OxRdtase_su1_CS. DR PANTHER; PTHR11432; PTHR11432; 1. DR Pfam; PF00146; NADHdh; 1. DR PROSITE; PS00667; COMPLEX1_ND1_1; 1. DR PROSITE; PS00668; COMPLEX1_ND1_2; 1. PE 1: Evidence at protein level; KW Complete proteome; Direct protein sequencing; Electron transport; KW Membrane; Mitochondrion; Mitochondrion inner membrane; NAD; KW Oxidoreductase; Reference proteome; Respiratory chain; Transmembrane; KW Transmembrane helix; Transport; Ubiquinone. FT CHAIN 1 318 NADH-ubiquinone oxidoreductase chain 1. FT /FTId=PRO_0000117431. FT TRANSMEM 2 22 Helical; (Potential). FT TRANSMEM 70 90 Helical; (Potential). FT TRANSMEM 100 120 Helical; (Potential). FT TRANSMEM 136 156 Helical; (Potential). FT TRANSMEM 171 191 Helical; (Potential). FT TRANSMEM 231 251 Helical; (Potential). FT TRANSMEM 253 273 Helical; (Potential). FT TRANSMEM 293 313 Helical; (Potential). SQ SEQUENCE 318 AA; 36059 MW; ECFAB96696610024 CRC64; MFFINILTLL VPILIAMAFL TLVERKILGY MQLRKGPNIV GPYGILQPFA DAMKLFMKEP MRPLTTSMSL FIIAPTLSLT LALSLWVPLP MPHPLINLNL GILFILATSS LSVYSILWSG WASNSKYSLF GALRAVAQTI SYEVTMAIIL LSVLLMNGSY SLQTLITTQE HMWLLLPAWP MAMMWFISTL AETNRAPFDL TEGESELVSG FNVEYAAGPF ALFFMAEYTN IILMNALTTI IFLGPLYYIN LPELYSTNFM MEALLLSSTF LWIRASYPRF RYDQLMHLLW KNFLPLTLAL CMWHISLPIF TAGVPPYM // ID NU2M_MOUSE Reviewed; 345 AA. AC P03893; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 21-JUL-1986, sequence version 1. DT 19-MAR-2014, entry version 101. DE RecName: Full=NADH-ubiquinone oxidoreductase chain 2; DE EC=1.6.5.3; DE AltName: Full=NADH dehydrogenase subunit 2; GN Name=Mtnd2; Synonyms=mt-Nd2, Nd2; OS Mus musculus (Mouse). OG Mitochondrion. OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=7332926; DOI=10.1016/0092-8674(81)90300-7; RA Bibb M.J., van Etten R.A., Wright C.T., Walberg M.W., Clayton D.A.; RT "Sequence and gene organization of mouse mitochondrial DNA."; RL Cell 26:167-180(1981). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=12954771; DOI=10.1093/nar/gkg739; RA Bayona-Bafaluy M.P., Acin-Perez R., Mullikin J.C., Park J.S., RA Moreno-Loshuertos R., Hu P., Perez-Martos A., Fernandez-Silva P., RA Bai Y., Enriquez J.A.; RT "Revisiting the mouse mitochondrial DNA sequence."; RL Nucleic Acids Res. 31:5349-5355(2003). RN [3] RP PROTEIN SEQUENCE OF 237-272 AND 296-312, AND MASS SPECTROMETRY. RC STRAIN=C57BL/6, and OF1; TISSUE=Brain, and Hippocampus; RA Lubec G., Kang S.U., Sunyer B., Chen W.-Q.; RL Submitted (JAN-2009) to UniProtKB. CC -!- FUNCTION: Core subunit of the mitochondrial membrane respiratory CC chain NADH dehydrogenase (Complex I) that is believed to belong to CC the minimal assembly required for catalysis. Complex I functions CC in the transfer of electrons from NADH to the respiratory chain. CC The immediate electron acceptor for the enzyme is believed to be CC ubiquinone (By similarity). CC -!- CATALYTIC ACTIVITY: NADH + ubiquinone + 5 H(+)(In) = NAD(+) + CC ubiquinol + 4 H(+)(Out). CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass CC membrane protein. CC -!- SIMILARITY: Belongs to the complex I subunit 2 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; J01420; AAB48645.1; -; Genomic_DNA. DR EMBL; V00711; CAA24081.1; -; Genomic_DNA. DR EMBL; AY339599; AAP89024.1; -; Genomic_DNA. DR PIR; A00416; QXMS2M. DR ProteinModelPortal; P03893; -. DR SMR; P03893; 2-344. DR IntAct; P03893; 1. DR PhosphoSite; P03893; -. DR PaxDb; P03893; -. DR PRIDE; P03893; -. DR MGI; MGI:102500; mt-Nd2. DR eggNOG; COG1007; -. DR HOGENOM; HOG000113879; -. DR HOVERGEN; HBG016692; -. DR InParanoid; P03893; -. DR NextBio; 35563511; -. DR Genevestigator; P03893; -. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell. DR GO; GO:0070469; C:respiratory chain; IEA:UniProtKB-KW. DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:UniProtKB-EC. DR GO; GO:0006120; P:mitochondrial electron transport, NADH to ubiquinone; IEA:InterPro. DR InterPro; IPR010933; NADH_DH_su2_C. DR InterPro; IPR001750; NADH_UbQ/plastoQ_OxRdtase. DR InterPro; IPR003917; NADH_UbQ_OxRdtase_chain2. DR Pfam; PF06444; NADH_dehy_S2_C; 1. DR Pfam; PF00361; Oxidored_q1; 1. DR PRINTS; PR01436; NADHDHGNASE2. PE 1: Evidence at protein level; KW Complete proteome; Direct protein sequencing; Electron transport; KW Membrane; Mitochondrion; Mitochondrion inner membrane; NAD; KW Oxidoreductase; Reference proteome; Respiratory chain; Transmembrane; KW Transmembrane helix; Transport; Ubiquinone. FT CHAIN 1 345 NADH-ubiquinone oxidoreductase chain 2. FT /FTId=PRO_0000117607. FT TRANSMEM 1 21 Helical; (Potential). FT TRANSMEM 25 45 Helical; (Potential). FT TRANSMEM 56 76 Helical; (Potential). FT TRANSMEM 92 114 Helical; (Potential). FT TRANSMEM 149 171 Helical; (Potential). FT TRANSMEM 178 198 Helical; (Potential). FT TRANSMEM 200 220 Helical; (Potential). FT TRANSMEM 241 261 Helical; (Potential). FT TRANSMEM 274 294 Helical; (Potential). FT TRANSMEM 324 344 Helical; (Potential). SQ SEQUENCE 345 AA; 38764 MW; F6855CB64CE45769 CRC64; MNPITLAIIY FTIFLGPVIT MSSTNLMLMW VGLEFSLLAI IPMLINKKNP RSTEAATKYF VTQATASMII LLAIVLNYKQ LGTWMFQQQT NGLILNMTLM ALSMKLGLAP FHFWLPEVTQ GIPLHMGLIL LTWQKIAPLS ILIQIYPLLN STIILMLAIT SIFMGAWGGL NQTQMRKIMA YSSIAHMGWM LAILPYNPSL TLLNLMIYII LTAPMFMALM LNNSMTINSI SLLWNKTPAM LTMISLMLLS LGGLPPLTGF LPKWIIITEL MKNNCLIMAT LMAMMALLNL FFYIRLIYST SLTMFPTNNN SKMMTHQTKT KPNLMFSTLA IMSTMTLPLA PQLIT // ID NU3M_MOUSE Reviewed; 115 AA. AC P03899; Q35039; Q35040; Q9MD73; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 16-NOV-2001, sequence version 3. DT 19-FEB-2014, entry version 99. DE RecName: Full=NADH-ubiquinone oxidoreductase chain 3; DE EC=1.6.5.3; DE AltName: Full=NADH dehydrogenase subunit 3; GN Name=Mtnd3; Synonyms=mt-Nd3, Nd3; OS Mus musculus (Mouse). OG Mitochondrion. OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=7332926; DOI=10.1016/0092-8674(81)90300-7; RA Bibb M.J., van Etten R.A., Wright C.T., Walberg M.W., Clayton D.A.; RT "Sequence and gene organization of mouse mitochondrial DNA."; RL Cell 26:167-180(1981). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=8022788; DOI=10.1073/pnas.91.14.6364; RA Nachman M.W., Boyer S.N., Aquadro C.F.; RT "Nonneutral evolution at the mitochondrial NADH dehydrogenase subunit RT 3 gene in mice."; RL Proc. Natl. Acad. Sci. U.S.A. 91:6364-6368(1994). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=AKR/J, C3H/He, SAMP1, SAMP8, and SAMR1; TISSUE=Liver; RX PubMed=11535650; DOI=10.1093/jhered/92.4.352; RA Mizutani J., Chiba T., Tanaka M., Higuchi K., Mori M.; RT "Unique mutations in mitochondrial DNA of senescence-accelerated mouse RT (SAM) strains."; RL J. Hered. 92:352-355(2001). CC -!- FUNCTION: Core subunit of the mitochondrial membrane respiratory CC chain NADH dehydrogenase (Complex I) that is believed to belong to CC the minimal assembly required for catalysis. Complex I functions CC in the transfer of electrons from NADH to the respiratory chain. CC The immediate electron acceptor for the enzyme is believed to be CC ubiquinone (By similarity). CC -!- CATALYTIC ACTIVITY: NADH + ubiquinone + 5 H(+)(In) = NAD(+) + CC ubiquinol + 4 H(+)(Out). CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane; Multi-pass membrane CC protein (By similarity). CC -!- SIMILARITY: Belongs to the complex I subunit 3 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; J01420; AAB48651.1; -; Genomic_DNA. DR EMBL; V00711; CAA24086.1; -; Genomic_DNA. DR EMBL; U09637; AAA19254.2; -; Genomic_DNA. DR EMBL; U09638; AAA19255.2; -; Genomic_DNA. DR EMBL; AB042432; BAA95623.1; -; Genomic_DNA. DR EMBL; AB042523; BAA95660.1; -; Genomic_DNA. DR EMBL; AB042524; BAA95647.1; -; Genomic_DNA. DR EMBL; AB042809; BAA95802.1; -; Genomic_DNA. DR EMBL; AB049357; BAB13808.1; -; Genomic_DNA. DR PIR; A55746; A55746. DR PIR; B55746; QXMS3M. DR RefSeq; NP_904335.1; NC_005089.1. DR RefSeq; YP_220557.1; NC_006914.1. DR ProteinModelPortal; P03899; -. DR SMR; P03899; 3-112. DR PhosphoSite; P03899; -. DR PaxDb; P03899; -. DR PRIDE; P03899; -. DR Ensembl; ENSMUST00000082411; ENSMUSP00000080998; ENSMUSG00000064360. DR GeneID; 17718; -. DR GeneID; 3338896; -. DR KEGG; mmu:17718; -. DR CTD; 4537; -. DR MGI; MGI:102499; mt-Nd3. DR eggNOG; COG0838; -. DR HOGENOM; HOG000100119; -. DR HOVERGEN; HBG017392; -. DR InParanoid; P03899; -. DR KO; K03880; -. DR OMA; LPFSMKF; -. DR OrthoDB; EOG7RV9K7; -. DR ProtClustDB; MTH00106; -. DR NextBio; 292338; -. DR PRO; PR:P03899; -. DR Genevestigator; P03899; -. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005747; C:mitochondrial respiratory chain complex I; IEA:Ensembl. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:UniProtKB-EC. DR InterPro; IPR000440; NADH_UbQ/plastoQ_OxRdtase_su3. DR PANTHER; PTHR11058; PTHR11058; 1. DR Pfam; PF00507; Oxidored_q4; 1. PE 3: Inferred from homology; KW Complete proteome; Electron transport; Membrane; Mitochondrion; NAD; KW Oxidoreductase; Reference proteome; Respiratory chain; Transmembrane; KW Transmembrane helix; Transport; Ubiquinone. FT CHAIN 1 115 NADH-ubiquinone oxidoreductase chain 3. FT /FTId=PRO_0000117765. FT TRANSMEM 3 23 Helical; (Potential). FT TRANSMEM 55 75 Helical; (Potential). FT TRANSMEM 86 106 Helical; (Potential). FT CONFLICT 16 16 T -> A (in Ref. 2; AAA19255). FT CONFLICT 33 33 Missing (in Ref. 1; AAB48651/CAA24086). SQ SEQUENCE 115 AA; 13219 MW; 6925F293601CB391 CRC64; MNLYTVIFIN ILLSLTLILV AFWLPQMNLY SEKANPYECG FDPTSSARLP FSMKFFLVAI TFLLFDLEIA LLLPLPWAIQ TIKTSTMMIM AFILVTILSL GLAYEWTQKG LEWTE // ID NU4LM_MOUSE Reviewed; 97 AA. AC P03903; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 21-JUL-1986, sequence version 1. DT 19-FEB-2014, entry version 88. DE RecName: Full=NADH-ubiquinone oxidoreductase chain 4L; DE EC=1.6.5.3; DE AltName: Full=NADH dehydrogenase subunit 4L; GN Name=Mtnd4l; Synonyms=mt-Nd4l, Nd4l; OS Mus musculus (Mouse). OG Mitochondrion. OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=7332926; DOI=10.1016/0092-8674(81)90300-7; RA Bibb M.J., van Etten R.A., Wright C.T., Walberg M.W., Clayton D.A.; RT "Sequence and gene organization of mouse mitochondrial DNA."; RL Cell 26:167-180(1981). CC -!- FUNCTION: Core subunit of the mitochondrial membrane respiratory CC chain NADH dehydrogenase (Complex I) that is believed to belong to CC the minimal assembly required for catalysis. Complex I functions CC in the transfer of electrons from NADH to the respiratory chain. CC The immediate electron acceptor for the enzyme is believed to be CC ubiquinone (By similarity). CC -!- CATALYTIC ACTIVITY: NADH + ubiquinone + 5 H(+)(In) = NAD(+) + CC ubiquinol + 4 H(+)(Out). CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane; Multi-pass membrane CC protein (By similarity). CC -!- SIMILARITY: Belongs to the complex I subunit 4L family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; J01420; AAB48652.1; -; Genomic_DNA. DR EMBL; V00711; CAA24087.1; -; Genomic_DNA. DR PIR; A00430; QXMS4L. DR ProteinModelPortal; P03903; -. DR SMR; P03903; 8-96. DR PaxDb; P03903; -. DR MGI; MGI:102497; mt-Nd4l. DR eggNOG; NOG260597; -. DR HOVERGEN; HBG071122; -. DR NextBio; 35563512; -. DR Bgee; P03903; -. DR Genevestigator; P03903; -. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell. DR GO; GO:0070469; C:respiratory chain; IEA:UniProtKB-KW. DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:UniProtKB-EC. DR GO; GO:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro. DR InterPro; IPR001133; NADH_UbQ_OxRdtase_chain4L/K. DR PANTHER; PTHR11434; PTHR11434; 1. DR Pfam; PF00420; Oxidored_q2; 1. PE 3: Inferred from homology; KW Complete proteome; Electron transport; Membrane; Mitochondrion; NAD; KW Oxidoreductase; Reference proteome; Respiratory chain; Transmembrane; KW Transmembrane helix; Transport; Ubiquinone. FT CHAIN 1 97 NADH-ubiquinone oxidoreductase chain 4L. FT /FTId=PRO_0000118448. FT TRANSMEM 2 22 Helical; (Potential). FT TRANSMEM 26 46 Helical; (Potential). FT TRANSMEM 58 78 Helical; (Potential). SQ SEQUENCE 97 AA; 10494 MW; FFA1596E86F91D34 CRC64; MPSTFFNLTM AFSLSLLGTL MFRSHLMSTL LCLEGMVLSL FIMTSVTSLN SNSMSSMPIP ITLVFAACEA AVGLALLVKV SNTYGTDYVQ NLNLLQC // ID NU4M_MOUSE Reviewed; 459 AA. AC P03911; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 21-JUL-1986, sequence version 1. DT 19-MAR-2014, entry version 102. DE RecName: Full=NADH-ubiquinone oxidoreductase chain 4; DE EC=1.6.5.3; DE AltName: Full=NADH dehydrogenase subunit 4; GN Name=Mtnd4; Synonyms=mt-Nd4, Nd4; OS Mus musculus (Mouse). OG Mitochondrion. OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=7332926; DOI=10.1016/0092-8674(81)90300-7; RA Bibb M.J., van Etten R.A., Wright C.T., Walberg M.W., Clayton D.A.; RT "Sequence and gene organization of mouse mitochondrial DNA."; RL Cell 26:167-180(1981). RN [2] RP PROTEIN SEQUENCE OF 246-255 AND 419-432, AND MASS SPECTROMETRY. RC STRAIN=C57BL/6; TISSUE=Brain; RA Lubec G., Kang S.U.; RL Submitted (APR-2007) to UniProtKB. CC -!- FUNCTION: Core subunit of the mitochondrial membrane respiratory CC chain NADH dehydrogenase (Complex I) that is believed to belong to CC the minimal assembly required for catalysis. Complex I functions CC in the transfer of electrons from NADH to the respiratory chain. CC The immediate electron acceptor for the enzyme is believed to be CC ubiquinone (By similarity). CC -!- CATALYTIC ACTIVITY: NADH + ubiquinone + 5 H(+)(In) = NAD(+) + CC ubiquinol + 4 H(+)(Out). CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane; Multi-pass membrane CC protein (By similarity). CC -!- SIMILARITY: Belongs to the complex I subunit 4 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; J01420; AAB48653.1; -; Genomic_DNA. DR EMBL; V00711; CAA24091.1; ALT_SEQ; Genomic_DNA. DR PIR; A00440; QXMS4M. DR RefSeq; NP_904337.1; NC_005089.1. DR ProteinModelPortal; P03911; -. DR SMR; P03911; 2-458. DR BioGrid; 201550; 1. DR IntAct; P03911; 1. DR PhosphoSite; P03911; -. DR PaxDb; P03911; -. DR PRIDE; P03911; -. DR Ensembl; ENSMUST00000082414; ENSMUSP00000081000; ENSMUSG00000064363. DR GeneID; 17719; -. DR KEGG; mmu:17719; -. DR CTD; 4538; -. DR MGI; MGI:102498; mt-Nd4. DR eggNOG; COG1008; -. DR HOGENOM; HOG000100683; -. DR HOVERGEN; HBG093667; -. DR InParanoid; P03911; -. DR KO; K03881; -. DR OMA; PNMIWIN; -. DR OrthoDB; EOG7DJSMN; -. DR ProtClustDB; MTH00110; -. DR TreeFam; TF343520; -. DR NextBio; 292341; -. DR Bgee; P03911; -. DR Genevestigator; P03911; -. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005747; C:mitochondrial respiratory chain complex I; IEA:Ensembl. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:UniProtKB-EC. DR GO; GO:0006120; P:mitochondrial electron transport, NADH to ubiquinone; IEA:InterPro. DR InterPro; IPR010227; NADH_Q_OxRdtase_chainM/4. DR InterPro; IPR001750; NADH_UbQ/plastoQ_OxRdtase. DR InterPro; IPR003918; NADH_UbQ_OxRdtase. DR InterPro; IPR000260; NADH_UbQ_OxRdtase_chain4_N. DR Pfam; PF00361; Oxidored_q1; 1. DR Pfam; PF01059; Oxidored_q5_N; 1. DR PRINTS; PR01437; NUOXDRDTASE4. DR TIGRFAMs; TIGR01972; NDH_I_M; 1. PE 1: Evidence at protein level; KW Complete proteome; Direct protein sequencing; Electron transport; KW Membrane; Mitochondrion; NAD; Oxidoreductase; Reference proteome; KW Respiratory chain; Transmembrane; Transmembrane helix; Transport; KW Ubiquinone. FT CHAIN 1 459 NADH-ubiquinone oxidoreductase chain 4. FT /FTId=PRO_0000117957. FT TRANSMEM 23 43 Helical; (Potential). FT TRANSMEM 60 80 Helical; (Potential). FT TRANSMEM 90 110 Helical; (Potential). FT TRANSMEM 113 133 Helical; (Potential). FT TRANSMEM 147 167 Helical; (Potential). FT TRANSMEM 194 214 Helical; (Potential). FT TRANSMEM 224 244 Helical; (Potential). FT TRANSMEM 257 277 Helical; (Potential). FT TRANSMEM 284 303 Helical; (Potential). FT TRANSMEM 308 330 Helical; (Potential). FT TRANSMEM 350 370 Helical; (Potential). FT TRANSMEM 392 412 Helical; (Potential). FT TRANSMEM 434 454 Helical; (Potential). SQ SEQUENCE 459 AA; 51882 MW; 62727CC11CCD137D CRC64; MLKIILPSLM LLPLTWLSSP KKTWTNVTSY SFLISLTSLT LLWQTDENYK NFSNMFSSDP LSTPLIILTA WLLPLMLMAS QNHLKKDNNV LQKLYISMLI SLQILLIMTF SATELIMFYI LFEATLIPTL IIITRWGNQT ERLNAGIYFL FYTLIGSIPL LIALILIQNH VGTLNLMILS FTTHTLDASW SNNLLWLACM MAFLIKMPLY GVHLWLPKAH VEAPIAGSMI LAAILLKLGS YGMIRISIIL DPLTKYMAYP FILLSLWGMI MTSSICLRQT DLKSLIAYSS VSHMALVIAS IMIQTPWSFM GATMLMIAHG LTSSLLFCLA NSNYERIHSR TMIMARGLQM VFPLMATWWL MASLANLALP PSINLMGELF ITMSLFSWSN FTIILMGINI IITGMYSMYM IITTQRGKLT NHMINLQPSH TRELTLMALH MIPLILLTTS PKLITGLTM // ID NU5M_MOUSE Reviewed; 607 AA. AC P03921; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1990, sequence version 2. DT 19-MAR-2014, entry version 91. DE RecName: Full=NADH-ubiquinone oxidoreductase chain 5; DE EC=1.6.5.3; DE AltName: Full=NADH dehydrogenase subunit 5; GN Name=Mtnd5; Synonyms=mt-Nd5, Nd5; OS Mus musculus (Mouse). OG Mitochondrion. OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=7332926; DOI=10.1016/0092-8674(81)90300-7; RA Bibb M.J., van Etten R.A., Wright C.T., Walberg M.W., Clayton D.A.; RT "Sequence and gene organization of mouse mitochondrial DNA."; RL Cell 26:167-180(1981). CC -!- FUNCTION: Core subunit of the mitochondrial membrane respiratory CC chain NADH dehydrogenase (Complex I) that is believed to belong to CC the minimal assembly required for catalysis. Complex I functions CC in the transfer of electrons from NADH to the respiratory chain. CC The immediate electron acceptor for the enzyme is believed to be CC ubiquinone (By similarity). CC -!- CATALYTIC ACTIVITY: NADH + ubiquinone + 5 H(+)(In) = NAD(+) + CC ubiquinol + 4 H(+)(Out). CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass CC membrane protein (By similarity). CC -!- SIMILARITY: Belongs to the complex I subunit 5 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; J01420; AAB48654.1; -; Genomic_DNA. DR EMBL; V00711; CAA24088.1; -; Genomic_DNA. DR PIR; A00451; QXMS5M. DR ProteinModelPortal; P03921; -. DR SMR; P03921; 8-602. DR IntAct; P03921; 1. DR PhosphoSite; P03921; -. DR PaxDb; P03921; -. DR PRIDE; P03921; -. DR MGI; MGI:102496; mt-Nd5. DR eggNOG; COG1009; -. DR HOGENOM; HOG000100570; -. DR HOVERGEN; HBG108343; -. DR InParanoid; P03921; -. DR NextBio; 35563513; -. DR Genevestigator; P03921; -. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell. DR GO; GO:0070469; C:respiratory chain; IEA:UniProtKB-KW. DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:UniProtKB-EC. DR GO; GO:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro. DR InterPro; IPR010934; NADH_DH_su5_C. DR InterPro; IPR001750; NADH_UbQ/plastoQ_OxRdtase. DR InterPro; IPR001516; NADH_UbQ_OxRdtase_chain5/L_N. DR InterPro; IPR003945; NADHpl_OxRdtase_5. DR Pfam; PF06455; NADH5_C; 1. DR Pfam; PF00361; Oxidored_q1; 1. DR Pfam; PF00662; Oxidored_q1_N; 1. DR TIGRFAMs; TIGR01974; NDH_I_L; 1. PE 3: Inferred from homology; KW Complete proteome; Electron transport; Membrane; Mitochondrion; KW Mitochondrion inner membrane; NAD; Oxidoreductase; Reference proteome; KW Respiratory chain; Transmembrane; Transmembrane helix; Transport; KW Ubiquinone. FT CHAIN 1 607 NADH-ubiquinone oxidoreductase chain 5. FT /FTId=PRO_0000118114. FT TRANSMEM 3 23 Helical; (Potential). FT TRANSMEM 35 55 Helical; (Potential). FT TRANSMEM 84 104 Helical; (Potential). FT TRANSMEM 117 137 Helical; (Potential). FT TRANSMEM 140 160 Helical; (Potential). FT TRANSMEM 171 191 Helical; (Potential). FT TRANSMEM 210 230 Helical; (Potential). FT TRANSMEM 241 261 Helical; (Potential). FT TRANSMEM 272 292 Helical; (Potential). FT TRANSMEM 301 320 Helical; (Potential). FT TRANSMEM 324 344 Helical; (Potential). FT TRANSMEM 365 385 Helical; (Potential). FT TRANSMEM 405 427 Helical; (Potential). FT TRANSMEM 457 477 Helical; (Potential). FT TRANSMEM 482 502 Helical; (Potential). FT TRANSMEM 586 606 Helical; (Potential). SQ SEQUENCE 607 AA; 68441 MW; 32ECC262CDC78B10 CRC64; MNIFTTSILL IFILLLSPIL ISMSNLIKHI NFPLYTTTSI KFSFIISLLP LLMFFHNNME YMITTWHWVT MNSMELKMSF KTDFFSILFT SVALFVTWSI MQLSSWYMHS DPNINRFIKY LTLFLITMLI LTSANNMFQL FIGWEGVGIM SFLLIGWWYG RTDANTAALQ AILYNRIGDI GFILAMVWFS LNMNSWELQQ IMFSNNNDNL IPLMGLLIAA TGKSAQFGLH PWLPSAMEGP TPVSALLHSS TMVVAGIFLL VRFHPLTTNN NFILTTMLCL GALTTLFTAI CALTQNDIKK IIAFSTSSQL GLMMVTLGMN QPHLAFLHIC THAFFKAMLF MCSGSIIHSL ADEQDIRKMG NITKIMPFTS SCLVIGSLAL TGMPFLTGFY SKDLIIEAIN TCNTNAWALL ITLIATSMTA MYSMRIIYFV TMTKPRFPPL ISINENDPDL MNPIKRLAFG SIFAGFVISY NIPPTSIPVL TMPWFLKTTA LIISVLGFLI ALELNNLTMK LSMNKANPYS SFSTLLGFFP SIIHRITPMK SLNLSLKTSL TLLDLIWLEK TIPKSTSTLH TNMTTLTTNQ KGLIKLYFMS FLINIILIII LYSINLE // ID NU6M_MOUSE Reviewed; 172 AA. AC P03925; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 21-JUL-1986, sequence version 1. DT 19-FEB-2014, entry version 86. DE RecName: Full=NADH-ubiquinone oxidoreductase chain 6; DE EC=1.6.5.3; DE AltName: Full=NADH dehydrogenase subunit 6; GN Name=Mtnd6; Synonyms=mt-Nd6, Nd6; OS Mus musculus (Mouse). OG Mitochondrion. OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=7332926; DOI=10.1016/0092-8674(81)90300-7; RA Bibb M.J., van Etten R.A., Wright C.T., Walberg M.W., Clayton D.A.; RT "Sequence and gene organization of mouse mitochondrial DNA."; RL Cell 26:167-180(1981). CC -!- FUNCTION: Core subunit of the mitochondrial membrane respiratory CC chain NADH dehydrogenase (Complex I) that is believed to belong to CC the minimal assembly required for catalysis. Complex I functions CC in the transfer of electrons from NADH to the respiratory chain. CC The immediate electron acceptor for the enzyme is believed to be CC ubiquinone (By similarity). CC -!- CATALYTIC ACTIVITY: NADH + ubiquinone + 5 H(+)(In) = NAD(+) + CC ubiquinol + 4 H(+)(Out). CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane; Multi-pass membrane CC protein (Potential). CC -!- SIMILARITY: Belongs to the complex I subunit 6 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; J01420; AAB48655.1; -; Genomic_DNA. DR EMBL; V00711; CAA24089.1; -; Genomic_DNA. DR PIR; A00457; DEMSN6. DR RefSeq; NP_904339.1; NC_005089.1. DR PhosphoSite; P03925; -. DR Ensembl; ENSMUST00000082419; ENSMUSP00000081002; ENSMUSG00000064368. DR GeneID; 17722; -. DR KEGG; mmu:17722; -. DR CTD; 4541; -. DR MGI; MGI:102495; mt-Nd6. DR eggNOG; NOG70008; -. DR HOGENOM; HOG000113881; -. DR HOVERGEN; HBG007487; -. DR InParanoid; P03925; -. DR KO; K03884; -. DR OMA; VVFGYTT; -. DR OrthoDB; EOG7HF1MX; -. DR ProtClustDB; MTH00109; -. DR TreeFam; TF343324; -. DR NextBio; 292350; -. DR PRO; PR:P03925; -. DR Bgee; P03925; -. DR Genevestigator; P03925; -. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR GO; GO:0070469; C:respiratory chain; IEA:UniProtKB-KW. DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:UniProtKB-EC. DR InterPro; IPR001457; NADH_UbQ/plastoQ_OxRdtase_su6. DR Pfam; PF00499; Oxidored_q3; 1. PE 3: Inferred from homology; KW Complete proteome; Electron transport; Membrane; Mitochondrion; NAD; KW Oxidoreductase; Reference proteome; Respiratory chain; Transmembrane; KW Transmembrane helix; Transport; Ubiquinone. FT CHAIN 1 172 NADH-ubiquinone oxidoreductase chain 6. FT /FTId=PRO_0000118304. FT TRANSMEM 1 21 Helical; (Potential). FT TRANSMEM 38 58 Helical; (Potential). FT TRANSMEM 86 106 Helical; (Potential). FT TRANSMEM 147 167 Helical; (Potential). SQ SEQUENCE 172 AA; 18626 MW; 55DE2331AB0A1115 CRC64; MNNYIFVLSS LFLVGCLGLA LKPSPIYGGL GLIVSGFVGC LMVLGFGGSF LGLMVFLIYL GGMLVVFGYT TAMATEEYPE TWGSNWLILG FLVLGVIMEV FLICVLNYYD EVGVINLDGL GDWLMYEVDD VGVMLEGGIG VAAMYSCATW MMVVAGWSLF AGIFIIIEIT RD // ID NXN_MOUSE Reviewed; 435 AA. AC P97346; Q5H8T6; Q5H8U0; Q99KF3; DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1997, sequence version 1. DT 19-MAR-2014, entry version 116. DE RecName: Full=Nucleoredoxin; DE EC=1.8.1.8; DE AltName: Full=Protein Red-1; GN Name=Nxn; Synonyms=Gn25; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, SUBCELLULAR RP LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE. RC STRAIN=C57BL/6J; TISSUE=Skin; RX PubMed=9119370; DOI=10.1006/geno.1996.4493; RA Kurooka H., Kato K., Minoguchi S., Takahashi Y., Ikeda J.-E., Habu S., RA Osawa N., Buchberg A.M., Moriwaki K., Shisa H., Honjo T.; RT "Cloning and characterization of the nucleoredoxin gene that encodes a RT novel nuclear protein related to thioredoxin."; RL Genomics 39:331-339(1997). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1). RC STRAIN=C3H, CTS, NOD, and NSY; TISSUE=Kidney, and Liver; RX PubMed=15670764; DOI=10.1016/j.bbrc.2004.12.149; RA Babaya N., Ikegami H., Fujisawa T., Nojima K., Itoi-Babaya M., RA Inoue K., Ohno T., Shibata M., Ogihara T.; RT "Susceptibility to streptozotocin-induced diabetes is mapped to mouse RT chromosome 11."; RL Biochem. Biophys. Res. Commun. 328:158-164(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC STRAIN=C57BL/6J; TISSUE=Sympathetic ganglion; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC STRAIN=Czech II; TISSUE=Mammary tumor, and Olfactory epithelium; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=10903915; DOI=10.1006/bbrc.2000.3106; RA Hirota K., Matsui M., Murata M., Takashima Y., Cheng F.S., Itoh T., RA Fukuda K., Yodoi J.; RT "Nucleoredoxin, glutaredoxin, and thioredoxin differentially regulate RT NF-kappaB, AP-1, and CREB activation in HEK293 cells."; RL Biochem. Biophys. Res. Commun. 274:177-182(2000). RN [7] RP FUNCTION, IDENTIFICATION IN A COMPLEX WITH PHOSPHATASE 2A, AND RP INTERACTION WITH PPP2CA. RX PubMed=16764867; DOI=10.1016/j.febslet.2006.04.101; RA Lechward K., Sugajska E., de Baere I., Goris J., Hemmings B.A., RA Zolnierowicz S.; RT "Interaction of nucleoredoxin with protein phosphatase 2A."; RL FEBS Lett. 580:3631-3637(2006). RN [8] RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, INTERACTION WITH DVL1, RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF CYS-205 AND CYS-208. RX PubMed=16604061; DOI=10.1038/ncb1405; RA Funato Y., Michiue T., Asashima M., Miki H.; RT "The thioredoxin-related redox-regulating protein nucleoredoxin RT inhibits Wnt-beta-catenin signalling through dishevelled."; RL Nat. Cell Biol. 8:501-508(2006). RN [9] RP FUNCTION, AND DISRUPTION PHENOTYPE. RX PubMed=20970343; DOI=10.1016/j.cub.2010.09.065; RA Funato Y., Terabayashi T., Sakamoto R., Okuzaki D., Ichise H., RA Nojima H., Yoshida N., Miki H.; RT "Nucleoredoxin sustains Wnt/beta-catenin signaling by retaining a pool RT of inactive dishevelled protein."; RL Curr. Biol. 20:1945-1952(2010). CC -!- FUNCTION: Functions as a redox-dependent negative regulator of the CC Wnt signaling pathway, possibly by preventing ubiquitination of CC DVL3 by the BCR(KLHL12) complex. May also function as a CC transcriptional regulator act as a regulator of protein CC phosphatase 2A (PP2A). CC -!- CATALYTIC ACTIVITY: Protein dithiol + NAD(P)(+) = protein CC disulfide + NAD(P)H. CC -!- SUBUNIT: Associates with the phosphatase 2A holoenzyme. Interacts CC with PPP2CA; the interaction is direct. Interacts with DVL1 (via CC PDZ domain); the interaction is direct and regulated by oxidative CC stress. CC -!- INTERACTION: CC P67775:PPP2CA (xeno); NbExp=2; IntAct=EBI-309684, EBI-712311; CC P30153:PPP2R1A (xeno); NbExp=2; IntAct=EBI-309684, EBI-302388; CC Q9UGP8:SEC63 (xeno); NbExp=6; IntAct=EBI-309684, EBI-1045560; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol. Nucleus. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P97346-1; Sequence=Displayed; CC Name=2; CC IsoId=P97346-2; Sequence=VSP_033396, VSP_033397; CC -!- TISSUE SPECIFICITY: Widely expressed with higher expression in CC testis and skin. CC -!- DEVELOPMENTAL STAGE: Specifically expressed form E9.5 to E12.5 in CC limb buds. CC -!- DISRUPTION PHENOTYPE: Perinatal lethality, possibly due abnormal CC cardiovascular development. Osteoblasts show an aberrant CC activation of the Wnt signaling pathway. CC -!- SIMILARITY: Belongs to the nucleoredoxin family. CC -!- SIMILARITY: Contains 1 thioredoxin domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X92750; CAA63408.1; -; Genomic_DNA. DR EMBL; AB095441; BAD88798.1; -; mRNA. DR EMBL; AB095442; BAD88799.1; -; mRNA. DR EMBL; AB095443; BAD88800.1; -; mRNA. DR EMBL; AB095444; BAD88801.1; -; mRNA. DR EMBL; AB096016; BAD88802.1; -; Genomic_DNA. DR EMBL; AB096017; BAD88803.1; -; Genomic_DNA. DR EMBL; AB096018; BAD88804.1; -; Genomic_DNA. DR EMBL; AB096019; BAD88805.1; -; Genomic_DNA. DR EMBL; AK149075; BAE28730.1; -; mRNA. DR EMBL; AL806529; CAI24674.1; -; Genomic_DNA. DR EMBL; AL663050; CAI24674.1; JOINED; Genomic_DNA. DR EMBL; AL663050; CAI25856.1; -; Genomic_DNA. DR EMBL; AL806529; CAI25856.1; JOINED; Genomic_DNA. DR EMBL; BC004688; AAH04688.1; -; mRNA. DR EMBL; BC058244; AAH58244.1; -; mRNA. DR RefSeq; NP_032776.1; NM_008750.5. DR UniGene; Mm.27915; -. DR ProteinModelPortal; P97346; -. DR SMR; P97346; 11-165, 196-296. DR IntAct; P97346; 6. DR MINT; MINT-2634582; -. DR PhosphoSite; P97346; -. DR PaxDb; P97346; -. DR PRIDE; P97346; -. DR Ensembl; ENSMUST00000021204; ENSMUSP00000021204; ENSMUSG00000020844. [P97346-1] DR GeneID; 18230; -. DR KEGG; mmu:18230; -. DR UCSC; uc007kfo.2; mouse. [P97346-1] DR CTD; 64359; -. DR MGI; MGI:109331; Nxn. DR eggNOG; NOG273116; -. DR GeneTree; ENSGT00530000063279; -. DR HOGENOM; HOG000007309; -. DR HOVERGEN; HBG053461; -. DR InParanoid; P97346; -. DR KO; K17609; -. DR OMA; WQDFVRD; -. DR OrthoDB; EOG70W3G2; -. DR TreeFam; TF331873; -. DR ChiTaRS; NXN; mouse. DR NextBio; 293664; -. DR PRO; PR:P97346; -. DR Bgee; P97346; -. DR Genevestigator; P97346; -. DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell. DR GO; GO:0005634; C:nucleus; IDA:MGI. DR GO; GO:0047134; F:protein-disulfide reductase activity; IEA:UniProtKB-EC. DR GO; GO:0004791; F:thioredoxin-disulfide reductase activity; IDA:MGI. DR GO; GO:0072358; P:cardiovascular system development; IMP:UniProtKB. DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW. DR GO; GO:0031397; P:negative regulation of protein ubiquitination; IMP:UniProtKB. DR GO; GO:0030178; P:negative regulation of Wnt signaling pathway; IMP:UniProtKB. DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW. DR Gene3D; 3.40.30.10; -; 2. DR InterPro; IPR012336; Thioredoxin-like_fold. DR SUPFAM; SSF52833; SSF52833; 3. DR PROSITE; PS51352; THIOREDOXIN_2; 1. PE 1: Evidence at protein level; KW Acetylation; Alternative splicing; Complete proteome; Cytoplasm; KW Developmental protein; Differentiation; NAD; Nucleus; Oxidoreductase; KW Reference proteome; Wnt signaling pathway. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 435 Nucleoredoxin. FT /FTId=PRO_0000332934. FT DOMAIN 167 314 Thioredoxin. FT MOD_RES 2 2 N-acetylserine (By similarity). FT VAR_SEQ 362 391 KEEEAPLLFFVAGEDDMTDSLRDYTNLPEA -> SAHHSGH FT VSPGQVRDGCRRDHPSHCGDFCE (in isoform 2). FT /FTId=VSP_033396. FT VAR_SEQ 392 435 Missing (in isoform 2). FT /FTId=VSP_033397. FT MUTAGEN 205 205 C->S: Loss of function and interaction FT with DVL1; when associated with S-208. FT MUTAGEN 208 208 C->S: Loss of function and interaction FT with DVL1; when associated with S-205. SQ SEQUENCE 435 AA; 48344 MW; C2AE7A65A5AB7843 CRC64; MSGFLEELLG DKLVTGGGEE VDVHSLGARG IALLGLYFGC SLSAPCAQLS ASLAAFYGRL RGDAAAGPGA GAGAGAAAEP EPRHRLEIVF VSSDQDQRQW QDFVRDMPWL ALPYKEKHRK LKLWNKYRVS NIPSLIFLDA TTGKVVCRNG LLVIRDDPEG LEFPWGPKPF REVIAGPLLR NNGQSLESSS LEGSHVGVYF SAHWCPPCRS LTRVLVESYR KIKEAGQEFE IIFVSADRSE ESFKQYFSEM PWLAVPYTDE ARRSRLNRLY GIQGIPTLIV LDPQGEVITR QGRVEVLNDE DCREFPWHPK PVLELSDSNA VQLNEGPCLV LFVDSEDDGE SEAAKQLIQP IAEKIIAKYK AKEEEAPLLF FVAGEDDMTD SLRDYTNLPE AAPLLTILDM SARAKYVMDV EEITPAIVET FVNDFLAEKL KPEPI // ID NXRD1_MOUSE Reviewed; 366 AA. AC Q9D3S5; DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 19-MAR-2014, entry version 82. DE RecName: Full=NADP-dependent oxidoreductase domain-containing protein 1; DE EC=1.-.-.-; DE AltName: Full=Pyrroline-5-carboxylate reductase-like protein C14orf148 homolog; GN Name=Noxred1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Testis; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: Probable oxidoreductase (By similarity). CC -!- SIMILARITY: Belongs to the pyrroline-5-carboxylate reductase CC family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK017096; BAB30594.1; -; mRNA. DR EMBL; BC125331; AAI25332.1; -; mRNA. DR EMBL; BC125333; AAI25334.1; -; mRNA. DR RefSeq; NP_082020.1; NM_027744.1. DR RefSeq; XP_006516294.1; XM_006516231.1. DR UniGene; Mm.79198; -. DR ProteinModelPortal; Q9D3S5; -. DR SMR; Q9D3S5; 81-176. DR STRING; 10090.ENSMUSP00000021423; -. DR PhosphoSite; Q9D3S5; -. DR PaxDb; Q9D3S5; -. DR PRIDE; Q9D3S5; -. DR Ensembl; ENSMUST00000021423; ENSMUSP00000021423; ENSMUSG00000072919. DR GeneID; 71275; -. DR KEGG; mmu:71275; -. DR UCSC; uc007oio.1; mouse. DR CTD; 122945; -. DR MGI; MGI:1918525; Noxred1. DR eggNOG; NOG331383; -. DR GeneTree; ENSGT00390000007632; -. DR HOGENOM; HOG000111827; -. DR HOVERGEN; HBG081280; -. DR InParanoid; Q9D3S5; -. DR OMA; HATFFCK; -. DR OrthoDB; EOG7HQN9P; -. DR TreeFam; TF335538; -. DR NextBio; 333423; -. DR PRO; PR:Q9D3S5; -. DR Bgee; Q9D3S5; -. DR CleanEx; MM_4933437F05RIK; -. DR Genevestigator; Q9D3S5; -. DR GO; GO:0004735; F:pyrroline-5-carboxylate reductase activity; IEA:InterPro. DR GO; GO:0006561; P:proline biosynthetic process; IEA:InterPro. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR000304; Pyrroline-COOH_reductase. DR PANTHER; PTHR11645; PTHR11645; 1. PE 2: Evidence at transcript level; KW Complete proteome; Oxidoreductase; Reference proteome. FT CHAIN 1 366 NADP-dependent oxidoreductase domain- FT containing protein 1. FT /FTId=PRO_0000280280. SQ SEQUENCE 366 AA; 41666 MW; AF86FD2D1979611B CRC64; MEMLEDLESL RFEFGIPEEE RYWLYLQGRY RGLMIKGCAH AAFFCKMFST LSNLLQNLPR TIHPRTVSFD NAATEDELLT VGIIGCGHLG KQLTNVLLKT VPIPAENLQI STRRPESLGE LRKLGVRCVY DNAAVASWAK VLFLCCLPAQ LPNICLEIQS KLNKHCTVYS FVSAIPLPRL KSLLNHTNIL RPQYQFAEDY DNIWGENEEV PIALQDTTII RGTCPYNNLG GVILNVKWIE GLCYALINAC TSRSVFHSQV LKLLNKLLLP MHLESCTTDP ESCPQFNLTD FMSKSYVKNL YQKRPFPWFD LTTVQLKETP FSQHISATPS LQDHISLLYC EVFGLTISEE ELPYISTVIR PLVEEK // ID ODBA_MOUSE Reviewed; 442 AA. AC P50136; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 19-MAR-2014, entry version 108. DE RecName: Full=2-oxoisovalerate dehydrogenase subunit alpha, mitochondrial; DE EC=1.2.4.4; DE AltName: Full=Branched-chain alpha-keto acid dehydrogenase E1 component alpha chain; DE Short=BCKDE1A; DE Short=BCKDH E1-alpha; DE Flags: Precursor; GN Name=Bckdha; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=C57BL/6J; TISSUE=Liver; RX PubMed=8761456; RA Costeas P.A., Chinsky J.M.; RT "Effects of insulin on the regulation of branched-chain alpha-keto RT acid dehydrogenase E1 alpha subunit gene expression."; RL Biochem. J. 318:85-92(1996). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=17242355; DOI=10.1073/pnas.0609836104; RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; RT "Large-scale phosphorylation analysis of mouse liver."; RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). RN [3] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-334, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006; RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M., RA Thibault P.; RT "The phagosomal proteome in interferon-gamma-activated macrophages."; RL Immunity 30:143-154(2009). RN [4] RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-353 AND LYS-377, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., RA Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). RN [5] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-353, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23576753; DOI=10.1073/pnas.1302961110; RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., RA Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.; RT "Label-free quantitative proteomics of the lysine acetylome in RT mitochondria identifies substrates of SIRT3 in metabolic pathways."; RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013). CC -!- FUNCTION: The branched-chain alpha-keto dehydrogenase complex CC catalyzes the overall conversion of alpha-keto acids to acyl-CoA CC and CO(2). It contains multiple copies of three enzymatic CC components: branched-chain alpha-keto acid decarboxylase (E1), CC lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3). CC -!- CATALYTIC ACTIVITY: 3-methyl-2-oxobutanoate + CC [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] CC lipoyllysine = [dihydrolipoyllysine-residue (2- CC methylpropanoyl)transferase] S-(2- CC methylpropanoyl)dihydrolipoyllysine + CO(2). CC -!- COFACTOR: Thiamine pyrophosphate. CC -!- SUBUNIT: Heterotetramer of alpha and beta chains (By similarity). CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix. CC -!- MISCELLANEOUS: Bound potassium ions stabilize the protein CC structure (By similarity). CC -!- SIMILARITY: Belongs to the BCKDHA family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L47335; AAB38422.1; -; mRNA. DR PIR; S71881; S71881. DR UniGene; Mm.25848; -. DR ProteinModelPortal; P50136; -. DR SMR; P50136; 48-442. DR IntAct; P50136; 4. DR MINT; MINT-4105779; -. DR PhosphoSite; P50136; -. DR SWISS-2DPAGE; P50136; -. DR PaxDb; P50136; -. DR PRIDE; P50136; -. DR MGI; MGI:107701; Bckdha. DR eggNOG; COG1071; -. DR HOVERGEN; HBG002459; -. DR InParanoid; P50136; -. DR PRO; PR:P50136; -. DR Genevestigator; P50136; -. DR GO; GO:0005947; C:mitochondrial alpha-ketoglutarate dehydrogenase complex; ISS:HGNC. DR GO; GO:0003863; F:3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) activity; IEA:UniProtKB-EC. DR GO; GO:0003826; F:alpha-ketoacid dehydrogenase activity; ISS:HGNC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0009083; P:branched-chain amino acid catabolic process; ISS:HGNC. DR InterPro; IPR001017; DH_E1. DR Pfam; PF00676; E1_dh; 1. PE 1: Evidence at protein level; KW Acetylation; Complete proteome; Metal-binding; Mitochondrion; KW Oxidoreductase; Phosphoprotein; Potassium; Reference proteome; KW Thiamine pyrophosphate; Transit peptide. FT TRANSIT 1 42 Mitochondrion (By similarity). FT CHAIN 43 442 2-oxoisovalerate dehydrogenase subunit FT alpha, mitochondrial. FT /FTId=PRO_0000020467. FT REGION 154 156 Thiamine pyrophosphate binding (By FT similarity). FT METAL 203 203 Potassium (By similarity). FT METAL 208 208 Potassium (By similarity). FT METAL 209 209 Potassium (By similarity). FT MOD_RES 334 334 Phosphoserine. FT MOD_RES 344 344 Phosphoserine (By similarity). FT MOD_RES 353 353 N6-acetyllysine; alternate. FT MOD_RES 353 353 N6-succinyllysine; alternate. FT MOD_RES 377 377 N6-succinyllysine. SQ SEQUENCE 442 AA; 50371 MW; 3388213D88BC7C92 CRC64; MSAAKIWRPS RGLRQAALLL LGRSGVRGLA RSHPSRQQQQ QFPSLDDKPQ FPGASAEFVD KLEFIQPNVI SGIPIYRVMD RQGQIINPSE DPHLPQEEVL KFYRSMTLLN TMDRILYESQ REGRISFYMT NYGEEGTHVG SAAALERTDL VFGQYREAGV LMYRDYPLEL FMSQCYGNVN DPGKGRQMPV HYGCKERHFV TISSPLATQI PQAVGAAYAA KRANANRIVI CYFGEGAASE GDAHAGFNFA ATLECPIIFF CRNNGYAIST PTSEQYRGDG IAARGPGYGI KSIRVDGNDV FAVYNATKEA RRRAVAENQP FLIEAMTYRI GHHSTSDDSS AYRSVDEVNY WDKQDHPISR LRQYLLNQGW WDEEQEKAWR KQSRKKVMEA FEQAERKLKP NPSLLFSDVY QEMPAQLRRQ QESLARHLQT YGEHYPLDHF EK // ID ODBB_MOUSE Reviewed; 390 AA. AC Q6P3A8; DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot. DT 04-DEC-2007, sequence version 2. DT 19-MAR-2014, entry version 75. DE RecName: Full=2-oxoisovalerate dehydrogenase subunit beta, mitochondrial; DE EC=1.2.4.4; DE AltName: Full=Branched-chain alpha-keto acid dehydrogenase E1 component beta chain; DE Short=BCKDE1B; DE Short=BCKDH E1-beta; DE Flags: Precursor; GN Name=Bckdhb; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=8268236; DOI=10.1016/0167-4781(93)90023-7; RA Chinsky J.M., Costeas P.A.; RT "Molecular cloning and analysis of the expression of the E1 beta RT subunit of branched chain alpha-ketoacid dehydrogenase in mice."; RL Biochim. Biophys. Acta 1216:499-503(1993). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC STRAIN=C57BL/6J; TISSUE=Mammary gland; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-230 AND LYS-239, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23576753; DOI=10.1073/pnas.1302961110; RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., RA Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.; RT "Label-free quantitative proteomics of the lysine acetylome in RT mitochondria identifies substrates of SIRT3 in metabolic pathways."; RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013). CC -!- FUNCTION: The branched-chain alpha-keto dehydrogenase complex CC catalyzes the overall conversion of alpha-keto acids to acyl-CoA CC and CO(2). It contains multiple copies of three enzymatic CC components: branched-chain alpha-keto acid decarboxylase (E1), CC lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3). CC -!- CATALYTIC ACTIVITY: 3-methyl-2-oxobutanoate + CC [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] CC lipoyllysine = [dihydrolipoyllysine-residue (2- CC methylpropanoyl)transferase] S-(2- CC methylpropanoyl)dihydrolipoyllysine + CO(2). CC -!- SUBUNIT: Heterotetramer of 2 alpha and 2 beta chains (By CC similarity). CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q6P3A8-1; Sequence=Displayed; CC Name=2; CC IsoId=Q6P3A8-2; Sequence=VSP_029841; CC Note=No experimental confirmation available; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L16992; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; BC064099; AAH64099.1; -; mRNA. DR RefSeq; NP_954665.1; NM_199195.1. DR RefSeq; XP_006510848.1; XM_006510785.1. DR UniGene; Mm.12819; -. DR ProteinModelPortal; Q6P3A8; -. DR SMR; Q6P3A8; 62-390. DR IntAct; Q6P3A8; 1. DR MINT; MINT-1860867; -. DR PaxDb; Q6P3A8; -. DR PRIDE; Q6P3A8; -. DR Ensembl; ENSMUST00000034801; ENSMUSP00000034801; ENSMUSG00000032263. [Q6P3A8-2] DR GeneID; 12040; -. DR KEGG; mmu:12040; -. DR UCSC; uc009qwr.1; mouse. [Q6P3A8-1] DR CTD; 594; -. DR MGI; MGI:88137; Bckdhb. DR eggNOG; COG0022; -. DR GeneTree; ENSGT00530000063423; -. DR HOGENOM; HOG000281451; -. DR HOVERGEN; HBG108210; -. DR InParanoid; Q6P3A8; -. DR KO; K00167; -. DR OMA; HAQEWDY; -. DR OrthoDB; EOG79SDXF; -. DR TreeFam; TF105947; -. DR NextBio; 280301; -. DR PRO; PR:Q6P3A8; -. DR Bgee; Q6P3A8; -. DR Genevestigator; Q6P3A8; -. DR GO; GO:0005947; C:mitochondrial alpha-ketoglutarate dehydrogenase complex; ISS:HGNC. DR GO; GO:0005743; C:mitochondrial inner membrane; TAS:MGI. DR GO; GO:0003863; F:3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) activity; IEA:UniProtKB-EC. DR GO; GO:0003826; F:alpha-ketoacid dehydrogenase activity; IDA:MGI. DR GO; GO:0009083; P:branched-chain amino acid catabolic process; ISS:HGNC. DR GO; GO:0051591; P:response to cAMP; IEA:Ensembl. DR GO; GO:0051384; P:response to glucocorticoid; IEA:Ensembl. DR GO; GO:0007584; P:response to nutrient; IEA:Ensembl. DR Gene3D; 3.40.50.920; -; 1. DR InterPro; IPR009014; Transketo_C/Pyr-ferredox_oxred. DR InterPro; IPR005475; Transketolase-like_Pyr-bd. DR InterPro; IPR005476; Transketolase_C. DR Pfam; PF02779; Transket_pyr; 1. DR Pfam; PF02780; Transketolase_C; 1. DR SMART; SM00861; Transket_pyr; 1. DR SUPFAM; SSF52922; SSF52922; 1. PE 1: Evidence at protein level; KW Acetylation; Alternative splicing; Complete proteome; Mitochondrion; KW Oxidoreductase; Reference proteome; Transit peptide. FT TRANSIT 1 48 Mitochondrion (Potential). FT CHAIN 49 390 2-oxoisovalerate dehydrogenase subunit FT beta, mitochondrial. FT /FTId=PRO_0000312367. FT MOD_RES 230 230 N6-acetyllysine. FT MOD_RES 239 239 N6-acetyllysine. FT VAR_SEQ 1 68 Missing (in isoform 2). FT /FTId=VSP_029841. SQ SEQUENCE 390 AA; 42880 MW; 507E04F01BCCD298 CRC64; MAAVAARAGG LLWLRAAGAE RRRCGLRCAA LVQGFLQPGG EDTAQKRRVA HFTFHPDPES LQYGQTQKMN LFQSITSALD NSLAKDPTAV IFGEDVAFGG VFRCTVGLRD KYGKDRVFNT PLCEQGIVGF GIGIAVTGAT AIAEIQFADY IFPAFDQIVN EAAKYRYRSG DLFNCGSLTI RAPWGCVGHG ALYHSQSPEA FFAHCPGIKV VIPRSPFQAK GLLLSCIEDK NPCIFFEPKI LYRAAVEQVP VEPYKIPLSQ AEVIQEGSDV TLVAWGTQVH VIREVASMAQ EKLGVSCEVI DLRTIVPWDV DTVCKSVIKT GRLLISHEAP LTGGFASEIS STVQEECFLN LEAPISRVCG YDTPFPHIFE PFYIPDKWKC YDALRKMINY // ID ODO1_MOUSE Reviewed; 1023 AA. AC Q60597; Q3UDM7; Q5DTI4; Q5SVX7; Q5SVX9; Q6PFZ2; Q80Y57; Q8K0K7; AC Q8K2Z3; Q8R3M2; Q91WP2; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2007, sequence version 3. DT 19-MAR-2014, entry version 131. DE RecName: Full=2-oxoglutarate dehydrogenase, mitochondrial; DE EC=1.2.4.2; DE AltName: Full=2-oxoglutarate dehydrogenase complex component E1; DE Short=OGDC-E1; DE AltName: Full=Alpha-ketoglutarate dehydrogenase; DE Flags: Precursor; GN Name=Ogdh; Synonyms=Kiaa4192; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC STRAIN=C57BL/6J; TISSUE=Bone marrow; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). RC TISSUE=Brain; RA Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O., RA Koga H.; RT "Prediction of the coding sequences of mouse homologues of KIAA gene. RT The complete nucleotide sequences of mouse KIAA-homologous cDNAs RT identified by screening of terminal sequences of cDNA clones randomly RT sampled from size-fractionated libraries."; RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 4). RC STRAIN=C57BL/6, and FVB/N; RC TISSUE=Brain, Colon, Mammary tumor, and Salivary gland; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP PROTEIN SEQUENCE OF 123-135; 185-204; 311-319; 561-568; 616-633 AND RP 916-925, AND MASS SPECTROMETRY. RC STRAIN=C57BL/6; TISSUE=Brain, and Hippocampus; RA Lubec G., Klug S., Kang S.U.; RL Submitted (APR-2007) to UniProtKB. RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] OF 829-958 (ISOFORMS 1/2/3/4). RC STRAIN=BALB/c; RX PubMed=8248240; DOI=10.1073/pnas.90.23.11272; RA Udaka K., Tsomides T.J., Walden P., Fukusen N., Eisen H.N.; RT "A ubiquitous protein is the source of naturally occurring peptides RT that are recognized by a CD8+ T-cell clone."; RL Proc. Natl. Acad. Sci. U.S.A. 90:11272-11276(1993). RN [7] RP PROTEIN SEQUENCE OF 933-939. RX PubMed=1606619; DOI=10.1016/0092-8674(92)90617-L; RA Udaka K., Tsomides T.J., Eisen H.N.; RT "A naturally occurring peptide recognized by alloreactive CD8+ RT cytotoxic T lymphocytes in association with a class I MHC protein."; RL Cell 69:989-998(1992). RN [8] RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-74 AND LYS-564, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., RA Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). RN [9] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-401, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23576753; DOI=10.1073/pnas.1302961110; RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., RA Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.; RT "Label-free quantitative proteomics of the lysine acetylome in RT mitochondria identifies substrates of SIRT3 in metabolic pathways."; RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013). CC -!- FUNCTION: The 2-oxoglutarate dehydrogenase complex catalyzes the CC overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). It CC contains multiple copies of three enzymatic components: 2- CC oxoglutarate dehydrogenase (E1), dihydrolipoamide CC succinyltransferase (E2) and lipoamide dehydrogenase (E3). CC -!- CATALYTIC ACTIVITY: 2-oxoglutarate + [dihydrolipoyllysine-residue CC succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue CC succinyltransferase] S-succinyldihydrolipoyllysine + CO(2). CC -!- COFACTOR: Thiamine pyrophosphate. CC -!- ENZYME REGULATION: Catabolite repressed. CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; CC IsoId=Q60597-1; Sequence=Displayed; CC Name=2; CC IsoId=Q60597-2; Sequence=VSP_024799; CC Name=3; CC IsoId=Q60597-3; Sequence=VSP_024801; CC Note=No experimental confirmation available; CC Name=4; CC IsoId=Q60597-4; Sequence=VSP_024800; CC -!- SIMILARITY: Belongs to the alpha-ketoglutarate dehydrogenase CC family. CC -!- SEQUENCE CAUTION: CC Sequence=AAH31165.1; Type=Erroneous initiation; CC Sequence=BAD90530.1; Type=Erroneous initiation; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK147289; BAE27824.1; -; mRNA. DR EMBL; AK150009; BAE29234.1; -; mRNA. DR EMBL; AK169286; BAE41044.1; -; mRNA. DR EMBL; AK220536; BAD90530.1; ALT_INIT; mRNA. DR EMBL; AL607152; CAI24404.1; -; Genomic_DNA. DR EMBL; AL607152; CAI24405.1; -; Genomic_DNA. DR EMBL; AL607152; CAI24406.1; -; Genomic_DNA. DR EMBL; BC025040; AAH25040.1; -; mRNA. DR EMBL; BC013670; AAH13670.1; -; mRNA. DR EMBL; BC029143; AAH29143.1; -; mRNA. DR EMBL; BC031165; AAH31165.1; ALT_INIT; mRNA. DR EMBL; BC049104; AAH49104.1; -; mRNA. DR EMBL; BC057354; AAH57354.1; -; mRNA. DR EMBL; U02971; AAC52130.1; -; mRNA. DR PIR; I48884; A41911. DR RefSeq; NP_001239211.1; NM_001252282.1. DR RefSeq; NP_001239212.1; NM_001252283.1. DR RefSeq; NP_001239216.1; NM_001252287.1. DR RefSeq; NP_001239217.1; NM_001252288.1. DR RefSeq; NP_035086.2; NM_010956.4. DR RefSeq; XP_006514645.1; XM_006514582.1. DR RefSeq; XP_006514646.1; XM_006514583.1. DR RefSeq; XP_006514647.1; XM_006514584.1. DR RefSeq; XP_006514648.1; XM_006514585.1. DR UniGene; Mm.276348; -. DR UniGene; Mm.479411; -. DR UniGene; Mm.490272; -. DR PDB; 3E2H; X-ray; 3.80 A; Q=932-940. DR PDB; 3TF7; X-ray; 2.75 A; B/F=932-940. DR PDBsum; 3E2H; -. DR PDBsum; 3TF7; -. DR ProteinModelPortal; Q60597; -. DR SMR; Q60597; 130-1014. DR IntAct; Q60597; 5. DR MINT; MINT-1860288; -. DR ChEMBL; CHEMBL2176831; -. DR PhosphoSite; Q60597; -. DR REPRODUCTION-2DPAGE; Q60597; -. DR PaxDb; Q60597; -. DR PRIDE; Q60597; -. DR Ensembl; ENSMUST00000003461; ENSMUSP00000003461; ENSMUSG00000020456. [Q60597-1] DR Ensembl; ENSMUST00000093350; ENSMUSP00000091041; ENSMUSG00000020456. [Q60597-4] DR Ensembl; ENSMUST00000101554; ENSMUSP00000099090; ENSMUSG00000020456. [Q60597-1] DR GeneID; 18293; -. DR KEGG; mmu:18293; -. DR UCSC; uc007hyf.2; mouse. [Q60597-1] DR UCSC; uc007hyg.2; mouse. [Q60597-3] DR UCSC; uc007hyh.2; mouse. [Q60597-4] DR CTD; 4967; -. DR MGI; MGI:1098267; Ogdh. DR eggNOG; COG0567; -. DR GeneTree; ENSGT00530000063092; -. DR HOVERGEN; HBG001892; -. DR KO; K00164; -. DR OMA; NEGVANE; -. DR OrthoDB; EOG7FXZXH; -. DR TreeFam; TF300695; -. DR ChiTaRS; OGDH; mouse. DR NextBio; 293740; -. DR PRO; PR:Q60597; -. DR ArrayExpress; Q60597; -. DR Bgee; Q60597; -. DR CleanEx; MM_OGDH; -. DR Genevestigator; Q60597; -. DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell. DR GO; GO:0031966; C:mitochondrial membrane; ISS:UniProtKB. DR GO; GO:0045252; C:oxoglutarate dehydrogenase complex; IEA:Ensembl. DR GO; GO:0034602; F:oxoglutarate dehydrogenase (NAD+) activity; IDA:MGI. DR GO; GO:0004591; F:oxoglutarate dehydrogenase (succinyl-transferring) activity; ISS:UniProtKB. DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro. DR GO; GO:0006103; P:2-oxoglutarate metabolic process; IEA:Ensembl. DR GO; GO:0021695; P:cerebellar cortex development; IEP:UniProtKB. DR GO; GO:0006091; P:generation of precursor metabolites and energy; ISS:UniProtKB. DR GO; GO:0006096; P:glycolysis; IEA:UniProtKB-KW. DR GO; GO:0021766; P:hippocampus development; IEP:UniProtKB. DR GO; GO:0006734; P:NADH metabolic process; IEA:Ensembl. DR GO; GO:0061034; P:olfactory bulb mitral cell layer development; IEP:UniProtKB. DR GO; GO:0021860; P:pyramidal neuron development; IEP:UniProtKB. DR GO; GO:0021756; P:striatum development; IEP:UniProtKB. DR GO; GO:0006104; P:succinyl-CoA metabolic process; IEA:Ensembl. DR GO; GO:0022028; P:tangential migration from the subventricular zone to the olfactory bulb; IEP:UniProtKB. DR GO; GO:0021794; P:thalamus development; IEP:UniProtKB. DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:Ensembl. DR InterPro; IPR011603; 2oxoglutarate_DH_E1. DR InterPro; IPR001017; DH_E1. DR InterPro; IPR005475; Transketolase-like_Pyr-bd. DR PANTHER; PTHR23152; PTHR23152; 1. DR Pfam; PF00676; E1_dh; 1. DR Pfam; PF02779; Transket_pyr; 1. DR PIRSF; PIRSF000157; Oxoglu_dh_E1; 1. DR SMART; SM00861; Transket_pyr; 1. DR TIGRFAMs; TIGR00239; 2oxo_dh_E1; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Complete proteome; KW Direct protein sequencing; Glycolysis; Isopeptide bond; Mitochondrion; KW Oxidoreductase; Reference proteome; Thiamine pyrophosphate; KW Transit peptide; Ubl conjugation. FT TRANSIT 1 40 Mitochondrion (By similarity). FT CHAIN 41 1023 2-oxoglutarate dehydrogenase, FT mitochondrial. FT /FTId=PRO_0000020434. FT REGION 933 939 Recognized by alloreactive CD8 cytotoxic FT T-lymphocytes in association with a class FT I MHC protein. FT MOD_RES 74 74 N6-succinyllysine. FT MOD_RES 401 401 N6-acetyllysine. FT MOD_RES 564 564 N6-succinyllysine. FT MOD_RES 970 970 N6-acetyllysine (By similarity). FT CROSSLNK 534 534 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in ubiquitin) (By FT similarity). FT VAR_SEQ 139 172 IRGHHVAQLDPLGILDADLDSSVPADIISSTDKL -> VRG FT HHIAKSCVNFDDAPVTVSSNV (in isoform 2). FT /FTId=VSP_024799. FT VAR_SEQ 139 172 IRGHHVAQLDPLGILDADLDSSVPADIISSTDKL -> VRG FT HHIAKLDPLGISCVNFDDAPVTVSSNVDLAVFKERLRMLTV FT G (in isoform 4). FT /FTId=VSP_024800. FT VAR_SEQ 172 172 L -> LDLAVFKERLRMLTVG (in isoform 3). FT /FTId=VSP_024801. FT CONFLICT 416 416 G -> V (in Ref. 4; AAH49104). FT CONFLICT 549 549 V -> F (in Ref. 4; AAH49104). FT CONFLICT 552 552 Q -> E (in Ref. 4; AAH57354). FT CONFLICT 576 576 E -> K (in Ref. 1; BAE29234). SQ SEQUENCE 1023 AA; 116449 MW; A0F3F8D36C7A76BC CRC64; MFHLRTCAAK LRPLTASQTV KTFSQNKPAA IRTFQQIRCY SAPVAAEPFL SGTSSNYVEE MYCAWLENPK SVHKSWDIFF RNTNAGAPPG TAYQSPLSLS RSSLATMAHA QSLVEAQPNV DKLVEDHLAV QSLIRAYQIR GHHVAQLDPL GILDADLDSS VPADIISSTD KLGFYGLHES DLDKVFHLPT TTFIGGQEPA LPLREIIRRL EMAYCQHIGV EFMFINDLEQ CQWIRQKFET PGIMQFTNEE KRTLLARLVR STRFEEFLQR KWSSEKRFGL EGCEVLIPAL KTIIDMSSAN GVDYVIMGMP HRGRLNVLAN VIRKELEQIF CQFDSKLEAA DEGSGDMKYH LGMYHRRINR VTDRNITLSL VANPSHLEAA DPVVMGKTKA EQFYCGDTEG KKVMSILLHG DAAFAGQGIV YETFHLSDLP SYTTHGTVHV VVNNQIGFTT DPRMARSSPY PTDVARVVNA PIFHVNSDDP EAVMYVCKVA AEWRNTFHKD VVVDLVCYRR NGHNEMDEPM FTQPLMYKQI RKQKPVLQKY AELLVSQGVV NQPEYEEEIS KYDKICEEAF TRSKDEKILH IKHWLDSPWP GFFTLDGQPR SMTCPSTGLE EDVLFHIGKV ASSVPVENFT IHGGLSRILK TRRELVTNRT VDWALAEYMA FGSLLKEGIH VRLSGQDVER GTFSHRHHVL HDQNVDKRTC IPMNHLWPNQ APYTVCNSSL SEYGVLGFEL GFAMASPNAL VLWEAQFGDF NNMAQCIIDQ FICPGQAKWV RQNGIVLLLP HGMEGMGPEH SSARPERFLQ MCNDDPDVLP DLQEENFDIN QLYDCNWIVV NCSTPGNFFH VLRRQILLPF RKPLIVFTPK SLLRHPEART SFDEMLPGTH FQRVIPENGP AAQDPHKVKR LLFCTGKVYY DLTRERKARN MEEEVAITRI EQLSPFPFDL LLKEAQKYPN AELAWCQEEH KNQGYYDYVK PRLRTTIDRA KPVWYAGRDP AAAPATGNKK THLTELQRFL DTAFDLDAFK KFS // ID ODPAT_MOUSE Reviewed; 391 AA. AC P35487; Q497M8; DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1994, sequence version 1. DT 19-FEB-2014, entry version 111. DE RecName: Full=Pyruvate dehydrogenase E1 component subunit alpha, testis-specific form, mitochondrial; DE EC=1.2.4.1; DE AltName: Full=PDHE1-A type II; DE Flags: Precursor; GN Name=Pdha2; Synonyms=Pdha-2, Pdhal; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=1581363; DOI=10.1016/0167-4781(92)90102-6; RA Fitzgerald G.F., Hutchison W.M., Dahl H.-H.M.; RT "Isolation and characterisation of the mouse pyruvate dehydrogenase E1 RT alpha genes."; RL Biochim. Biophys. Acta 1131:83-90(1992). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Testis; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Testis; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall CC conversion of pyruvate to acetyl-CoA and CO(2), and thereby links CC the glycolytic pathway to the tricarboxylic cycle (By similarity). CC -!- CATALYTIC ACTIVITY: Pyruvate + [dihydrolipoyllysine-residue CC acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue CC acetyltransferase] S-acetyldihydrolipoyllysine + CO(2). CC -!- COFACTOR: Thiamine pyrophosphate (By similarity). CC -!- ENZYME REGULATION: Pyruvate dehydrogenase activity is inhibited by CC phosphorylation of PDHA2; it is reactivated by dephosphorylation CC (By similarity). CC -!- SUBUNIT: Heterotetramer of two PDHA2 and two PDHB subunits. The CC heterotetramer interacts with DLAT, and is part of the multimeric CC pyruvate dehydrogenase complex that contains multiple copies of CC pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase CC (DLAT, E2) and lipoamide dehydrogenase (DLD, E3). These subunits CC are bound to an inner core composed of about 48 DLAT and 12 PDHX CC molecules (By similarity). CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix (By similarity). CC -!- TISSUE SPECIFICITY: Testis. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M76728; AAA53047.1; -; mRNA. DR EMBL; AK076791; BAC36482.1; -; mRNA. DR EMBL; BC100460; AAI00461.1; -; mRNA. DR PIR; S23507; S23507. DR RefSeq; NP_032837.1; NM_008811.2. DR UniGene; Mm.4223; -. DR ProteinModelPortal; P35487; -. DR SMR; P35487; 31-391. DR PhosphoSite; P35487; -. DR REPRODUCTION-2DPAGE; P35487; -. DR PaxDb; P35487; -. DR PRIDE; P35487; -. DR Ensembl; ENSMUST00000057860; ENSMUSP00000060774; ENSMUSG00000047674. DR GeneID; 18598; -. DR KEGG; mmu:18598; -. DR UCSC; uc008rob.1; mouse. DR CTD; 5161; -. DR MGI; MGI:97533; Pdha2. DR eggNOG; COG1071; -. DR GeneTree; ENSGT00530000063174; -. DR HOGENOM; HOG000281336; -. DR HOVERGEN; HBG001863; -. DR InParanoid; Q497M8; -. DR KO; K00161; -. DR OMA; ELTINIY; -. DR OrthoDB; EOG73JKVQ; -. DR TreeFam; TF300742; -. DR NextBio; 294494; -. DR PRO; PR:P35487; -. DR Bgee; P35487; -. DR CleanEx; MM_PDHA2; -. DR Genevestigator; P35487; -. DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; ISS:UniProtKB. DR GO; GO:0006096; P:glycolysis; IEA:InterPro. DR GO; GO:0006090; P:pyruvate metabolic process; ISS:UniProtKB. DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW. DR InterPro; IPR001017; DH_E1. DR InterPro; IPR017597; Pyrv_DH_E1_asu_subgrp-y. DR Pfam; PF00676; E1_dh; 1. DR TIGRFAMs; TIGR03182; PDH_E1_alph_y; 1. PE 2: Evidence at transcript level; KW Carbohydrate metabolism; Complete proteome; Glucose metabolism; KW Mitochondrion; Oxidoreductase; Phosphoprotein; Pyruvate; KW Reference proteome; Thiamine pyrophosphate; Transit peptide; KW Tricarboxylic acid cycle. FT TRANSIT 1 30 Mitochondrion (By similarity). FT CHAIN 31 391 Pyruvate dehydrogenase E1 component FT subunit alpha, testis-specific form, FT mitochondrial. FT /FTId=PRO_0000020448. FT MOD_RES 294 294 Phosphoserine; by PDK1, PDK2, PDK3 and FT PDK4 (By similarity). FT MOD_RES 301 301 Phosphoserine; by PDK3 (By similarity). SQ SEQUENCE 391 AA; 43413 MW; A2DE823362485977 CRC64; MRKMLTAVLS HVFSGMVQKP ALRGLLSSLK FSNDATCDIK KCDLYRLEEG PPTSTVLTRA EALKYYRTMQ VIRRMELKAD QLYKQKFIRG FCHLCDGQEA CCVGLEAGIN PTDHVITSYR AHGFCYTRGL SVKSILAELT GRKGGCAKGK GGSMHMYGKN FYGGNGIVGA QVPLGAGVAF ACKYLKNGQV CLALYGDGAA NQGQVFEAYN MSALWKLPCV FICENNLYGM GTSNERSAAS TDYHKKGFII PGLRVNGMDI LCVREATKFA ADHCRSGKGP IVMELQTYRY HGHSMSDPGI SYRSREEVHN VRSKSDPIML LRERIISNNL SNIEELKEID ADVKKEVEDA AQFATTDPEP AVEDIANYLY HQDPPFEVRG AHKWLKYKSH S // ID ODPA_MOUSE Reviewed; 390 AA. AC P35486; DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1994, sequence version 1. DT 19-MAR-2014, entry version 120. DE RecName: Full=Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial; DE EC=1.2.4.1; DE AltName: Full=PDHE1-A type I; DE Flags: Precursor; GN Name=Pdha1; Synonyms=Pdha-1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=1581363; DOI=10.1016/0167-4781(92)90102-6; RA Fitzgerald G.F., Hutchison W.M., Dahl H.-H.M.; RT "Isolation and characterisation of the mouse pyruvate dehydrogenase E1 RT alpha genes."; RL Biochim. Biophys. Acta 1131:83-90(1992). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Mammary gland; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP PROTEIN SEQUENCE OF 46-58; 120-127; 133-141; 159-182; 216-244; RP 246-263; 268-274; 278-321; 324-343 AND 379-385, AND MASS SPECTROMETRY. RC STRAIN=C57BL/6; TISSUE=Brain, and Hippocampus; RA Lubec G., Klug S., Kang S.U.; RL Submitted (APR-2007) to UniProtKB. RN [4] RP DISRUPTION PHENOTYPE, CATALYTIC ACTIVITY, AND FUNCTION. RX PubMed=11708858; DOI=10.1006/mgme.2001.3249; RA Johnson M.T., Mahmood S., Hyatt S.L., Yang H.S., Soloway P.D., RA Hanson R.W., Patel M.S.; RT "Inactivation of the murine pyruvate dehydrogenase (Pdha1) gene and RT its effect on early embryonic development."; RL Mol. Genet. Metab. 74:293-302(2001). RN [5] RP DISRUPTION PHENOTYPE. RX PubMed=17314311; DOI=10.1095/biolreprod.106.059899; RA Johnson M.T., Freeman E.A., Gardner D.K., Hunt P.A.; RT "Oxidative metabolism of pyruvate is required for meiotic maturation RT of murine oocytes in vivo."; RL Biol. Reprod. 77:2-8(2007). RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232; SER-293; SER-295 RP AND SER-300, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Liver; RX PubMed=17242355; DOI=10.1073/pnas.0609836104; RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; RT "Large-scale phosphorylation analysis of mouse liver."; RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). RN [7] RP DISRUPTION PHENOTYPE. RX PubMed=18586888; DOI=10.1152/ajpheart.00363.2008; RA Sidhu S., Gangasani A., Korotchkina L.G., Suzuki G., RA Fallavollita J.A., Canty J.M. Jr., Patel M.S.; RT "Tissue-specific pyruvate dehydrogenase complex deficiency causes RT cardiac hypertrophy and sudden death of weaned male mice."; RL Am. J. Physiol. 295:H946-H952(2008). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-301, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain; RX PubMed=18034455; DOI=10.1021/pr0701254; RA Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.; RT "Large-scale identification and evolution indexing of tyrosine RT phosphorylation sites from murine brain."; RL J. Proteome Res. 7:311-318(2008). RN [9] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=18630941; DOI=10.1021/pr800223m; RA Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.; RT "Specific phosphopeptide enrichment with immobilized titanium ion RT affinity chromatography adsorbent for phosphoproteome analysis."; RL J. Proteome Res. 7:3957-3967(2008). RN [10] RP SUBCELLULAR LOCATION, AND PHOSPHORYLATION AT SER-232; SER-293 AND RP SER-300. RX PubMed=19341700; DOI=10.1016/j.ab.2009.03.040; RA Rardin M.J., Wiley S.E., Naviaux R.K., Murphy A.N., Dixon J.E.; RT "Monitoring phosphorylation of the pyruvate dehydrogenase complex."; RL Anal. Biochem. 389:157-164(2009). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-293, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006; RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M., RA Thibault P.; RT "The phagosomal proteome in interferon-gamma-activated macrophages."; RL Immunity 30:143-154(2009). RN [12] RP DISRUPTION PHENOTYPE, CATALYTIC ACTIVITY, AND FUNCTION. RX PubMed=20841503; DOI=10.1152/ajpendo.00339.2010; RA Srinivasan M., Choi C.S., Ghoshal P., Pliss L., Pandya J.D., Hill D., RA Cline G., Patel M.S.; RT "Beta-cell-specific pyruvate dehydrogenase deficiency impairs glucose- RT stimulated insulin secretion."; RL Am. J. Physiol. 299:E910-E917(2010). RN [13] RP ACETYLATION AT LYS-336, AND MUTAGENESIS OF LYS-336. RX PubMed=23835326; DOI=10.2337/db12-1650; RA Jing E., O'Neill B.T., Rardin M.J., Kleinridders A., Ilkeyeva O.R., RA Ussar S., Bain J.R., Lee K.Y., Verdin E.M., Newgard C.B., Gibson B.W., RA Kahn C.R.; RT "Sirt3 regulates metabolic flexibility of skeletal muscle through RT reversible enzymatic deacetylation."; RL Diabetes 62:3404-3417(2013). RN [14] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-313, SUCCINYLATION [LARGE RP SCALE ANALYSIS] AT LYS-63; LYS-244; LYS-277; LYS-313 AND LYS-385, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic fibroblast, and Liver; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., RA Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). RN [15] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-63; LYS-244; LYS-267 AND RP LYS-321, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Liver; RX PubMed=23576753; DOI=10.1073/pnas.1302961110; RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., RA Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.; RT "Label-free quantitative proteomics of the lysine acetylome in RT mitochondria identifies substrates of SIRT3 in metabolic pathways."; RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013). CC -!- FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall CC conversion of pyruvate to acetyl-CoA and CO(2), and thereby links CC the glycolytic pathway to the tricarboxylic cycle. CC -!- CATALYTIC ACTIVITY: Pyruvate + [dihydrolipoyllysine-residue CC acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue CC acetyltransferase] S-acetyldihydrolipoyllysine + CO(2). CC -!- COFACTOR: Thiamine pyrophosphate. CC -!- ENZYME REGULATION: Pyruvate dehydrogenase activity is inhibited by CC phosphorylation of PDHA1; it is reactivated by dephosphorylation. CC -!- SUBUNIT: Heterotetramer of two PDHA1 and two PDHB subunits. The CC heterotetramer interacts with DLAT, and is part of the multimeric CC pyruvate dehydrogenase complex that contains multiple copies of CC pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase CC (DLAT, E2) and lipoamide dehydrogenase (DLD, E3). These subunits CC are bound to an inner core composed of about 48 DLAT and 12 PDHX CC molecules (By similarity). CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix. CC -!- TISSUE SPECIFICITY: In all tissues, but in very low amount in CC testis. CC -!- PTM: Phosphorylation at Ser-232, Ser-293 and Ser-300 by PDK family CC kinases inactivates the enzyme; for this phosphorylation at a CC single site is sufficient. Phosphorylation at Ser-293 interferes CC with access to active site, and thereby inactivates the enzyme. CC Dephosphorylation at all three sites, i.e. at Ser-232, Ser-293 and CC Ser-300, is required for reactivation (By similarity). CC -!- PTM: Acetylation alters the phosphorylation pattern. Deacetylated CC by SIRT3. CC -!- DISRUPTION PHENOTYPE: Complete embryonic lethality. Normal CC embryonic development ceases about 9.5 dpc. Conditional gene CC disruption in the heart causes death shortly after weaning in male CC mice fed normal chow, while mice on high fat diet survive, but CC develop left ventricular hypertrophy, due to impaired glucose and CC energy metabolism in the heart. Likewise, conditional gene CC disruption in pancreas islet beta cells disrupts normal insulin CC secretion in response to glucose stimuli, while conditional gene CC disruption in oocytes causes reduced ATP levels and thereby CC prevents normal meiosis during oocyte maturation. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M76727; AAA53046.1; -; mRNA. DR EMBL; BC007142; AAH07142.1; -; mRNA. DR PIR; S23506; S23506. DR RefSeq; NP_032836.1; NM_008810.2. DR UniGene; Mm.34775; -. DR ProteinModelPortal; P35486; -. DR SMR; P35486; 29-390. DR IntAct; P35486; 6. DR MINT; MINT-4105793; -. DR STRING; 10090.ENSMUSP00000033662; -. DR PhosphoSite; P35486; -. DR REPRODUCTION-2DPAGE; P35486; -. DR PaxDb; P35486; -. DR PRIDE; P35486; -. DR Ensembl; ENSMUST00000033662; ENSMUSP00000033662; ENSMUSG00000031299. DR GeneID; 18597; -. DR KEGG; mmu:18597; -. DR UCSC; uc009utc.1; mouse. DR CTD; 5160; -. DR MGI; MGI:97532; Pdha1. DR eggNOG; COG1071; -. DR HOGENOM; HOG000281336; -. DR HOVERGEN; HBG001863; -. DR InParanoid; P35486; -. DR KO; K00161; -. DR OMA; EVKHYRE; -. DR OrthoDB; EOG73JKVQ; -. DR TreeFam; TF300742; -. DR ChiTaRS; PDHA1; mouse. DR NextBio; 294490; -. DR PRO; PR:P35486; -. DR ArrayExpress; P35486; -. DR Bgee; P35486; -. DR CleanEx; MM_PDHA1; -. DR Genevestigator; P35486; -. DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR GO; GO:0045254; C:pyruvate dehydrogenase complex; ISS:UniProtKB. DR GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; IEA:UniProtKB-EC. DR GO; GO:0004738; F:pyruvate dehydrogenase activity; IMP:MGI. DR GO; GO:0006086; P:acetyl-CoA biosynthetic process from pyruvate; ISS:UniProtKB. DR GO; GO:0006096; P:glycolysis; IEA:InterPro. DR GO; GO:0006099; P:tricarboxylic acid cycle; ISS:UniProtKB. DR InterPro; IPR001017; DH_E1. DR InterPro; IPR017597; Pyrv_DH_E1_asu_subgrp-y. DR Pfam; PF00676; E1_dh; 1. DR TIGRFAMs; TIGR03182; PDH_E1_alph_y; 1. PE 1: Evidence at protein level; KW Acetylation; Carbohydrate metabolism; Complete proteome; KW Direct protein sequencing; Glucose metabolism; Mitochondrion; KW Oxidoreductase; Phosphoprotein; Pyruvate; Reference proteome; KW Thiamine pyrophosphate; Transit peptide; Tricarboxylic acid cycle. FT TRANSIT 1 29 Mitochondrion (By similarity). FT CHAIN 30 390 Pyruvate dehydrogenase E1 component FT subunit alpha, somatic form, FT mitochondrial. FT /FTId=PRO_0000020442. FT MOD_RES 63 63 N6-acetyllysine; alternate. FT MOD_RES 63 63 N6-succinyllysine; alternate. FT MOD_RES 232 232 Phosphoserine; by PDK1. FT MOD_RES 244 244 N6-acetyllysine; alternate. FT MOD_RES 244 244 N6-succinyllysine; alternate. FT MOD_RES 267 267 N6-acetyllysine. FT MOD_RES 277 277 N6-succinyllysine. FT MOD_RES 293 293 Phosphoserine; by PDK1, PDK2, PDK3 and FT PDK4. FT MOD_RES 295 295 Phosphoserine. FT MOD_RES 300 300 Phosphoserine; by PDK1, PDK2, PDK3 and FT PDK4. FT MOD_RES 301 301 Phosphotyrosine. FT MOD_RES 313 313 N6-acetyllysine; alternate. FT MOD_RES 313 313 N6-succinyllysine; alternate. FT MOD_RES 321 321 N6-acetyllysine. FT MOD_RES 336 336 N6-acetyllysine. FT MOD_RES 385 385 N6-succinyllysine. FT MUTAGEN 336 336 K->Q,R: Decreases phosphorylation at S- FT 232 and S-300 but does not affect FT activity or substrate metabolism. SQ SEQUENCE 390 AA; 43232 MW; 40898944CE8E0A03 CRC64; MRKMLAAVSR VLAGSAQKPA SRVLVASRNF ANDATFEIKK CDLHRLEEGP PVTTVLTRED GLKYYRMMQT VRRMELKADQ LYKQKIIRGF CHLCDGQEAC CVGLEAGINP TDHLITAYRA HGFTFTRGLP VRAILAELTG RRGGCAKGKG GSMHMYAKNF YGGNGIVGAQ VPLGAGIALA CKYNGKDEVC LTLYGDGAAN QGQIFEAYNM AALWKLPCIF ICENNRYGMG TSVERAAAST DYYKRGDFIP GLRVDGMDIL CVREATKFAA AYCRSGKGPI LMELQTYRYH GHSMSDPGVS YRTREEIQEV RSKSDPIMLL KDRMVNSNLA SVEELKEIDV EVRKEIEDAA QFATADPEPP LEELGYHIYS SDPPFEVRGA NQWIKFKSVS // ID ODPB_MOUSE Reviewed; 359 AA. AC Q9D051; Q3TL86; Q505N8; Q99LW9; DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 19-MAR-2014, entry version 103. DE RecName: Full=Pyruvate dehydrogenase E1 component subunit beta, mitochondrial; DE Short=PDHE1-B; DE EC=1.2.4.1; DE Flags: Precursor; GN Name=Pdhb; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Bone marrow, and Embryo; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N-3; TISSUE=Liver, and Mammary tumor; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP PROTEIN SEQUENCE OF 309-324, AND MASS SPECTROMETRY. RC TISSUE=Hippocampus; RA Lubec G., Klug S.; RL Submitted (MAR-2007) to UniProtKB. RN [4] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-67, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain; RX PubMed=18034455; DOI=10.1021/pr0701254; RA Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.; RT "Large-scale identification and evolution indexing of tyrosine RT phosphorylation sites from murine brain."; RL J. Proteome Res. 7:311-318(2008). RN [5] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-354, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23576753; DOI=10.1073/pnas.1302961110; RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., RA Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.; RT "Label-free quantitative proteomics of the lysine acetylome in RT mitochondria identifies substrates of SIRT3 in metabolic pathways."; RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013). CC -!- FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall CC conversion of pyruvate to acetyl-CoA and CO(2), and thereby links CC the glycolytic pathway to the tricarboxylic cycle (By similarity). CC -!- CATALYTIC ACTIVITY: Pyruvate + [dihydrolipoyllysine-residue CC acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue CC acetyltransferase] S-acetyldihydrolipoyllysine + CO(2). CC -!- COFACTOR: Thiamine pyrophosphate (By similarity). CC -!- SUBUNIT: Heterotetramer of two PDHA1 and two PDHB subunits. The CC heterotetramer interacts with DLAT, and is part of the multimeric CC pyruvate dehydrogenase complex that contains multiple copies of CC pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase CC (DLAT, E2) and lipoamide dehydrogenase (DLD, E3). These subunits CC are bound to an inner core composed of about 48 DLAT and 12 PDHX CC molecules (By similarity). CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix (By similarity). CC -!- SEQUENCE CAUTION: CC Sequence=AAH02188.1; Type=Erroneous initiation; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK011810; BAB27855.1; -; mRNA. DR EMBL; AK153058; BAE31684.1; -; mRNA. DR EMBL; AK166631; BAE38906.1; -; mRNA. DR EMBL; BC002188; AAH02188.1; ALT_INIT; mRNA. DR EMBL; BC019512; AAH19512.1; -; mRNA. DR EMBL; BC094468; AAH94468.1; -; mRNA. DR PIR; PT0096; PT0096. DR RefSeq; NP_077183.1; NM_024221.3. DR UniGene; Mm.301527; -. DR ProteinModelPortal; Q9D051; -. DR SMR; Q9D051; 30-359. DR BioGrid; 212768; 2. DR IntAct; Q9D051; 9. DR MINT; MINT-1860720; -. DR PhosphoSite; Q9D051; -. DR REPRODUCTION-2DPAGE; Q9D051; -. DR UCD-2DPAGE; Q9D051; -. DR PaxDb; Q9D051; -. DR PRIDE; Q9D051; -. DR Ensembl; ENSMUST00000022268; ENSMUSP00000022268; ENSMUSG00000021748. DR GeneID; 68263; -. DR KEGG; mmu:68263; -. DR UCSC; uc007sev.1; mouse. DR CTD; 5162; -. DR MGI; MGI:1915513; Pdhb. DR eggNOG; COG0022; -. DR GeneTree; ENSGT00530000063423; -. DR HOGENOM; HOG000281450; -. DR HOVERGEN; HBG000917; -. DR InParanoid; Q9D051; -. DR KO; K00162; -. DR OMA; DIPTPYN; -. DR OrthoDB; EOG7KSX8S; -. DR TreeFam; TF105674; -. DR ChiTaRS; PDHB; mouse. DR NextBio; 326854; -. DR PRO; PR:Q9D051; -. DR Bgee; Q9D051; -. DR CleanEx; MM_PDHB; -. DR Genevestigator; Q9D051; -. DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR GO; GO:0045254; C:pyruvate dehydrogenase complex; ISS:UniProtKB. DR GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; IEA:UniProtKB-EC. DR GO; GO:0004738; F:pyruvate dehydrogenase activity; ISS:UniProtKB. DR GO; GO:0006086; P:acetyl-CoA biosynthetic process from pyruvate; ISS:UniProtKB. DR GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW. DR GO; GO:0006099; P:tricarboxylic acid cycle; ISS:UniProtKB. DR Gene3D; 3.40.50.920; -; 1. DR InterPro; IPR009014; Transketo_C/Pyr-ferredox_oxred. DR InterPro; IPR005475; Transketolase-like_Pyr-bd. DR InterPro; IPR005476; Transketolase_C. DR Pfam; PF02779; Transket_pyr; 1. DR Pfam; PF02780; Transketolase_C; 1. DR SMART; SM00861; Transket_pyr; 1. DR SUPFAM; SSF52922; SSF52922; 1. PE 1: Evidence at protein level; KW Acetylation; Carbohydrate metabolism; Complete proteome; KW Direct protein sequencing; Glucose metabolism; Mitochondrion; KW Oxidoreductase; Phosphoprotein; Pyruvate; Reference proteome; KW Thiamine pyrophosphate; Transit peptide; Tricarboxylic acid cycle. FT TRANSIT 1 30 Mitochondrion (By similarity). FT CHAIN 31 359 Pyruvate dehydrogenase E1 component FT subunit beta, mitochondrial. FT /FTId=PRO_0000020458. FT BINDING 89 89 Thiamine pyrophosphate (By similarity). FT MOD_RES 67 67 Phosphotyrosine. FT MOD_RES 354 354 N6-acetyllysine. FT CONFLICT 237 237 I -> M (in Ref. 1; BAE38906). SQ SEQUENCE 359 AA; 38937 MW; F5CD2A186DF58DDE CRC64; MAVVAGLVRG PLRQASGLLK RRFHRSAPAA VQLTVREAIN QGMDEELERD EKVFLLGEEV AQYDGAYKVS RGLWKKYGDK RIIDTPISEM GFAGIAVGAA MAGLRPICEF MTFNFSMQAI DQVINSAAKT YYMSAGLQPV PIVFRGPNGA SAGVAAQHSQ CFAAWYGHCP GLKVVSPWNS EDAKGLIKSA IRDNNPVVML ENELMYGVAF ELPAEAQSKD FLIPIGKAKI ERQGTHITVV AHSRPVGHCL EAAAVLSKEG IECEVINLRT IRPMDIEAIE ASVMKTNHLV TVEGGWPQFG VGAEICARIM EGPAFNFLDA PAVRVTGADV PMPYAKVLED NSVPQVKDII FAVKKTLNI // ID OGFD2_MOUSE Reviewed; 349 AA. AC Q9CQ04; Q78IV7; Q8BMW3; DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 19-MAR-2014, entry version 85. DE RecName: Full=2-oxoglutarate and iron-dependent oxygenase domain-containing protein 2; DE EC=1.14.11.-; GN Name=Ogfod2; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Colon, Embryo, and Liver; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Colon, and Salivary gland; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- COFACTOR: Binds 1 Fe(2+) ion per subunit (By similarity). CC -!- COFACTOR: Ascorbate (By similarity). CC -!- SIMILARITY: Belongs to the OGFOD2 family. CC -!- SIMILARITY: Contains 1 Fe2OG dioxygenase domain. CC -!- SEQUENCE CAUTION: CC Sequence=AAH22762.1; Type=Erroneous initiation; CC Sequence=BAC25517.1; Type=Frameshift; Positions=258; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK004943; BAB23687.1; -; mRNA. DR EMBL; AK017497; BAC25517.1; ALT_FRAME; mRNA. DR EMBL; AK018534; BAB31259.1; -; mRNA. DR EMBL; BC022762; AAH22762.1; ALT_INIT; mRNA. DR EMBL; BC069872; AAH69872.1; -; mRNA. DR RefSeq; NP_079947.1; NM_025671.2. DR UniGene; Mm.7050; -. DR ProteinModelPortal; Q9CQ04; -. DR SMR; Q9CQ04; 136-318. DR PhosphoSite; Q9CQ04; -. DR PaxDb; Q9CQ04; -. DR PRIDE; Q9CQ04; -. DR Ensembl; ENSMUST00000024470; ENSMUSP00000024470; ENSMUSG00000023707. DR GeneID; 66627; -. DR KEGG; mmu:66627; -. DR UCSC; uc008zox.1; mouse. DR CTD; 79676; -. DR MGI; MGI:1913877; Ogfod2. DR eggNOG; NOG248193; -. DR GeneTree; ENSGT00390000016796; -. DR HOGENOM; HOG000008117; -. DR HOVERGEN; HBG108212; -. DR InParanoid; Q9CQ04; -. DR OMA; LCPMCCR; -. DR OrthoDB; EOG776SQB; -. DR TreeFam; TF329650; -. DR NextBio; 322212; -. DR PRO; PR:Q9CQ04; -. DR ArrayExpress; Q9CQ04; -. DR Bgee; Q9CQ04; -. DR Genevestigator; Q9CQ04; -. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0031418; F:L-ascorbic acid binding; IEA:UniProtKB-KW. DR GO; GO:0016706; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors; IEA:InterPro. DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase. DR InterPro; IPR006620; Pro_4_hyd_alph. DR SMART; SM00702; P4Hc; 1. DR PROSITE; PS51471; FE2OG_OXY; 1. PE 2: Evidence at transcript level; KW Complete proteome; Dioxygenase; Iron; Metal-binding; Oxidoreductase; KW Reference proteome; Vitamin C. FT CHAIN 1 349 2-oxoglutarate and iron-dependent FT oxygenase domain-containing protein 2. FT /FTId=PRO_0000288979. FT DOMAIN 214 308 Fe2OG dioxygenase. FT METAL 234 234 Iron (By similarity). FT METAL 236 236 Iron (By similarity). FT METAL 289 289 Iron (By similarity). FT BINDING 299 299 2-oxoglutarate (Potential). FT CONFLICT 8 8 R -> G (in Ref. 1; BAC25517). FT CONFLICT 47 47 S -> T (in Ref. 1; BAC25517). FT CONFLICT 72 73 RL -> SV (in Ref. 1; BAC25517). SQ SEQUENCE 349 AA; 39270 MW; E03BA81E019BB194 CRC64; MATAAQRRFC RCACFCSQNL YVARYGLHLR FRDEHQLRRD YGQLLRSRGC VTSKDFQQLL EELEQEVGRR RRLGQESAVR KALIASSYHP ARPEVYSSLQ DAALAPEFMA AAEYSTSPGA DLEGLLQRLE TVSEEKRIYR VPVFSAKFCQ TLLEELEHFE QSDMPKGRPN TMNNHGVLMY ELGLDDPLVT PLRERFLLPL MALLYPDYGG GYLDSHRAFV VKYALGQDLD LGCHYDNAEL TLNVALGKDF TGGALYFGGL FQAPAALKET LEVEHVVGSG ILHRGGQLHG ARPLCKGERW NLVVWLRASA VRNRLCPMCC QKPELVDDEG FGDGFTREEP TTVDVCVLT // ID OGFD1_MOUSE Reviewed; 545 AA. AC Q3U0K8; Q3TLS5; Q3TPR4; Q80TB3; Q8CFR6; DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2005, sequence version 1. DT 19-MAR-2014, entry version 68. DE RecName: Full=2-oxoglutarate and iron-dependent oxygenase domain-containing protein 1; DE EC=1.14.11.-; GN Name=Ogfod1; Synonyms=Kiaa1612; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE RP SEQUENCE [LARGE SCALE MRNA] OF 9-545 (ISOFORM 2). RC STRAIN=C57BL/6J, and NOD; RC TISSUE=Hippocampus, Mammary gland, and Spleen; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Eye; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-545 (ISOFORM 3). RC TISSUE=Brain; RX PubMed=12693553; DOI=10.1093/dnares/10.1.35; RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S., RA Nakajima D., Nagase T., Ohara O., Koga H.; RT "Prediction of the coding sequences of mouse homologues of KIAA gene: RT II. The complete nucleotide sequences of 400 mouse KIAA-homologous RT cDNAs identified by screening of terminal sequences of cDNA clones RT randomly sampled from size-fractionated libraries."; RL DNA Res. 10:35-48(2003). CC -!- COFACTOR: Binds 1 Fe(2+) ion per subunit (By similarity). CC -!- COFACTOR: Ascorbate (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By CC similarity). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q3U0K8-1; Sequence=Displayed; CC Name=2; CC IsoId=Q3U0K8-2; Sequence=VSP_025854; CC Name=3; CC IsoId=Q3U0K8-3; Sequence=VSP_025853; CC Note=No experimental confirmation available; CC -!- SIMILARITY: Belongs to the TPA1 family. CC -!- SIMILARITY: Contains 1 Fe2OG dioxygenase domain. CC -!- CAUTION: Contains Thr-228 instead of the expected predicted active CC site Lys. CC -!- SEQUENCE CAUTION: CC Sequence=AAH40267.1; Type=Erroneous initiation; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK156765; BAE33844.1; -; mRNA. DR EMBL; AK164189; BAE37671.1; -; mRNA. DR EMBL; AK166343; BAE38717.1; -; mRNA. DR EMBL; BC040267; AAH40267.1; ALT_INIT; mRNA. DR EMBL; AK122532; BAC65814.1; -; mRNA. DR RefSeq; NP_001087226.1; NM_001093757.1. DR RefSeq; NP_808435.3; NM_177767.4. DR UniGene; Mm.251085; -. DR ProteinModelPortal; Q3U0K8; -. DR SMR; Q3U0K8; 72-329. DR BioGrid; 234757; 1. DR STRING; 10090.ENSMUSP00000105183; -. DR PhosphoSite; Q3U0K8; -. DR PaxDb; Q3U0K8; -. DR PRIDE; Q3U0K8; -. DR Ensembl; ENSMUST00000093301; ENSMUSP00000090991; ENSMUSG00000033009. [Q3U0K8-2] DR Ensembl; ENSMUST00000109556; ENSMUSP00000105183; ENSMUSG00000033009. [Q3U0K8-1] DR GeneID; 270086; -. DR KEGG; mmu:270086; -. DR UCSC; uc009mvq.1; mouse. [Q3U0K8-1] DR UCSC; uc009mvr.1; mouse. [Q3U0K8-2] DR UCSC; uc012gim.1; mouse. [Q3U0K8-3] DR CTD; 55239; -. DR MGI; MGI:2442978; Ogfod1. DR eggNOG; COG3751; -. DR GeneTree; ENSGT00390000002349; -. DR HOGENOM; HOG000007015; -. DR HOVERGEN; HBG056995; -. DR InParanoid; Q3U0K8; -. DR OMA; ALLCHDD; -. DR OrthoDB; EOG7FBRHW; -. DR TreeFam; TF105920; -. DR NextBio; 393192; -. DR PRO; PR:Q3U0K8; -. DR ArrayExpress; Q3U0K8; -. DR Bgee; Q3U0K8; -. DR Genevestigator; Q3U0K8; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0031418; F:L-ascorbic acid binding; IEA:UniProtKB-KW. DR GO; GO:0016706; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors; IEA:InterPro. DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase. DR InterPro; IPR019601; Oxoglutarate/Fe-dep_Oase_C. DR InterPro; IPR006620; Pro_4_hyd_alph. DR Pfam; PF13640; 2OG-FeII_Oxy_3; 1. DR Pfam; PF10637; Ofd1_CTDD; 1. DR SMART; SM00702; P4Hc; 1. DR PROSITE; PS51471; FE2OG_OXY; 1. PE 2: Evidence at transcript level; KW Alternative splicing; Complete proteome; Cytoplasm; Dioxygenase; Iron; KW Metal-binding; Nucleus; Oxidoreductase; Reference proteome; Vitamin C. FT CHAIN 1 545 2-oxoglutarate and iron-dependent FT oxygenase domain-containing protein 1. FT /FTId=PRO_0000288975. FT DOMAIN 137 239 Fe2OG dioxygenase. FT METAL 155 155 Iron (By similarity). FT METAL 157 157 Iron (By similarity). FT METAL 218 218 Iron (By similarity). FT VAR_SEQ 52 52 Missing (in isoform 3). FT /FTId=VSP_025853. FT VAR_SEQ 220 262 Missing (in isoform 2). FT /FTId=VSP_025854. FT CONFLICT 12 12 A -> V (in Ref. 1; BAE38717). FT CONFLICT 48 48 P -> S (in Ref. 1; BAE38717). FT CONFLICT 58 58 M -> V (in Ref. 1; BAE38717). FT CONFLICT 80 80 H -> Q (in Ref. 1; BAE38717). FT CONFLICT 397 397 R -> Q (in Ref. 1; BAE38717). SQ SEQUENCE 545 AA; 62734 MW; 92F376ABC86CB410 CRC64; MNGKRPADPG PARPMKKGKK QVSAEFSDAV TEEILRKQVA EAWSCRTPFS HEAIALDMDP FLHCVIPNFI QSQDFLEGLH KELLSLDFHE KYNDLYKFQQ SDDLKNRKEP HISALRKLMF EDFRAWLSKV SGIDLEPTID MSCAKYEFTD ALLCHDDELE GRRIAFILYL VPSWDRDLGG TLDLYDTDEH LQPKQIVKSL IPSWNKLVFF EVSPVSFHQV SEVLSEETSR LSISGWFYGP SLTRPPTYFE PPIPRNPHIP QDHEILYEWI NPAYLEMDYQ MQIQEEFEER SEILLKEFLK PEKFAEVCEA LEKGDVEWKS HGPPNKRFYE KAEENNLPDV LKECMGLFRS EALFLLLSNL TGLKLHFLAP SEDDETEEKG EGETASAAAG TEEGTSRRPS GPENNQVAAG SHSQENGEQA DPEAQEEEAK KESSVPMCQG ELRRWKTGHY TLVHDNTKTE FALDLFLYCG CEGWEPEYGG FTSYIAKGED EELLIVNPEN NSLALVYRDR ETLRFVKHIN HRSLEQSKAF PSRSGFWDFA FIYYE // ID OGFD3_MOUSE Reviewed; 315 AA. AC Q9D136; DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 19-FEB-2014, entry version 85. DE RecName: Full=2-oxoglutarate and iron-dependent oxygenase domain-containing protein 3; DE EC=1.14.11.-; GN Name=Ogfod3; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=BALB/c, and C57BL/6J; TISSUE=Embryo, and Placenta; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Kidney; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- COFACTOR: Binds 1 Fe(2+) ion per subunit (By similarity). CC -!- COFACTOR: Ascorbate (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane CC protein (Potential). CC -!- SIMILARITY: Belongs to the OGFOD3 family. CC -!- SIMILARITY: Contains 1 Fe2OG dioxygenase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK004005; BAB23119.1; -; mRNA. DR EMBL; AK145938; BAE26768.1; -; mRNA. DR EMBL; AK168300; BAE40241.1; -; mRNA. DR EMBL; BC024349; AAH24349.1; -; mRNA. DR RefSeq; NP_079678.1; NM_025402.2. DR UniGene; Mm.390403; -. DR ProteinModelPortal; Q9D136; -. DR PhosphoSite; Q9D136; -. DR PaxDb; Q9D136; -. DR PRIDE; Q9D136; -. DR Ensembl; ENSMUST00000026169; ENSMUSP00000026169; ENSMUSG00000025169. DR GeneID; 66179; -. DR KEGG; mmu:66179; -. DR UCSC; uc007mvk.1; mouse. DR CTD; 79701; -. DR MGI; MGI:1913429; Ogfod3. DR eggNOG; NOG42757; -. DR GeneTree; ENSGT00390000005895; -. DR HOGENOM; HOG000007407; -. DR InParanoid; Q9D136; -. DR OMA; TIHDEYW; -. DR OrthoDB; EOG7JQBNZ; -. DR TreeFam; TF329031; -. DR NextBio; 320874; -. DR Bgee; Q9D136; -. DR CleanEx; MM_1110031I02RIK; -. DR Genevestigator; Q9D136; -. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0031418; F:L-ascorbic acid binding; IEA:UniProtKB-KW. DR GO; GO:0016706; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors; IEA:InterPro. DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase. DR InterPro; IPR006620; Pro_4_hyd_alph. DR Pfam; PF13640; 2OG-FeII_Oxy_3; 1. DR SMART; SM00702; P4Hc; 1. DR PROSITE; PS51471; FE2OG_OXY; 1. PE 2: Evidence at transcript level; KW Complete proteome; Dioxygenase; Glycoprotein; Iron; Membrane; KW Metal-binding; Oxidoreductase; Reference proteome; Signal-anchor; KW Transmembrane; Transmembrane helix; Vitamin C. FT CHAIN 1 315 2-oxoglutarate and iron-dependent FT oxygenase domain-containing protein 3. FT /FTId=PRO_0000325886. FT TOPO_DOM 1 41 Cytoplasmic (Potential). FT TRANSMEM 42 62 Helical; Signal-anchor for type II FT membrane protein; (Potential). FT TOPO_DOM 63 315 Lumenal (Potential). FT DOMAIN 203 305 Fe2OG dioxygenase. FT ACT_SITE 294 294 Potential. FT METAL 226 226 Iron (By similarity). FT METAL 228 228 Iron (By similarity). FT METAL 284 284 Iron (By similarity). FT BINDING 294 294 2-oxoglutarate (Potential). FT CARBOHYD 211 211 N-linked (GlcNAc...) (Potential). FT CARBOHYD 263 263 N-linked (GlcNAc...) (Potential). SQ SEQUENCE 315 AA; 35385 MW; 7D4C5CD55F55EA36 CRC64; MAPQRRGPPR IPEGSSAAER RRATSTKKDR LPREAQRTWL RIVAFGVGLA LVTCLLWSSV GIDDDVAEVV ARRGEVLEGR FIEVPCSEDY DGHRRFEGCT PRKCGRGVTD IVITREEAEQ IRRIAEKGLS LGGSDGGASI LDLHSGALSV GKHFVNLYRY FGDKIQNIFS EEDFQLYRDI RQKVQLTIAE AFGISASLLY LTKPTFFSRI NSTEARTAHD EYWHAHVDKV TYGSFDYTSL LYLSDYLEDF GGGRFVFMEE GSNKTVEPRA GRVSFFTSGS ENLHRVEKVL WGTRYAITIA FTCNPDHGIE DPVLT // ID OXDA_MOUSE Reviewed; 345 AA. AC P18894; Q64465; Q8VCW7; DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot. DT 29-APR-2008, sequence version 3. DT 19-MAR-2014, entry version 118. DE RecName: Full=D-amino-acid oxidase; DE Short=DAAO; DE Short=DAMOX; DE Short=DAO; DE EC=1.4.3.3; GN Name=Dao; Synonyms=Dao1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Kidney; RX PubMed=1976103; DOI=10.1016/0378-1119(90)90193-U; RA Tada M., Fukui K., Momoi K., Miyake Y.; RT "Cloning and expression of a cDNA encoding mouse kidney D-amino acid RT oxidase."; RL Gene 90:293-297(1990). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION OF VARIANT ARG-181. RC TISSUE=Kidney; RX PubMed=1355365; DOI=10.1016/0925-4439(92)90107-X; RA Sasaki M., Konno R., Nishio M., Niwa A., Yasumura Y., Enami J.; RT "A single-base-pair substitution abolishes D-amino-acid oxidase RT activity in the mouse."; RL Biochim. Biophys. Acta 1139:315-318(1992). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Medulla oblongata; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Kidney; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: Regulates the level of the neuromodulator D-serine in CC the brain. Has high activity towards D-DOPA and contributes to CC dopamine synthesis. Could act as a detoxifying agent which removes CC D-amino acids accumulated during aging. Acts on a variety of D- CC amino acids with a preference for those having small hydrophobic CC side chains followed by those bearing polar, aromatic, and basic CC groups. Does not act on acidic amino acids. CC -!- CATALYTIC ACTIVITY: A D-amino acid + H(2)O + O(2) = a 2-oxo acid + CC NH(3) + H(2)O(2). CC -!- COFACTOR: FAD. CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SUBCELLULAR LOCATION: Peroxisome. CC -!- SIMILARITY: Belongs to the DAMOX/DASOX family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M32299; AAA39367.1; -; mRNA. DR EMBL; D10210; BAA01062.1; -; mRNA. DR EMBL; D10211; BAA01063.1; -; mRNA. DR EMBL; AK134813; BAE22296.1; -; mRNA. DR EMBL; BC018377; AAH18377.1; -; mRNA. DR PIR; JH0185; JH0185. DR RefSeq; NP_001273325.1; NM_001286396.1. DR RefSeq; NP_034148.2; NM_010018.3. DR RefSeq; XP_006530224.1; XM_006530161.1. DR RefSeq; XP_006530225.1; XM_006530162.1. DR UniGene; Mm.20115; -. DR PDB; 2DXO; Model; -; @=1-336. DR PDBsum; 2DXO; -. DR ProteinModelPortal; P18894; -. DR SMR; P18894; 1-338. DR IntAct; P18894; 2. DR MINT; MINT-4105961; -. DR ChEMBL; CHEMBL2331068; -. DR PaxDb; P18894; -. DR PRIDE; P18894; -. DR Ensembl; ENSMUST00000112292; ENSMUSP00000107911; ENSMUSG00000042096. DR Ensembl; ENSMUST00000161610; ENSMUSP00000125588; ENSMUSG00000042096. DR GeneID; 13142; -. DR KEGG; mmu:13142; -. DR UCSC; uc008yza.1; mouse. DR CTD; 1610; -. DR MGI; MGI:94859; Dao. DR eggNOG; COG0665; -. DR GeneTree; ENSGT00390000018635; -. DR HOGENOM; HOG000046303; -. DR HOVERGEN; HBG003493; -. DR InParanoid; P18894; -. DR KO; K00273; -. DR OrthoDB; EOG7B31NB; -. DR TreeFam; TF313887; -. DR NextBio; 283222; -. DR PRO; PR:P18894; -. DR ArrayExpress; P18894; -. DR Bgee; P18894; -. DR CleanEx; MM_DAO1; -. DR Genevestigator; P18894; -. DR GO; GO:0005829; C:cytosol; IEA:Ensembl. DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:Ensembl. DR GO; GO:0005778; C:peroxisomal membrane; IEA:Ensembl. DR GO; GO:0048037; F:cofactor binding; IDA:UniProtKB. DR GO; GO:0003884; F:D-amino-acid oxidase activity; IDA:UniProtKB. DR GO; GO:0071949; F:FAD binding; IEA:Ensembl. DR GO; GO:0055130; P:D-alanine catabolic process; IDA:UniProtKB. DR GO; GO:0036088; P:D-serine catabolic process; IEA:Ensembl. DR GO; GO:0042416; P:dopamine biosynthetic process; IEA:Ensembl. DR GO; GO:0006551; P:leucine metabolic process; IMP:MGI. DR GO; GO:0006562; P:proline catabolic process; IEA:Ensembl. DR Gene3D; 3.40.50.720; -; 3. DR InterPro; IPR023209; D-aa_oxidase. DR InterPro; IPR006181; D-amino_acid_oxidase_CS. DR InterPro; IPR006076; FAD-dep_OxRdtase. DR InterPro; IPR016040; NAD(P)-bd_dom. DR PANTHER; PTHR11530; PTHR11530; 1. DR Pfam; PF01266; DAO; 1. DR PIRSF; PIRSF000189; D-aa_oxidase; 1. DR PROSITE; PS00677; DAO; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; FAD; Flavoprotein; Oxidoreductase; KW Peroxisome; Polymorphism; Reference proteome. FT CHAIN 1 345 D-amino-acid oxidase. FT /FTId=PRO_0000162762. FT NP_BIND 3 17 FAD (By similarity). FT NP_BIND 36 37 FAD (By similarity). FT NP_BIND 43 44 FAD (By similarity). FT NP_BIND 48 50 FAD (By similarity). FT NP_BIND 310 314 FAD (By similarity). FT MOTIF 343 345 Microbody targeting signal. FT BINDING 52 52 Substrate (By similarity). FT BINDING 163 163 FAD; via amide nitrogen and carbonyl FT oxygen (By similarity). FT BINDING 180 180 FAD (By similarity). FT BINDING 215 215 Substrate (By similarity). FT BINDING 226 226 Substrate (By similarity). FT BINDING 281 281 Substrate (By similarity). FT BINDING 311 311 Substrate; via carbonyl oxygen (By FT similarity). FT BINDING 315 315 FAD (By similarity). FT VARIANT 181 181 G -> R (abolishes activity). FT CONFLICT 64 64 A -> V (in Ref. 1; AAA39367 and 2; FT BAA01063). FT CONFLICT 157 157 K -> N (in Ref. 2; BAA01062). FT CONFLICT 171 171 R -> RG (in Ref. 2; BAA01062). FT CONFLICT 296 296 H -> F (in Ref. 1; AAA39367 and 2; FT BAA01062/BAA01063). SQ SEQUENCE 345 AA; 38661 MW; 29A5D9B55D64700F CRC64; MRVAVIGAGV IGLSTALCIH ERYHPTQPLH MKIYADRFTP FTTSDVAAGL WQPYLSDPSN PQEAEWSQQT FDYLLSCLHS PNAEKMGLAL ISGYNLFRDE VPDPFWKNAV LGFRKLTPSE MDLFPDYGYG WFNTSLLLEG KSYLPWLTER LTERGVKLIH RKVESLEEVA RGVDVIINCT GVWAGALQAD ASLQPGRGQI IQVEAPWIKH FILTHDPSLG IYNSPYIIPG SKTVTLGGIF QLGNWSGLNS VRDHNTIWKS CCKLEPTLKN ARIVGELTGF RPVRPQVRLE REWLRHGSSS AEVIHNYGHG GYGLTIHWGC AMEAANLFGK ILEEKKLSRL PPSHL // ID OXDD_MOUSE Reviewed; 341 AA. AC Q922Z0; Q3TT69; Q8R2R2; DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 19-FEB-2014, entry version 91. DE RecName: Full=D-aspartate oxidase; DE Short=DASOX; DE Short=DDO; DE EC=1.4.3.1; GN Name=Ddo; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Heart, Lung, and Pituitary; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Czech II, and FVB/N; TISSUE=Mammary tumor; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: Selectively catalyzes the oxidative deamination of D- CC aspartate and its N-methylated derivative, N-methyl D-aspartate CC (By similarity). CC -!- CATALYTIC ACTIVITY: D-aspartate + H(2)O + O(2) = oxaloacetate + CC NH(3) + H(2)O(2). CC -!- COFACTOR: FAD or 6-hydroxyflavin adenine dinucleotide (By CC similarity). CC -!- SUBCELLULAR LOCATION: Peroxisome (By similarity). CC -!- SIMILARITY: Belongs to the DAMOX/DASOX family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK033375; BAC28253.1; -; mRNA. DR EMBL; AK085947; BAC39577.1; -; mRNA. DR EMBL; AK161548; BAE36456.1; -; mRNA. DR EMBL; BC006690; AAH06690.1; -; mRNA. DR EMBL; BC027312; AAH27312.1; -; mRNA. DR RefSeq; NP_081718.2; NM_027442.5. DR UniGene; Mm.252862; -. DR ProteinModelPortal; Q922Z0; -. DR SMR; Q922Z0; 6-324. DR PhosphoSite; Q922Z0; -. DR PaxDb; Q922Z0; -. DR PRIDE; Q922Z0; -. DR Ensembl; ENSMUST00000019977; ENSMUSP00000019977; ENSMUSG00000063428. DR GeneID; 70503; -. DR KEGG; mmu:70503; -. DR UCSC; uc007exa.2; mouse. DR CTD; 8528; -. DR MGI; MGI:1925528; Ddo. DR eggNOG; COG0665; -. DR GeneTree; ENSGT00390000018635; -. DR HOGENOM; HOG000046303; -. DR HOVERGEN; HBG003493; -. DR InParanoid; Q922Z0; -. DR KO; K00272; -. DR OMA; RIGDLWE; -. DR OrthoDB; EOG7B31NB; -. DR TreeFam; TF313887; -. DR NextBio; 331757; -. DR PRO; PR:Q922Z0; -. DR Bgee; Q922Z0; -. DR CleanEx; MM_DDO; -. DR Genevestigator; Q922Z0; -. DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell. DR GO; GO:0048037; F:cofactor binding; IDA:UniProtKB. DR GO; GO:0008445; F:D-aspartate oxidase activity; IDA:UniProtKB. DR GO; GO:0006533; P:aspartate catabolic process; IEA:Ensembl. DR GO; GO:0006531; P:aspartate metabolic process; IMP:MGI. DR GO; GO:0019478; P:D-amino acid catabolic process; IDA:UniProtKB. DR GO; GO:0007625; P:grooming behavior; IMP:MGI. DR GO; GO:0042445; P:hormone metabolic process; IMP:MGI. DR GO; GO:0007320; P:insemination; IMP:MGI. DR InterPro; IPR023209; D-aa_oxidase. DR InterPro; IPR006181; D-amino_acid_oxidase_CS. DR InterPro; IPR006076; FAD-dep_OxRdtase. DR PANTHER; PTHR11530; PTHR11530; 1. DR Pfam; PF01266; DAO; 1. DR PIRSF; PIRSF000189; D-aa_oxidase; 1. DR PROSITE; PS00677; DAO; 1. PE 2: Evidence at transcript level; KW Complete proteome; FAD; Flavoprotein; Oxidoreductase; Peroxisome; KW Reference proteome. FT CHAIN 1 341 D-aspartate oxidase. FT /FTId=PRO_0000162771. FT NP_BIND 6 20 FAD (By similarity). FT NP_BIND 36 37 FAD (By similarity). FT NP_BIND 43 44 FAD (By similarity). FT NP_BIND 48 50 FAD (By similarity). FT NP_BIND 307 311 FAD (By similarity). FT MOTIF 339 341 Microbody targeting signal (Potential). FT BINDING 166 166 FAD; via amide nitrogen and carbonyl FT oxygen (By similarity). FT BINDING 183 183 FAD (By similarity). FT BINDING 223 223 Substrate (By similarity). FT BINDING 278 278 Substrate (By similarity). FT BINDING 312 312 FAD (By similarity). FT CONFLICT 56 56 C -> Y (in Ref. 2; AAH27312). FT CONFLICT 67 67 W -> C (in Ref. 2; AAH27312). SQ SEQUENCE 341 AA; 37546 MW; A80BC74CC44A601D CRC64; MDTVCIAVVG AGVIGLSTAA CISQLVPGCT VTVISDRFTP DTTSNVAAGM LIPHTCADTP VPTQKRWFRE TFEHLSEIAK SAEAADAGVH LVSGWQIFRS VPAEEVPFWA DVVLGFRKMT EAELKRFPQY VFGQAFTTLK CETSAYLPWL ERRIKGSGGL LLTRRIEDLW ELQPSFDIVV NCSGLGSRRL VGDPMISPVR GQVLQARAPW VKHFIRDGGG LTYVYPGMSY VTLGGTRQKG DWNRSPDAEL SREIFSRCCT LEPSLHRAYD IKEKVGLRPS RPGVRLQKEI LVRGQQTLPV VHNYGHGSGG ISVHWGSALE ATRLVMECIH TLRTPASLSK L // ID OXLA_MOUSE Reviewed; 630 AA. AC O09046; Q1LZI6; Q3T9N9; Q3U7S6; Q3V0K2; Q6Y632; Q6YBV6; Q6YDI8; AC Q8R2G8; Q9CXK7; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1997, sequence version 1. DT 19-MAR-2014, entry version 119. DE RecName: Full=L-amino-acid oxidase; DE Short=LAAO; DE Short=LAO; DE EC=1.4.3.2; DE AltName: Full=Interleukin-4-induced protein 1; DE Short=IL4-induced protein 1; DE AltName: Full=Protein Fig-1; DE Short=mFIG1; DE Flags: Precursor; GN Name=Il4i1; Synonyms=Fig1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1). RC STRAIN=BALB/c, and CBA/J; RX PubMed=9122225; DOI=10.1073/pnas.94.6.2507; RA Chu C.C., Paul W.E.; RT "Fig1, an interleukin 4-induced mouse B cell gene isolated by cDNA RT representational difference analysis."; RL Proc. Natl. Acad. Sci. U.S.A. 94:2507-2512(1997). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1). RC STRAIN=CBA/J, MRL, and NZW; RA Chu C.C., Kim J.A., Gupta N., Yuen G.J., Thomas R.R., George J., RA Hsueh K.; RT "Interleukin-four induced gene-1 polymorphisms correlate with Sle3 RT autoimmune susceptibility."; RL Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC STRAIN=C57BL/6J, and NOD; RC TISSUE=Bone marrow, Embryonic head, Spleen, and Testis; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 122-289. RC STRAIN=BALB/c; TISSUE=Spleen; RX PubMed=9798653; DOI=10.1016/S0161-5890(98)00031-5; RA Chu C.C., Paul W.E.; RT "Expressed genes in interleukin-4 treated B cells identified by cDNA RT representational difference analysis."; RL Mol. Immunol. 35:487-502(1998). RN [6] RP CHARACTERIZATION, FUNCTION, GLYCOSYLATION, AND SUBCELLULAR LOCATION. RX PubMed=15383589; RA Mason J.M., Naidu M.D., Barcia M., Porti D., Chavan S.S., Chu C.C.; RT "IL-4-induced gene-1 is a leukocyte L-amino acid oxidase with an RT unusual acidic pH preference and lysosomal localization."; RL J. Immunol. 173:4561-4567(2004). RN [7] RP ALTERNATIVE PROMOTER USAGE, AND TISSUE SPECIFICITY. RX PubMed=16029492; DOI=10.1186/1741-7007-3-16; RA Wiemann S., Kolb-Kokocinski A., Poustka A.; RT "Alternative pre-mRNA processing regulates cell-type specific RT expression of the IL4l1 and NUP62 genes."; RL BMC Biol. 3:16-16(2005). CC -!- FUNCTION: Lysosomal L-amino-acid oxidase with highest specific CC activity with phenylalanine. May play a role in lysosomal antigen CC processing and presentation. CC -!- CATALYTIC ACTIVITY: An L-amino acid + H(2)O + O(2) = a 2-oxo acid CC + NH(3) + H(2)O(2). CC -!- COFACTOR: FAD. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=6.5 mM for phenylalanine (at 37 degrees Celsius); CC Vmax=0.0099 nmol/min/mg enzyme toward phenylalanine (at 37 CC degrees Celsius); CC pH dependence: CC Optimum pH is 4.0; CC -!- SUBCELLULAR LOCATION: Isoform 1: Lysosome. CC -!- SUBCELLULAR LOCATION: Isoform 2: Lysosome. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative promoter usage; Named isoforms=2; CC Name=1; CC IsoId=O09046-1; Sequence=Displayed; CC Name=2; Synonyms=IL4I1_2; CC IsoId=O09046-2; Sequence=VSP_017174; CC Note=Uses the promoter of the upstream NUP62 gene and shares the CC first 2 non-coding exons with NUP62; CC -!- TISSUE SPECIFICITY: Isoform 1 primarily found in immune tissues, CC mostly in B-lymphocytes. Isoform 2 restricted to the testis, CC predominantly in Sertoli cells at the periphery of the ducts, and CC the brain, including Purkinje cells, hippocampus and mitral cells CC in the olfactory bulb. No isoform 2 expression in fetal tissues. CC -!- INDUCTION: By interleukin-4. CC -!- SIMILARITY: Belongs to the flavin monoamine oxidase family. FIG1 CC subfamily. CC -!- SEQUENCE CAUTION: CC Sequence=BAB29253.1; Type=Erroneous initiation; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U70429; AAB51353.1; -; mRNA. DR EMBL; U70430; AAB51354.1; -; Genomic_RNA. DR EMBL; AF538041; AAM15529.1; -; Genomic_DNA. DR EMBL; AY442170; AAM15530.2; -; Genomic_DNA. DR EMBL; AY157537; AAO17038.1; -; Genomic_DNA. DR EMBL; AY157538; AAO17039.1; -; mRNA. DR EMBL; AY161348; AAO23118.1; -; Genomic_DNA. DR EMBL; AY178834; AAO65453.1; -; Genomic_DNA. DR EMBL; AY442343; AAS00457.1; -; Genomic_DNA. DR EMBL; AK014297; BAB29253.1; ALT_INIT; mRNA. DR EMBL; AK133082; BAE21502.1; -; mRNA. DR EMBL; AK150582; BAE29676.1; -; mRNA. DR EMBL; AK151030; BAE30047.1; -; mRNA. DR EMBL; AK151171; BAE30174.1; -; mRNA. DR EMBL; AK152538; BAE31293.1; -; mRNA. DR EMBL; AK172393; BAE42981.1; -; mRNA. DR EMBL; BC115960; AAI15961.1; -; mRNA. DR EMBL; U89428; AAC36534.1; -; Transcribed_RNA. DR EMBL; U89429; AAC36535.1; -; mRNA. DR RefSeq; NP_001164495.1; NM_001171024.1. DR RefSeq; NP_034345.2; NM_010215.3. DR UniGene; Mm.2565; -. DR PDB; 2I8W; Model; -; @=30-502. DR PDBsum; 2I8W; -. DR ProteinModelPortal; O09046; -. DR SMR; O09046; 28-506. DR MINT; MINT-1727921; -. DR PhosphoSite; O09046; -. DR PaxDb; O09046; -. DR PRIDE; O09046; -. DR Ensembl; ENSMUST00000033015; ENSMUSP00000033015; ENSMUSG00000074141. DR GeneID; 100328588; -. DR GeneID; 14204; -. DR KEGG; mmu:100328588; -. DR KEGG; mmu:14204; -. DR CTD; 100328588; -. DR CTD; 259307; -. DR MGI; MGI:109552; Il4i1. DR eggNOG; COG1231; -. DR GeneTree; ENSGT00730000110942; -. DR HOVERGEN; HBG005729; -. DR KO; K03334; -. DR NextBio; 285446; -. DR PRO; PR:O09046; -. DR ArrayExpress; O09046; -. DR Bgee; O09046; -. DR CleanEx; MM_IL4I1; -. DR Genevestigator; O09046; -. DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell. DR GO; GO:0001716; F:L-amino-acid oxidase activity; IEA:UniProtKB-EC. DR InterPro; IPR002937; Amino_oxidase. DR InterPro; IPR001613; Flavin_amine_oxidase. DR Pfam; PF01593; Amino_oxidase; 1. DR PRINTS; PR00757; AMINEOXDASEF. PE 1: Evidence at protein level; KW 3D-structure; Alternative promoter usage; Complete proteome; KW Disulfide bond; FAD; Flavoprotein; Glycoprotein; Lysosome; KW Oxidoreductase; Reference proteome; Signal. FT SIGNAL 1 21 Potential. FT CHAIN 22 630 L-amino-acid oxidase. FT /FTId=PRO_0000001711. FT NP_BIND 114 115 FAD (By similarity). FT NP_BIND 488 491 FAD (By similarity). FT BINDING 88 88 FAD (By similarity). FT BINDING 96 96 FAD (By similarity). FT BINDING 115 115 Substrate (By similarity). FT BINDING 286 286 FAD; via amide nitrogen and carbonyl FT oxygen (By similarity). FT BINDING 395 395 Substrate (By similarity). FT BINDING 479 479 FAD (By similarity). FT CARBOHYD 53 53 N-linked (GlcNAc...) (Potential). FT CARBOHYD 133 133 N-linked (GlcNAc...) (Potential). FT CARBOHYD 219 219 N-linked (GlcNAc...) (Potential). FT DISULFID 35 198 By similarity. FT VAR_SEQ 1 5 MAGLA -> MGARRAPQRPPCT (in isoform 2). FT /FTId=VSP_017174. FT CONFLICT 12 12 A -> V (in Ref. 2; AAO17038/AAO17039). FT CONFLICT 56 56 S -> L (in Ref. 2; AAO65453/AAS00457). FT CONFLICT 184 184 M -> V (in Ref. 3; BAE30174/BAE31293). FT CONFLICT 385 385 R -> Q (in Ref. 2; AAO23118 and 3; FT BAE21502/BAE29676/BAE30047/BAE30174/ FT BAE31293). FT CONFLICT 454 454 Q -> R (in Ref. 3; BAE21502). FT CONFLICT 537 537 E -> Q (in Ref. 3; BAE21502). FT CONFLICT 551 551 P -> L (in Ref. 2; AAO17038/AAO17039). FT CONFLICT 568 568 A -> M (in Ref. 2; AAO17038/AAO17039). FT CONFLICT 598 630 PSEHVQVHGEVIPEWHGHGGSGTPQMHRVGDHS -> LRSM FT YRCMGKSSLSGMVMGDLAPRKCTEWGTTPNRKEEVSTQLLS FT QPSSGQTDHLH (in Ref. 3; BAB29253). SQ SEQUENCE 630 AA; 70191 MW; A674C5D60D89A071 CRC64; MAGLALRLVL AATLLGLAGS LDWKAASSLN PIEKCMEDHD YEQLLKVVTL GLNRTSKPQK VVVVGAGVAG LVAAKMLSDA GHKVTILEAD NRIGGRIFTF RDEKTGWIGE LGAMRMPSSH RILHKLCRTL GLNLTQFTQY DENTWTEVHN VKLRNYVVEK MPEKLGYNLN NRERGHSPED IYQMALNKAF KDLKALGCKK AMNKFNKHTL LEYLLEEGNL SRPAVQLLGD VMSEEGFFYL SFAEALRAHA CLSDRLRYSR IVGGWDLLPR ALLSSLSGAL LLNAPVVSIT QGRNDVRVHI ATSLHSEKTL TADVVLLTAS GPALQRITFS PPLTRKRQEA LRALHYVAAS KVFLSFRRPF WHEEHIEGGH SNTDRPSRLI FYPARGEGSL LLASYTWSDA AAPFAGLSTD QTLRLVLQDV AALHGPVVFR LWDGRGVVKR WAEDPHSQGG FVVQPPLYGR EAEDYDWSAP FGRIYFAGEH TALPHGWVET AVKSGLRAAV RINNNYGYGE VDPQMMEHAY AEANYLDQYP EGERPEEQQA REEVSPDEQE PSHKHLLVET SPEGQQHAFV EAIPELQGHV FVETVPQEKG HAHQNIYPSE HVQVHGEVIP EWHGHGGSGT PQMHRVGDHS // ID OXND1_MOUSE Reviewed; 311 AA. AC Q8VE38; Q3UT09; Q8C093; DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot. DT 11-SEP-2007, sequence version 2. DT 19-MAR-2014, entry version 75. DE RecName: Full=Oxidoreductase NAD-binding domain-containing protein 1; DE EC=1.-.-.-; DE Flags: Precursor; GN Name=Oxnad1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC STRAIN=C57BL/6J; TISSUE=Egg, and Medulla oblongata; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC STRAIN=Czech II; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q8VE38-1; Sequence=Displayed; CC Name=2; CC IsoId=Q8VE38-2; Sequence=VSP_027765; CC -!- SIMILARITY: Contains 1 FAD-binding FR-type domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK031978; BAC27636.1; -; mRNA. DR EMBL; AK139884; BAE24171.1; -; mRNA. DR EMBL; BC019806; AAH19806.1; -; mRNA. DR RefSeq; NP_663435.2; NM_145460.2. DR UniGene; Mm.202257; -. DR ProteinModelPortal; Q8VE38; -. DR SMR; Q8VE38; 77-307. DR PhosphoSite; Q8VE38; -. DR PaxDb; Q8VE38; -. DR PRIDE; Q8VE38; -. DR Ensembl; ENSMUST00000022462; ENSMUSP00000022462; ENSMUSG00000021906. [Q8VE38-1] DR GeneID; 218885; -. DR KEGG; mmu:218885; -. DR UCSC; uc007syg.2; mouse. [Q8VE38-1] DR CTD; 92106; -. DR MGI; MGI:1916953; Oxnad1. DR eggNOG; COG0543; -. DR GeneTree; ENSGT00390000004280; -. DR HOGENOM; HOG000078573; -. DR HOVERGEN; HBG108225; -. DR InParanoid; Q8VE38; -. DR OMA; ADKDFSF; -. DR TreeFam; TF329774; -. DR NextBio; 376475; -. DR PRO; PR:Q8VE38; -. DR ArrayExpress; Q8VE38; -. DR Bgee; Q8VE38; -. DR CleanEx; MM_OXNAD1; -. DR Genevestigator; Q8VE38; -. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW. DR InterPro; IPR017927; Fd_Rdtase_FAD-bd. DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd. DR InterPro; IPR001221; Phe_hydroxylase. DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl. DR Pfam; PF00175; NAD_binding_1; 1. DR PRINTS; PR00410; PHEHYDRXLASE. DR SUPFAM; SSF63380; SSF63380; 1. DR PROSITE; PS51384; FAD_FR; 1. PE 2: Evidence at transcript level; KW Alternative splicing; Complete proteome; NAD; Oxidoreductase; KW Reference proteome; Signal. FT SIGNAL 1 16 Potential. FT CHAIN 17 311 Oxidoreductase NAD-binding domain- FT containing protein 1. FT /FTId=PRO_0000299572. FT DOMAIN 60 171 FAD-binding FR-type. FT NP_BIND 177 182 NAD (By similarity). FT VAR_SEQ 1 61 Missing (in isoform 2). FT /FTId=VSP_027765. FT CONFLICT 202 203 RS -> SG (in Ref. 2; AAH19806). FT CONFLICT 253 253 A -> V (in Ref. 2; AAH19806). SQ SEQUENCE 311 AA; 34727 MW; 7F8B5A18C32FD33E CRC64; MAHVALIPGL SRGSVGAVCT QAASWGLKAS TLRHLTLASI IKSRRKTDHL ERTASVLRRE VMAAAKVCEI THESPSVKSL RLLVADKDFS FKAGQWVDFF IPGVSVVGGF SICSSPQRLE RDRIIELAVK YADHPPAVWV HNKCTLDSEV ALRVGGEFFF DPQPTDAPRN LILIAGGVGI NPLLSILRHS ADLHRDHADK GRSYEIGTVK LFYSAKNTSE LLFKKDILDL VHEFPEKISC SFHVTKQTAQ ISAELKPYVT DGRITEKEIR DHISAETLFY VCGPPPMTDF FSKHLESCHV PKEHICFEKW W // ID P33MX_MOUSE Reviewed; 303 AA. AC Q9DBN4; Q3TJ26; Q3UMA7; Q69ZP2; Q8C1J8; Q9D4T9; DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 19-MAR-2014, entry version 87. DE RecName: Full=Putative monooxygenase p33MONOX; DE EC=1.-.-.-; GN Name=P33monox; Synonyms=Kiaa1191; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RX PubMed=15368895; DOI=10.1093/dnares/11.3.205; RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H., RA Nagase T., Ohara O., Koga H.; RT "Prediction of the coding sequences of mouse homologues of KIAA gene: RT IV. The complete nucleotide sequences of 500 mouse KIAA-homologous RT cDNAs identified by screening of terminal sequences of cDNA clones RT randomly sampled from size-fractionated libraries."; RL DNA Res. 11:205-218(2004). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3). RC STRAIN=C57BL/6J; RC TISSUE=Amnion, Head, Liver, Mammary gland, Placenta, Skin, and Testis; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC STRAIN=C57BL/6, and FVB/N; TISSUE=Brain, Kidney, and Mammary tumor; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=17242355; DOI=10.1073/pnas.0609836104; RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; RT "Large-scale phosphorylation analysis of mouse liver."; RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). RN [5] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006; RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M., RA Thibault P.; RT "The phagosomal proteome in interferon-gamma-activated macrophages."; RL Immunity 30:143-154(2009). RN [6] RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION. RX PubMed=21153684; DOI=10.1007/s11010-010-0690-4; RA Mishra M., Inoue N., Heese K.; RT "Characterizing the novel protein p33MONOX."; RL Mol. Cell. Biochem. 350:127-134(2011). CC -!- FUNCTION: Potential NADPH-dependent oxidoreductase. May be CC involved in the regulation of neuronal survival, differentiation CC and axonal outgrowth (By similarity). CC -!- SUBUNIT: Interacts with COBRA1, NOL12 and PRNP (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q9DBN4-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9DBN4-2; Sequence=VSP_028802, VSP_028803; CC Note=Ref.2 (BAC25449) sequence differs from that shown due to a CC frameshift in position 38; CC Name=3; CC IsoId=Q9DBN4-3; Sequence=VSP_028804, VSP_028805; CC -!- TISSUE SPECIFICITY: Expressed in neuronal pyramidal cells of the CC hippocampus and in the neurons of the cortex. CC -!- SIMILARITY: Belongs to the P33MONOX family. CC -!- SEQUENCE CAUTION: CC Sequence=BAD32404.1; Type=Erroneous initiation; Note=Translation N-terminally shortened; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK173126; BAD32404.1; ALT_INIT; mRNA. DR EMBL; AK004845; BAB23611.1; -; mRNA. DR EMBL; AK014792; BAC25449.1; ALT_FRAME; mRNA. DR EMBL; AK016176; BAB30137.1; -; mRNA. DR EMBL; AK028697; BAC26072.1; -; mRNA. DR EMBL; AK145025; BAE26191.1; -; mRNA. DR EMBL; AK159945; BAE35501.1; -; mRNA. DR EMBL; AK167616; BAE39669.1; -; mRNA. DR EMBL; AK169399; BAE41145.1; -; mRNA. DR EMBL; BC033445; AAH33445.1; -; mRNA. DR EMBL; BC039775; AAH39775.1; -; mRNA. DR EMBL; BC043040; AAH43040.1; -; mRNA. DR EMBL; BC054417; AAH54417.1; -; mRNA. DR RefSeq; NP_001239574.1; NM_001252645.1. DR RefSeq; NP_001239575.1; NM_001252646.1. DR RefSeq; NP_001239576.1; NM_001252647.1. DR RefSeq; NP_001239577.1; NM_001252648.1. DR RefSeq; NP_598558.1; NM_133797.4. DR RefSeq; XP_006517541.1; XM_006517478.1. DR UniGene; Mm.24593; -. DR UniGene; Mm.451378; -. DR UniGene; Mm.489745; -. DR ProteinModelPortal; Q9DBN4; -. DR IntAct; Q9DBN4; 1. DR MINT; MINT-4128317; -. DR PhosphoSite; Q9DBN4; -. DR PaxDb; Q9DBN4; -. DR PRIDE; Q9DBN4; -. DR DNASU; 97820; -. DR Ensembl; ENSMUST00000026989; ENSMUSP00000026989; ENSMUSG00000025871. [Q9DBN4-1] DR GeneID; 97820; -. DR KEGG; mmu:97820; -. DR UCSC; uc007qof.3; mouse. [Q9DBN4-1] DR MGI; MGI:1921162; 4833439L19Rik. DR eggNOG; NOG82876; -. DR GeneTree; ENSGT00390000000537; -. DR HOGENOM; HOG000088653; -. DR HOVERGEN; HBG055539; -. DR InParanoid; Q9DBN4; -. DR OMA; LPIGMYR; -. DR OrthoDB; EOG76MK94; -. DR TreeFam; TF332226; -. DR NextBio; 353088; -. DR ArrayExpress; Q9DBN4; -. DR Bgee; Q9DBN4; -. DR CleanEx; MM_4833439L19RIK; -. DR Genevestigator; Q9DBN4; -. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW. DR InterPro; IPR026759; P33MONOX. DR PANTHER; PTHR32113; PTHR32113; 1. PE 1: Evidence at protein level; KW Alternative splicing; Complete proteome; Cytoplasm; NADP; KW Oxidoreductase; Reference proteome. FT CHAIN 1 303 Putative monooxygenase p33MONOX. FT /FTId=PRO_0000307731. FT MOTIF 67 77 Flavin-containing monooxygenase motif. FT VAR_SEQ 1 70 Missing (in isoform 2). FT /FTId=VSP_028802. FT VAR_SEQ 71 112 EEGAASVSSLAVTPSPATDSSDKAPVVKAKATHVIMSSLIT FT K -> MGAFVALSRWLCSVQPSSLLGHLEPRSLFSAGSRAA FT GGGRAE (in isoform 2). FT /FTId=VSP_028803. FT VAR_SEQ 152 164 LHKLKLQSGETAK -> PHFPFKTASVIPF (in FT isoform 3). FT /FTId=VSP_028804. FT VAR_SEQ 165 303 Missing (in isoform 3). FT /FTId=VSP_028805. FT CONFLICT 13 13 P -> H (in Ref. 2; BAE26191). FT CONFLICT 127 139 LRDAGYTPHKGLT -> RRDSCITPQWGLS (in Ref. FT 2; BAB30137). FT CONFLICT 143 143 T -> A (in Ref. 2; BAE39669). FT CONFLICT 145 145 Y -> L (in Ref. 2; BAB30137). SQ SEQUENCE 303 AA; 32715 MW; 2203ADB0AC7EB153 CRC64; MASRQPEVPA LAPSGPLGKM SLPIGMCRRA FSYDDALEDP APMTPPPSDM GSIPWKPVIP ERKYQHLDKT EEGAASVSSL AVTPSPATDS SDKAPVVKAK ATHVIMSSLI TKQTQESIQR FEQQAGLRDA GYTPHKGLTT EETKYLRVAE ALHKLKLQSG ETAKEEKHPA SAQSTPSSTP HASPKQKSRG WFPSGSSTAL PAPNPHTMDP GSGNDRNSAD KWSLFGPRPL QKSDSGFAIQ AYKGAPRPSP MEVMRAQATR VGEDPATFKP PKMDVPMVEG KKQPLRTHNL KPRDLNVLTP TGF // ID P3H3_MOUSE Reviewed; 732 AA. AC Q8CG70; O88836; DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 19-MAR-2014, entry version 88. DE RecName: Full=Prolyl 3-hydroxylase 3; DE EC=1.14.11.7; DE AltName: Full=Leprecan-like protein 2; DE AltName: Full=Protein B; DE Flags: Precursor; GN Name=Leprel2; Synonyms=P3h3; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=C57BL/6J; RX PubMed=15063763; DOI=10.1016/j.bbrc.2004.03.060; RA Jaernum S., Kjellman C., Darabi A., Nilsson I., Edvardsen K., RA Aaman P.; RT "LEPREL1, a novel ER and Golgi resident member of the Leprecan RT family."; RL Biochem. Biophys. Res. Commun. 317:342-351(2004). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=15044469; DOI=10.1074/jbc.M312807200; RA Vranka J.A., Sakai L.Y., Bachinger H.P.; RT "Prolyl 3-hydroxylase 1, enzyme characterization and identification of RT a novel family of enzymes."; RL J. Biol. Chem. 279:23615-23621(2004). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] OF 139-732. RC STRAIN=FVB/N; TISSUE=Mammary tumor; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 165-732. RX PubMed=9445485; RA Ansari-Lari M.A., Oeltjen J.C., Schwartz S., Zhang Z., Muzny D.M., RA Lu J., Gorrell J.H., Chinault A.C., Belmont J.W., Miller W., RA Gibbs R.A.; RT "Comparative sequence analysis of a gene-rich cluster at human RT chromosome 12p13 and its syntenic region in mouse chromosome 6."; RL Genome Res. 8:29-40(1998). CC -!- FUNCTION: Has prolyl 3-hydroxylase activity catalyzing the post- CC translational formation of 3-hydroxyproline in -Xaa-Pro-Gly- CC sequences in collagens, especially types IV and V (By similarity). CC -!- CATALYTIC ACTIVITY: L-proline-[procollagen] + 2-oxoglutarate + CC O(2) = trans-3-hydroxy-L-proline-[procollagen] + succinate + CC CO(2). CC -!- COFACTOR: Iron (By similarity). CC -!- COFACTOR: Ascorbate (By similarity). CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum (By similarity). CC -!- SIMILARITY: Belongs to the leprecan family. CC -!- SIMILARITY: Contains 1 Fe2OG dioxygenase domain. CC -!- SIMILARITY: Contains 4 TPR repeats. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJ441086; CAD29580.1; -; mRNA. DR EMBL; AY463530; AAS45239.1; -; mRNA. DR EMBL; BC003726; AAH03726.1; -; mRNA. DR EMBL; BC016431; AAH16431.1; -; mRNA. DR EMBL; AC002397; AAC36012.1; -; Genomic_DNA. DR RefSeq; NP_038562.2; NM_013534.4. DR UniGene; Mm.35708; -. DR ProteinModelPortal; Q8CG70; -. DR SMR; Q8CG70; 36-80, 153-200, 216-243, 315-354. DR PhosphoSite; Q8CG70; -. DR PaxDb; Q8CG70; -. DR PRIDE; Q8CG70; -. DR Ensembl; ENSMUST00000023958; ENSMUSP00000023958; ENSMUSG00000023191. DR GeneID; 14789; -. DR KEGG; mmu:14789; -. DR UCSC; uc009dsf.1; mouse. DR CTD; 10536; -. DR MGI; MGI:1315208; Leprel2. DR eggNOG; NOG269251; -. DR GeneTree; ENSGT00550000074573; -. DR HOGENOM; HOG000231087; -. DR HOVERGEN; HBG053224; -. DR InParanoid; Q8CG70; -. DR OMA; RAYYQLK; -. DR OrthoDB; EOG7BZVSS; -. DR TreeFam; TF320837; -. DR ChiTaRS; LEPREL2; mouse. DR NextBio; 286923; -. DR PRO; PR:Q8CG70; -. DR ArrayExpress; Q8CG70; -. DR Bgee; Q8CG70; -. DR CleanEx; MM_LEPREL2; -. DR Genevestigator; Q8CG70; -. DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0031418; F:L-ascorbic acid binding; IEA:UniProtKB-KW. DR GO; GO:0019797; F:procollagen-proline 3-dioxygenase activity; IEA:UniProtKB-EC. DR GO; GO:0008285; P:negative regulation of cell proliferation; IEA:Ensembl. DR Gene3D; 1.25.40.10; -; 3. DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase. DR InterPro; IPR006620; Pro_4_hyd_alph. DR InterPro; IPR011990; TPR-like_helical. DR Pfam; PF13640; 2OG-FeII_Oxy_3; 1. DR SMART; SM00702; P4Hc; 1. DR PROSITE; PS00014; ER_TARGET; 1. DR PROSITE; PS51471; FE2OG_OXY; 1. PE 2: Evidence at transcript level; KW Coiled coil; Complete proteome; Dioxygenase; Endoplasmic reticulum; KW Glycoprotein; Iron; Metal-binding; Oxidoreductase; Reference proteome; KW Repeat; Signal; TPR repeat; Vitamin C. FT SIGNAL 1 19 Potential. FT CHAIN 20 732 Prolyl 3-hydroxylase 3. FT /FTId=PRO_0000240361. FT REPEAT 39 72 TPR 1. FT REPEAT 152 185 TPR 2. FT REPEAT 214 247 TPR 3. FT REPEAT 312 345 TPR 4. FT DOMAIN 557 671 Fe2OG dioxygenase. FT COILED 674 703 Potential. FT MOTIF 729 732 Prevents secretion from ER (Potential). FT COMPBIAS 14 39 Pro-rich. FT COMPBIAS 689 697 Poly-Glu. FT ACT_SITE 662 662 By similarity. FT METAL 580 580 Iron. FT METAL 582 582 Iron. FT METAL 652 652 Iron. FT CARBOHYD 327 327 N-linked (GlcNAc...) (Potential). FT CARBOHYD 458 458 N-linked (GlcNAc...) (Potential). SQ SEQUENCE 732 AA; 81701 MW; BD54733B60F1687A CRC64; MLRLLRLLLL LLLPPPGSPE PPEPPGLAQL SPGSPPQAPD LLYADGLRAY SAGAWAPAVA LLREALRSRA ALGRARQECG ASCAAEPGAA LPSQLLGAPH PVSGPGVWEP LLLRATLRRA ECLTQCAVRR LGPGGAARLR VGSALRDAFR RREPYNYLQR AYYQLKKLDL AASAAHTFFV ANPTHLQMRE DMAKYRRMSA IRPQSFRDLV TPLYWAAYDT GLELLEQREA ALALPQLEEA LQGSLAHMES CRAACEGPEE HQGAEEEGEG SQGGLYEAIA GHWIRVLQCR QHCVADTATR PGRSFPVQDF LLSQLRRLHE AYAQVGNMSQ AMENVLSVLL FYPEDEAAKK ALNQYQTQLG EPRPDLGPRE DIQRFILRSL GEKRQLYYAM EHLGTSFKDP DSWTPEALIP KALRERLRED QEKKPWDHQP PQQKPLAHWK DALLMEGVTL TQDAQQLNGS ERAVLDGLLT SAECGVLLQL AKDAAQAGAR SGYRGRRSPH SPHERFEGLT VLKAAQLARA GTVGRPGAKL LLEVSERVRT LTQAYFSPER PLHLSFTHLV CRSAIEGEQE QRMDLSHPVH ADNCVLDPDT GECWREPPAY TYRDYSGLLY LNDDFKGGDL FFTQPNALTV TAQVRPRCGR LVAFSSGGEN PHGVWAVTRG RRCALALWHT WAPEHSEQEW TEAKELLQEE EEEEEEEDIL SRDPSPEPPS HKLQRVQEKA GKPRRVRVRE EL // ID P3H1_MOUSE Reviewed; 739 AA. AC Q3V1T4; A2A7Q4; A6PW85; Q3TWX8; Q8BSV2; Q8CFL3; Q9CWK5; Q9QZT6; AC Q9QZT7; DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot. DT 27-JUN-2006, sequence version 2. DT 19-MAR-2014, entry version 81. DE RecName: Full=Prolyl 3-hydroxylase 1; DE EC=1.14.11.7; DE AltName: Full=Growth suppressor 1; DE AltName: Full=Leucine- and proline-enriched proteoglycan 1; DE Short=Leprecan-1; DE Flags: Precursor; GN Name=Lepre1; Synonyms=Gros1, P3h1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2). RC STRAIN=CD-1/ICR; TISSUE=Fibroblast, and Testis; RX PubMed=10951563; DOI=10.1038/sj.onc.1203696; RA Kaul S.C., Sugihara T., Yoshida A., Nomura H., Wadhwa R.; RT "Gros1, a potential growth suppressor on chromosome 1: its identity to RT basement membrane-associated proteoglycan, leprecan."; RL Oncogene 19:3576-3583(2000). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3). RC STRAIN=C57BL/6J; TISSUE=Embryonic stem cell, Pituitary, and Placenta; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC STRAIN=FVB/N; TISSUE=Mammary tumor; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: Basement membrane-associated chondroitin sulfate CC proteoglycan (CSPG). Has prolyl 3-hydroxylase activity catalyzing CC the post-translational formation of 3-hydroxyproline in -Xaa-Pro- CC Gly- sequences in collagens, especially types IV and V. May be CC involved in the secretory pathway of cells. Has growth suppressive CC activity in fibroblasts (By similarity). CC -!- CATALYTIC ACTIVITY: L-proline-[procollagen] + 2-oxoglutarate + CC O(2) = trans-3-hydroxy-L-proline-[procollagen] + succinate + CC CO(2). CC -!- COFACTOR: Iron (By similarity). CC -!- COFACTOR: Ascorbate (By similarity). CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum (By similarity). CC Secreted, extracellular space, extracellular matrix (By CC similarity). Note=Secreted into the extracellular matrix as a CC chondroitin sulfate proteoglycan (CSPG). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; Synonyms=GROS1-L; CC IsoId=Q3V1T4-1; Sequence=Displayed; CC Name=2; Synonyms=GROS1-S; CC IsoId=Q3V1T4-2; Sequence=VSP_019350, VSP_019351; CC Name=3; CC IsoId=Q3V1T4-3; Sequence=VSP_019349; CC Note=No experimental confirmation available; CC -!- PTM: O-glycosylated; chondroitin sulfate (By similarity). CC -!- SIMILARITY: Belongs to the leprecan family. CC -!- SIMILARITY: Contains 1 Fe2OG dioxygenase domain. CC -!- SIMILARITY: Contains 4 TPR repeats. CC -!- SEQUENCE CAUTION: CC Sequence=BAB27041.1; Type=Frameshift; Positions=707; CC Sequence=BAE21065.1; Type=Miscellaneous discrepancy; Note=Intron retention; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF165163; AAF04806.1; ALT_SEQ; mRNA. DR EMBL; AF165164; AAF04807.1; ALT_SEQ; mRNA. DR EMBL; AK010578; BAB27041.1; ALT_FRAME; mRNA. DR EMBL; AK030436; BAC26962.1; -; mRNA. DR EMBL; AK132262; BAE21065.1; ALT_SEQ; mRNA. DR EMBL; AK159505; BAE35138.1; -; mRNA. DR EMBL; AL606975; CAM21645.1; -; Genomic_DNA. DR EMBL; AL606975; CAO78098.1; -; Genomic_DNA. DR EMBL; BC024047; AAH24047.1; -; mRNA. DR RefSeq; NP_001035874.1; NM_001042411.1. DR RefSeq; NP_001273077.1; NM_001286148.1. DR RefSeq; NP_062756.2; NM_019782.3. DR RefSeq; NP_062757.2; NM_019783.2. DR UniGene; Mm.27961; -. DR ProteinModelPortal; Q3V1T4; -. DR SMR; Q3V1T4; 37-69, 148-236, 305-372. DR IntAct; Q3V1T4; 1. DR MINT; MINT-4125499; -. DR PhosphoSite; Q3V1T4; -. DR PaxDb; Q3V1T4; -. DR PRIDE; Q3V1T4; -. DR Ensembl; ENSMUST00000081606; ENSMUSP00000080312; ENSMUSG00000028641. [Q3V1T4-3] DR Ensembl; ENSMUST00000121111; ENSMUSP00000112504; ENSMUSG00000028641. [Q3V1T4-1] DR GeneID; 56401; -. DR KEGG; mmu:56401; -. DR UCSC; uc008ulq.1; mouse. [Q3V1T4-1] DR CTD; 64175; -. DR MGI; MGI:1888921; Lepre1. DR eggNOG; NOG269251; -. DR GeneTree; ENSGT00550000074573; -. DR HOVERGEN; HBG053224; -. DR KO; K08134; -. DR OrthoDB; EOG7BZVSS; -. DR NextBio; 312512; -. DR PRO; PR:Q3V1T4; -. DR ArrayExpress; Q3V1T4; -. DR Bgee; Q3V1T4; -. DR CleanEx; MM_LEPRE1; -. DR Genevestigator; Q3V1T4; -. DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI. DR GO; GO:0005634; C:nucleus; IDA:MGI. DR GO; GO:0005886; C:plasma membrane; TAS:MGI. DR GO; GO:0005578; C:proteinaceous extracellular matrix; IEA:UniProtKB-SubCell. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0031418; F:L-ascorbic acid binding; IEA:UniProtKB-KW. DR GO; GO:0019797; F:procollagen-proline 3-dioxygenase activity; ISO:MGI. DR GO; GO:0016049; P:cell growth; IDA:MGI. DR GO; GO:0030199; P:collagen fibril organization; IMP:MGI. DR GO; GO:0032963; P:collagen metabolic process; ISO:MGI. DR GO; GO:0030278; P:regulation of ossification; IMP:MGI. DR Gene3D; 1.25.40.10; -; 3. DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase. DR InterPro; IPR006620; Pro_4_hyd_alph. DR InterPro; IPR011990; TPR-like_helical. DR Pfam; PF13640; 2OG-FeII_Oxy_3; 1. DR SMART; SM00702; P4Hc; 1. DR PROSITE; PS00014; ER_TARGET; 1. DR PROSITE; PS51471; FE2OG_OXY; 1. PE 2: Evidence at transcript level; KW Alternative splicing; Coiled coil; Complete proteome; Dioxygenase; KW Endoplasmic reticulum; Extracellular matrix; Glycoprotein; Iron; KW Metal-binding; Oxidoreductase; Reference proteome; Repeat; Secreted; KW Signal; TPR repeat; Vitamin C. FT SIGNAL 1 25 Potential. FT CHAIN 26 739 Prolyl 3-hydroxylase 1. FT /FTId=PRO_0000240353. FT REPEAT 36 69 TPR 1. FT REPEAT 146 179 TPR 2. FT REPEAT 208 241 TPR 3. FT REPEAT 304 337 TPR 4. FT DOMAIN 567 681 Fe2OG dioxygenase. FT COILED 404 442 Potential. FT MOTIF 736 739 Prevents secretion from ER (Potential). FT ACT_SITE 672 672 By similarity. FT METAL 590 590 Iron. FT METAL 592 592 Iron. FT METAL 662 662 Iron. FT CARBOHYD 319 319 N-linked (GlcNAc...) (Potential). FT CARBOHYD 470 470 N-linked (GlcNAc...) (Potential). FT CARBOHYD 543 543 N-linked (GlcNAc...) (Potential). FT VAR_SEQ 1 179 Missing (in isoform 3). FT /FTId=VSP_019349. FT VAR_SEQ 540 543 MYYN -> TALQ (in isoform 2). FT /FTId=VSP_019350. FT VAR_SEQ 544 739 Missing (in isoform 2). FT /FTId=VSP_019351. FT CONFLICT 4 25 SERRLLAAMLAVAAAAALRVAA -> TKGGCWHDASGRRRR FT RLTGCG (in Ref. 1; AAF04806/AAF04807). FT CONFLICT 50 50 G -> R (in Ref. 1; AAF04806/AAF04807). FT CONFLICT 371 372 RS -> PN (in Ref. 1; AAF04806/AAF04807). FT CONFLICT 403 403 P -> T (in Ref. 2; BAE21065). FT CONFLICT 420 420 Missing (in Ref. 2; BAC26962). FT CONFLICT 484 484 D -> N (in Ref. 2; BAE35138). FT CONFLICT 569 569 L -> F (in Ref. 1; AAF04806). FT CONFLICT 589 589 V -> D (in Ref. 2; BAE21065). FT CONFLICT 601 601 L -> F (in Ref. 1; AAF04806). FT CONFLICT 614 614 D -> E (in Ref. 1; AAF04806). FT CONFLICT 685 685 H -> Q (in Ref. 2; BAC26962). FT CONFLICT 716 716 D -> G (in Ref. 2; BAE35138 and 3; FT AAH24047). FT CONFLICT 727 739 SLSDRGSLHKDEL -> FLHGATVLGVGIA (in Ref. FT 1; AAF04806). SQ SEQUENCE 739 AA; 83651 MW; 3484AE68E80B68E8 CRC64; MAVSERRLLA AMLAVAAAAA LRVAAESEPG WDVAAPDLLY AEGTAAYSRG DWPGVVLNME RALRSRAALR ALRLRCRTRC ATELPWAPDL DLGPDPSLSQ DPGAAALHDL RFFGAVLRRA ACLRRCLGPP SAHLLSEELD LEFNKRSPYN YLQVAYFKIN KLEKAVAAAH TFFVGNPEHM EMRQNLDYYQ TMSGVKEADF RDLEAKPHMH EFRLGVRLYS EEKPQEAVPH LEAALQEYFV ADEECRALCE GPYDYDGYNY LDYSADLFQA ITDHYVQVLN CKQNCVTELA SHPSREKPFE DFLPSHYNYL QFAYYNIGNY TQAIECAKTY LLFFPNDEVM HQNLAYYTAM LGEEEASSIS PRENAEEYRR RSLLEKELLF FAYDIFGIPF VDPDSWTPEE VIPKRLQEKQ KSERETAVRI SQEIGNLMKE IETLVEEKTK ESLDVSRLTR EGGPLLYEGI SLTMNSKVLN GSQRVVMDGV ISDDECQELQ RLTNAAATSG DGYRGQTSPH TPNEKFYGVT VLKALKLGQE GKVPLQSARM YYNVTEKVRR VMESYFRLDT PLYFSYSHLV CRTAIEESQA ERKDSSHPVH VDNCILNAEA LMCIKEPPAY TFRDYSAILY LNGDFDGGNF YFTELDAKTV TAEVQPQCGR AVGFSSGTEN PHGVKAVTRG QRCAIALWFT LDPRHSERDR VQADDLVKML FSPEEVDLPQ EQPLPDQQGS PEPGEESLSD RGSLHKDEL // ID P3H2_MOUSE Reviewed; 703 AA. AC Q8CG71; Q8C673; DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 19-MAR-2014, entry version 91. DE RecName: Full=Prolyl 3-hydroxylase 2; DE EC=1.14.11.7; DE AltName: Full=Leprecan-like protein 1; DE Flags: Precursor; GN Name=Leprel1; Synonyms=P3h2; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=C57BL/6; RX PubMed=15063763; DOI=10.1016/j.bbrc.2004.03.060; RA Jaernum S., Kjellman C., Darabi A., Nilsson I., Edvardsen K., RA Aaman P.; RT "LEPREL1, a novel ER and Golgi resident member of the Leprecan RT family."; RL Biochem. Biophys. Res. Commun. 317:342-351(2004). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 295-703. RC STRAIN=C57BL/6J; TISSUE=Head; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). CC -!- FUNCTION: Shows prolyl 3-hydroxylase activity catalyzing the post- CC translational formation of 3-hydroxyproline in -Xaa-Pro-Gly- CC sequences in collagens, especially types II, IV and V (By CC similarity). CC -!- CATALYTIC ACTIVITY: L-proline-[procollagen] + 2-oxoglutarate + CC O(2) = trans-3-hydroxy-L-proline-[procollagen] + succinate + CC CO(2). CC -!- COFACTOR: Iron (By similarity). CC -!- COFACTOR: Ascorbate (By similarity). CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum. Golgi apparatus (By CC similarity). CC -!- SIMILARITY: Belongs to the leprecan family. CC -!- SIMILARITY: Contains 1 Fe2OG dioxygenase domain. CC -!- SIMILARITY: Contains 4 TPR repeats. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJ430350; CAD23038.1; -; mRNA. DR EMBL; AK076434; BAC36342.1; -; mRNA. DR RefSeq; NP_775555.1; NM_173379.2. DR UniGene; Mm.326869; -. DR ProteinModelPortal; Q8CG71; -. DR SMR; Q8CG71; 41-72, 147-181, 207-235, 305-347. DR PhosphoSite; Q8CG71; -. DR PaxDb; Q8CG71; -. DR PRIDE; Q8CG71; -. DR DNASU; 210530; -. DR Ensembl; ENSMUST00000039990; ENSMUSP00000038056; ENSMUSG00000038168. DR GeneID; 210530; -. DR KEGG; mmu:210530; -. DR UCSC; uc007yuy.1; mouse. DR CTD; 55214; -. DR MGI; MGI:2146663; Leprel1. DR eggNOG; NOG269251; -. DR GeneTree; ENSGT00550000074573; -. DR HOGENOM; HOG000231087; -. DR HOVERGEN; HBG053224; -. DR InParanoid; Q8CG71; -. DR OMA; QGKHELN; -. DR OrthoDB; EOG7BZVSS; -. DR TreeFam; TF320837; -. DR NextBio; 372972; -. DR PRO; PR:Q8CG71; -. DR Bgee; Q8CG71; -. DR CleanEx; MM_LEPREL1; -. DR Genevestigator; Q8CG71; -. DR GO; GO:0005604; C:basement membrane; IDA:UniProtKB. DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB. DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0031418; F:L-ascorbic acid binding; IEA:UniProtKB-KW. DR GO; GO:0019797; F:procollagen-proline 3-dioxygenase activity; ISS:UniProtKB. DR GO; GO:0032963; P:collagen metabolic process; ISS:UniProtKB. DR GO; GO:0008285; P:negative regulation of cell proliferation; ISS:UniProtKB. DR GO; GO:0019511; P:peptidyl-proline hydroxylation; ISS:UniProtKB. DR Gene3D; 1.25.40.10; -; 4. DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase. DR InterPro; IPR006620; Pro_4_hyd_alph. DR InterPro; IPR011990; TPR-like_helical. DR InterPro; IPR013105; TPR_2. DR Pfam; PF13640; 2OG-FeII_Oxy_3; 1. DR Pfam; PF07719; TPR_2; 2. DR SMART; SM00702; P4Hc; 1. DR PROSITE; PS00014; ER_TARGET; 1. DR PROSITE; PS51471; FE2OG_OXY; 1. PE 2: Evidence at transcript level; KW Complete proteome; Dioxygenase; Endoplasmic reticulum; Glycoprotein; KW Golgi apparatus; Iron; Metal-binding; Oxidoreductase; KW Reference proteome; Repeat; Signal; TPR repeat; Vitamin C. FT SIGNAL 1 21 Potential. FT CHAIN 22 703 Prolyl 3-hydroxylase 2. FT /FTId=PRO_0000240357. FT REPEAT 42 75 TPR 1. FT REPEAT 144 177 TPR 2. FT REPEAT 205 238 TPR 3. FT REPEAT 301 334 TPR 4. FT DOMAIN 552 666 Fe2OG dioxygenase. FT MOTIF 700 703 Prevents secretion from ER (Potential). FT ACT_SITE 657 657 By similarity. FT METAL 575 575 Iron. FT METAL 577 577 Iron. FT METAL 647 647 Iron. FT CARBOHYD 444 444 N-linked (GlcNAc...) (Potential). FT CARBOHYD 544 544 N-linked (GlcNAc...) (Potential). FT CONFLICT 497 497 P -> A (in Ref. 2; BAC36342). SQ SEQUENCE 703 AA; 80154 MW; 1F42F9B9938573E4 CRC64; MRESTWVSLL LLLLLPTPQR GGPQDGRRSP EPEPERGPLQ PFDLLYASGV AAYYSGDYER AVRDLEAALS SHRRLRDIRT RCARHCAARR PLAPPGAGPG AELPFFRAVL ERARCSRSCQ SQRLGGPASR HRVSEDVRSD FQRRVPYNYL QRAYIKLNQL EKAMEAAHTF FMANPEHMEM QQDLEDYKAT ARVEAPLLDR EAKPHLESYN AGVKHYEADD FESAIKYFEQ ALREYFNEDM ECRALCEGPQ RFEEYEYLGY KGGLYEAIAD HYMQVLVCQH ECVRELATRP GRLSPIENFL PLHYDYLQFA YYRVGEYVKA LECAKAYLMF HPDNEDVLDN VDFYESLLDD STDPASIEAR EDLTAFVKRH KLEAELIKLA AEGLGFSYAE PNYWISYGGR QDENRVPSGV NMDGAEVHGL SMGKKSPPKI GRDLREGGPL LYENITFVYN SEQLNGTQRV LLDNVLSQEQ CRELHSVANG IMLVGDGYRG KTSPHTPNEK FEGATVLKAL KFGYEGRVPL KSARLFYDIS EKARKIVESY FMLNSTLYFS YTHMVCRTAL SGQQDRRNDL SHPIHADNCL LDPEANECWK EPPAYTFRDY SALLYMNDDF DGGEFIFTEM DAKTVTASIK PKCGRMISFS SGGENPHGVK AVTRGQRCAV ALWFTLDPLY RELERIQADE VIAILDQEQR GKHGLNINPK DEL // ID P4HA2_MOUSE Reviewed; 537 AA. AC Q60716; Q8VBU4; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 19-MAR-2014, entry version 123. DE RecName: Full=Prolyl 4-hydroxylase subunit alpha-2; DE Short=4-PH alpha-2; DE EC=1.14.11.2; DE AltName: Full=Procollagen-proline,2-oxoglutarate-4-dioxygenase subunit alpha-2; DE Flags: Precursor; GN Name=P4ha2; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM IIB). RX PubMed=7753822; DOI=10.1073/pnas.92.10.4427; RA Helaakoski T., Annunen P., Vuori K., Macneil I.A., Pihlajaniemi T., RA Kivirikko K.I.; RT "Cloning, baculovirus expression, and characterization of a second RT mouse prolyl 4-hydroxylase alpha-subunit isoform: formation of an RT alpha 2 beta 2 tetramer with the protein disulfide-isomerase/beta RT subunit."; RL Proc. Natl. Acad. Sci. U.S.A. 92:4427-4431(1995). RN [2] RP NUCLEOTIDE SEQUENCE (ISOFORMS IIA AND IIB). RX PubMed=11606192; DOI=10.1046/j.0014-2956.2001.02464.x; RA Nokelainen M., Nissi R., Kukkola L., Helaakoski T., Myllyharju J.; RT "Characterization of the human and mouse genes for the alpha subunit RT of type II prolyl 4-hydroxylase. Identification of a previously RT unknown alternatively spliced exon and its expression in various RT tissues."; RL Eur. J. Biochem. 268:5300-5309(2001). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM IIA). RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-482, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic fibroblast; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., RA Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). CC -!- FUNCTION: Catalyzes the post-translational formation of 4- CC hydroxyproline in -Xaa-Pro-Gly- sequences in collagens and other CC proteins. CC -!- CATALYTIC ACTIVITY: L-proline-[procollagen] + 2-oxoglutarate + CC O(2) = trans-4-hydroxy-L-proline-[procollagen] + succinate + CC CO(2). CC -!- COFACTOR: Binds 1 Fe(2+) ion per subunit. CC -!- COFACTOR: Ascorbate. CC -!- ENZYME REGULATION: In contrast to the subunit alpha-1, alpha-2 is CC inhibited by poly(L-proline) only at very high concentrations. CC -!- SUBUNIT: Heterotetramer of two alpha-2 chains and two beta chains CC (the beta chain is the multi-functional PDI). CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=IIb; CC IsoId=Q60716-1; Sequence=Displayed; CC Name=IIa; CC IsoId=Q60716-2; Sequence=VSP_004507; CC -!- TISSUE SPECIFICITY: Expressed in a variety of tissues. CC -!- SIMILARITY: Belongs to the P4HA family. CC -!- SIMILARITY: Contains 1 Fe2OG dioxygenase domain. CC -!- SIMILARITY: Contains 1 TPR repeat. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U16163; AAC52198.1; -; mRNA. DR EMBL; AJ314858; CAC85690.1; -; Genomic_DNA. DR EMBL; AJ314858; CAC85691.1; -; Genomic_DNA. DR EMBL; BC018411; AAH18411.1; -; mRNA. DR PIR; I49135; I49135. DR RefSeq; NP_001129548.1; NM_001136076.2. DR RefSeq; NP_035161.2; NM_011031.2. DR UniGene; Mm.3705; -. DR ProteinModelPortal; Q60716; -. DR SMR; Q60716; 25-259, 337-521. DR BioGrid; 202007; 1. DR IntAct; Q60716; 2. DR MINT; MINT-4106103; -. DR PhosphoSite; Q60716; -. DR PaxDb; Q60716; -. DR PRIDE; Q60716; -. DR Ensembl; ENSMUST00000093107; ENSMUSP00000091749; ENSMUSG00000018906. [Q60716-2] DR Ensembl; ENSMUST00000174616; ENSMUSP00000133275; ENSMUSG00000018906. [Q60716-2] DR GeneID; 18452; -. DR KEGG; mmu:18452; -. DR CTD; 8974; -. DR MGI; MGI:894286; P4ha2. DR eggNOG; NOG78926; -. DR GeneTree; ENSGT00390000018885; -. DR HOGENOM; HOG000230465; -. DR HOVERGEN; HBG006834; -. DR InParanoid; Q60716; -. DR KO; K00472; -. DR NextBio; 294140; -. DR PRO; PR:Q60716; -. DR ArrayExpress; Q60716; -. DR Bgee; Q60716; -. DR Genevestigator; Q60716; -. DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell. DR GO; GO:0016222; C:procollagen-proline 4-dioxygenase complex; IDA:MGI. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0031418; F:L-ascorbic acid binding; IEA:UniProtKB-KW. DR GO; GO:0016702; F:oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen; IEA:InterPro. DR GO; GO:0004656; F:procollagen-proline 4-dioxygenase activity; IEA:UniProtKB-EC. DR GO; GO:0018401; P:peptidyl-proline hydroxylation to 4-hydroxy-L-proline; IDA:MGI. DR Gene3D; 1.25.40.10; -; 2. DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase. DR InterPro; IPR006620; Pro_4_hyd_alph. DR InterPro; IPR013547; Pro_4_hyd_alph_N. DR InterPro; IPR013026; TPR-contain_dom. DR InterPro; IPR011990; TPR-like_helical. DR InterPro; IPR019734; TPR_repeat. DR Pfam; PF03171; 2OG-FeII_Oxy; 1. DR Pfam; PF08336; P4Ha_N; 1. DR SMART; SM00702; P4Hc; 1. DR PROSITE; PS51471; FE2OG_OXY; 1. DR PROSITE; PS50005; TPR; 1. DR PROSITE; PS50293; TPR_REGION; 1. PE 1: Evidence at protein level; KW Alternative splicing; Complete proteome; Dioxygenase; KW Endoplasmic reticulum; Glycoprotein; Iron; Metal-binding; KW Oxidoreductase; Reference proteome; Signal; TPR repeat; Vitamin C. FT SIGNAL 1 23 Potential. FT CHAIN 24 537 Prolyl 4-hydroxylase subunit alpha-2. FT /FTId=PRO_0000022727. FT REPEAT 209 242 TPR. FT DOMAIN 414 522 Fe2OG dioxygenase. FT METAL 432 432 Iron (By similarity). FT METAL 434 434 Iron (By similarity). FT METAL 503 503 Iron (By similarity). FT BINDING 513 513 2-oxoglutarate (Potential). FT MOD_RES 482 482 N6-succinyllysine. FT CARBOHYD 117 117 N-linked (GlcNAc...) (Potential). FT CARBOHYD 266 266 N-linked (GlcNAc...) (Potential). FT VAR_SEQ 438 453 SDDEDAFKRLGTGNRV -> RPFDSGLKTEGNRL (in FT isoform IIa). FT /FTId=VSP_004507. SQ SEQUENCE 537 AA; 61002 MW; C47D976C75E82518 CRC64; MKLQVLVLVL LMSWFGVLSW VQAEFFTSIG HMTDLIYAEK DLVQSLKEYI LVEEAKLAKI KSWASKMEAL TSRSAADPEG YLAHPVNAYK LVKRLNTDWP ALGDLVLQDA SAGFVANLSV QRQFFPTDED ESGAARALMR LQDTYKLDPD TISRGELPGT KYQAMLSVDD CFGLGRSAYN EGDYYHTVLW MEQVLKQLDA GEEATVTKSL VLDYLSYAVF QLGDLHRAVE LTRRLLSLDP SHERAGGNLR YFERLLEEER GKSLSNQTDA GLATQENLYE RPTDYLPERD VYESLCRGEG VKLTPRRQKK LFCRYHHGNR VPQLLIAPFK EEDEWDSPHI VRYYDVMSDE EIERIKEIAK PKLARATVRD PKTGVLTVAS YRVSKSSWLE EDDDPVVARV NRRMQHITGL TVKTAELLQV ANYGMGGQYE PHFDFSRSDD EDAFKRLGTG NRVATFLNYM SDVEAGGATV FPDLGAAIWP KKGTAVFWYN LLRSGEGDYR TRHAACPVLV GCKWVSNKWF HERGQEFLRP CGTTEVD // ID P4HA1_MOUSE Reviewed; 534 AA. AC Q60715; Q3TEB7; Q80T05; Q91VJ7; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 02-MAY-2002, sequence version 2. DT 19-MAR-2014, entry version 122. DE RecName: Full=Prolyl 4-hydroxylase subunit alpha-1; DE Short=4-PH alpha-1; DE EC=1.14.11.2; DE AltName: Full=Procollagen-proline,2-oxoglutarate-4-dioxygenase subunit alpha-1; DE Flags: Precursor; GN Name=P4ha1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC STRAIN=C57BL/6J, and NOD; TISSUE=Embryo, Head, and Thymus; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Mammary tumor; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] OF 9-534 (ISOFORM 2). RX PubMed=7753822; DOI=10.1073/pnas.92.10.4427; RA Helaakoski T., Annunen P., Vuori K., Macneil I.A., Pihlajaniemi T., RA Kivirikko K.I.; RT "Cloning, baculovirus expression, and characterization of a second RT mouse prolyl 4-hydroxylase alpha-subunit isoform: formation of an RT alpha 2 beta 2 tetramer with the protein disulfide-isomerase/beta RT subunit."; RL Proc. Natl. Acad. Sci. U.S.A. 92:4427-4431(1995). CC -!- FUNCTION: Catalyzes the post-translational formation of 4- CC hydroxyproline in -Xaa-Pro-Gly- sequences in collagens and other CC proteins. CC -!- CATALYTIC ACTIVITY: L-proline-[procollagen] + 2-oxoglutarate + CC O(2) = trans-4-hydroxy-L-proline-[procollagen] + succinate + CC CO(2). CC -!- COFACTOR: Binds 1 Fe(2+) ion per subunit. CC -!- COFACTOR: Ascorbate. CC -!- SUBUNIT: Heterotetramer of two alpha-1 chains and two beta chains CC (the beta chain is the multi-functional PDI). CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q60715-1; Sequence=Displayed; CC Name=2; CC IsoId=Q60715-2; Sequence=VSP_004505; CC -!- SIMILARITY: Belongs to the P4HA family. CC -!- SIMILARITY: Contains 1 Fe2OG dioxygenase domain. CC -!- SIMILARITY: Contains 1 TPR repeat. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK045008; BAC32183.1; -; mRNA. DR EMBL; AK160798; BAE36020.1; -; mRNA. DR EMBL; AK169726; BAE41331.1; -; mRNA. DR EMBL; BC009654; AAH09654.1; -; mRNA. DR EMBL; U16162; AAC52197.1; -; mRNA. DR PIR; I49134; I49134. DR RefSeq; NP_035160.1; NM_011030.2. DR RefSeq; XP_006513403.1; XM_006513340.1. DR UniGene; Mm.2212; -. DR ProteinModelPortal; Q60715; -. DR SMR; Q60715; 18-254, 335-518. DR BioGrid; 202006; 1. DR IntAct; Q60715; 4. DR MINT; MINT-4106073; -. DR PhosphoSite; Q60715; -. DR PaxDb; Q60715; -. DR PRIDE; Q60715; -. DR Ensembl; ENSMUST00000009789; ENSMUSP00000009789; ENSMUSG00000019916. [Q60715-1] DR Ensembl; ENSMUST00000105466; ENSMUSP00000101106; ENSMUSG00000019916. [Q60715-2] DR GeneID; 18451; -. DR KEGG; mmu:18451; -. DR UCSC; uc007fdo.2; mouse. [Q60715-1] DR UCSC; uc007fdp.2; mouse. [Q60715-2] DR CTD; 5033; -. DR MGI; MGI:97463; P4ha1. DR eggNOG; NOG78926; -. DR GeneTree; ENSGT00390000018885; -. DR HOGENOM; HOG000230465; -. DR HOVERGEN; HBG006834; -. DR KO; K00472; -. DR OMA; AKEKDDN; -. DR OrthoDB; EOG7W6WKC; -. DR TreeFam; TF313393; -. DR ChiTaRS; P4HA1; mouse. DR NextBio; 294136; -. DR PRO; PR:Q60715; -. DR ArrayExpress; Q60715; -. DR Bgee; Q60715; -. DR Genevestigator; Q60715; -. DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell. DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl. DR GO; GO:0016222; C:procollagen-proline 4-dioxygenase complex; IDA:MGI. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0031418; F:L-ascorbic acid binding; IEA:UniProtKB-KW. DR GO; GO:0016702; F:oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen; IEA:InterPro. DR GO; GO:0004656; F:procollagen-proline 4-dioxygenase activity; IMP:MGI. DR GO; GO:0030199; P:collagen fibril organization; IMP:MGI. DR GO; GO:0018401; P:peptidyl-proline hydroxylation to 4-hydroxy-L-proline; IDA:MGI. DR Gene3D; 1.25.40.10; -; 2. DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase. DR InterPro; IPR006620; Pro_4_hyd_alph. DR InterPro; IPR013547; Pro_4_hyd_alph_N. DR InterPro; IPR013026; TPR-contain_dom. DR InterPro; IPR011990; TPR-like_helical. DR InterPro; IPR019734; TPR_repeat. DR Pfam; PF03171; 2OG-FeII_Oxy; 1. DR Pfam; PF08336; P4Ha_N; 1. DR SMART; SM00702; P4Hc; 1. DR PROSITE; PS51471; FE2OG_OXY; 1. DR PROSITE; PS50005; TPR; 1. DR PROSITE; PS50293; TPR_REGION; 1. PE 2: Evidence at transcript level; KW Alternative splicing; Complete proteome; Dioxygenase; KW Endoplasmic reticulum; Glycoprotein; Iron; Metal-binding; KW Oxidoreductase; Reference proteome; Signal; TPR repeat; Vitamin C. FT SIGNAL 1 17 By similarity. FT CHAIN 18 534 Prolyl 4-hydroxylase subunit alpha-1. FT /FTId=PRO_0000022724. FT REPEAT 205 238 TPR. FT DOMAIN 411 519 Fe2OG dioxygenase. FT METAL 429 429 Iron (By similarity). FT METAL 431 431 Iron (By similarity). FT METAL 500 500 Iron (By similarity). FT BINDING 510 510 2-oxoglutarate (Potential). FT CARBOHYD 113 113 N-linked (GlcNAc...) (Potential). FT CARBOHYD 259 259 N-linked (GlcNAc...) (Potential). FT VAR_SEQ 361 380 RRATISNPVTGALETVHYRI -> SRATVHDPETGKLTTAQ FT YRV (in isoform 2). FT /FTId=VSP_004505. FT CONFLICT 69 69 T -> R (in Ref. 3; AAC52197). FT CONFLICT 147 147 T -> N (in Ref. 3; AAC52197). FT CONFLICT 354 354 D -> Y (in Ref. 3; AAC52197). SQ SEQUENCE 534 AA; 60910 MW; 81F6C61019E79460 CRC64; MIWVVLMMAI LLPQSLAHPG FFTSIGQMTD LIHNEKDLVT SLKDYIKAEE DKLEQIKKWA EKLDRLTSTA TKDPEGFVGH PVNAFKLMKR LNTEWSELEN LILKDMSDGF ISNLTIQRQY FPNDEDQVGA AKALFRLQDT YNLDTNTISK GNLPGVQHKS FLTAEDCFEL GKVAYTEADY YHTELWMEQA LTQLEEGELS TVDKVSVLDY LSYAVYQQGD LDKALLLTKK LLELDPEHQR ANGNLVYFEY IMSKEKDANK SASGDQSDQK TAPKKKGIAV DYLPERQKYE MLCRGEGIKM TPRRQKRLFC RYHDGNRNPK FILAPAKQED EWDKPRIIRF HDIISDAEIE IVKDLAKPRL RRATISNPVT GALETVHYRI SKSAWLSGYE DPVVSRINMR IQDLTGLDVS TAEELQVANY GVGGQYEPHF DFARKDEPDA FRELGTGNRI ATWLFYMSDV SAGGATVFPE VGASVWPKKG TAVFWYNLFA SGEGDYSTRH AACPVLVGNK WVSNKWLHER GQEFRRPCTL SELE // ID P4HA3_MOUSE Reviewed; 542 AA. AC Q6W3F0; Q640R2; Q8C3A6; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 19-MAR-2014, entry version 78. DE RecName: Full=Prolyl 4-hydroxylase subunit alpha-3; DE Short=4-PH alpha-3; DE EC=1.14.11.2; DE AltName: Full=Procollagen-proline,2-oxoglutarate-4-dioxygenase subunit alpha-3; DE Flags: Precursor; GN Name=P4ha3; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC STRAIN=Webster; RX PubMed=14500733; DOI=10.1074/jbc.M306806200; RA Kukkola L., Hieta R., Kivirikko K.I., Myllyharju J.; RT "Identification and characterization of a third human, rat, and mouse RT collagen prolyl 4-hydroxylase isoenzyme."; RL J. Biol. Chem. 278:47685-47693(2003). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). RC STRAIN=C57BL/6J; TISSUE=Head; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC STRAIN=C57BL/6; TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: Catalyzes the post-translational formation of 4- CC hydroxyproline in -Xaa-Pro-Gly- sequences in collagens and other CC proteins (By similarity). CC -!- CATALYTIC ACTIVITY: L-proline-[procollagen] + 2-oxoglutarate + CC O(2) = trans-4-hydroxy-L-proline-[procollagen] + succinate + CC CO(2). CC -!- COFACTOR: Binds 1 Fe(2+) ion per subunit (By similarity). CC -!- COFACTOR: Ascorbate (By similarity). CC -!- SUBUNIT: Heterotetramer of two alpha-3 chains and two beta chains CC (the beta chain is the multi-functional PDI) (By similarity). CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen (By similarity). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q6W3F0-1; Sequence=Displayed; CC Name=2; CC IsoId=Q6W3F0-2; Sequence=VSP_031148; CC Note=No experimental confirmation available; CC Name=3; CC IsoId=Q6W3F0-3; Sequence=VSP_031148, VSP_031149; CC Note=No experimental confirmation available; CC -!- PTM: N-glycosylation plays no role in the catalytic activity (By CC similarity). CC -!- SIMILARITY: Belongs to the P4HA family. CC -!- SIMILARITY: Contains 1 Fe2OG dioxygenase domain. CC -!- SIMILARITY: Contains 1 TPR repeat. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AY313449; AAQ87604.1; -; mRNA. DR EMBL; AK086468; BAC39675.1; -; mRNA. DR EMBL; BC082538; AAH82538.1; -; mRNA. DR UniGene; Mm.150294; -. DR ProteinModelPortal; Q6W3F0; -. DR SMR; Q6W3F0; 42-274, 336-526. DR PhosphoSite; Q6W3F0; -. DR PRIDE; Q6W3F0; -. DR UCSC; uc009imt.2; mouse. [Q6W3F0-1] DR UCSC; uc012fqc.1; mouse. [Q6W3F0-3] DR MGI; MGI:2444049; P4ha3. DR eggNOG; NOG289769; -. DR HOGENOM; HOG000230465; -. DR HOVERGEN; HBG006834; -. DR InParanoid; Q6W3F0; -. DR BRENDA; 1.14.11.2; 3474. DR ChiTaRS; P4HA3; mouse. DR PRO; PR:Q6W3F0; -. DR Genevestigator; Q6W3F0; -. DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0031418; F:L-ascorbic acid binding; IEA:UniProtKB-KW. DR GO; GO:0016702; F:oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen; IEA:InterPro. DR GO; GO:0004656; F:procollagen-proline 4-dioxygenase activity; IEA:UniProtKB-EC. DR Gene3D; 1.25.40.10; -; 1. DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase. DR InterPro; IPR006620; Pro_4_hyd_alph. DR InterPro; IPR013547; Pro_4_hyd_alph_N. DR InterPro; IPR011990; TPR-like_helical. DR Pfam; PF03171; 2OG-FeII_Oxy; 1. DR Pfam; PF08336; P4Ha_N; 1. DR SMART; SM00702; P4Hc; 1. DR PROSITE; PS51471; FE2OG_OXY; 1. PE 2: Evidence at transcript level; KW Alternative splicing; Coiled coil; Complete proteome; Dioxygenase; KW Endoplasmic reticulum; Glycoprotein; Iron; Metal-binding; KW Oxidoreductase; Reference proteome; Signal; TPR repeat; Vitamin C. FT SIGNAL 1 24 Potential. FT CHAIN 25 542 Prolyl 4-hydroxylase subunit alpha-3. FT /FTId=PRO_0000317767. FT REPEAT 225 258 TPR. FT DOMAIN 420 527 Fe2OG dioxygenase. FT COILED 105 129 Potential. FT METAL 438 438 Iron (By similarity). FT METAL 440 440 Iron (By similarity). FT METAL 508 508 Iron (By similarity). FT BINDING 518 518 2-oxoglutarate (Potential). FT CARBOHYD 240 240 N-linked (GlcNAc...) (Potential). FT CARBOHYD 480 480 N-linked (GlcNAc...) (Potential). FT VAR_SEQ 1 138 Missing (in isoform 2 and isoform 3). FT /FTId=VSP_031148. FT VAR_SEQ 444 464 Missing (in isoform 3). FT /FTId=VSP_031149. SQ SEQUENCE 542 AA; 60975 MW; 76329127F1C7BA83 CRC64; MGPGARLALL ALLALGGDPA AATGREDTFS ALTSVARALA PERRLLGTLR RYLRGEEARL RDLTRFYDKV LSLHEDLKIP VVNPLLAFTV IKRLQSDWRN VVHSLEATEN IRALKDGYEK VEQDLPAFED LEGAARALMR LQDVYMLNVK GLARGVFQRV TGSSITDLYS PRQLFSLTAD DCFQVGKVAY DTGDYYHAIP WLEEAVSLFR RAHGEWKTED EASLEDALDY LAFACFQVGN VSCALSLSRE FLVYSPDNKR MARNVLKYER LLAENGHQMA AETAIQRPNV PHLQTRDTYE GLCQTLGSQP THYQIPSLYC SYETNSSPYL LLQPARKEVV HLRPLIALYH DFVSDEEAQK IRELAEPWLQ RSVVASGEKQ LQVEYRISKS AWLKDTVDPM LVTLDHRIAA LTGLDIQPPY AEYLQVVNYG IGGHYEPHFD HATSPSSPLY RMKSGNRVAT FMIYLSSVEA GGATAFIYGN FSVPVVKNAA LFWWNLHRSG EGDGDTLHAG CPVLVGDKWV ANKWIHEYGQ EFRRPCSTNP ED // ID P4HTM_MOUSE Reviewed; 503 AA. AC Q8BG58; Q8CAF1; Q9D499; DT 16-JUN-2003, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 19-MAR-2014, entry version 95. DE RecName: Full=Transmembrane prolyl 4-hydroxylase; DE Short=P4H-TM; DE EC=1.14.11.-; DE AltName: Full=Hypoxia-inducible factor prolyl hydroxylase 4; DE Short=HIF-PH4; DE Short=HIF-prolyl hydroxylase 4; DE Short=HPH-4; GN Name=P4htm; Synonyms=Ph4; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC STRAIN=C57BL/6J; RC TISSUE=Corpus striatum, Medulla oblongata, and Testis; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). CC -!- FUNCTION: Catalyzes the post-translational formation of 4- CC hydroxyproline in hypoxia-inducible factor (HIF) alpha proteins. CC Hydroxylates HIF1A at 'Pro-402' and 'Pro-564'. May function as a CC cellular oxygen sensor and, under normoxic conditions, may target CC HIF through the hydroxylation for proteasomal degradation via the CC von Hippel-Lindau ubiquitination complex (By similarity). CC -!- CATALYTIC ACTIVITY: An HIF alpha chain L-proline + 2-oxoglutarate CC + O(2) = An HIF alpha chain trans-4-hydroxy-L-proline + succinate CC + CO(2). CC -!- COFACTOR: Binds 1 Fe(2+) ion per subunit (By similarity). CC -!- COFACTOR: Ascorbate (By similarity). CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass CC type II membrane protein (By similarity). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q8BG58-1; Sequence=Displayed; CC Name=2; CC IsoId=Q8BG58-2; Sequence=VSP_007575, VSP_007576; CC Note=No experimental confirmation available; CC -!- PTM: Glycosylated (By similarity). CC -!- SIMILARITY: Contains 2 EF-hand domains. CC -!- SIMILARITY: Contains 1 Fe2OG dioxygenase domain. CC -!- SEQUENCE CAUTION: CC Sequence=BAB30379.2; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the N-terminal part; CC Sequence=BAC30172.1; Type=Frameshift; Positions=9; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK046783; BAC32866.1; -; mRNA. DR EMBL; AK047714; BAC33135.1; -; mRNA. DR EMBL; AK016685; BAB30379.2; ALT_SEQ; mRNA. DR EMBL; AK038927; BAC30172.1; ALT_SEQ; mRNA. DR RefSeq; NP_083220.3; NM_028944.3. DR UniGene; Mm.226534; -. DR ProteinModelPortal; Q8BG58; -. DR SMR; Q8BG58; 134-465. DR PhosphoSite; Q8BG58; -. DR PaxDb; Q8BG58; -. DR PRIDE; Q8BG58; -. DR Ensembl; ENSMUST00000006853; ENSMUSP00000006853; ENSMUSG00000006675. [Q8BG58-1] DR GeneID; 74443; -. DR KEGG; mmu:74443; -. DR UCSC; uc009rqk.1; mouse. [Q8BG58-1] DR UCSC; uc009rql.1; mouse. [Q8BG58-2] DR CTD; 54681; -. DR MGI; MGI:1921693; P4htm. DR eggNOG; NOG284419; -. DR GeneTree; ENSGT00390000014570; -. DR HOGENOM; HOG000115323; -. DR InParanoid; Q8BG58; -. DR KO; K06711; -. DR OMA; NMDLRDF; -. DR OrthoDB; EOG7VDXP9; -. DR TreeFam; TF332923; -. DR NextBio; 340775; -. DR PRO; PR:Q8BG58; -. DR ArrayExpress; Q8BG58; -. DR Bgee; Q8BG58; -. DR CleanEx; MM_4933406E20RIK; -. DR Genevestigator; Q8BG58; -. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0031418; F:L-ascorbic acid binding; IEA:UniProtKB-KW. DR GO; GO:0016706; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors; IEA:InterPro. DR Gene3D; 1.10.238.10; -; 1. DR InterPro; IPR011992; EF-hand-dom_pair. DR InterPro; IPR018247; EF_Hand_1_Ca_BS. DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase. DR InterPro; IPR006620; Pro_4_hyd_alph. DR Pfam; PF13640; 2OG-FeII_Oxy_3; 1. DR Pfam; PF13499; EF-hand_7; 1. DR SMART; SM00702; P4Hc; 1. DR PROSITE; PS00018; EF_HAND_1; 2. DR PROSITE; PS51471; FE2OG_OXY; 1. PE 2: Evidence at transcript level; KW Alternative splicing; Calcium; Complete proteome; Dioxygenase; KW Endoplasmic reticulum; Glycoprotein; Iron; Membrane; Metal-binding; KW Oxidoreductase; Reference proteome; Repeat; Signal-anchor; KW Transmembrane; Transmembrane helix; Vitamin C; Zinc; Zinc-finger. FT CHAIN 1 503 Transmembrane prolyl 4-hydroxylase. FT /FTId=PRO_0000206669. FT TOPO_DOM 1 61 Cytoplasmic (Potential). FT TRANSMEM 62 82 Helical; Signal-anchor for type II FT membrane protein; (Potential). FT TOPO_DOM 83 503 Lumenal (Potential). FT DOMAIN 186 221 EF-hand 1. FT DOMAIN 225 260 EF-hand 2. FT DOMAIN 310 461 Fe2OG dioxygenase. FT CA_BIND 199 211 1 (Potential). FT CA_BIND 238 250 2 (Potential). FT METAL 329 329 Iron (By similarity). FT METAL 331 331 Iron (By similarity). FT METAL 375 375 Iron (By similarity). FT BINDING 452 452 2-oxoglutarate (Potential). FT CARBOHYD 349 349 N-linked (GlcNAc...) (Potential). FT CARBOHYD 369 369 N-linked (GlcNAc...) (Potential). FT CARBOHYD 383 383 N-linked (GlcNAc...) (Potential). FT VAR_SEQ 212 225 LAQTRLGNGRWMTP -> RTPPAMWVGTGEN (in FT isoform 2). FT /FTId=VSP_007575. FT VAR_SEQ 226 503 Missing (in isoform 2). FT /FTId=VSP_007576. SQ SEQUENCE 503 AA; 57049 MW; C220CA0840F1BAFF CRC64; MAAAVATVQR PEAETVEEAS NLQWPLPPEH RPSGAATRPG DSEDAPVRPL CKPRGICSRA YFLVLMVFVH LYLGNVLALL LFVHYSNGDE STDPGPQRRE QSPQPVPTLG PLTRLEGIKV GYERKVQVVA GRDHFIRTLS LKPLLFEIPG FLSDEECRLI IHLAQMKGLQ RSQILPTEEY EEAMSAMQVS QLDLFQLLDQ NHDGRLQLRE VLAQTRLGNG RWMTPENIQE MYSAIKADPD GDGVLSLQEF SNMDLRDFHK YMRSHKAESN ELVRNSHHTW LHQGEGAHHV MRAIRQRVLR LTRLSPEIVE FSEPLQVVRY GEGGHYHAHV DSGPVYPETI CSHTKLVANE SVPFETSCRY MTVLFYLNNV TGGGETVFPV ADNRTYDEMS LIQDDVDLRD TRRHCDKGNL RVKPQQGTAV FWYNYLPDGQ GWVGEVDDYS LHGGCLVTRG TKWIANNWIN VDPSRARQAL FQQEMARLAR EGGMDSQPEW ALDRAYSDAR VEL // ID P5CR2_MOUSE Reviewed; 320 AA. AC Q922Q4; DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 22-JAN-2014, entry version 92. DE RecName: Full=Pyrroline-5-carboxylate reductase 2; DE Short=P5C reductase 2; DE Short=P5CR 2; DE EC=1.5.1.2; GN Name=Pycr2; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Mammary tumor; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: Housekeeping enzyme that catalyzes the last step in CC proline biosynthesis. In some cell types, such as erythrocytes, CC its primary function may be the generation of NADP(+). Can utilize CC both NAD and NADP. Has higher affinity for NADP, but higher CC catalytic efficiency with NADH (By similarity). CC -!- CATALYTIC ACTIVITY: L-proline + NAD(P)(+) = 1-pyrroline-5- CC carboxylate + NAD(P)H. CC -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L- CC proline from L-glutamate 5-semialdehyde: step 1/1. CC -!- SUBUNIT: Homodecamer; composed of 5 homodimers (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the pyrroline-5-carboxylate reductase CC family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BC006882; AAH06882.1; -; mRNA. DR RefSeq; NP_598466.1; NM_133705.2. DR UniGene; Mm.274180; -. DR ProteinModelPortal; Q922Q4; -. DR SMR; Q922Q4; 1-275. DR IntAct; Q922Q4; 1. DR MINT; MINT-1853710; -. DR STRING; 10090.ENSMUSP00000027802; -. DR PhosphoSite; Q922Q4; -. DR PaxDb; Q922Q4; -. DR PRIDE; Q922Q4; -. DR Ensembl; ENSMUST00000027802; ENSMUSP00000027802; ENSMUSG00000026520. DR GeneID; 69051; -. DR KEGG; mmu:69051; -. DR UCSC; uc007dwv.2; mouse. DR CTD; 29920; -. DR MGI; MGI:1277956; Pycr2. DR eggNOG; COG0345; -. DR GeneTree; ENSGT00390000007443; -. DR HOGENOM; HOG000230247; -. DR HOVERGEN; HBG053399; -. DR InParanoid; Q922Q4; -. DR KO; K00286; -. DR OMA; SAHKIMA; -. DR OrthoDB; EOG7N0C5N; -. DR UniPathway; UPA00098; UER00361. DR ChiTaRS; PYCR2; mouse. DR NextBio; 328484; -. DR PRO; PR:Q922Q4; -. DR ArrayExpress; Q922Q4; -. DR Bgee; Q922Q4; -. DR Genevestigator; Q922Q4; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004735; F:pyrroline-5-carboxylate reductase activity; IEA:UniProtKB-EC. DR GO; GO:0055129; P:L-proline biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR008927; 6-PGluconate_DH_C-like. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR000304; Pyrroline-COOH_reductase. DR PANTHER; PTHR11645; PTHR11645; 1. DR PIRSF; PIRSF000193; Pyrrol-5-carb_rd; 1. DR SUPFAM; SSF48179; SSF48179; 1. DR TIGRFAMs; TIGR00112; proC; 1. DR PROSITE; PS00521; P5CR; 1. PE 2: Evidence at transcript level; KW Acetylation; Amino-acid biosynthesis; Complete proteome; Cytoplasm; KW NADP; Oxidoreductase; Phosphoprotein; Proline biosynthesis; KW Reference proteome. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 320 Pyrroline-5-carboxylate reductase 2. FT /FTId=PRO_0000187318. FT NP_BIND 6 11 NADP (By similarity). FT NP_BIND 69 72 NADP (By similarity). FT NP_BIND 95 97 NADP (By similarity). FT BINDING 34 34 NADP; via carbonyl oxygen (By FT similarity). FT BINDING 56 56 NADP (By similarity). FT MOD_RES 2 2 N-acetylserine (By similarity). FT MOD_RES 304 304 Phosphoserine (By similarity). SQ SEQUENCE 320 AA; 33659 MW; 64DD7F96FB8C4BC5 CRC64; MSVGFIGAGQ LACALARGFT AAGVLSAHKI IASSPDMDLP TVSALRRMGV NLTRSNKDTV RHSDVLFLAV KPHIIPFILD EIGADVQERH IVVSCAAGVT ISSVEKKLMA FQPAPKVIRC MTNTPVVVRE GATVYATGTH ALVEDGKLLE QLMSSVGFCT EVEEDLIDAI TGLSGSGPAY AFMALDALAD GGVKMGVPRR LAVRLGAQAL LGAAKMLLDS EDHPGQLKDN VCSPGGATIH ALHFLESGGF RSLLINAVEA SCIRTRELQS MADQEKVSPA ALKKTLLDRV KLESPTVSTL APPSSGKLLT RNPAQGSKKE // ID P5CR3_MOUSE Reviewed; 274 AA. AC Q9DCC4; Q8R0P9; Q9D0X2; DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot. DT 18-MAR-2008, sequence version 2. DT 19-FEB-2014, entry version 89. DE RecName: Full=Pyrroline-5-carboxylate reductase 3; DE Short=P5C reductase 3; DE Short=P5CR 3; DE EC=1.5.1.2; DE AltName: Full=Pyrroline-5-carboxylate reductase-like protein; GN Name=Pycrl; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Kidney; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Colon; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- CATALYTIC ACTIVITY: L-proline + NAD(P)(+) = 1-pyrroline-5- CC carboxylate + NAD(P)H. CC -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L- CC proline from L-glutamate 5-semialdehyde: step 1/1. CC -!- SUBUNIT: Homodecamer; composed of 5 homodimers (By similarity). CC -!- SIMILARITY: Belongs to the pyrroline-5-carboxylate reductase CC family. CC -!- SEQUENCE CAUTION: CC Sequence=BAB23252.1; Type=Frameshift; Positions=231, 242; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK002912; BAB22451.1; -; mRNA. DR EMBL; AK004291; BAB23252.1; ALT_FRAME; mRNA. DR EMBL; BC026536; AAH26536.1; -; mRNA. DR RefSeq; NP_079688.2; NM_025412.2. DR UniGene; Mm.250599; -. DR ProteinModelPortal; Q9DCC4; -. DR SMR; Q9DCC4; 11-271. DR IntAct; Q9DCC4; 5. DR MINT; MINT-218248; -. DR PhosphoSite; Q9DCC4; -. DR REPRODUCTION-2DPAGE; IPI00153234; -. DR REPRODUCTION-2DPAGE; Q9DCC4; -. DR PaxDb; Q9DCC4; -. DR PRIDE; Q9DCC4; -. DR Ensembl; ENSMUST00000053918; ENSMUSP00000049605; ENSMUSG00000022571. DR GeneID; 66194; -. DR KEGG; mmu:66194; -. DR UCSC; uc007whq.1; mouse. DR CTD; 65263; -. DR MGI; MGI:1913444; Pycrl. DR eggNOG; COG0345; -. DR GeneTree; ENSGT00390000007443; -. DR HOGENOM; HOG000230247; -. DR HOVERGEN; HBG053399; -. DR InParanoid; Q9DCC4; -. DR KO; K00286; -. DR OMA; IFATKPQ; -. DR OrthoDB; EOG7N0C5N; -. DR UniPathway; UPA00098; UER00361. DR NextBio; 320915; -. DR PRO; PR:Q9DCC4; -. DR Bgee; Q9DCC4; -. DR CleanEx; MM_PYCRL; -. DR Genevestigator; Q9DCC4; -. DR GO; GO:0004735; F:pyrroline-5-carboxylate reductase activity; IEA:UniProtKB-EC. DR GO; GO:0055129; P:L-proline biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR008927; 6-PGluconate_DH_C-like. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR000304; Pyrroline-COOH_reductase. DR PANTHER; PTHR11645; PTHR11645; 1. DR PIRSF; PIRSF000193; Pyrrol-5-carb_rd; 1. DR SUPFAM; SSF48179; SSF48179; 1. DR TIGRFAMs; TIGR00112; proC; 1. PE 2: Evidence at transcript level; KW Acetylation; Amino-acid biosynthesis; Complete proteome; NADP; KW Oxidoreductase; Proline biosynthesis; Reference proteome. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 274 Pyrroline-5-carboxylate reductase 3. FT /FTId=PRO_0000324563. FT MOD_RES 2 2 N-acetylalanine (By similarity). FT CONFLICT 59 59 T -> N (in Ref. 1; BAB23252). FT CONFLICT 68 68 N -> S (in Ref. 1; BAB22451). FT CONFLICT 92 93 VT -> IN (in Ref. 1; BAB23252). FT CONFLICT 107 110 LSTM -> HGTK (in Ref. 1; BAB23252). FT CONFLICT 120 120 V -> A (in Ref. 1; BAB23252). FT CONFLICT 128 128 P -> T (in Ref. 1; BAB23252). FT CONFLICT 152 152 L -> I (in Ref. 1; BAB23252). FT CONFLICT 164 164 E -> K (in Ref. 1; BAB23252). FT CONFLICT 190 190 A -> G (in Ref. 1; BAB23252). FT CONFLICT 198 198 M -> I (in Ref. 1; BAB23252). FT CONFLICT 268 268 A -> V (in Ref. 1; BAB23252). SQ SEQUENCE 274 AA; 28721 MW; E01FB7133B45BD7C CRC64; MAATMSEPRR VGFVGAGRMA EAIARGLIQA GKVEAKQVLA SAPTDNNLCH FRALGCQTTH SNHEVLQNCP LVIFATKPQV LPTVLAEVAP IVTTEHIIVS VAAGISLSTM EGLLPPNTRV LRVSPNLPCV VQEGAMVMAR GHHAGNDDAE LLQNLLEACG QCIEVPESYV DIHTGLSGSG VAFVCTFSEA LAEGAIKMGM PSGLAHRIAA QTLLGTAKML QQEGKHPAQL RTDVLTPAGT TIHGLHALER GGFRAATMSA VEAATCRAKE LSKK // ID P5CR1_MOUSE Reviewed; 309 AA. AC Q922W5; DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 19-MAR-2014, entry version 92. DE RecName: Full=Pyrroline-5-carboxylate reductase 1, mitochondrial; DE Short=P5C reductase 1; DE Short=P5CR 1; DE EC=1.5.1.2; GN Name=Pycr1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Mammary tumor; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [2] RP TISSUE SPECIFICITY. RX PubMed=19648921; DOI=10.1038/ng.413; RA Reversade B., Escande-Beillard N., Dimopoulou A., Fischer B., RA Chng S.C., Li Y., Shboul M., Tham P.-Y., Kayserili H., Al-Gazali L., RA Shahwan M., Brancati F., Lee H., O'Connor B.D., Schmidt-von Kegler M., RA Merriman B., Nelson S.F., Masri A., Alkazaleh F., Guerra D., RA Ferrari P., Nanda A., Rajab A., Markie D., Gray M., Nelson J., RA Grix A., Sommer A., Savarirayan R., Janecke A.R., Steichen E., RA Sillence D., Hausser I., Budde B., Nuernberg G., Nuernberg P., RA Seemann P., Kunkel D., Zambruno G., Dallapiccola B., Schuelke M., RA Robertson S., Hamamy H., Wollnik B., Van Maldergem L., Mundlos S., RA Kornak U.; RT "Mutations in PYCR1 cause cutis laxa with progeroid features."; RL Nat. Genet. 41:1016-1021(2009). CC -!- FUNCTION: Housekeeping enzyme that catalyzes the last step in CC proline biosynthesis. Can utilize both NAD and NADP, but has CC higher affinity for NAD. Involved in the cellular response to CC oxidative stress (By similarity). CC -!- CATALYTIC ACTIVITY: L-proline + NAD(P)(+) = 1-pyrroline-5- CC carboxylate + NAD(P)H. CC -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L- CC proline from L-glutamate 5-semialdehyde: step 1/1. CC -!- SUBUNIT: Homodecamer; composed of 5 homodimers (By similarity). CC -!- SUBCELLULAR LOCATION: Mitochondrion. CC -!- TISSUE SPECIFICITY: Highly expressed in osteoblasts and skin. CC -!- SIMILARITY: Belongs to the pyrroline-5-carboxylate reductase CC family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BC006727; AAH06727.1; -; mRNA. DR RefSeq; NP_659044.1; NM_144795.3. DR RefSeq; XP_006532798.1; XM_006532735.1. DR UniGene; Mm.127731; -. DR ProteinModelPortal; Q922W5; -. DR SMR; Q922W5; 1-275. DR IntAct; Q922W5; 1. DR PhosphoSite; Q922W5; -. DR PaxDb; Q922W5; -. DR PRIDE; Q922W5; -. DR Ensembl; ENSMUST00000026133; ENSMUSP00000026133; ENSMUSG00000025140. DR Ensembl; ENSMUST00000170556; ENSMUSP00000131199; ENSMUSG00000025140. DR GeneID; 209027; -. DR KEGG; mmu:209027; -. DR UCSC; uc007mtv.1; mouse. DR CTD; 5831; -. DR MGI; MGI:2384795; Pycr1. DR eggNOG; COG0345; -. DR GeneTree; ENSGT00390000007443; -. DR HOGENOM; HOG000230247; -. DR HOVERGEN; HBG053399; -. DR InParanoid; Q922W5; -. DR KO; K00286; -. DR OMA; YFFLMLE; -. DR OrthoDB; EOG7N0C5N; -. DR UniPathway; UPA00098; UER00361. DR NextBio; 372532; -. DR PRO; PR:Q922W5; -. DR ArrayExpress; Q922W5; -. DR Bgee; Q922W5; -. DR CleanEx; MM_PYCR1; -. DR Genevestigator; Q922W5; -. DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB. DR GO; GO:0004735; F:pyrroline-5-carboxylate reductase activity; ISS:UniProtKB. DR GO; GO:0034599; P:cellular response to oxidative stress; ISS:UniProtKB. DR GO; GO:0055129; P:L-proline biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0006561; P:proline biosynthetic process; ISS:UniProtKB. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR008927; 6-PGluconate_DH_C-like. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR000304; Pyrroline-COOH_reductase. DR PANTHER; PTHR11645; PTHR11645; 1. DR PIRSF; PIRSF000193; Pyrrol-5-carb_rd; 1. DR SUPFAM; SSF48179; SSF48179; 1. DR TIGRFAMs; TIGR00112; proC; 1. DR PROSITE; PS00521; P5CR; 1. PE 2: Evidence at transcript level; KW Acetylation; Amino-acid biosynthesis; Complete proteome; KW Mitochondrion; NADP; Oxidoreductase; Proline biosynthesis; KW Reference proteome; Stress response. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 309 Pyrroline-5-carboxylate reductase 1, FT mitochondrial. FT /FTId=PRO_0000187315. FT NP_BIND 6 11 NADP (By similarity). FT NP_BIND 69 72 NADP (By similarity). FT NP_BIND 95 97 NADP (By similarity). FT BINDING 34 34 NADP; via carbonyl oxygen (By FT similarity). FT BINDING 56 56 NADP (By similarity). FT MOD_RES 2 2 N-acetylserine (By similarity). SQ SEQUENCE 309 AA; 32373 MW; A3CD24AACDD53DEF CRC64; MSVGFIGAGQ LAFALAKGFT AAGVLAAHKI MASSPDMDQA TVSALRKIGV NLTPHNKETV RHSDVLFLAV KPHIIPFILD EIGANIEDRH IVVSCAAGVT INSIEKKLTA FQPAPKVIRC MTNTPVVVRE GVTVYATGTH AQVEDGRLVE QLMGSVGFCT EVEEDLIDAV TGLSGSGPAY AFTALDALAD GGVKMGLPRR LAVRLGAQAL LGAAKMLLDS EQHPSQLKDN VCSPGGATIH ALHVLESGGF RSLLINAVEA SCIRTRELQT MADQETISPA AIKKTVLDKV KLDSSAGASL SSDHVKPLP // ID P5CS_MOUSE Reviewed; 795 AA. AC Q9Z110; Q8BGM2; Q9R1P6; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 2. DT 19-MAR-2014, entry version 129. DE RecName: Full=Delta-1-pyrroline-5-carboxylate synthase; DE Short=P5CS; DE AltName: Full=Aldehyde dehydrogenase family 18 member A1; DE Includes: DE RecName: Full=Glutamate 5-kinase; DE Short=GK; DE EC=2.7.2.11; DE AltName: Full=Gamma-glutamyl kinase; DE Includes: DE RecName: Full=Gamma-glutamyl phosphate reductase; DE Short=GPR; DE EC=1.2.1.41; DE AltName: Full=Glutamate-5-semialdehyde dehydrogenase; DE AltName: Full=Glutamyl-gamma-semialdehyde dehydrogenase; GN Name=Aldh18a1; Synonyms=P5cs, Pycs; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE SPLICING, AND ENZYME RP REGULATION. RX PubMed=10037775; DOI=10.1074/jbc.274.10.6754; RA Hu C.A., Lin W.-W., Obie C., Valle D.; RT "Molecular enzymology of mammalian delta1-pyrroline-5-carboxylate RT synthase. Alternative splice donor utilization generates isoforms with RT different sensitivity to ornithine inhibition."; RL J. Biol. Chem. 274:6754-6762(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J, and NOD; TISSUE=Bone marrow, Kidney, and Thymus; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N, and FVB/N-3; TISSUE=Mammary tumor, and Salivary gland; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-311; LYS-347 AND LYS-550, RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic fibroblast; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., RA Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). CC -!- FUNCTION: Bifunctional enzyme that converts glutamate to glutamate CC 5-semialdehyde, an intermediate in the biosynthesis of proline, CC ornithine and arginine (By similarity). CC -!- CATALYTIC ACTIVITY: ATP + L-glutamate = ADP + L-glutamate 5- CC phosphate. CC -!- CATALYTIC ACTIVITY: L-glutamate 5-semialdehyde + phosphate + CC NADP(+) = L-glutamyl 5-phosphate + NADPH. CC -!- ENZYME REGULATION: The short isoform is inhibited by L-ornithine CC with a Ki of approximately 0.25 mm. The long isoform is CC insensitive to ornithine inhibition. Thus, the two amino acid CC insert in the long isoform abolishes feedback inhibition of P5CS CC activity by L-ornithine. CC -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L- CC glutamate 5-semialdehyde from L-glutamate: step 1/2. CC -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L- CC glutamate 5-semialdehyde from L-glutamate: step 2/2. CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=Long; CC IsoId=Q9Z110-1; Sequence=Displayed; CC Name=Short; CC IsoId=Q9Z110-2; Sequence=VSP_005216; CC -!- SIMILARITY: In the N-terminal section; belongs to the glutamate 5- CC kinase family. CC -!- SIMILARITY: In the C-terminal section; belongs to the gamma- CC glutamyl phosphate reductase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF056573; AAD17517.1; -; mRNA. DR EMBL; AF056574; AAD17518.1; -; mRNA. DR EMBL; AK151072; BAE30088.1; -; mRNA. DR EMBL; AK153946; BAE32270.1; -; mRNA. DR EMBL; AK168905; BAE40719.1; -; mRNA. DR EMBL; CH466534; EDL41837.1; -; Genomic_DNA. DR EMBL; BC033427; AAH33427.1; -; mRNA. DR EMBL; BC037699; AAH37699.1; -; mRNA. DR RefSeq; NP_062672.2; NM_019698.2. DR RefSeq; NP_705782.2; NM_153554.2. DR RefSeq; XP_006527292.1; XM_006527229.1. DR UniGene; Mm.233117; -. DR ProteinModelPortal; Q9Z110; -. DR SMR; Q9Z110; 70-353, 362-793. DR IntAct; Q9Z110; 1. DR MINT; MINT-4998531; -. DR STRING; 10090.ENSMUSP00000025979; -. DR PhosphoSite; Q9Z110; -. DR PaxDb; Q9Z110; -. DR PRIDE; Q9Z110; -. DR Ensembl; ENSMUST00000025979; ENSMUSP00000025979; ENSMUSG00000025007. [Q9Z110-1] DR Ensembl; ENSMUST00000176939; ENSMUSP00000135426; ENSMUSG00000025007. [Q9Z110-2] DR GeneID; 56454; -. DR KEGG; mmu:56454; -. DR UCSC; uc008hkw.2; mouse. [Q9Z110-2] DR UCSC; uc008hkx.2; mouse. [Q9Z110-1] DR CTD; 5832; -. DR MGI; MGI:1888908; Aldh18a1. DR eggNOG; COG0014; -. DR GeneTree; ENSGT00500000044903; -. DR HOGENOM; HOG000246357; -. DR HOVERGEN; HBG007911; -. DR InParanoid; Q8BGM2; -. DR KO; K12657; -. DR OMA; LLPWVQS; -. DR OrthoDB; EOG7WX07N; -. DR TreeFam; TF314372; -. DR UniPathway; UPA00098; UER00359. DR UniPathway; UPA00098; UER00360. DR ChiTaRS; ALDH18A1; mouse. DR NextBio; 312680; -. DR PRO; PR:Q9Z110; -. DR ArrayExpress; Q9Z110; -. DR Bgee; Q9Z110; -. DR CleanEx; MM_ALDH18A1; -. DR Genevestigator; Q9Z110; -. DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004349; F:glutamate 5-kinase activity; IDA:MGI. DR GO; GO:0004350; F:glutamate-5-semialdehyde dehydrogenase activity; ISS:UniProtKB. DR GO; GO:0019240; P:citrulline biosynthetic process; ISS:UniProtKB. DR GO; GO:0006536; P:glutamate metabolic process; ISS:UniProtKB. DR GO; GO:0055129; P:L-proline biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0006592; P:ornithine biosynthetic process; IEA:Ensembl. DR GO; GO:0006561; P:proline biosynthetic process; ISS:UniProtKB. DR Gene3D; 3.40.1160.10; -; 1. DR Gene3D; 3.40.309.10; -; 1. DR Gene3D; 3.40.605.10; -; 2. DR InterPro; IPR016161; Ald_DH/histidinol_DH. DR InterPro; IPR016163; Ald_DH_C. DR InterPro; IPR016162; Ald_DH_N. DR InterPro; IPR015590; Aldehyde_DH_dom. DR InterPro; IPR001048; Asp/Glu/Uridylate_kinase. DR InterPro; IPR000965; G-glutamylP_reductase. DR InterPro; IPR020593; G-glutamylP_reductase_CS. DR InterPro; IPR001057; Glu/AcGlu_kinase. DR InterPro; IPR019797; Glutamate_5-kinase_CS. DR InterPro; IPR005766; P5_carboxy_syn. DR Pfam; PF00696; AA_kinase; 1. DR Pfam; PF00171; Aldedh; 1. DR PIRSF; PIRSF036429; P5C_syn; 1. DR PRINTS; PR00474; GLU5KINASE. DR SUPFAM; SSF53633; SSF53633; 1. DR SUPFAM; SSF53720; SSF53720; 1. DR TIGRFAMs; TIGR01092; P5CS; 1. DR TIGRFAMs; TIGR00407; proA; 1. DR PROSITE; PS00902; GLUTAMATE_5_KINASE; 1. DR PROSITE; PS01223; PROA; 1. PE 1: Evidence at protein level; KW Alternative splicing; Amino-acid biosynthesis; ATP-binding; KW Complete proteome; Kinase; Membrane; Mitochondrion; KW Mitochondrion inner membrane; Multifunctional enzyme; NADP; KW Nucleotide-binding; Oxidoreductase; Proline biosynthesis; KW Reference proteome; Transferase. FT CHAIN 1 795 Delta-1-pyrroline-5-carboxylate synthase. FT /FTId=PRO_0000109770. FT NP_BIND 266 267 ATP (By similarity). FT NP_BIND 305 311 ATP (By similarity). FT REGION 1 361 Glutamate 5-kinase. FT REGION 362 795 Gamma-glutamyl phosphate reductase. FT BINDING 117 117 Substrate (By similarity). FT BINDING 223 223 Substrate (By similarity). FT BINDING 246 246 Substrate; via amide nitrogen (By FT similarity). FT MOD_RES 311 311 N6-succinyllysine. FT MOD_RES 347 347 N6-succinyllysine. FT MOD_RES 550 550 N6-succinyllysine. FT VAR_SEQ 239 240 Missing (in isoform Short). FT /FTId=VSP_005216. FT CONFLICT 582 582 G -> S (in Ref. 1; AAD17517/AAD17518). SQ SEQUENCE 795 AA; 87266 MW; 877DF1A7B5F84247 CRC64; MLRHMHRSGV QPFRQRLLPW VQSIAVPRSN RVQPSAIRHV RSWSNIPFIT VPLSRAHGKP FAHRSELKHA KRIVVKLGSA VVTRGDECGL ALGRLASIVE QVSVLQNQGR EMMLVTSGAV AFGKQRLRHE ILLSQSVRQA LHSGQNHLKE MAIPVLEARA CAAAGQSGLM ALYEAMFTQY SICAAQILVT NLDFHDEQKR RNLNGTLHEL LRMNIVPIVN TNDAVVPPAE PNSDLQGVNV ISVKDNDSLA ARLAVEMKTD LLIVLSDVEG LFDSPPGSDD AKLIDIFYPG DQQSVTFGTK SRVGLGGMEA KVKAALWALQ GGTSVVIANG THPKVSGHVI TDIVEGKKVG TFFSEVKPAG PTVEQQGEMA RSGGRMLATL EPEQRAEIIN HLADLLTDQR EEILLANKKD LEEAEGRLAS PLLKRLSLST SKLNSLAIGL RQIAASSQES VGRVLRRTRI AKNLELEQVT VPIGVLLVIF ESRPDCLPQV AALAIASGNG LLLKGGKEAA HSNRILHLLT QEALSIHGVK EAIQLVNTRE EVEDLCRLDK IIDLIIPRGS SQLVRDIQKA AKGIPVMGHS EGICHMYVDS EASVDKVTRL VRDSKCEYPA ACNALETLLI HRDLLRTPLF DQIIDMLRVE QVKIHAGPKF ASYLTFSPSE VKSLRTEYGD LEVCIEVVDS VQEAIDHIHK YGSSHTDVIV TENEKTAEFF LQHVDSACVF WNASTRFSDG YRFGLGAEVG ISTSRIHARG PVGLEGLLTT KWLLRGQDHV VSDFSEHGSL KYLHENLPVP QRNFS // ID PAHX_MOUSE Reviewed; 338 AA. AC O35386; O08527; DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1998, sequence version 1. DT 19-MAR-2014, entry version 116. DE RecName: Full=Phytanoyl-CoA dioxygenase, peroxisomal; DE EC=1.14.11.18; DE AltName: Full=Lupus nephritis-associated peptide 1; DE AltName: Full=Phytanic acid oxidase; DE AltName: Full=Phytanoyl-CoA alpha-hydroxylase; DE Short=PhyH; DE Flags: Precursor; GN Name=Phyh; Synonyms=Ln1, Lnap1, Pahx; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=9326939; DOI=10.1038/ng1097-185; RA Mihalik S.J., Morrell J.C., Kim D., Sachsteder K.A., Watkins P.A., RA Gould S.J.; RT "Identification of PAHX, a Refsum disease gene."; RL Nat. Genet. 17:185-189(1997). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=BALB/c; TISSUE=Kidney; RX PubMed=8954131; DOI=10.1006/bbrc.1996.1805; RA Iwano M., Ueno M., Miyazaki M., Harada T., Nagai Y., Hirano M., RA Dohi Y., Akai Y., Kurioka H., Dohi K.; RT "Molecular cloning and expression of a novel peptide (LN1) gene: RT reduced expression in the renal cortex of lupus nephritis in MRL/lpr RT mouse."; RL Biochem. Biophys. Res. Commun. 229:355-360(1996). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Mammary gland; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP TISSUE SPECIFICITY, AND INTERACTION WITH PHYHIP. RX PubMed=10686344; DOI=10.1016/S0169-328X(99)00304-6; RA Lee Z.H., Kim H.-H., Ahn K.Y., Seo K.H., Kim J.K., Bae C.S., Kim K.K.; RT "Identification of a brain specific protein that associates with a RT Refsum disease gene product, phytanoyl-CoA alpha-hydroxylase."; RL Brain Res. Mol. Brain Res. 75:237-247(2000). RN [5] RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-59; LYS-108; LYS-231 AND RP LYS-252, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Liver; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., RA Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). CC -!- FUNCTION: Converts phytanoyl-CoA to 2-hydroxyphytanoyl-CoA. CC -!- CATALYTIC ACTIVITY: Phytanoyl-CoA + 2-oxoglutarate + O(2) = 2- CC hydroxyphytanoyl-CoA + succinate + CO(2). CC -!- COFACTOR: Iron. CC -!- COFACTOR: Ascorbate. CC -!- PATHWAY: Lipid metabolism; fatty acid metabolism. CC -!- SUBUNIT: Interacts specifically with the immunophilin FKBP52 and CC PHYHIP. CC -!- SUBCELLULAR LOCATION: Peroxisome. CC -!- TISSUE SPECIFICITY: Ubiquitously expressed in all tissues with CC significant levels detected in the embryonic and neonatal heart CC and liver. In the adult, significant levels are detected in the CC liver, kidney, heart, gut, brain and aorta. CC -!- DISEASE: Note=Defects in Phyh are the cause of lupus nephritis, a CC severe autoimmune disease. Phyh could be involved in a reaction CC against the progression of the disease, because its expression is CC low in the early stage of the disease in the renal cortex of CC MRL/lpr mice. CC -!- SIMILARITY: Belongs to the PhyH family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF023463; AAB81835.1; -; mRNA. DR EMBL; D88670; BAA19003.1; -; mRNA. DR EMBL; BC002018; AAH02018.1; -; mRNA. DR PIR; JC5242; JC5242. DR RefSeq; NP_034856.1; NM_010726.2. DR UniGene; Mm.391704; -. DR ProteinModelPortal; O35386; -. DR SMR; O35386; 44-338. DR BioGrid; 201185; 1. DR IntAct; O35386; 2. DR MINT; MINT-1864642; -. DR PhosphoSite; O35386; -. DR PaxDb; O35386; -. DR PRIDE; O35386; -. DR DNASU; 16922; -. DR Ensembl; ENSMUST00000027975; ENSMUSP00000027975; ENSMUSG00000026664. DR GeneID; 16922; -. DR KEGG; mmu:16922; -. DR UCSC; uc008ifd.2; mouse. DR CTD; 5264; -. DR MGI; MGI:891978; Phyh. DR eggNOG; COG5285; -. DR HOGENOM; HOG000007341; -. DR HOVERGEN; HBG000392; -. DR InParanoid; O35386; -. DR KO; K00477; -. DR OMA; RKSISCH; -. DR OrthoDB; EOG7NGQC7; -. DR TreeFam; TF313667; -. DR UniPathway; UPA00199; -. DR NextBio; 290972; -. DR PRO; PR:O35386; -. DR ArrayExpress; O35386; -. DR Bgee; O35386; -. DR CleanEx; MM_PHYH; -. DR Genevestigator; O35386; -. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR GO; GO:0005777; C:peroxisome; TAS:MGI. DR GO; GO:0003824; F:catalytic activity; IDA:MGI. DR GO; GO:0048037; F:cofactor binding; IEA:Ensembl. DR GO; GO:0031418; F:L-ascorbic acid binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0048244; F:phytanoyl-CoA dioxygenase activity; IEA:UniProtKB-EC. DR GO; GO:0001561; P:fatty acid alpha-oxidation; IDA:MGI. DR GO; GO:0006720; P:isoprenoid metabolic process; IEA:Ensembl. DR GO; GO:0097089; P:methyl-branched fatty acid metabolic process; IEA:Ensembl. DR InterPro; IPR008775; Phytyl_CoA_dOase. DR Pfam; PF05721; PhyH; 1. PE 1: Evidence at protein level; KW Complete proteome; Dioxygenase; Iron; Metal-binding; Oxidoreductase; KW Peroxisome; Reference proteome; Transit peptide; Vitamin C. FT TRANSIT 1 30 Peroxisome (By similarity). FT CHAIN 31 338 Phytanoyl-CoA dioxygenase, peroxisomal. FT /FTId=PRO_0000024054. FT REGION 175 177 Alpha-ketoglutarate binding (By FT similarity). FT METAL 175 175 Iron (By similarity). FT METAL 177 177 Iron (By similarity). FT METAL 264 264 Iron (By similarity). FT BINDING 120 120 Alpha-ketoglutarate (By similarity). FT BINDING 157 157 Alpha-ketoglutarate (By similarity). FT BINDING 193 193 Alpha-ketoglutarate (By similarity). FT BINDING 266 266 Alpha-ketoglutarate (By similarity). FT BINDING 275 275 Alpha-ketoglutarate (By similarity). FT MOD_RES 59 59 N6-succinyllysine. FT MOD_RES 108 108 N6-succinyllysine. FT MOD_RES 231 231 N6-succinyllysine. FT MOD_RES 252 252 N6-succinyllysine. FT CONFLICT 2 2 N -> K (in Ref. 2; BAA19003). SQ SEQUENCE 338 AA; 38607 MW; 9363F4322D59360E CRC64; MNLTRAGARL QVLLGHLGRP SAPTIVAQPV SGLASPASFQ PEQFQYTLDN NVLTLEQRKF YEENGFLVIK NLVSDDDIQR FRAEFERICR EEVKPPGIVI MRDVALAKQD YMPSDRMVSK IQDFQEDEEL FRYCLLPEIL KYVECFTGPN IMALHGMLIN KPPDVGKKTS RHPLHQDLHY FPFRPSNLIV CAWTAMEHID RNNGCLVVLP GTHKGTLKPH DYPKWEGGVN KMYHGIQDYD PNSPRVHLVM EKGDTVFFHP LLIHGSGRNK TQGFRKAISC HFGSSDCQCI DVSGTSQENI AREVVEMAEK KYGFQGVMDF KDTWIFRSRL VKGERINI // ID PAOX_MOUSE Reviewed; 504 AA. AC Q8C0L6; Q8K254; DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 19-MAR-2014, entry version 91. DE RecName: Full=Peroxisomal N(1)-acetyl-spermine/spermidine oxidase; DE EC=1.5.3.13; DE AltName: Full=Polyamine oxidase; GN Name=Paox; Synonyms=Pao; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, COFACTOR, RP AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=12660232; DOI=10.1074/jbc.M302149200; RA Wu T., Yankovskaya V., McIntire W.S.; RT "Cloning, sequencing, and heterologous expression of the murine RT peroxisomal flavoprotein, N(1)-acetylated polyamine oxidase."; RL J. Biol. Chem. 278:20514-20525(2003). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC STRAIN=C57BL/6J; TISSUE=Head; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC STRAIN=FVB/N; TISSUE=Colon, and Mammary gland; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: Flavoenzyme which catalyzes the oxidation of N(1)- CC acetylspermine to spermidine and is thus involved in the polyamine CC back-conversion. Can also oxidize N(1)-acetylspermidine to CC putrescine. Substrate specificity: N(1)-acetylspermine = N(1)- CC acetylspermidine > N(1),N(12)-diacylspermine >> spermine. Does not CC oxidize spermidine. Plays an important role in the regulation of CC polyamine intracellular concentration and has the potential to act CC as a determinant of cellular sensitivity to the antitumor CC polyamine analogs. CC -!- CATALYTIC ACTIVITY: N(1)-acetylspermine + O(2) + H(2)O = CC spermidine + 3-acetamidopropanal + H(2)O(2). CC -!- CATALYTIC ACTIVITY: N(1)-acetylspermidine + O(2) + H(2)O = CC putrescine + 3-acetamidopropanal + H(2)O(2). CC -!- CATALYTIC ACTIVITY: N(1),N(12)-diacetylspermine + O(2) + H(2)O = CC N(1)-acetylspermidine + 3-acetamidobutanal + H(2)O(2). CC -!- COFACTOR: Binds 1 FAD per subunit. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=1.78 uM for N(1)-acetylspermine; CC KM=36.8 uM for N(1)-acetylspermidine; CC KM=716 uM for spermine; CC KM=150 uM for N(1),N(12)-diacetylspermine; CC -!- PATHWAY: Amine and polyamine metabolism; spermine metabolism. CC -!- SUBUNIT: Monomer. CC -!- SUBCELLULAR LOCATION: Peroxisome (By similarity). Cytoplasm (By CC similarity). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q8C0L6-1; Sequence=Displayed; CC Name=2; CC IsoId=Q8C0L6-2; Sequence=VSP_011263, VSP_011264; CC -!- TISSUE SPECIFICITY: Widely expressed at different developmental CC stages. Expressed at high level in the liver and the stomach, CC expressed at lower level in heart, spleen, thymus, small CC intestine, muscle, pancreas, uterus, and breast and expressed at CC very low level in brain, kidney, lung, testis, skin, adrenal gland CC and prostate gland. CC -!- DEVELOPMENTAL STAGE: Expression increased during embryonic CC development: there is a gradual increase in the tissues on going CC from 8.5 to 19 day embryos. In the breast, expression is very low CC in virgin mouse and quite high in pregnant mouse, but decreases in CC lactating and involuting breasts. CC -!- INDUCTION: By polyamine analogs. CC -!- MISCELLANEOUS: Oxidizes N(1)-acetylated polyamines on the exo-side CC of their N(4)-amino groups. Plant PAO oxidizes spermine on the CC endo-side of the N(4)-nitrogen (By similarity). CC -!- MISCELLANEOUS: N-ethylated polyamines are also good substrates for CC this enzyme: they have been used for cancer clinical trials. They CC down-regulate polyamine biosynthetic enzymes, but dramatically up- CC regulate SSAT synthesis, which results in mammalian cells becoming CC apaptotic. CC -!- SIMILARITY: Belongs to the flavin monoamine oxidase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF226656; AAN40705.2; -; mRNA. DR EMBL; AK030664; BAC27070.1; -; mRNA. DR EMBL; BC033913; AAH33913.1; -; mRNA. DR EMBL; BC082783; AAH82783.1; -; mRNA. DR RefSeq; NP_722478.2; NM_153783.4. DR UniGene; Mm.486735; -. DR ProteinModelPortal; Q8C0L6; -. DR SMR; Q8C0L6; 4-491. DR BindingDB; Q8C0L6; -. DR ChEMBL; CHEMBL3408; -. DR PhosphoSite; Q8C0L6; -. DR PaxDb; Q8C0L6; -. DR PRIDE; Q8C0L6; -. DR Ensembl; ENSMUST00000026537; ENSMUSP00000026537; ENSMUSG00000025464. [Q8C0L6-1] DR GeneID; 212503; -. DR KEGG; mmu:212503; -. DR UCSC; uc009kha.1; mouse. [Q8C0L6-2] DR UCSC; uc009khb.1; mouse. [Q8C0L6-1] DR CTD; 196743; -. DR MGI; MGI:1916983; Paox. DR eggNOG; COG1231; -. DR GeneTree; ENSGT00530000062888; -. DR HOGENOM; HOG000037651; -. DR HOVERGEN; HBG053499; -. DR InParanoid; Q8C0L6; -. DR KO; K00308; -. DR OMA; SAHVLCG; -. DR OrthoDB; EOG751NFD; -. DR TreeFam; TF318348; -. DR BioCyc; MetaCyc:MONOMER-14466; -. DR BRENDA; 1.5.3.11; 3474. DR UniPathway; UPA00826; -. DR NextBio; 373584; -. DR PRO; PR:Q8C0L6; -. DR ArrayExpress; Q8C0L6; -. DR Bgee; Q8C0L6; -. DR CleanEx; MM_PAOX; -. DR Genevestigator; Q8C0L6; -. DR GO; GO:0005782; C:peroxisomal matrix; IEA:Ensembl. DR GO; GO:0052899; F:N(1),N(12)-diacetylspermine:oxygen oxidoreductase (3-acetamidopropanal-forming) activity; IEA:UniProtKB-EC. DR GO; GO:0052904; F:N1-acetylspermidine:oxygen oxidoreductase (3-acetamidopropanal-forming) activity; IEA:UniProtKB-EC. DR GO; GO:0052903; F:N1-acetylspermine:oxygen oxidoreductase (3-acetamidopropanal-forming) activity; IEA:UniProtKB-EC. DR GO; GO:0046592; F:polyamine oxidase activity; IDA:MGI. DR GO; GO:0052902; F:spermidine:oxygen oxidoreductase (3-aminopropanal-forming) activity; IEA:UniProtKB-EC. DR GO; GO:0052901; F:spermine:oxygen oxidoreductase (spermidine-forming) activity; IEA:UniProtKB-EC. DR GO; GO:0006598; P:polyamine catabolic process; IDA:MGI. DR GO; GO:1901307; P:positive regulation of spermidine biosynthetic process; IEA:Ensembl. DR GO; GO:0009446; P:putrescine biosynthetic process; IEA:Ensembl. DR GO; GO:0009447; P:putrescine catabolic process; IEA:Ensembl. DR GO; GO:0046203; P:spermidine catabolic process; IEA:Ensembl. DR GO; GO:0046208; P:spermine catabolic process; IEA:Ensembl. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR002937; Amino_oxidase. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Pfam; PF01593; Amino_oxidase; 1. PE 1: Evidence at protein level; KW Alternative splicing; Complete proteome; Cytoplasm; FAD; Flavoprotein; KW Oxidoreductase; Peroxisome; Reference proteome. FT CHAIN 1 504 Peroxisomal N(1)-acetyl- FT spermine/spermidine oxidase. FT /FTId=PRO_0000099876. FT MOTIF 502 504 Microbody targeting signal (Potential). FT VAR_SEQ 1 280 Missing (in isoform 2). FT /FTId=VSP_011263. FT VAR_SEQ 281 282 PL -> ME (in isoform 2). FT /FTId=VSP_011264. SQ SEQUENCE 504 AA; 55447 MW; B40BD34C7A0B98F1 CRC64; MAFPGPRVLV VGSGIAGLGA AQKLCSHRAA PHLRVLEATA SAGGRIRSER CFGGVVELGA HWIHGPSQDN PVFQLAAEFG LLGEKELSEE NQLVDTGGHV ALPSMIWSSS GTSVSLELMT EMARLFYGLI ERTREFLNES ETPMASVGEF LKKEISQQVA SWTEDDEDTR KRKLAILNTF FNIECCVSGT HSMDLVALAP FGEYTVLPGL DCILAGGYQG LTDRILASLP KDTVAFDKPV KTIHWNGSFQ EAAFPGETFP VLVECEDGAR LPAHHVIVTV PLGFLKEHQD TFFEPPLPAK KAEAIKKLGF GTNNKIFLEF EEPFWEPDCQ FIQVVWEDTS PLQDTALSLQ DTWFKKLIGF LVQPSFESSH VLCGFIAGLE SEFMETLSDE EVLLSLTQVL RRVTGNPQLP AAKSVRRSQW HSAPYTRGSY SYVAVGSTGD DLDLMAQPLP EDGTGTQLQV LFAGEATHRT FYSTTHGALL SGWREADRLV SLWDSQVEQS RPRL // ID PCYXL_MOUSE Reviewed; 495 AA. AC Q8C7K6; DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 19-MAR-2014, entry version 85. DE RecName: Full=Prenylcysteine oxidase-like; DE EC=1.8.3.-; DE Flags: Precursor; GN Name=Pcyox1l; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Hippocampus; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6; TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: Probable oxidoreductase (By similarity). CC -!- COFACTOR: FAD (By similarity). CC -!- SUBCELLULAR LOCATION: Secreted (By similarity). CC -!- SIMILARITY: Belongs to the prenylcysteine oxidase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK050006; BAC34029.1; -; mRNA. DR EMBL; BC060677; AAH60677.1; -; mRNA. DR RefSeq; NP_766420.1; NM_172832.4. DR UniGene; Mm.234457; -. DR ProteinModelPortal; Q8C7K6; -. DR SMR; Q8C7K6; 27-100. DR PhosphoSite; Q8C7K6; -. DR PaxDb; Q8C7K6; -. DR PRIDE; Q8C7K6; -. DR Ensembl; ENSMUST00000025472; ENSMUSP00000025472; ENSMUSG00000024579. DR GeneID; 240334; -. DR KEGG; mmu:240334; -. DR UCSC; uc008fcm.1; mouse. DR CTD; 78991; -. DR MGI; MGI:3606062; Pcyox1l. DR eggNOG; NOG73316; -. DR GeneTree; ENSGT00390000011206; -. DR HOGENOM; HOG000241149; -. DR HOVERGEN; HBG053532; -. DR InParanoid; Q8C7K6; -. DR OMA; DWYLLNL; -. DR OrthoDB; EOG7VB2F5; -. DR TreeFam; TF329001; -. DR NextBio; 384562; -. DR PRO; PR:Q8C7K6; -. DR Bgee; Q8C7K6; -. DR CleanEx; MM_PCYOX1L; -. DR Genevestigator; Q8C7K6; -. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0001735; F:prenylcysteine oxidase activity; IEA:InterPro. DR GO; GO:0030328; P:prenylcysteine catabolic process; IEA:InterPro. DR InterPro; IPR010795; Prenylcys_lyase. DR InterPro; IPR017046; Prenylcysteine_Oxase. DR Pfam; PF07156; Prenylcys_lyase; 1. DR PIRSF; PIRSF036292; Prenylcysteine_oxidase; 1. PE 2: Evidence at transcript level; KW Complete proteome; FAD; Flavoprotein; Glycoprotein; Oxidoreductase; KW Reference proteome; Secreted; Signal. FT SIGNAL 1 22 By similarity. FT CHAIN 23 495 Prenylcysteine oxidase-like. FT /FTId=PRO_0000280287. FT CARBOHYD 185 185 N-linked (GlcNAc...) (Potential). FT CARBOHYD 343 343 N-linked (GlcNAc...) (Potential). SQ SEQUENCE 495 AA; 54875 MW; DA86F56E6B108198 CRC64; MARAAPLLAV LATVLTTAAA GGDAPPGKIA VIGAGIGGSA VAHFLQQHFG PRVQIVVYEK GTVGGRLATI SVNKQNYESG AASFHSLSLH MQDFVKLLGL RQRREVVGRS AIFGGEHFVL EETDWYLLNL FRLWWYYGIS FLRLQMWVEE VMEKFMRIYK YQAHGYAFSG VEELLYSLGE ATFVNMTQRS VAESLLQVGV TQRFIDDVVS AVLRASYGQS ASMPAFAGAM SLAGAQGNLW SVEGGNKLVC SGLLKLAKAT VIHATVTSVT LHSTEGKALY QVAYESDKGN SSDFYDIVVI ATPLHLDNSS NNNITFEGFT PPIEDIQGSF QPTVVSLVHG YLNSSYFGFP DPKLFPFANI LTTDFPSFFC TLDNICPVNI SASFRRKQPQ EAAVWRVQSP KPLFRTELKT LFRSYYSVQT AEWQAHPLYG SRRTLPRFAL HDQLFYLNAL EWAASSVEVT AVAAKNVALL AYNRWYQDLD KIDQKDLIHK VKTEL // ID PCYOX_MOUSE Reviewed; 505 AA. AC Q9CQF9; Q3UHV6; Q69ZW0; Q8BZX1; DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 19-MAR-2014, entry version 99. DE RecName: Full=Prenylcysteine oxidase; DE EC=1.8.3.5; DE Flags: Precursor; GN Name=Pcyox1; Synonyms=Kiaa0908; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Amnion, Liver, Lung, and Testis; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Mammary tumor; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 5-505. RC TISSUE=Fetal brain; RX PubMed=15368895; DOI=10.1093/dnares/11.3.205; RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H., RA Nagase T., Ohara O., Koga H.; RT "Prediction of the coding sequences of mouse homologues of KIAA gene: RT IV. The complete nucleotide sequences of 500 mouse KIAA-homologous RT cDNAs identified by screening of terminal sequences of cDNA clones RT randomly sampled from size-fractionated libraries."; RL DNA Res. 11:205-218(2004). RN [4] RP PROTEIN SEQUENCE OF 145-151; 169-193; 292-298; 328-349 AND 421-430, RP AND MASS SPECTROMETRY. RC STRAIN=C57BL/6; TISSUE=Brain; RA Lubec G., Kang S.U.; RL Submitted (APR-2007) to UniProtKB. RN [5] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-196. RC STRAIN=C57BL/6; TISSUE=Plasma; RX PubMed=16944957; DOI=10.1021/pr060186m; RA Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J., RA Gevaert K.; RT "Proteome-wide characterization of N-glycosylation events by diagonal RT chromatography."; RL J. Proteome Res. 5:2438-2447(2006). RN [6] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-353. RX PubMed=19349973; DOI=10.1038/nbt.1532; RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., RA Schiess R., Aebersold R., Watts J.D.; RT "Mass-spectrometric identification and relative quantification of N- RT linked cell surface glycoproteins."; RL Nat. Biotechnol. 27:378-386(2009). CC -!- FUNCTION: Involved in the degradation of prenylated proteins. CC Cleaves the thioether bond of prenyl-L-cysteines, such as CC farnesylcysteine and geranylgeranylcysteine (By similarity). CC -!- CATALYTIC ACTIVITY: An S-prenyl-L-cysteine + O(2) + H(2)O = a CC prenal + L-cysteine + H(2)O(2). CC -!- COFACTOR: FAD (By similarity). CC -!- SUBCELLULAR LOCATION: Lysosome (By similarity). CC -!- SIMILARITY: Belongs to the prenylcysteine oxidase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK004799; BAB23572.1; -; mRNA. DR EMBL; AK004840; BAB23607.1; -; mRNA. DR EMBL; AK031585; BAC27462.1; -; mRNA. DR EMBL; AK033373; BAC28252.1; -; mRNA. DR EMBL; AK049412; BAC33741.1; -; mRNA. DR EMBL; AK145366; BAE26391.1; -; mRNA. DR EMBL; AK147190; BAE27750.1; -; mRNA. DR EMBL; AK161616; BAE36494.1; -; mRNA. DR EMBL; AK169209; BAE40981.1; -; mRNA. DR EMBL; BC028308; AAH28308.1; -; mRNA. DR EMBL; AK173058; BAD32336.1; -; mRNA. DR RefSeq; NP_080099.1; NM_025823.4. DR UniGene; Mm.30849; -. DR ProteinModelPortal; Q9CQF9; -. DR SMR; Q9CQF9; 34-109. DR IntAct; Q9CQF9; 5. DR MINT; MINT-1858396; -. DR STRING; 10090.ENSMUSP00000032065; -. DR PhosphoSite; Q9CQF9; -. DR PaxDb; Q9CQF9; -. DR PRIDE; Q9CQF9; -. DR Ensembl; ENSMUST00000032065; ENSMUSP00000032065; ENSMUSG00000029998. DR GeneID; 66881; -. DR KEGG; mmu:66881; -. DR UCSC; uc009cro.2; mouse. DR CTD; 51449; -. DR MGI; MGI:1914131; Pcyox1. DR eggNOG; NOG73316; -. DR GeneTree; ENSGT00390000011206; -. DR HOGENOM; HOG000241149; -. DR HOVERGEN; HBG053532; -. DR InParanoid; Q9CQF9; -. DR KO; K05906; -. DR OMA; NGIECAA; -. DR OrthoDB; EOG7VB2F5; -. DR TreeFam; TF329001; -. DR NextBio; 322917; -. DR PRO; PR:Q9CQF9; -. DR ArrayExpress; Q9CQF9; -. DR Bgee; Q9CQF9; -. DR CleanEx; MM_PCYOX1; -. DR Genevestigator; Q9CQF9; -. DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl. DR GO; GO:0034361; C:very-low-density lipoprotein particle; IEA:Ensembl. DR GO; GO:0008555; F:chloride-transporting ATPase activity; IEA:Ensembl. DR GO; GO:0001735; F:prenylcysteine oxidase activity; IMP:MGI. DR GO; GO:0006200; P:ATP catabolic process; IEA:GOC. DR GO; GO:1902476; P:chloride transmembrane transport; IEA:GOC. DR GO; GO:0030327; P:prenylated protein catabolic process; IEA:Ensembl. DR GO; GO:0030328; P:prenylcysteine catabolic process; IMP:MGI. DR InterPro; IPR010795; Prenylcys_lyase. DR InterPro; IPR017046; Prenylcysteine_Oxase. DR Pfam; PF07156; Prenylcys_lyase; 1. DR PIRSF; PIRSF036292; Prenylcysteine_oxidase; 1. PE 1: Evidence at protein level; KW Complete proteome; Direct protein sequencing; FAD; Flavoprotein; KW Glycoprotein; Isopeptide bond; Lysosome; Oxidoreductase; KW Reference proteome; Signal; Ubl conjugation. FT SIGNAL 1 28 Potential. FT CHAIN 29 505 Prenylcysteine oxidase. FT /FTId=PRO_0000023300. FT CARBOHYD 196 196 N-linked (GlcNAc...). FT CARBOHYD 323 323 N-linked (GlcNAc...) (Potential). FT CARBOHYD 353 353 N-linked (GlcNAc...). FT CROSSLNK 162 162 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in ubiquitin) (By FT similarity). FT CONFLICT 114 114 S -> T (in Ref. 1; BAC28252). SQ SEQUENCE 505 AA; 56495 MW; 9169BC4CC7D97561 CRC64; MGRFAAALVG SLFWLGLLLC GLGSLASAEP RAPPNRIAIV GAGIGGTSSA YYLRKKFGKD VKIDVFEREE VGGRLATLKV QGHDYEAGGS VIHPLNLHMK RFVKELGLSS VPASGGLVGV YNGKSLVFEE SSWFVINVIK LVWRYGFQSL RMHMWVEDLL DKFMRIYRYQ SHDYAFSSVE KLMHAIGGDD YVRLLNQTLR ENLKKAGFSE TFLNEMIAPV MKVNYGQSTD INAFVGAVSL TAADSNLWAV EGGNKIVCSG LLQASSSNLI SGSVMSIEEK TRTKQTGNPT KMYEVVYKTG SETHSDFYDI VLVAAPLNRK MSNITFRNFD PPIEEFNDPY QQLVTTFIKG ELNSTLFSSR PKDQFGLSAI LVTDDSDMFI NSLSIVASVR QKEGPPPAVD GMHVWKTFSR DILTKEQISK LFLSYDYAVR KPWLSYPHYE PPQKCPSIIL HDRLYYLNGI EFAASCMEMS AIAGYNAALL AYHRWNGNED MIDQDDLYER LKTEL // ID PECR_MOUSE Reviewed; 303 AA. AC Q99MZ7; Q9CX01; Q9JIF4; DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 19-MAR-2014, entry version 103. DE RecName: Full=Peroxisomal trans-2-enoyl-CoA reductase; DE Short=TERP; DE EC=1.3.1.38; GN Name=Pecr; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY. RC TISSUE=Liver; RX PubMed=10811639; DOI=10.1074/jbc.M001168200; RA Das A.K., Uhler M.D., Hajra A.K.; RT "Molecular cloning and expression of mammalian peroxisomal trans-2- RT enoyl-coenzyme A reductase cDNAs."; RL J. Biol. Chem. 275:24333-24340(2000). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=11669066; RA Amery L., Mannaerts G.P., Subramani S., Van Veldhoven P.P., RA Fransen M.; RT "Identification of a novel human peroxisomal 2,4-dienoyl-CoA reductase RT related protein using the M13 phage protein VI phage display RT technology."; RL Comb. Chem. High Throughput Screen. 4:545-552(2001). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Kidney; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP ACETYLATION [LARGE SCALE ANALYSIS] AT GLY-2, SUCCINYLATION [LARGE RP SCALE ANALYSIS] AT LYS-5; LYS-17 AND LYS-32, IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS], AND CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., RA Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). RN [6] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-17; LYS-83 AND LYS-97, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23576753; DOI=10.1073/pnas.1302961110; RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., RA Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.; RT "Label-free quantitative proteomics of the lysine acetylome in RT mitochondria identifies substrates of SIRT3 in metabolic pathways."; RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013). CC -!- FUNCTION: Participates in chain elongation of fatty acids. Has no CC 2,4-dienoyl-CoA reductase activity (By similarity). CC -!- CATALYTIC ACTIVITY: Acyl-CoA + NADP(+) = trans-2,3-dehydroacyl-CoA CC + NADPH. CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis. CC -!- SUBUNIT: Interacts with PEX5, probably required to target it into CC peroxisomes (By similarity). CC -!- SUBCELLULAR LOCATION: Peroxisome (By similarity). CC -!- TISSUE SPECIFICITY: Highly expressed in liver and kidney. CC Expressed at lowe level in heart and skeletal muscle. Expressed at CC weak level in other tissues. CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases CC (SDR) family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF232011; AAF69800.1; -; mRNA. DR EMBL; AF242204; AAK28336.1; -; mRNA. DR EMBL; AK010260; BAB26803.1; -; mRNA. DR EMBL; BC013530; AAH13530.1; -; mRNA. DR RefSeq; NP_076012.3; NM_023523.5. DR UniGene; Mm.281738; -. DR ProteinModelPortal; Q99MZ7; -. DR SMR; Q99MZ7; 7-303. DR IntAct; Q99MZ7; 2. DR MINT; MINT-2514438; -. DR PhosphoSite; Q99MZ7; -. DR REPRODUCTION-2DPAGE; Q99MZ7; -. DR PaxDb; Q99MZ7; -. DR PRIDE; Q99MZ7; -. DR Ensembl; ENSMUST00000027381; ENSMUSP00000027381; ENSMUSG00000026189. DR GeneID; 111175; -. DR KEGG; mmu:111175; -. DR UCSC; uc007bki.2; mouse. DR CTD; 55825; -. DR MGI; MGI:2148199; Pecr. DR eggNOG; COG1028; -. DR GeneTree; ENSGT00740000115347; -. DR HOVERGEN; HBG105268; -. DR InParanoid; Q99MZ7; -. DR KO; K07753; -. DR OMA; AYEWGHA; -. DR TreeFam; TF315256; -. DR UniPathway; UPA00094; -. DR NextBio; 365461; -. DR PRO; PR:Q99MZ7; -. DR ArrayExpress; Q99MZ7; -. DR Bgee; Q99MZ7; -. DR CleanEx; MM_PECR; -. DR Genevestigator; Q99MZ7; -. DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB. DR GO; GO:0005778; C:peroxisomal membrane; ISS:UniProtKB. DR GO; GO:0019166; F:trans-2-enoyl-CoA reductase (NADPH) activity; ISS:UniProtKB. DR GO; GO:0030497; P:fatty acid elongation; ISA:MGI. DR GO; GO:0033306; P:phytol metabolic process; IEA:Ensembl. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR002347; Glc/ribitol_DH. DR InterPro; IPR016040; NAD(P)-bd_dom. DR PRINTS; PR00081; GDHRDH. PE 1: Evidence at protein level; KW Acetylation; Complete proteome; Fatty acid biosynthesis; KW Fatty acid metabolism; Lipid biosynthesis; Lipid metabolism; NADP; KW Oxidoreductase; Peroxisome; Reference proteome. FT INIT_MET 1 1 Removed. FT CHAIN 2 303 Peroxisomal trans-2-enoyl-CoA reductase. FT /FTId=PRO_0000054741. FT NP_BIND 23 47 NADP (By similarity). FT MOTIF 301 303 Microbody targeting signal (By FT similarity). FT ACT_SITE 179 179 Proton acceptor (By similarity). FT MOD_RES 2 2 N-acetylglycine. FT MOD_RES 5 5 N6-succinyllysine. FT MOD_RES 17 17 N6-acetyllysine; alternate. FT MOD_RES 17 17 N6-succinyllysine; alternate. FT MOD_RES 32 32 N6-succinyllysine. FT MOD_RES 83 83 N6-acetyllysine. FT MOD_RES 97 97 N6-acetyllysine. FT CONFLICT 89 89 N -> Y (in Ref. 3; BAB26803). FT CONFLICT 230 232 AKR -> VSA (in Ref. 1; AAF69800). FT CONFLICT 241 244 PLVC -> LLAR (in Ref. 1; AAF69800). FT CONFLICT 268 268 Y -> H (in Ref. 1; AAF69800). SQ SEQUENCE 303 AA; 32410 MW; 97AD4047A20B30D0 CRC64; MGSWKTGQSY LAAGLLKNQV AVVTGGGTGI GKAVSRELLH LGCNVVIASR KLDRLTAAVD ELRASLPPSS SAEVSAIQCN IRKEEEVSNL VKSTLAKYGK INFLVNNGGG QFMAPVEDIT AKGWHAVIET NLTGTFYMCK EVYNSWMREH GGSIVNIIVL LNNGFPTAAH TGAAREGVYN LTKSMALAWA SSGVRINCVA PGTIYSQTAV DNYGEMGQTL FEMAFDSIPA KRLGVPEEIS PLVCFLLSPA ASYITGQLIN VDGGQALYTH AFSIPDHDNW PVGAGDLSIV KRIKESFKKK AKL // ID PERE_MOUSE Reviewed; 716 AA. AC P49290; Q5SW51; Q61798; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 2. DT 19-MAR-2014, entry version 114. DE RecName: Full=Eosinophil peroxidase; DE Short=EPO; DE EC=1.11.1.7; DE Contains: DE RecName: Full=Eosinophil peroxidase light chain; DE Contains: DE RecName: Full=Eosinophil peroxidase heavy chain; DE Flags: Precursor; GN Name=Epx; Synonyms=Eper; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=C57BL/6; RA Ohmori J., Itoh H., Tomita M., Nawa Y.; RL Submitted (NOV-1995) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=C57BL/6J; TISSUE=Bone marrow; RX PubMed=8773591; RA Horton M.A., Larson K.A., Lee J.J., Lee N.A.; RT "Cloning of the murine eosinophil peroxidase gene (mEPO): RT characterization of a conserved subgroup of mammalian hematopoietic RT peroxidases."; RL J. Leukoc. Biol. 60:285-294(1996). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [4] RP FUNCTION, AND NITRATION. RX PubMed=18694936; DOI=10.1074/jbc.M801196200; RA Ulrich M., Petre A., Youhnovski N., Proemm F., Schirle M., Schumm M., RA Pero R.S., Doyle A., Checkel J., Kita H., Thiyagarajan N., RA Acharya K.R., Schmid-Grendelmeier P., Simon H.-U., Schwarz H., RA Tsutsui M., Shimokawa H., Bellon G., Lee J.J., Przybylski M., RA Doering G.; RT "Post-translational tyrosine nitration of eosinophil granule toxins RT mediated by eosinophil peroxidase."; RL J. Biol. Chem. 283:28629-28640(2008). CC -!- FUNCTION: Mediates tyrosine nitration of secondary granule CC proteins in mature resting eosinophils (By similarity). CC -!- CATALYTIC ACTIVITY: 2 phenolic donor + H(2)O(2) = 2 phenoxyl CC radical of the donor + 2 H(2)O. CC -!- COFACTOR: Binds 1 calcium ion per heterodimer (By similarity). CC -!- COFACTOR: Binds 1 heme B (iron-protoporphyrin IX) group covalently CC per heterodimer (By similarity). CC -!- SUBUNIT: Tetramer of two light chains and two heavy chains (By CC similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasmic granule. Note=Cytoplasmic CC granules of eosinophils. CC -!- SIMILARITY: Belongs to the peroxidase family. XPO subfamily. CC -!- SEQUENCE CAUTION: CC Sequence=AAB40403.1; Type=Erroneous initiation; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; D78353; BAA11370.1; -; mRNA. DR EMBL; L77979; AAB40403.1; ALT_INIT; mRNA. DR EMBL; AL606805; CAI25724.1; -; Genomic_DNA. DR RefSeq; NP_031972.2; NM_007946.2. DR UniGene; Mm.1315; -. DR ProteinModelPortal; P49290; -. DR SMR; P49290; 143-716. DR PeroxiBase; 3346; MmEPO. DR PhosphoSite; P49290; -. DR PaxDb; P49290; -. DR PRIDE; P49290; -. DR DNASU; 13861; -. DR Ensembl; ENSMUST00000049768; ENSMUSP00000050497; ENSMUSG00000052234. DR GeneID; 13861; -. DR KEGG; mmu:13861; -. DR UCSC; uc007kuw.1; mouse. DR CTD; 8288; -. DR MGI; MGI:107569; Epx. DR eggNOG; NOG262194; -. DR GeneTree; ENSGT00550000074325; -. DR HOGENOM; HOG000016084; -. DR HOVERGEN; HBG000071; -. DR InParanoid; Q5SW51; -. DR KO; K10788; -. DR OMA; MHVALGL; -. DR OrthoDB; EOG7M0NQW; -. DR TreeFam; TF314316; -. DR NextBio; 284746; -. DR PRO; PR:P49290; -. DR ArrayExpress; P49290; -. DR Bgee; P49290; -. DR CleanEx; MM_EPX; -. DR Genevestigator; P49290; -. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004601; F:peroxidase activity; IDA:MGI. DR GO; GO:0002215; P:defense response to nematode; IMP:MGI. DR GO; GO:0072677; P:eosinophil migration; IMP:MGI. DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-KW. DR GO; GO:0032693; P:negative regulation of interleukin-10 production; IMP:MGI. DR GO; GO:0032714; P:negative regulation of interleukin-5 production; IMP:MGI. DR GO; GO:0032753; P:positive regulation of interleukin-4 production; IMP:MGI. DR Gene3D; 1.10.640.10; -; 1. DR InterPro; IPR010255; Haem_peroxidase. DR InterPro; IPR002007; Haem_peroxidase_animal. DR InterPro; IPR019791; Haem_peroxidase_animal_subgr. DR Pfam; PF03098; An_peroxidase; 1. DR PRINTS; PR00457; ANPEROXIDASE. DR SUPFAM; SSF48113; SSF48113; 1. DR PROSITE; PS00435; PEROXIDASE_1; 1. DR PROSITE; PS50292; PEROXIDASE_3; 1. PE 1: Evidence at protein level; KW Calcium; Complete proteome; Disulfide bond; Glycoprotein; Heme; KW Hydrogen peroxide; Iron; Metal-binding; Nitration; Oxidoreductase; KW Peroxidase; Reference proteome; Signal. FT SIGNAL 1 18 Potential. FT PROPEP 19 140 Potential. FT /FTId=PRO_0000023642. FT CHAIN 141 251 Eosinophil peroxidase light chain. FT /FTId=PRO_0000023643. FT CHAIN 252 716 Eosinophil peroxidase heavy chain. FT /FTId=PRO_0000023644. FT ACT_SITE 234 234 Proton acceptor (By similarity). FT METAL 235 235 Calcium (By similarity). FT METAL 307 307 Calcium (By similarity). FT METAL 309 309 Calcium; via carbonyl oxygen (By FT similarity). FT METAL 311 311 Calcium (By similarity). FT METAL 313 313 Calcium (By similarity). FT METAL 475 475 Iron (heme axial ligand) (By similarity). FT BINDING 233 233 Heme (covalent; via 2 links) (By FT similarity). FT BINDING 381 381 Heme (covalent; via 2 links) (By FT similarity). FT SITE 378 378 Transition state stabilizer (By FT similarity). FT MOD_RES 489 489 Nitrated tyrosine (By similarity). FT CARBOHYD 53 53 N-linked (GlcNAc...) (Potential). FT CARBOHYD 114 114 N-linked (GlcNAc...) (Potential). FT CARBOHYD 328 328 N-linked (GlcNAc...) (Potential). FT CARBOHYD 364 364 N-linked (GlcNAc...) (Potential). FT CARBOHYD 709 709 N-linked (GlcNAc...) (Potential). FT DISULFID 142 153 By similarity. FT DISULFID 254 264 By similarity. FT DISULFID 258 282 By similarity. FT DISULFID 360 371 By similarity. FT DISULFID 579 636 By similarity. FT DISULFID 677 702 By similarity. FT CONFLICT 167 167 A -> P (in Ref. 2; AAB40403). FT CONFLICT 400 400 A -> P (in Ref. 2; AAB40403). FT CONFLICT 524 524 M -> K (in Ref. 1; BAA11370). FT CONFLICT 531 531 N -> Y (in Ref. 1; BAA11370). SQ SEQUENCE 716 AA; 81380 MW; 9D1D1A88E6E259A1 CRC64; MMQQLLALVG ALATLILTQH AEGTAPASPS PVEISVLRDC IAEAKLLVDT AYNHTQKSIM QRLRSGSASP MDLLAYFKQP VAATRRVVQA ADYMHVALGL LEERLQPRGS RPFNATDVLT EPQLRLLSQA SGCALQDQAE RCSNKYRTIT GRCNNKKHPW LGASNQALAR WLPAEYEDHR SLPFGWTPGK RRNGFLLPLV RDVSNQIVRF PSKKLTSDRG RALMFMQWGQ FIDHDLDFSP ESPARVAFSM GVDCEKTCAQ LPPCFPIKIP RNDPRIKNQR DCIPFFRSAP ACPQNRNKVR NQINALTSFV DASMVYGSEV TLALRLRNRT NFLGLLATNQ RFQDNGRALL PFDNLHEDPC LLTNRSARIP CFLAGDTRSS ETPKLTALHT LFVREHNRLA AELRRLNPHW SGDKLYNEAR KIVGAMVQII TYRDFLPLVL GRARIRRTLG PYRGYCSNVD PRVANVFTLA FRFGHTMLQP FMFRLDSQYR ASAPNSHVPL SSVFFASWRI IHEGGIDPIL RGLMATPAKL NRQDSMLVDE LRDKLFQQVR RIGLDLAALN MQRSRDHGLP GYNAWRRFCG LSQPRNLAQL SRVLKNQDLA RKFLRLYKTP DNIDIWVGAI AEPLLPGARV GPLLACLFEN QFRRARDGDR FWWQKWGVFT KRQRKALRRI SLSRIVCDNT GITTVSRDIF RANIYPQGFV SCSRIPKLNL SAWRGK // ID PERM_MOUSE Reviewed; 718 AA. AC P11247; Q5NCP1; DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 2. DT 19-MAR-2014, entry version 133. DE RecName: Full=Myeloperoxidase; DE Short=MPO; DE EC=1.11.2.2; DE Contains: DE RecName: Full=Myeloperoxidase light chain; DE Contains: DE RecName: Full=Myeloperoxidase heavy chain; DE Flags: Precursor; GN Name=Mpo; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=C3H; RX PubMed=2548170; DOI=10.1093/nar/17.14.5852; RA Venturelli D., Shirsat N., Gemperlein I., Bittenbender S., Rovera G.; RT "Nucleotide sequence of cDNA for murine myeloperoxidase."; RL Nucleic Acids Res. 17:5852-5852(1989). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=2552419; DOI=10.1093/nar/17.19.7987; RA Venturelli D., Bittenbender S., Rovera G.; RT "Sequence of the murine myeloperoxidase (MPO) gene."; RL Nucleic Acids Res. 17:7987-7988(1989). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). CC -!- FUNCTION: Part of the host defense system of polymorphonuclear CC leukocytes. It is responsible for microbicidal activity against a CC wide range of organisms. In the stimulated PMN, MPO catalyzes the CC production of hypohalous acids, primarily hypochlorous acid in CC physiologic situations, and other toxic intermediates that greatly CC enhance PMN microbicidal activity (By similarity). CC -!- CATALYTIC ACTIVITY: Cl(-) + H(2)O(2) + H(+) = HClO + H(2)O. CC -!- CATALYTIC ACTIVITY: Cl(-) + H(2)O(2) = HOCl + 2 H(2)O. CC -!- COFACTOR: Binds 1 calcium ion per monomer (By similarity). CC -!- COFACTOR: Binds 1 heme B (iron-protoporphyrin IX) group covalently CC per monomer (By similarity). CC -!- SUBUNIT: Homodimer; disulfide-linked. Each monomer consists of a CC light and a heavy chain (By similarity). CC -!- SUBCELLULAR LOCATION: Lysosome. CC -!- SIMILARITY: Belongs to the peroxidase family. XPO subfamily. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X15313; CAA33373.1; -; mRNA. DR EMBL; X15378; CAA33439.1; -; Genomic_DNA. DR EMBL; AL604022; CAI35961.1; -; Genomic_DNA. DR PIR; S06068; S06068. DR RefSeq; NP_034954.2; NM_010824.2. DR RefSeq; XP_006532467.1; XM_006532404.1. DR RefSeq; XP_006532468.1; XM_006532405.1. DR UniGene; Mm.4668; -. DR ProteinModelPortal; P11247; -. DR SMR; P11247; 131-717. DR STRING; 10090.ENSMUSP00000103563; -. DR ChEMBL; CHEMBL2440; -. DR PeroxiBase; 3344; MmMPO. DR PhosphoSite; P11247; -. DR PaxDb; P11247; -. DR PRIDE; P11247; -. DR Ensembl; ENSMUST00000020779; ENSMUSP00000020779; ENSMUSG00000009350. DR Ensembl; ENSMUST00000121303; ENSMUSP00000112837; ENSMUSG00000009350. DR GeneID; 17523; -. DR KEGG; mmu:17523; -. DR UCSC; uc011ycc.1; mouse. DR CTD; 4353; -. DR MGI; MGI:97137; Mpo. DR eggNOG; NOG262194; -. DR GeneTree; ENSGT00550000074325; -. DR HOGENOM; HOG000016084; -. DR HOVERGEN; HBG000071; -. DR InParanoid; Q5NCP1; -. DR KO; K10789; -. DR OMA; QDKYRTI; -. DR OrthoDB; EOG7M0NQW; -. DR TreeFam; TF314316; -. DR ChiTaRS; MPO; mouse. DR NextBio; 292132; -. DR PRO; PR:P11247; -. DR ArrayExpress; P11247; -. DR Bgee; P11247; -. DR CleanEx; MM_MPO; -. DR Genevestigator; P11247; -. DR GO; GO:0042582; C:azurophil granule; ISS:UniProtKB. DR GO; GO:0005615; C:extracellular space; IEA:Ensembl. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0008201; F:heparin binding; IEA:Ensembl. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004601; F:peroxidase activity; IDA:MGI. DR GO; GO:0007568; P:aging; IEA:Ensembl. DR GO; GO:0050832; P:defense response to fungus; IMP:MGI. DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IDA:MGI. DR GO; GO:0002149; P:hypochlorous acid biosynthetic process; IMP:MGI. DR GO; GO:0034374; P:low-density lipoprotein particle remodeling; IEA:Ensembl. DR GO; GO:0044130; P:negative regulation of growth of symbiont in host; IMP:MGI. DR GO; GO:0019430; P:removal of superoxide radicals; IMP:MGI. DR GO; GO:0002679; P:respiratory burst involved in defense response; IMP:MGI. DR GO; GO:0032094; P:response to food; IEA:Ensembl. DR GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl. DR GO; GO:0009612; P:response to mechanical stimulus; IEA:Ensembl. DR GO; GO:0001878; P:response to yeast; IMP:MGI. DR Gene3D; 1.10.640.10; -; 2. DR InterPro; IPR010255; Haem_peroxidase. DR InterPro; IPR002007; Haem_peroxidase_animal. DR InterPro; IPR019791; Haem_peroxidase_animal_subgr. DR Pfam; PF03098; An_peroxidase; 1. DR PRINTS; PR00457; ANPEROXIDASE. DR SUPFAM; SSF48113; SSF48113; 1. DR PROSITE; PS00435; PEROXIDASE_1; 1. DR PROSITE; PS50292; PEROXIDASE_3; 1. PE 2: Evidence at transcript level; KW Calcium; Complete proteome; Disulfide bond; Glycoprotein; Heme; KW Hydrogen peroxide; Iron; Lysosome; Metal-binding; Oxidation; KW Oxidoreductase; Peroxidase; Reference proteome; Signal. FT SIGNAL 1 15 FT PROPEP 16 138 Potential. FT /FTId=PRO_0000023657. FT CHAIN 139 718 Myeloperoxidase. FT /FTId=PRO_0000023658. FT CHAIN 139 252 Myeloperoxidase light chain. FT /FTId=PRO_0000023659. FT CHAIN 253 718 Myeloperoxidase heavy chain. FT /FTId=PRO_0000023660. FT ACT_SITE 235 235 Proton acceptor (By similarity). FT METAL 236 236 Calcium (By similarity). FT METAL 308 308 Calcium (By similarity). FT METAL 310 310 Calcium; via carbonyl oxygen (By FT similarity). FT METAL 312 312 Calcium (By similarity). FT METAL 314 314 Calcium (By similarity). FT METAL 476 476 Iron (heme axial ligand) (By similarity). FT BINDING 234 234 Heme (covalent; via 3 links) (By FT similarity). FT BINDING 382 382 Heme (covalent; via 3 links) (By FT similarity). FT BINDING 383 383 Heme (covalent; via 3 links) (By FT similarity). FT SITE 379 379 Transition state stabilizer (By FT similarity). FT MOD_RES 290 290 Cysteine sulfenic acid (-SOH) (By FT similarity). FT CARBOHYD 113 113 N-linked (GlcNAc...) (Potential). FT CARBOHYD 297 297 N-linked (GlcNAc...) (Potential). FT CARBOHYD 329 329 N-linked (GlcNAc...) (Potential). FT CARBOHYD 365 365 N-linked (GlcNAc...) (Potential). FT CARBOHYD 457 457 N-linked (GlcNAc...) (Potential). FT CARBOHYD 711 711 N-linked (GlcNAc...) (Potential). FT DISULFID 141 154 By similarity. FT DISULFID 255 265 By similarity. FT DISULFID 259 283 By similarity. FT DISULFID 361 372 By similarity. FT DISULFID 580 637 By similarity. FT DISULFID 678 704 By similarity. FT CONFLICT 61 61 S -> T (in Ref. 1; CAA33373 and 2; FT CAA33439). FT CONFLICT 138 138 R -> G (in Ref. 1; CAA33373 and 2; FT CAA33439). FT CONFLICT 339 339 I -> V (in Ref. 1; CAA33373 and 2; FT CAA33439). FT CONFLICT 494 495 GP -> AA (in Ref. 1; CAA33373 and 2; FT CAA33439). FT CONFLICT 676 676 I -> L (in Ref. 1; CAA33373 and 2; FT CAA33439). SQ SEQUENCE 718 AA; 81182 MW; E6763BE528E2ED83 CRC64; MKLLLALAGL LAPLAMLQTS NGATPALLGE VENSVVLSCM EEAKQLVDRA YKERRESIKR SLQSGSASPT ELLFYFKQPV AGTRTAVRAA DYLHVALDLL KRKLQPLWPR PFNVTDVLTP AQLNLLSVSS GCAYQDVRVT CPPNDKYRTI TGHCNNRRSP TLGASNRAFV RWLPAEYEDG VSMPFGWTPG VNRNGFKVPL ARQVSNAIVR FPNDQLTKDQ ERALMFMQWG QFLDHDITLT PEPATRFSFF TGLNCETSCL QQPPCFPLKI PPNDPRIKNQ KDCIPFFRSC PACTRNNITI RNQINALTSF VDASGVYGSE DPLARKLRNL TNQLGLLAIN TRFQDNGRAL MPFDSLHDDP CLLTNRSARI PCFLAGDMRS SEMPELTSMH TLFVREHNRL ATQLKRLNPR WNGEKLYQEA RKIVGAMVQI ITYRDYLPLV LGPAAMKKYL PQYRSYNDSV DPRIANVFTN AFRYGHTLIQ PFMFRLNNQY RPTGPNPRVP LSKVFFASWR VVLEGGIDPI LRGLMATPAK LNRQNQIVVD EIRERLFEQV MRIGLDLPAL NMQRSRDHGL PGYNAWRRFC GLPQPSTVGE LGTVLKNLEL ARKLMAQYGT PNNIDIWMGG VSEPLEPNGR VGQLLACLIG TQFRKLRDGD RFWWENPGVF SKQQRQALAS ISLPRIICDN TGITTVSKNN IFMSNTYPRD FVSCNTLPKL NLTSWKET // ID PERT_MOUSE Reviewed; 914 AA. AC P35419; Q8C8B1; DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1994, sequence version 1. DT 19-MAR-2014, entry version 142. DE RecName: Full=Thyroid peroxidase; DE Short=TPO; DE EC=1.11.1.8; DE Flags: Precursor; GN Name=Tpo; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=C57BL/6; TISSUE=Thyroid; RX PubMed=7916704; DOI=10.1016/0378-1119(93)90141-O; RA Kotani T., Umeki K., Yamamoto I., Takeuchi M., Takechi S., RA Nakayama T., Ohtaki S.; RT "Nucleotide sequence of the cDNA encoding mouse thyroid peroxidase."; RL Gene 123:289-290(1993). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Head; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). CC -!- FUNCTION: Iodination and coupling of the hormonogenic tyrosines in CC thyroglobulin to yield the thyroid hormones T(3) and T(4). CC -!- CATALYTIC ACTIVITY: 2 iodide + H(2)O(2) + 2 H(+) = 2 iodine + 2 CC H(2)O. CC -!- CATALYTIC ACTIVITY: [Thyroglobulin]-L-tyrosine + iodide + H(2)O(2) CC = [thyroglobulin]-3-iodo-L-tyrosine + 2 H(2)O. CC -!- CATALYTIC ACTIVITY: [Thyroglobulin]-3-iodo-L-tyrosine + iodide + CC H(2)O(2) = [thyroglobulin]-3,5-diiodo-L-tyrosine + 2 H(2)O. CC -!- CATALYTIC ACTIVITY: 2 [thyroglobulin]-3,5-diiodo-L-tyrosine + CC H(2)O(2) = [thyroglobulin]-L-thyroxine + [thyroglobulin]- CC aminoacrylate + 2 H(2)O. CC -!- CATALYTIC ACTIVITY: [Thyroglobulin]-3-iodo-L-tyrosine + CC [thyroglobulin]-3,5-diiodo-L-tyrosine + H(2)O(2) = CC [thyroglobulin]-3,5,3'-triiodo-L-thyronine + [thyroglobulin]- CC aminoacrylate + 2 H(2)O. CC -!- COFACTOR: Binds 1 calcium ion per heterodimer (By similarity). CC -!- COFACTOR: Binds 1 heme B (iron-protoporphyrin IX) group covalently CC per heterodimer (By similarity). CC -!- PATHWAY: Hormone biosynthesis; thyroid hormone biosynthesis. CC -!- SUBUNIT: Interacts with DUOX1, DUOX2 and CYBA (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane CC protein (By similarity). CC -!- PTM: Heme is covalently bound through a H(2)O(2)-dependent CC autocatalytic process. Heme insertion is important for the CC delivery of protein at the cell surface (By similarity). CC -!- PTM: Cleaved in its N-terminal part (By similarity). CC -!- SIMILARITY: Belongs to the peroxidase family. XPO subfamily. CC -!- SIMILARITY: Contains 1 EGF-like domain. CC -!- SIMILARITY: Contains 1 Sushi (CCP/SCR) domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X60703; CAA43114.1; -; mRNA. DR EMBL; AK047843; BAC33171.1; -; mRNA. DR PIR; JN0550; JN0550. DR RefSeq; NP_033443.1; NM_009417.2. DR UniGene; Mm.4991; -. DR ProteinModelPortal; P35419; -. DR SMR; P35419; 143-831. DR PeroxiBase; 3345; MmTPO. DR PhosphoSite; P35419; -. DR PRIDE; P35419; -. DR DNASU; 22018; -. DR Ensembl; ENSMUST00000021005; ENSMUSP00000021005; ENSMUSG00000020673. DR GeneID; 22018; -. DR KEGG; mmu:22018; -. DR UCSC; uc007ngo.1; mouse. DR CTD; 7173; -. DR MGI; MGI:98813; Tpo. DR eggNOG; NOG262194; -. DR GeneTree; ENSGT00550000074325; -. DR HOGENOM; HOG000016084; -. DR HOVERGEN; HBG000071; -. DR InParanoid; P35419; -. DR KO; K00431; -. DR OMA; IMETSIQ; -. DR OrthoDB; EOG7D2FD6; -. DR TreeFam; TF314316; -. DR UniPathway; UPA00194; -. DR NextBio; 301744; -. DR PRO; PR:P35419; -. DR ArrayExpress; P35419; -. DR Bgee; P35419; -. DR CleanEx; MM_TPO; -. DR Genevestigator; P35419; -. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0004447; F:iodide peroxidase activity; IEA:UniProtKB-EC. DR GO; GO:0035162; P:embryonic hemopoiesis; IEA:Ensembl. DR GO; GO:0042446; P:hormone biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-KW. DR GO; GO:0006590; P:thyroid hormone generation; IEA:UniProtKB-UniPathway. DR Gene3D; 1.10.640.10; -; 2. DR InterPro; IPR000742; EG-like_dom. DR InterPro; IPR001881; EGF-like_Ca-bd_dom. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site. DR InterPro; IPR018097; EGF_Ca-bd_CS. DR InterPro; IPR010255; Haem_peroxidase. DR InterPro; IPR002007; Haem_peroxidase_animal. DR InterPro; IPR019791; Haem_peroxidase_animal_subgr. DR InterPro; IPR000436; Sushi_SCR_CCP. DR Pfam; PF03098; An_peroxidase; 1. DR Pfam; PF07645; EGF_CA; 1. DR Pfam; PF00084; Sushi; 1. DR PRINTS; PR00457; ANPEROXIDASE. DR SMART; SM00032; CCP; 1. DR SMART; SM00179; EGF_CA; 1. DR SUPFAM; SSF48113; SSF48113; 1. DR SUPFAM; SSF57535; SSF57535; 1. DR PROSITE; PS00010; ASX_HYDROXYL; 1. DR PROSITE; PS01186; EGF_2; 1. DR PROSITE; PS50026; EGF_3; 1. DR PROSITE; PS01187; EGF_CA; 1. DR PROSITE; PS00435; PEROXIDASE_1; 1. DR PROSITE; PS50292; PEROXIDASE_3; 1. DR PROSITE; PS50923; SUSHI; 1. PE 2: Evidence at transcript level; KW Calcium; Complete proteome; Disulfide bond; EGF-like domain; KW Glycoprotein; Heme; Hydrogen peroxide; Iron; Membrane; Metal-binding; KW Oxidoreductase; Peroxidase; Reference proteome; Signal; Sushi; KW Thyroid hormones biosynthesis; Transmembrane; Transmembrane helix. FT SIGNAL 1 31 Potential. FT CHAIN 32 914 Thyroid peroxidase. FT /FTId=PRO_0000023663. FT TOPO_DOM 32 834 Extracellular (Potential). FT TRANSMEM 835 859 Helical; (Potential). FT TOPO_DOM 860 914 Cytoplasmic (Potential). FT DOMAIN 728 783 Sushi. FT DOMAIN 784 827 EGF-like; calcium-binding (Potential). FT ACT_SITE 233 233 Proton acceptor (By similarity). FT METAL 234 234 Calcium (By similarity). FT METAL 313 313 Calcium (By similarity). FT METAL 315 315 Calcium; via carbonyl oxygen (By FT similarity). FT METAL 317 317 Calcium (By similarity). FT METAL 319 319 Calcium (By similarity). FT METAL 482 482 Iron (heme axial ligand) (By similarity). FT BINDING 232 232 Heme (covalent; via 2 links) (By FT similarity). FT BINDING 387 387 Heme (covalent; via 2 links) (By FT similarity). FT SITE 384 384 Transition state stabilizer (By FT similarity). FT CARBOHYD 123 123 N-linked (GlcNAc...) (Potential). FT CARBOHYD 271 271 N-linked (GlcNAc...) (Potential). FT CARBOHYD 299 299 N-linked (GlcNAc...) (Potential). FT CARBOHYD 334 334 N-linked (GlcNAc...) (Potential). FT CARBOHYD 603 603 N-linked (GlcNAc...) (Potential). FT DISULFID 136 152 By similarity. FT DISULFID 253 263 By similarity. FT DISULFID 257 278 By similarity. FT DISULFID 586 643 By similarity. FT DISULFID 684 709 By similarity. FT DISULFID 730 770 By similarity. FT DISULFID 756 782 By similarity. FT DISULFID 788 802 By similarity. FT DISULFID 796 811 By similarity. FT DISULFID 813 826 By similarity. FT CONFLICT 614 614 Y -> H (in Ref. 2; BAC33171). SQ SEQUENCE 914 AA; 101342 MW; 595E9A0B71F3DD01 CRC64; MRTLGAMAIM LVVMGTVIFL SFILRSRDIL CGKTMKSHVI SAVETSQLMV DHAVYNTMKR NLKKREVLSP AQLLSFFKLP ESTSGAISRA AEIMETSIQV MKREQSQFST DALSADILGT IANLSGCLPF MLPPRCPDTC LANKYRPITG ACNNRDHPRW GASNTALARW LPPVYEDGFS QPKGWNPNFL YHGFPLPPVR EVTRHLIQVS NEAVTEDDQY SDFLPVWGQY IDHDIALTPQ STSTAAFWGG VDCQLTCENQ NPCFPIQLPS NSSGTTACLP FYRSSAACGT GDQGALFGNL SAANPRQQMN GLTSFLDAST VYGSSPGVEK QLRNWSSSAG LLRVNTLHLD AGRAYLPFAT AACAPEPGTP RTNRTPCFLA GDGRASEVPA LAAVHTLWLR EHNRLASAFK AINKHWSANT AYQEARKVVG ALHQIITMRD YIPKILGPDA FRQYVGPYEG YNPTVNPTVS NIFSTAAFRF GHATVHPLVR RLNTDFQEHT ELPRLQLRDV FFRPWRLIQE GGLDPIVRGL LARAAKLQVQ GQLMNEELTE RLFVLSNVGT LDLASLNLQR GRDHGLPDYN EWREFCGLSR LETPAELNKA IANRSMVNKI MDLYKHADNI DVWLGGLAEK FLPGARTGPL FACIIGKQMK ALRDGDRFWW ENTNVFTDAQ RQELEKHSLP RVICDNTGLT RVPVDAFRIG KFPQDFESCE DIPSMDLELW RETFPQDDKC VFPEEVDNGN FVHCEESGKL VLVYSCFHGY KLQGQEQVTC TQKGWDSEPP VCKDVNECAD LTHPPCHPSA QCKNTKGSFQ CVCTDPYVLG EDEKTCIDSG RLPRASWVSI ALGALLIGGL ASLTWIVICR WTHADKKATL PITERVTTQS GCRKSQGRGI SPHKAAAQDT GQEPASGSRV LLCE // ID PGDH_MOUSE Reviewed; 269 AA. AC Q8VCC1; Q61106; DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2002, sequence version 1. DT 19-FEB-2014, entry version 97. DE RecName: Full=15-hydroxyprostaglandin dehydrogenase [NAD(+)]; DE Short=15-PGDH; DE EC=1.1.1.141; DE AltName: Full=Prostaglandin dehydrogenase 1; GN Name=Hpgd; Synonyms=Pgdh1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY. RC TISSUE=Lung; RX PubMed=8950170; DOI=10.1016/S0167-4781(96)00123-6; RA Matsuo M., Ensor C.M., Tai H.H.; RT "Cloning and expression of the cDNA for mouse NAD(+)-dependent 15- RT hydroxyprostaglandin dehydrogenase."; RL Biochim. Biophys. Acta 1309:21-24(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Placenta; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Colon; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: Prostaglandin inactivation. Contributes to the CC regulation of events that are under the control of prostaglandin CC levels. Catalyzes the NAD-dependent dehydrogenation of lipoxin A4 CC to form 15-oxo-lipoxin A4 (By similarity). CC -!- CATALYTIC ACTIVITY: (5Z,13E,15S)-11-alpha,15-dihydroxy-9-oxoprost- CC 5,13-dienoate + NAD(+) = (5Z,13E)-11-alpha-hydroxy-9,15- CC dioxoprost-5,13-dienoate + NADH. CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- TISSUE SPECIFICITY: Expressed in lung, intestine, stomach and CC liver. CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases CC (SDR) family. CC -!- SEQUENCE CAUTION: CC Sequence=AAB41825.1; Type=Frameshift; Positions=267; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U44389; AAB41825.1; ALT_FRAME; mRNA. DR EMBL; AK146038; BAE26850.1; -; mRNA. DR EMBL; BC021157; AAH21157.1; -; mRNA. DR RefSeq; NP_032304.2; NM_008278.2. DR UniGene; Mm.18832; -. DR ProteinModelPortal; Q8VCC1; -. DR SMR; Q8VCC1; 3-256. DR IntAct; Q8VCC1; 1. DR MINT; MINT-1855369; -. DR PhosphoSite; Q8VCC1; -. DR PaxDb; Q8VCC1; -. DR PRIDE; Q8VCC1; -. DR Ensembl; ENSMUST00000034026; ENSMUSP00000034026; ENSMUSG00000031613. DR GeneID; 15446; -. DR KEGG; mmu:15446; -. DR UCSC; uc009lso.1; mouse. DR CTD; 3248; -. DR MGI; MGI:108085; Hpgd. DR eggNOG; COG1028; -. DR GeneTree; ENSGT00710000106273; -. DR HOVERGEN; HBG107379; -. DR InParanoid; Q8VCC1; -. DR KO; K00069; -. DR OMA; IHFQNYD; -. DR OrthoDB; EOG7966HT; -. DR TreeFam; TF324093; -. DR ChiTaRS; HPGD; mouse. DR NextBio; 288244; -. DR PRO; PR:Q8VCC1; -. DR Bgee; Q8VCC1; -. DR CleanEx; MM_HPGD; -. DR Genevestigator; Q8VCC1; -. DR GO; GO:0016323; C:basolateral plasma membrane; IDA:MGI. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005634; C:nucleus; IEA:Ensembl. DR GO; GO:0016404; F:15-hydroxyprostaglandin dehydrogenase (NAD+) activity; ISS:UniProtKB. DR GO; GO:0070403; F:NAD+ binding; ISS:UniProtKB. DR GO; GO:0004957; F:prostaglandin E receptor activity; ISS:UniProtKB. DR GO; GO:0097070; P:ductus arteriosus closure; IMP:UniProtKB. DR GO; GO:0007565; P:female pregnancy; ISS:UniProtKB. DR GO; GO:0045786; P:negative regulation of cell cycle; ISS:UniProtKB. DR GO; GO:0030728; P:ovulation; ISS:UniProtKB. DR GO; GO:0007567; P:parturition; ISS:UniProtKB. DR GO; GO:0006693; P:prostaglandin metabolic process; ISS:UniProtKB. DR GO; GO:0070493; P:thrombin receptor signaling pathway; ISS:UniProtKB. DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; ISS:UniProtKB. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR002198; DH_sc/Rdtase_SDR. DR InterPro; IPR002347; Glc/ribitol_DH. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR020904; Sc_DH/Rdtase_CS. DR Pfam; PF00106; adh_short; 1. DR PRINTS; PR00081; GDHRDH. DR PRINTS; PR00080; SDRFAMILY. DR PROSITE; PS00061; ADH_SHORT; 1. PE 2: Evidence at transcript level; KW Complete proteome; Cytoplasm; Fatty acid metabolism; Lipid metabolism; KW NAD; Oxidoreductase; Prostaglandin metabolism; Reference proteome; KW Tumor suppressor. FT CHAIN 1 269 15-hydroxyprostaglandin dehydrogenase FT [NAD(+)]. FT /FTId=PRO_0000253626. FT NP_BIND 12 20 NAD (By similarity). FT NP_BIND 36 37 NAD (By similarity). FT NP_BIND 63 65 NAD (By similarity). FT NP_BIND 151 155 NAD (By similarity). FT NP_BIND 186 188 NAD (By similarity). FT ACT_SITE 151 151 Proton acceptor (By similarity). FT BINDING 91 91 NAD; via carbonyl oxygen (By similarity). FT BINDING 138 138 Substrate (By similarity). FT BINDING 148 148 Substrate (By similarity). FT CONFLICT 113 113 S -> G (in Ref. 1; AAB41825). FT CONFLICT 153 153 A -> S (in Ref. 1; AAB41825). FT CONFLICT 205 205 E -> G (in Ref. 1; AAB41825). FT CONFLICT 224 224 T -> A (in Ref. 1; AAB41825). FT CONFLICT 231 231 N -> D (in Ref. 1; AAB41825). FT CONFLICT 241 241 A -> P (in Ref. 1; AAB41825). FT CONFLICT 246 246 T -> S (in Ref. 1; AAB41825). FT CONFLICT 249 249 K -> E (in Ref. 1; AAB41825). SQ SEQUENCE 269 AA; 29181 MW; 10E879A7E31A8E34 CRC64; MHVNGKVALV TGAAQGIGKA FAEALLLHGA KVALVDWNLE AGVKCKAALD EQFEPQKTLF VQCDVADQKQ LRDTFRKVVD HFGRLDILVN NAGVNNEKNW EQTLQINLVS VISGTYLGLD YMSKQNGGEG GIIINMSSLA GLMPVAQQPV YCASKHGIIG FTRSAAMAAN LMKSGVRLNV ICPGFVDTPI LESIEKEENM GQYIEYKDQI KAMMKFYGVL HPSTIANGLI NLIEDDALNG AIMKITASKG IHFQDYDISP LLVKAPLTS // ID PGFS_MOUSE Reviewed; 201 AA. AC Q9DB60; DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 19-MAR-2014, entry version 89. DE RecName: Full=Prostamide/prostaglandin F synthase; DE Short=Prostamide/PG F synthase; DE Short=Prostamide/PGF synthase; DE EC=1.11.1.20; GN Name=Fam213b; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Cerebellum; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Eye; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE RP SPECIFICITY, AND MUTAGENESIS OF CYS-44 AND CYS-47. RX PubMed=18006499; DOI=10.1074/jbc.M705638200; RA Moriuchi H., Koda N., Okuda-Ashitaka E., Daiyasu H., Ogasawara K., RA Toh H., Ito S., Woodward D.F., Watanabe K.; RT "Molecular characterization of a novel type of RT prostamide/prostaglandin F synthase, belonging to the thioredoxin-like RT superfamily."; RL J. Biol. Chem. 283:792-801(2008). RN [5] RP TISSUE SPECIFICITY. RX PubMed=20950588; DOI=10.1016/j.brainres.2010.10.019; RA Yoshikawa K., Takei S., Hasegawa-Ishii S., Chiba Y., Furukawa A., RA Kawamura N., Hosokawa M., Woodward D.F., Watanabe K., Shimada A.; RT "Preferential localization of prostamide/prostaglandin F synthase in RT myelin sheaths of the central nervous system."; RL Brain Res. 1367:22-32(2011). CC -!- FUNCTION: Catalyzes the reduction of prostaglandin-ethanolamide CC H(2) (prostamide H(2)) to prostamide F(2alpha) with NADPH as CC proton donor. Also able to reduce prostaglandin H(2) to CC prostaglandin F(2alpha). CC -!- CATALYTIC ACTIVITY: Thioredoxin + prostaglandin H(2) = thioredoxin CC disulfide + prostaglandin F(2-alpha). CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol. CC -!- TISSUE SPECIFICITY: Mainly present in brain and spinal cord. In CC spinal cord, present in the superficial layer of the dorsal horn, CC in motor neurons of the ventral horn and in glia of the white CC matter of the spinal cord. In brain, expressed preferentially in CC the white matter bundles of the entire CNS of adult with less CC marked expression in neuronal cell bodies. Colocalizes with MBP in CC myelin sheaths but not in axons. Localizes to myelin sheaths (at CC protein level). CC -!- SIMILARITY: Belongs to the peroxiredoxin-like FAM213 family. CC Prostamide/prostaglandin F synthase subfamily. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK005188; BAB23870.1; -; mRNA. DR EMBL; AL607032; CAM15790.1; -; Genomic_DNA. DR EMBL; BC030453; AAH30453.1; -; mRNA. DR RefSeq; NP_079858.2; NM_025582.3. DR UniGene; Mm.41868; -. DR ProteinModelPortal; Q9DB60; -. DR PhosphoSite; Q9DB60; -. DR PaxDb; Q9DB60; -. DR PRIDE; Q9DB60; -. DR DNASU; 66469; -. DR Ensembl; ENSMUST00000030935; ENSMUSP00000030935; ENSMUSG00000029059. DR GeneID; 66469; -. DR KEGG; mmu:66469; -. DR UCSC; uc008wch.1; mouse. DR CTD; 127281; -. DR MGI; MGI:1913719; Fam213b. DR eggNOG; NOG276778; -. DR GeneTree; ENSGT00530000063724; -. DR HOVERGEN; HBG106494; -. DR InParanoid; Q9DB60; -. DR KO; K15717; -. DR OMA; DEEVCGR; -. DR OrthoDB; EOG7WDN4D; -. DR TreeFam; TF313804; -. DR Reactome; REACT_188937; Metabolism. DR NextBio; 321782; -. DR PRO; PR:Q9DB60; -. DR ArrayExpress; Q9DB60; -. DR Bgee; Q9DB60; -. DR CleanEx; MM_2810405K02RIK; -. DR Genevestigator; Q9DB60; -. DR GO; GO:0005829; C:cytosol; IDA:MGI. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProt. DR GO; GO:0043209; C:myelin sheath; IDA:UniProt. DR GO; GO:0047017; F:prostaglandin-F synthase activity; IMP:UniProt. DR GO; GO:0001516; P:prostaglandin biosynthetic process; IDA:UniProtKB. DR InterPro; IPR012336; Thioredoxin-like_fold. DR SUPFAM; SSF52833; SSF52833; 1. PE 1: Evidence at protein level; KW Complete proteome; Cytoplasm; Fatty acid biosynthesis; KW Fatty acid metabolism; Lipid biosynthesis; Lipid metabolism; NADP; KW Oxidoreductase; Prostaglandin biosynthesis; Prostaglandin metabolism; KW Reference proteome. FT CHAIN 1 201 Prostamide/prostaglandin F synthase. FT /FTId=PRO_0000284638. FT MUTAGEN 44 44 C->S: Almost abolishes enzyme activity. FT MUTAGEN 47 47 C->S: Decreased enzyme activity to retain FT 63% of wild type activity. SQ SEQUENCE 201 AA; 21670 MW; 4F392EF111AC6B42 CRC64; MNVVDLGRVG ACVLKHAVTG EAVELRSLWQ EKACVVAGLR RFGCMVCRWI AQDLSNLRSI LDQHDVRLVG VGPEALGLQE FLDGGYFSGE LYLDESKQIY KELGFKRYNS LSILPAALGK PVRDVASKAK AVGIQGNLSG DLLQSGGLLV VSKGGDKVLL HFIQKSPGDY VPQENILQAL GISAEVCSSK PPQCDEEVCG R // ID PGH1_MOUSE Reviewed; 602 AA. AC P22437; DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1991, sequence version 1. DT 19-MAR-2014, entry version 146. DE RecName: Full=Prostaglandin G/H synthase 1; DE EC=1.14.99.1; DE AltName: Full=Cyclooxygenase-1; DE Short=COX-1; DE AltName: Full=Prostaglandin H2 synthase 1; DE Short=PGH synthase 1; DE Short=PGHS-1; DE Short=PHS 1; DE AltName: Full=Prostaglandin-endoperoxide synthase 1; DE Flags: Precursor; GN Name=Ptgs1; Synonyms=Cox-1, Cox1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=2108169; RA Dewitt D.L., El-Harith E.A., Kraemer S.A., Andrews M.J., Yao E.F., RA Armstrong R.L., Smith W.L.; RT "The aspirin and heme-binding sites of ovine and murine prostaglandin RT endoperoxide synthases."; RL J. Biol. Chem. 265:5192-5198(1990). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Mammary gland; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: May play an important role in regulating or promoting CC cell proliferation in some normal and neoplastically transformed CC cells. CC -!- CATALYTIC ACTIVITY: Arachidonate + AH(2) + 2 O(2) = prostaglandin CC H(2) + A + H(2)O. CC -!- COFACTOR: Binds 1 heme B (iron-protoporphyrin IX) group per CC subunit (By similarity). CC -!- PATHWAY: Lipid metabolism; prostaglandin biosynthesis. CC -!- SUBUNIT: Homodimer. CC -!- SUBCELLULAR LOCATION: Microsome membrane; Peripheral membrane CC protein. Endoplasmic reticulum membrane; Peripheral membrane CC protein. CC -!- MISCELLANEOUS: This enzyme acts both as a dioxygenase and as a CC peroxidase. CC -!- MISCELLANEOUS: This enzyme is the target of nonsteroidal anti- CC inflammatory drugs such as aspirin. CC -!- SIMILARITY: Belongs to the prostaglandin G/H synthase family. CC -!- SIMILARITY: Contains 1 EGF-like domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M34141; AAA39913.1; -; mRNA. DR EMBL; BC005573; AAH05573.1; -; mRNA. DR PIR; A35564; A35564. DR RefSeq; NP_032995.1; NM_008969.3. DR RefSeq; XP_006497853.1; XM_006497790.1. DR RefSeq; XP_006497854.1; XM_006497791.1. DR RefSeq; XP_006497855.1; XM_006497792.1. DR RefSeq; XP_006497856.1; XM_006497793.1. DR UniGene; Mm.275434; -. DR ProteinModelPortal; P22437; -. DR SMR; P22437; 34-586. DR BioGrid; 202462; 2. DR IntAct; P22437; 3. DR MINT; MINT-4107353; -. DR BindingDB; P22437; -. DR ChEMBL; CHEMBL2649; -. DR PeroxiBase; 3361; MmPGHS01. DR PhosphoSite; P22437; -. DR PaxDb; P22437; -. DR PRIDE; P22437; -. DR Ensembl; ENSMUST00000062069; ENSMUSP00000059977; ENSMUSG00000047250. DR GeneID; 19224; -. DR KEGG; mmu:19224; -. DR UCSC; uc008jll.1; mouse. DR CTD; 5742; -. DR MGI; MGI:97797; Ptgs1. DR eggNOG; NOG39991; -. DR HOGENOM; HOG000013149; -. DR HOVERGEN; HBG000366; -. DR InParanoid; P22437; -. DR KO; K00509; -. DR OMA; FKTSGKM; -. DR OrthoDB; EOG7RFTHC; -. DR TreeFam; TF329675; -. DR UniPathway; UPA00662; -. DR NextBio; 296008; -. DR PRO; PR:P22437; -. DR ArrayExpress; P22437; -. DR Bgee; P22437; -. DR CleanEx; MM_PTGS1; -. DR Genevestigator; P22437; -. DR GO; GO:0005737; C:cytoplasm; IDA:MGI. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0001750; C:photoreceptor outer segment; IDA:MGI. DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW. DR GO; GO:0004666; F:prostaglandin-endoperoxide synthase activity; IEA:UniProtKB-EC. DR GO; GO:0019371; P:cyclooxygenase pathway; IEA:Ensembl. DR GO; GO:0030216; P:keratinocyte differentiation; NAS:UniProtKB. DR GO; GO:0001516; P:prostaglandin biosynthetic process; IMP:MGI. DR GO; GO:0008217; P:regulation of blood pressure; IMP:MGI. DR GO; GO:0042127; P:regulation of cell proliferation; IGI:MGI. DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro. DR Gene3D; 1.10.640.10; -; 1. DR InterPro; IPR000742; EG-like_dom. DR InterPro; IPR010255; Haem_peroxidase. DR InterPro; IPR002007; Haem_peroxidase_animal. DR InterPro; IPR019791; Haem_peroxidase_animal_subgr. DR Pfam; PF03098; An_peroxidase; 2. DR PRINTS; PR00457; ANPEROXIDASE. DR SMART; SM00181; EGF; 1. DR SUPFAM; SSF48113; SSF48113; 1. DR PROSITE; PS50026; EGF_3; 1. DR PROSITE; PS50292; PEROXIDASE_3; 1. PE 2: Evidence at transcript level; KW Complete proteome; Dioxygenase; Disulfide bond; EGF-like domain; KW Endoplasmic reticulum; Fatty acid biosynthesis; Fatty acid metabolism; KW Glycoprotein; Heme; Iron; Lipid biosynthesis; Lipid metabolism; KW Membrane; Metal-binding; Microsome; Oxidoreductase; Peroxidase; KW Prostaglandin biosynthesis; Prostaglandin metabolism; KW Reference proteome; Signal. FT SIGNAL 1 26 FT CHAIN 27 602 Prostaglandin G/H synthase 1. FT /FTId=PRO_0000023869. FT DOMAIN 34 72 EGF-like. FT ACT_SITE 209 209 Proton acceptor (By similarity). FT ACT_SITE 387 387 For cyclooxygenase activity (By FT similarity). FT METAL 390 390 Iron (heme axial ligand) (By similarity). FT SITE 532 532 Aspirin-acetylated serine. FT CARBOHYD 70 70 N-linked (GlcNAc...) (Potential). FT CARBOHYD 106 106 N-linked (GlcNAc...) (Potential). FT CARBOHYD 146 146 N-linked (GlcNAc...) (Potential). FT DISULFID 38 49 By similarity. FT DISULFID 39 161 By similarity. FT DISULFID 43 59 By similarity. FT DISULFID 61 71 By similarity. FT DISULFID 571 577 By similarity. SQ SEQUENCE 602 AA; 69042 MW; 634C0E602045C3A0 CRC64; MSRRSLSLWF PLLLLLLLPP TPSVLLADPG VPSPVNPCCY YPCQNQGVCV RFGLDNYQCD CTRTGYSGPN CTIPEIWTWL RNSLRPSPSF THFLLTHGYW LWEFVNATFI REVLMRLVLT VRSNLIPSPP TYNSAHDYIS WESFSNVSYY TRILPSVPKD CPTPMGTKGK KQLPDVQLLA QQLLLRREFI PAPQGTNILF AFFAQHFTHQ FFKTSGKMGP GFTKALGHGV DLGHIYGDNL ERQYHLRLFK DGKLKYQVLD GEVYPPSVEQ ASVLMRYPPG VPPERQMAVG QEVFGLLPGL MLFSTIWLRE HNRVCDLLKE EHPTWDDEQL FQTTRLILIG ETIKIVIEEY VQHLSGYFLQ LKFDPELLFR AQFQYRNRIA MEFNHLYHWH PLMPNSFQVG SQEYSYEQFL FNTSMLVDYG VEALVDAFSR QRAGRIGGGR NFDYHVLHVA VDVIKESREM RLQPFNEYRK RFGLKPYTSF QELTGEKEMA AELEELYGDI DALEFYPGLL LEKCQPNSIF GESMIEMGAP FSLKGLLGNP ICSPEYWKPS TFGGDVGFNL VNTASLKKLV CLNTKTCPYV SFRVPDYPGD DGSVLVRRST EL // ID PGH2_MOUSE Reviewed; 604 AA. AC Q05769; Q543K3; DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1994, sequence version 1. DT 19-MAR-2014, entry version 155. DE RecName: Full=Prostaglandin G/H synthase 2; DE EC=1.14.99.1; DE AltName: Full=Cyclooxygenase-2; DE Short=COX-2; DE AltName: Full=Glucocorticoid-regulated inflammatory cyclooxygenase; DE AltName: Full=Gripghs; DE AltName: Full=Macrophage activation-associated marker protein P71/73; DE AltName: Full=PES-2; DE AltName: Full=PHS II; DE AltName: Full=Prostaglandin H2 synthase 2; DE Short=PGH synthase 2; DE Short=PGHS-2; DE AltName: Full=Prostaglandin-endoperoxide synthase 2; DE AltName: Full=TIS10 protein; DE Flags: Precursor; GN Name=Ptgs2; Synonyms=Cox-2, Cox2, Pghs-b, Tis10; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=Swiss; RX PubMed=1712772; RA Kujubu D.A., Fletcher B.S., Varnum B.C., Lim R.W., Herschman H.R.; RT "TIS10, a phorbol ester tumor promoter-inducible mRNA from Swiss 3T3 RT cells, encodes a novel prostaglandin synthase/cyclooxygenase RT homologue."; RL J. Biol. Chem. 266:12866-12872(1991). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=1339449; RA Fletcher B.S., Kujubu D.A., Perrin D.M., Herschman H.R.; RT "Structure of the mitogen-inducible TIS10 gene and demonstration that RT the TIS10-encoded protein is a functional prostaglandin G/H RT synthase."; RL J. Biol. Chem. 267:4338-4344(1992). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=1419907; RA Ryseck R.-P., Raynoschek C., Macdonald-Bravo H., Dorfman K., RA Mattei M.-G., Bravo R.; RT "Identification of an immediate early gene, pghs-B, whose protein RT product has prostaglandin synthase/cyclooxygenase activity."; RL Cell Growth Differ. 3:443-450(1992). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=1594589; DOI=10.1073/pnas.89.11.4888; RA O'Banion M.K., Winn V.D., Young D.A.; RT "cDNA cloning and functional activity of a glucocorticoid-regulated RT inflammatory cyclooxygenase."; RL Proc. Natl. Acad. Sci. U.S.A. 89:4888-4892(1992). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J, and NOD; RC TISSUE=Hippocampus, Mammary gland, and Spleen; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [MRNA] OF 281-360. RX PubMed=1744122; RA O'Banion M.K., Sadowski H.B., Winn V., Young D.A.; RT "A serum- and glucocorticoid-regulated 4-kilobase mRNA encodes a RT cyclooxygenase-related protein."; RL J. Biol. Chem. 266:23261-23267(1991). RN [8] RP PARTIAL PROTEIN SEQUENCE. RX PubMed=8482922; RA Phillips T.A., Kujubu D.A., Mackay R.J., Herschman H.R., Russell S.W., RA Pace J.L.; RT "The mouse macrophage activation-associated marker protein, p71/73, is RT an inducible prostaglandin endoperoxide synthase (cyclooxygenase)."; RL J. Leukoc. Biol. 53:411-419(1993). RN [9] RP GLYCOSYLATION AT ASN-53; ASN-130; ASN-396 AND ASN-580, AND ABSENCE OF RP GLYCOSYLATION AT ASN-592. RX PubMed=8349699; RA Otto J.C., Dewitt D.L., Smith W.L.; RT "N-glycosylation of prostaglandin endoperoxide synthases-1 and -2 and RT their orientations in the endoplasmic reticulum."; RL J. Biol. Chem. 268:18234-18242(1993). RN [10] RP FUNCTION IN INTESTINAL WOUND REPAIR, TISSUE SPECIFICITY, DEVELOPMENTAL RP STAGE, AND DISRUPTION PHENOTYPE. RX PubMed=22465430; DOI=10.1053/j.gastro.2012.03.037; RA Manieri N.A., Drylewicz M.R., Miyoshi H., Stappenbeck T.S.; RT "Igf2bp1 is required for full induction of Ptgs2 mRNA in colonic RT mesenchymal stem cells in mice."; RL Gastroenterology 143:110-121(2012). RN [11] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH RP (S)-FLURBIPROFEN; INDOMETHACIN; HEME AND RP 1-PHENYLSULFONAMIDE-3-TRIFLUOROMETHYL-5-PARABROMOPHENYLPYRAZOLE, RP COFACTOR, AND GLYCOSYLATION AT ASN-53; ASN-130 AND ASN-396. RX PubMed=8967954; DOI=10.1038/384644a0; RA Kurumbail R.G., Stevens A.M., Gierse J.K., McDonald J.J., RA Stegeman R.A., Pay J.Y., Gildehaus D., Miyashiro J.M., Penning T.D., RA Seibert K., Isakson P.C., Stallings W.C.; RT "Structural basis for selective inhibition of cyclooxygenase-2 by RT anti-inflammatory agents."; RL Nature 384:644-648(1996). RN [12] RP ERRATUM. RA Kurumbail R.G., Stevens A.M., Gierse J.K., McDonald J.J., RA Stegeman R.A., Pay J.Y., Gildehaus D., Miyashiro J.M., Penning T.D., RA Seibert K., Isakson P.C., Stallings W.C.; RL Nature 385:555-555(1997). RN [13] RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 18-569 IN COMPLEX WITH RP ARACHIDONIC ACID, AND GLYCOSYLATION AT ASN-53; ASN-130 AND ASN-396. RX PubMed=10811226; DOI=10.1038/35011103; RA Kiefer J.R., Pawlitz J.L., Moreland K.T., Stegeman R.A., Hood W.F., RA Gierse J.K., Stevens A.M., Goodwin D.C., Rowlinson S.W., Marnett L.J., RA Stallings W.C., Kurumbail R.G.; RT "Structural insights into the stereochemistry of the cyclooxygenase RT reaction."; RL Nature 405:97-101(2000). RN [14] RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) IN COMPLEX WITH HEME AND RP DICLOFENAC, CATALYTIC ACTIVITY, FUNCTION, COFACTOR, DISULFIDE BONDS, RP ENZYME REGULATION, AND GLYCOSYLATION AT ASN-53; ASN-130 AND ASN-396. RX PubMed=12925531; DOI=10.1074/jbc.M305481200; RA Rowlinson S.W., Kiefer J.R., Prusakiewicz J.J., Pawlitz J.L., RA Kozak K.R., Kalgutkar A.S., Stallings W.C., Kurumbail R.G., RA Marnett L.J.; RT "A novel mechanism of cyclooxygenase-2 inhibition involving RT interactions with Ser-530 and Tyr-385."; RL J. Biol. Chem. 278:45763-45769(2003). RN [15] RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 20-604 IN COMPLEX WITH HEME; RP ACRYLIC ACID; ARACHIDONIC ACID AND DOCOSAHEXAENOIC ACID, CATALYTIC RP ACTIVITY, ACTIVE SITE, SUBUNIT, COFACTOR, FUNCTION, DISULFIDE BONDS, RP MUTAGENESIS OF LEU-517 AND ASN-580, AND GLYCOSYLATION AT ASN-53; RP ASN-130; ASN-396 AND ASN-580. RX PubMed=20463020; DOI=10.1074/jbc.M110.119867; RA Vecchio A.J., Simmons D.M., Malkowski M.G.; RT "Structural basis of fatty acid substrate binding to cyclooxygenase- RT 2."; RL J. Biol. Chem. 285:22152-22163(2010). RN [16] RP X-RAY CRYSTALLOGRAPHY (1.73 ANGSTROMS) OF 18-604 IN COMPLEXES WITH RP HEME AND NAPROXEN ANALOGS, FUNCTION, CATALYTIC ACTIVITY, ENZYME RP REGULATION, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-53; ASN-130 AND RP ASN-396. RX PubMed=20810665; DOI=10.1074/jbc.M110.162982; RA Duggan K.C., Walters M.J., Musee J., Harp J.M., Kiefer J.R., RA Oates J.A., Marnett L.J.; RT "Molecular basis for cyclooxygenase inhibition by the non-steroidal RT anti-inflammatory drug naproxen."; RL J. Biol. Chem. 285:34950-34959(2010). RN [17] RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 20-599 IN COMPLEX WITH HEME; RP ACRYLIC ACID AND ARACHIDONIC ACID, FUNCTION, CATALYTIC ACTIVITY, AND RP GLYCOSYLATION AT ASN-53; ASN-130 AND ASN-396. RX PubMed=21489986; DOI=10.1074/jbc.M111.230367; RA Vecchio A.J., Malkowski M.G.; RT "The structural basis of endocannabinoid oxygenation by RT cyclooxygenase-2."; RL J. Biol. Chem. 286:20736-20745(2011). CC -!- FUNCTION: Mediates the formation of prostaglandins from CC arachidonate. May have a role as a major mediator of inflammation CC and/or a role for prostanoid signaling in activity-dependent CC plasticity. Critical component of colonic mucosal wound repair. CC -!- CATALYTIC ACTIVITY: Arachidonate + AH(2) + 2 O(2) = prostaglandin CC H(2) + A + H(2)O. CC -!- COFACTOR: Binds 1 heme B (iron-protoporphyrin IX) group per CC subunit. CC -!- ENZYME REGULATION: Inhibited by the nonsteroidal anti-inflammatory CC drugs aspirin, naproxen, diclofenac, meclofenamic acid, CC indomethacin and their analogs. CC -!- PATHWAY: Lipid metabolism; prostaglandin biosynthesis. CC -!- SUBUNIT: Homodimer. CC -!- SUBCELLULAR LOCATION: Microsome membrane; Peripheral membrane CC protein. Endoplasmic reticulum membrane; Peripheral membrane CC protein. CC -!- TISSUE SPECIFICITY: Following colon injury, expressed in the wound CC bed mesenchyme during the first phase of repair, probably by CC colonic mesenchymal stem cells (at protein level). CC -!- DEVELOPMENTAL STAGE: During colonic wound repair, highly up- CC regulated (more than 1600-fold) in the mesenchyme of the wound bed CC 2 days after injury as compared to uninjured mucosa. Further CC increase in expression is observed at day 4 following injury CC (close to 2200-fold). Down-regulated at day 6 (only 93-fold CC increase as compared to uninjured mucosa). CC -!- INDUCTION: By cytokines and mitogens. CC -!- PTM: S-nitrosylation by NOS2 (iNOS) activates enzyme activity. S- CC nitrosylation may take place on different Cys residues in addition CC to Cys-561 (By similarity). CC -!- DISRUPTION PHENOTYPE: Mutant mice exhibit defects in colonic CC mucosal wound repair. CC -!- MISCELLANEOUS: Acts both as a dioxygenase and as a peroxidase. CC -!- MISCELLANEOUS: Target of nonsteroidal anti-inflammatory drugs, CC such as aspirin. CC -!- SIMILARITY: Belongs to the prostaglandin G/H synthase family. CC -!- SIMILARITY: Contains 1 EGF-like domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M64291; AAA39924.1; -; mRNA. DR EMBL; M94967; AAA39918.1; -; mRNA. DR EMBL; M82866; AAA40448.1; -; Genomic_DNA. DR EMBL; M82862; AAA40448.1; JOINED; Genomic_DNA. DR EMBL; M82863; AAA40448.1; JOINED; Genomic_DNA. DR EMBL; M82864; AAA40448.1; JOINED; Genomic_DNA. DR EMBL; M82865; AAA40448.1; JOINED; Genomic_DNA. DR EMBL; M88242; AAA37740.1; -; mRNA. DR EMBL; AK049923; BAC33986.1; -; mRNA. DR EMBL; AK144956; BAE26154.1; -; mRNA. DR EMBL; AK166221; BAE38639.1; -; mRNA. DR EMBL; AK172161; BAE42855.1; -; mRNA. DR EMBL; CH466520; EDL39487.1; -; Genomic_DNA. DR PIR; A49010; A49010. DR RefSeq; NP_035328.2; NM_011198.3. DR UniGene; Mm.292547; -. DR PDB; 1CVU; X-ray; 2.40 A; A/B=18-569. DR PDB; 1CX2; X-ray; 3.00 A; A/B/C/D=18-604. DR PDB; 1DCX; Model; -; A/B=18-569. DR PDB; 1DD0; Model; -; A/B=18-569. DR PDB; 1DDX; X-ray; 3.00 A; A/B/C/D=18-569. DR PDB; 1PXX; X-ray; 2.90 A; A/B/C/D=1-604. DR PDB; 3HS5; X-ray; 2.10 A; A/B=20-604. DR PDB; 3HS6; X-ray; 2.40 A; A/B=20-604. DR PDB; 3HS7; X-ray; 2.65 A; A/B=20-604. DR PDB; 3KRK; X-ray; 2.40 A; A/B=20-604. DR PDB; 3LN0; X-ray; 2.20 A; A/B/C/D=18-604. DR PDB; 3LN1; X-ray; 2.40 A; A/B/C/D=18-604. DR PDB; 3MDL; X-ray; 2.20 A; A/B=20-599. DR PDB; 3MQE; X-ray; 2.80 A; A/B/C/D=18-604. DR PDB; 3NT1; X-ray; 1.73 A; A/B=18-604. DR PDB; 3NTB; X-ray; 2.27 A; A/B/C/D=18-604. DR PDB; 3NTG; X-ray; 2.19 A; A/B/C/D=18-569. DR PDB; 3OLT; X-ray; 2.45 A; A/B=20-604. DR PDB; 3OLU; X-ray; 2.35 A; A/B=20-604. DR PDB; 3PGH; X-ray; 2.50 A; A/B/C/D=18-604. DR PDB; 3Q7D; X-ray; 2.40 A; A/B=18-604. DR PDB; 3QH0; X-ray; 2.10 A; A/B=1-604. DR PDB; 3QMO; X-ray; 3.00 A; A/B=1-604. DR PDB; 3RR3; X-ray; 2.84 A; A/B/C/D=18-577. DR PDB; 3TZI; X-ray; 2.15 A; A/B=20-604. DR PDB; 4COX; X-ray; 2.90 A; A/B/C/D=18-604. DR PDB; 4E1G; X-ray; 2.10 A; A/B=1-604. DR PDB; 4FM5; X-ray; 2.81 A; A/B/C/D=1-604. DR PDB; 4LLZ; X-ray; 2.35 A; A/B=18-604. DR PDB; 4M10; X-ray; 2.01 A; A/B/C/D=18-604. DR PDB; 4M11; X-ray; 2.45 A; A/B/C/D=18-569. DR PDB; 5COX; X-ray; 3.00 A; A/B/C/D=18-604. DR PDB; 6COX; X-ray; 2.80 A; A/B=18-604. DR PDBsum; 1CVU; -. DR PDBsum; 1CX2; -. DR PDBsum; 1DCX; -. DR PDBsum; 1DD0; -. DR PDBsum; 1DDX; -. DR PDBsum; 1PXX; -. DR PDBsum; 3HS5; -. DR PDBsum; 3HS6; -. DR PDBsum; 3HS7; -. DR PDBsum; 3KRK; -. DR PDBsum; 3LN0; -. DR PDBsum; 3LN1; -. DR PDBsum; 3MDL; -. DR PDBsum; 3MQE; -. DR PDBsum; 3NT1; -. DR PDBsum; 3NTB; -. DR PDBsum; 3NTG; -. DR PDBsum; 3OLT; -. DR PDBsum; 3OLU; -. DR PDBsum; 3PGH; -. DR PDBsum; 3Q7D; -. DR PDBsum; 3QH0; -. DR PDBsum; 3QMO; -. DR PDBsum; 3RR3; -. DR PDBsum; 3TZI; -. DR PDBsum; 4COX; -. DR PDBsum; 4E1G; -. DR PDBsum; 4FM5; -. DR PDBsum; 4LLZ; -. DR PDBsum; 4M10; -. DR PDBsum; 4M11; -. DR PDBsum; 5COX; -. DR PDBsum; 6COX; -. DR ProteinModelPortal; Q05769; -. DR SMR; Q05769; 18-569. DR BioGrid; 202463; 5. DR DIP; DIP-31082N; -. DR IntAct; Q05769; 1. DR BindingDB; Q05769; -. DR ChEMBL; CHEMBL4321; -. DR PeroxiBase; 3360; MmPGHS02. DR PhosphoSite; Q05769; -. DR UniCarbKB; Q05769; -. DR PaxDb; Q05769; -. DR PRIDE; Q05769; -. DR Ensembl; ENSMUST00000035065; ENSMUSP00000035065; ENSMUSG00000032487. DR GeneID; 19225; -. DR KEGG; mmu:19225; -. DR UCSC; uc007cxv.1; mouse. DR CTD; 5743; -. DR MGI; MGI:97798; Ptgs2. DR eggNOG; NOG39991; -. DR GeneTree; ENSGT00390000010743; -. DR HOGENOM; HOG000013149; -. DR HOVERGEN; HBG000366; -. DR InParanoid; Q05769; -. DR KO; K11987; -. DR OMA; ICNNVKG; -. DR OrthoDB; EOG7RFTHC; -. DR TreeFam; TF329675; -. DR UniPathway; UPA00662; -. DR EvolutionaryTrace; Q05769; -. DR NextBio; 296012; -. DR PRO; PR:Q05769; -. DR Bgee; Q05769; -. DR CleanEx; MM_PTGS2; -. DR Genevestigator; Q05769; -. DR GO; GO:0005737; C:cytoplasm; IDA:MGI. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0043005; C:neuron projection; IDA:MGI. DR GO; GO:0043234; C:protein complex; IEA:Ensembl. DR GO; GO:0020037; F:heme binding; IDA:UniProtKB. DR GO; GO:0008289; F:lipid binding; IEA:Ensembl. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0016702; F:oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen; IEA:Ensembl. DR GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW. DR GO; GO:0004666; F:prostaglandin-endoperoxide synthase activity; IDA:UniProtKB. DR GO; GO:0042640; P:anagen; IMP:MGI. DR GO; GO:0001525; P:angiogenesis; IEA:Ensembl. DR GO; GO:0030282; P:bone mineralization; ISO:MGI. DR GO; GO:0050873; P:brown fat cell differentiation; IMP:BHF-UCL. DR GO; GO:0071318; P:cellular response to ATP; IEA:Ensembl. DR GO; GO:0071456; P:cellular response to hypoxia; IEA:Ensembl. DR GO; GO:0071260; P:cellular response to mechanical stimulus; IEA:Ensembl. DR GO; GO:0034644; P:cellular response to UV; IEA:Ensembl. DR GO; GO:0019371; P:cyclooxygenase pathway; IDA:UniProtKB. DR GO; GO:0046697; P:decidualization; IEA:Ensembl. DR GO; GO:0007566; P:embryo implantation; IEA:Ensembl. DR GO; GO:0006954; P:inflammatory response; IEA:Ensembl. DR GO; GO:0030216; P:keratinocyte differentiation; NAS:UniProtKB. DR GO; GO:0007612; P:learning; IEA:Ensembl. DR GO; GO:0035633; P:maintenance of blood-brain barrier; IEA:Ensembl. DR GO; GO:0007613; P:memory; IEA:Ensembl. DR GO; GO:0051926; P:negative regulation of calcium ion transport; IEA:Ensembl. DR GO; GO:0045786; P:negative regulation of cell cycle; IEA:Ensembl. DR GO; GO:0008285; P:negative regulation of cell proliferation; IEA:Ensembl. DR GO; GO:0045986; P:negative regulation of smooth muscle contraction; IEA:Ensembl. DR GO; GO:0032227; P:negative regulation of synaptic transmission, dopaminergic; IEA:Ensembl. DR GO; GO:0030728; P:ovulation; IEA:Ensembl. DR GO; GO:0043065; P:positive regulation of apoptotic process; IEA:Ensembl. DR GO; GO:0090336; P:positive regulation of brown fat cell differentiation; IMP:BHF-UCL. DR GO; GO:0090050; P:positive regulation of cell migration involved in sprouting angiogenesis; IEA:Ensembl. DR GO; GO:0031622; P:positive regulation of fever generation; IDA:BHF-UCL. DR GO; GO:0090271; P:positive regulation of fibroblast growth factor production; IEA:Ensembl. DR GO; GO:0042346; P:positive regulation of NF-kappaB import into nucleus; IEA:Ensembl. DR GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; IEA:Ensembl. DR GO; GO:0090362; P:positive regulation of platelet-derived growth factor production; IEA:Ensembl. DR GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; IEA:Ensembl. DR GO; GO:0045987; P:positive regulation of smooth muscle contraction; IEA:Ensembl. DR GO; GO:0031915; P:positive regulation of synaptic plasticity; IEA:Ensembl. DR GO; GO:0051968; P:positive regulation of synaptic transmission, glutamatergic; IEA:Ensembl. DR GO; GO:0071636; P:positive regulation of transforming growth factor beta production; IEA:Ensembl. DR GO; GO:0045907; P:positive regulation of vasoconstriction; IEA:Ensembl. DR GO; GO:0010575; P:positive regulation vascular endothelial growth factor production; IEA:Ensembl. DR GO; GO:0008217; P:regulation of blood pressure; IMP:MGI. DR GO; GO:0042127; P:regulation of cell proliferation; IGI:MGI. DR GO; GO:0042493; P:response to drug; IEA:Ensembl. DR GO; GO:0032355; P:response to estradiol; IEA:Ensembl. DR GO; GO:0070542; P:response to fatty acid; IEA:Ensembl. DR GO; GO:0009750; P:response to fructose; IEA:Ensembl. DR GO; GO:0051384; P:response to glucocorticoid; IEA:Ensembl. DR GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl. DR GO; GO:0010226; P:response to lithium ion; IEA:Ensembl. DR GO; GO:0010042; P:response to manganese ion; IEA:Ensembl. DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro. DR GO; GO:0034612; P:response to tumor necrosis factor; IEA:Ensembl. DR GO; GO:0033280; P:response to vitamin D; IEA:Ensembl. DR GO; GO:0019233; P:sensory perception of pain; IEA:Ensembl. DR Gene3D; 1.10.640.10; -; 1. DR InterPro; IPR000742; EG-like_dom. DR InterPro; IPR010255; Haem_peroxidase. DR InterPro; IPR002007; Haem_peroxidase_animal. DR InterPro; IPR019791; Haem_peroxidase_animal_subgr. DR Pfam; PF03098; An_peroxidase; 2. DR PRINTS; PR00457; ANPEROXIDASE. DR SMART; SM00181; EGF; 1. DR SUPFAM; SSF48113; SSF48113; 1. DR PROSITE; PS50026; EGF_3; 1. DR PROSITE; PS50292; PEROXIDASE_3; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Dioxygenase; KW Direct protein sequencing; Disulfide bond; Endoplasmic reticulum; KW Fatty acid biosynthesis; Fatty acid metabolism; Glycoprotein; Heme; KW Iron; Lipid biosynthesis; Lipid metabolism; Membrane; Metal-binding; KW Microsome; Oxidoreductase; Peroxidase; Prostaglandin biosynthesis; KW Prostaglandin metabolism; Reference proteome; Signal. FT SIGNAL 1 17 FT CHAIN 18 604 Prostaglandin G/H synthase 2. FT /FTId=PRO_0000023876. FT DOMAIN 18 55 EGF-like. FT ACT_SITE 193 193 Proton acceptor. FT ACT_SITE 371 371 For cyclooxygenase activity. FT METAL 374 374 Iron (heme axial ligand). FT BINDING 106 106 Substrate. FT BINDING 341 341 Substrate. FT BINDING 371 371 Substrate. FT SITE 516 516 Aspirin-acetylated serine. FT SITE 592 592 Not glycosylated. FT CARBOHYD 53 53 N-linked (GlcNAc...). FT /FTId=CAR_000222. FT CARBOHYD 130 130 N-linked (GlcNAc...). FT /FTId=CAR_000223. FT CARBOHYD 396 396 N-linked (GlcNAc...). FT /FTId=CAR_000224. FT CARBOHYD 580 580 N-linked (GlcNAc...). FT /FTId=CAR_000225. FT DISULFID 21 32 FT DISULFID 22 145 FT DISULFID 26 42 FT DISULFID 44 54 FT DISULFID 555 561 FT MUTAGEN 517 517 L->A,F,P,T: Slightly reduced activity. FT MUTAGEN 580 580 N->A: Loss of glycosylation site. FT CONFLICT 98 98 I -> T (in Ref. 1; AAA39924). FT CONFLICT 142 142 A -> R (in Ref. 3; AAA39918). FT CONFLICT 301 301 I -> L (in Ref. 7; no nucleotide entry). FT CONFLICT 585 585 H -> R (in Ref. 3; AAA39918). FT TURN 20 23 FT HELIX 27 29 FT STRAND 31 36 FT STRAND 39 43 FT STRAND 47 50 FT TURN 51 54 FT HELIX 59 67 FT HELIX 71 78 FT HELIX 82 89 FT HELIX 92 107 FT STRAND 117 119 FT STRAND 120 122 FT HELIX 125 129 FT STRAND 131 133 FT STRAND 135 138 FT STRAND 145 147 FT STRAND 150 153 FT HELIX 160 167 FT HELIX 182 192 FT TURN 193 195 FT TURN 200 202 FT STRAND 206 208 FT STRAND 213 215 FT HELIX 217 220 FT HELIX 224 230 FT STRAND 241 243 FT STRAND 246 248 FT HELIX 252 255 FT STRAND 263 265 FT HELIX 267 269 FT TURN 276 279 FT HELIX 282 305 FT HELIX 311 332 FT HELIX 334 339 FT HELIX 349 352 FT HELIX 365 370 FT HELIX 374 376 FT STRAND 379 383 FT STRAND 386 388 FT HELIX 390 393 FT HELIX 398 414 FT STRAND 420 424 FT HELIX 428 430 FT HELIX 431 443 FT HELIX 449 455 FT HELIX 464 468 FT STRAND 469 471 FT HELIX 472 481 FT HELIX 484 486 FT HELIX 489 495 FT STRAND 503 505 FT HELIX 506 521 FT HELIX 524 526 FT TURN 528 530 FT HELIX 533 536 FT HELIX 539 546 FT HELIX 550 557 FT STRAND 558 560 SQ SEQUENCE 604 AA; 69013 MW; DFE1658295C92064 CRC64; MLFRAVLLCA ALGLSQAANP CCSNPCQNRG ECMSTGFDQY KCDCTRTGFY GENCTTPEFL TRIKLLLKPT PNTVHYILTH FKGVWNIVNN IPFLRSLIMK YVLTSRSYLI DSPPTYNVHY GYKSWEAFSN LSYYTRALPP VADDCPTPMG VKGNKELPDS KEVLEKVLLR REFIPDPQGS NMMFAFFAQH FTHQFFKTDH KRGPGFTRGL GHGVDLNHIY GETLDRQHKL RLFKDGKLKY QVIGGEVYPP TVKDTQVEMI YPPHIPENLQ FAVGQEVFGL VPGLMMYATI WLREHNRVCD ILKQEHPEWG DEQLFQTSRL ILIGETIKIV IEDYVQHLSG YHFKLKFDPE LLFNQQFQYQ NRIASEFNTL YHWHPLLPDT FNIEDQEYSF KQFLYNNSIL LEHGLTQFVE SFTRQIAGRV AGGRNVPIAV QAVAKASIDQ SREMKYQSLN EYRKRFSLKP YTSFEELTGE KEMAAELKAL YSDIDVMELY PALLVEKPRP DAIFGETMVE LGAPFSLKGL MGNPICSPQY WKPSTFGGEV GFKIINTASI QSLICNNVKG CPFTSFNVQD PQPTKTATIN ASASHSRLDD INPTVLIKRR STEL // ID PH4H_MOUSE Reviewed; 453 AA. AC P16331; Q91WV1; DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 4. DT 19-FEB-2014, entry version 140. DE RecName: Full=Phenylalanine-4-hydroxylase; DE Short=PAH; DE EC=1.14.16.1; DE AltName: Full=Phe-4-monooxygenase; GN Name=Pah; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=C57BL/6J; TISSUE=Liver; RX PubMed=2334400; RA Ledley F.D., Grenett H.E., Dunbar B.S., Woo S.L.C.; RT "Mouse phenylalanine hydroxylase. Homology and divergence from human RT phenylalanine hydroxylase."; RL Biochem. J. 267:399-406(1990). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Kidney; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP PROTEIN SEQUENCE OF 2-13; 54-68; 160-169 AND 253-261, CLEAVAGE OF RP INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND MASS SPECTROMETRY. RC STRAIN=C57BL/6; TISSUE=Liver; RA Bienvenut W.V.; RL Submitted (JUL-2005) to UniProtKB. RN [5] RP PROTEIN SEQUENCE OF 12-21. RX PubMed=7387651; RA Wretborn M., Humble E., Ragnarsson U., Engstrom L.; RT "Amino acid sequence at the phosphorylated site of rat liver RT phenylalanine hydroxylase and phosphorylation of a corresponding RT synthetic peptide."; RL Biochem. Biophys. Res. Commun. 93:403-408(1980). RN [6] RP PROTEIN SEQUENCE OF 277-294. RX PubMed=6098294; DOI=10.1021/bi00319a001; RA Robson K.J.H., Beattie W., James R.J., Cotton R.C.H., Morgan F.J., RA Woo S.L.C.; RT "Sequence comparison of rat liver phenylalanine hydroxylase and its RT cDNA clones."; RL Biochemistry 23:5671-5675(1984). RN [7] RP VARIANTS PAH-ENU1 ALA-106 AND PAH-ENU2 SER-263. RX PubMed=9119379; DOI=10.1006/geno.1996.4508; RA McDonald J.D., Charlton C.K.; RT "Characterization of mutations at the mouse phenylalanine hydroxylase RT locus."; RL Genomics 39:402-405(1997). CC -!- CATALYTIC ACTIVITY: L-phenylalanine + tetrahydrobiopterin + O(2) = CC L-tyrosine + 4a-hydroxytetrahydrobiopterin. CC -!- COFACTOR: Fe(2+) ion. CC -!- ENZYME REGULATION: N-terminal region of PAH is thought to contain CC allosteric binding sites for phenylalanine and to constitute an CC "inhibitory" domain that regulates the activity of a catalytic CC domain in the C-terminal portion of the molecule. CC -!- PATHWAY: Amino-acid degradation; L-phenylalanine degradation; CC acetoacetate and fumarate from L-phenylalanine: step 1/6. CC -!- SUBUNIT: Homodimer and homotetramer (By similarity). CC -!- PTM: Phosphorylation at Ser-16 increases basal activity and CC facilitates activation by the substrate phenylalanine (By CC similarity). CC -!- DISEASE: Note=Mouse strains deficient in phenylalanine hydroxylase CC (Pah) were created as models of phenylketonuria (PKU). CC -!- SIMILARITY: Belongs to the biopterin-dependent aromatic amino acid CC hydroxylase family. CC -!- SIMILARITY: Contains 1 ACT domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X51942; CAA36205.1; -; mRNA. DR EMBL; AC122360; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC013458; AAH13458.1; -; mRNA. DR PIR; S15758; S15758. DR RefSeq; NP_032803.2; NM_008777.3. DR UniGene; Mm.263539; -. DR ProteinModelPortal; P16331; -. DR SMR; P16331; 19-427. DR IntAct; P16331; 3. DR MINT; MINT-1855311; -. DR STRING; 10090.ENSMUSP00000020241; -. DR PhosphoSite; P16331; -. DR PaxDb; P16331; -. DR PRIDE; P16331; -. DR Ensembl; ENSMUST00000020241; ENSMUSP00000020241; ENSMUSG00000020051. DR GeneID; 18478; -. DR KEGG; mmu:18478; -. DR UCSC; uc007gqt.2; mouse. DR CTD; 5053; -. DR MGI; MGI:97473; Pah. DR eggNOG; COG3186; -. DR GeneTree; ENSGT00390000010268; -. DR HOGENOM; HOG000233373; -. DR HOVERGEN; HBG006841; -. DR InParanoid; Q91WV1; -. DR KO; K00500; -. DR OMA; RYNAYTQ; -. DR OrthoDB; EOG7KM5T1; -. DR TreeFam; TF313327; -. DR UniPathway; UPA00139; UER00337. DR ChiTaRS; PAH; mouse. DR NextBio; 294182; -. DR PRO; PR:P16331; -. DR ArrayExpress; P16331; -. DR Bgee; P16331; -. DR CleanEx; MM_PAH; -. DR Genevestigator; P16331; -. DR GO; GO:0016597; F:amino acid binding; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0004505; F:phenylalanine 4-monooxygenase activity; IMP:MGI. DR GO; GO:0006559; P:L-phenylalanine catabolic process; IEA:UniProtKB-UniPathway. DR Gene3D; 1.10.800.10; -; 1. DR InterPro; IPR002912; ACT_dom. DR InterPro; IPR001273; ArAA_hydroxylase. DR InterPro; IPR018301; ArAA_hydroxylase_Fe/CU_BS. DR InterPro; IPR019774; Aromatic-AA_hydroxylase_C. DR InterPro; IPR005961; Phe-4-hydroxylase_tetra. DR InterPro; IPR019773; Tyrosine_3-monooxygenase-like. DR PANTHER; PTHR11473; PTHR11473; 1. DR Pfam; PF01842; ACT; 1. DR Pfam; PF00351; Biopterin_H; 1. DR PIRSF; PIRSF000336; TH; 1. DR PRINTS; PR00372; FYWHYDRXLASE. DR SUPFAM; SSF56534; SSF56534; 1. DR TIGRFAMs; TIGR01268; Phe4hydrox_tetr; 1. DR PROSITE; PS51671; ACT; 1. DR PROSITE; PS00367; BH4_AAA_HYDROXYL_1; 1. DR PROSITE; PS51410; BH4_AAA_HYDROXYL_2; 1. PE 1: Evidence at protein level; KW Acetylation; Allosteric enzyme; Complete proteome; KW Direct protein sequencing; Disease mutation; Iron; Metal-binding; KW Monooxygenase; Oxidoreductase; Phenylalanine catabolism; KW Phosphoprotein; Reference proteome. FT INIT_MET 1 1 Removed. FT CHAIN 2 453 Phenylalanine-4-hydroxylase. FT /FTId=PRO_0000205549. FT DOMAIN 36 114 ACT. FT METAL 285 285 Iron (By similarity). FT METAL 290 290 Iron (By similarity). FT METAL 330 330 Iron (By similarity). FT MOD_RES 2 2 N-acetylalanine. FT MOD_RES 16 16 Phosphoserine; by PKA (By similarity). FT VARIANT 106 106 V -> A (in PAH-ENU1; mild PKU phenotype). FT VARIANT 263 263 F -> S (in PAH-ENU2; severe PKU FT phenotype). FT CONFLICT 383 383 Q -> R (in Ref. 1; CAA36205). FT CONFLICT 432 432 I -> N (in Ref. 1; CAA36205). SQ SEQUENCE 453 AA; 51900 MW; 551F181FA59DEA5B CRC64; MAAVVLENGV LSRKLSDFGQ ETSYIEDNSN QNGAVSLIFS LKEEVGALAK VLRLFEENEI NLTHIESRPS RLNKDEYEFF TYLDKRSKPV LGSIIKSLRN DIGATVHELS RDKEKNTVPW FPRTIQELDR FANQILSYGA ELDADHPGFK DPVYRARRKQ FADIAYNYRH GQPIPRVEYT EEERKTWGTV FRTLKALYKT HACYEHNHIF PLLEKYCGFR EDNIPQLEDV SQFLQTCTGF RLRPVAGLLS SRDFLGGLAF RVFHCTQYIR HGSKPMYTPE PDICHELLGH VPLFSDRSFA QFSQEIGLAS LGAPDEYIEK LATIYWFTVE FGLCKEGDSI KAYGAGLLSS FGELQYCLSD KPKLLPLELE KTACQEYTVT EFQPLYYVAE SFNDAKEKVR TFAATIPRPF SVRYDPYTQR VEVLDNTQQL KILADSINSE VGILCHALQK IKS // ID PHF8_MOUSE Reviewed; 1023 AA. AC Q80TJ7; A2ABU8; A2ABV0; A2ABV2; Q8BLX8; Q8BLY0; Q8BZ61; Q8CG26; DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot. DT 16-AUG-2005, sequence version 2. DT 19-MAR-2014, entry version 91. DE RecName: Full=Histone lysine demethylase PHF8; DE EC=1.14.11.27; DE AltName: Full=PHD finger protein 8; GN Name=Phf8; Synonyms=Kiaa1111; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), AND RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-490 (ISOFORM 1). RC STRAIN=C57BL/6J; TISSUE=Bone; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 19-1023 (ISOFORM 1). RC TISSUE=Brain; RX PubMed=12693553; DOI=10.1093/dnares/10.1.35; RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S., RA Nakajima D., Nagase T., Ohara O., Koga H.; RT "Prediction of the coding sequences of mouse homologues of KIAA gene: RT II. The complete nucleotide sequences of 400 mouse KIAA-homologous RT cDNAs identified by screening of terminal sequences of cDNA clones RT randomly sampled from size-fractionated libraries."; RL DNA Res. 10:35-48(2003). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 1-899. RC STRAIN=129/Sv; RX PubMed=15112104; DOI=10.1007/s00335-003-2329-1; RA Abe K., Yuzuriha M., Sugimoto M., Ko M.S., Brathwaite M.E., Waeltz P., RA Nagaraja R.; RT "Gene content of the 750-kb critical region for mouse embryonic RT ectoderm lethal tcl-w5."; RL Mamm. Genome 15:265-276(2004). RN [5] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-820, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=17242355; DOI=10.1073/pnas.0609836104; RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; RT "Large-scale phosphorylation analysis of mouse liver."; RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-615 AND SER-820, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006; RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M., RA Thibault P.; RT "The phagosomal proteome in interferon-gamma-activated macrophages."; RL Immunity 30:143-154(2009). RN [7] RP STRUCTURE BY NMR OF 1-66. RG RIKEN structural genomics initiative (RSGI); RT "Solution structure of PHD domain in protein AA017385."; RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Histone lysine demethylase with selectivity for the di- CC and monomethyl states that plays a key role cell cycle CC progression, rDNA transcription and brain development. CC Demethylates mono- and dimethylated histone H3 'Lys-9' residue CC (H3K9Me1 and H3K9Me2), dimethylated H3 'Lys-27' (H3K27Me2) and CC monomethylated histone H4 'Lys-20' residue (H4K20Me1). Acts as a CC transcription activator as H3K9Me1, H3K9Me2, H3K27Me2 and H4K20Me1 CC are epigenetic repressive marks. Involved in cell cycle CC progression by being required to control G1-S transition. Acts as CC a coactivator of rDNA transcription, by activating polymerase I CC (pol I) mediated transcription of rRNA genes. Required for brain CC development, probably by regulating expression of neuron-specific CC genes. Has activity toward H4K20Me1 only when nucleosome is used CC as a substrate and when not histone octamer is used as substrate. CC May also have weak activity toward dimethylated H3 'Lys-36' CC (H3K36Me2), however, the relevance of this result remains unsure CC in vivo. Specifically binds trimethylated 'Lys-4' of histone H3 CC (H3K4me3), affecting histone demethylase specificity: has weak CC activity toward H3K9Me2 in absence of H3K4me3, while it has high CC activity toward H3K9me2 when binding H3K4me3 (By similarity). CC -!- CATALYTIC ACTIVITY: Protein N(6),N(6)-dimethyl-L-lysine + 2- CC oxoglutarate + O(2) = protein N(6)-methyl-L-lysine + succinate + CC formaldehyde + CO(2). CC -!- CATALYTIC ACTIVITY: Protein N(6)-methyl-L-lysine + 2-oxoglutarate CC + O(2) = protein L-lysine + succinate + formaldehyde + CO(2). CC -!- COFACTOR: Binds 1 Fe(2+) ion per subunit (By similarity). CC -!- SUBUNIT: Interacts with POLR1B, UBTF, SETD1A, HCFC1, E2F1 and CC ZNF711 (By similarity). CC -!- SUBCELLULAR LOCATION: Nucleus (By similarity). Nucleus, nucleolus CC (By similarity). Note=Recruited to H3K4me3 sites on chromatin CC during interphase. Dissociates from chromatin when cells enter CC mitosis (By similarity). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q80TJ7-1; Sequence=Displayed; CC Name=2; CC IsoId=Q80TJ7-2; Sequence=VSP_014966, VSP_014969, VSP_014970; CC Note=No experimental confirmation available; CC Name=3; CC IsoId=Q80TJ7-3; Sequence=VSP_014967, VSP_014968; CC Note=No experimental confirmation available; CC -!- DOMAIN: The PHD-type zinc finger mediates the binding to H3K4me3. CC Binding to H3K4me3 promotes its access to H3K9me2 (By similarity). CC -!- DOMAIN: The linker region is a critical determinant of demethylase CC specificity. It enables the active site of JmjC to reach the CC target H3K9me2 when the PHD-type zinc finger binds to H3K4me3 (By CC similarity). CC -!- PTM: Phosphorylation at Ser-33 and Ser-84 are required for CC dissociation from chromatin and accumulation of H4K20Me1 levels CC during prophase (By similarity). CC -!- SIMILARITY: Belongs to the JHDM1 histone demethylase family. CC JHDM1D subfamily. CC -!- SIMILARITY: Contains 1 JmjC domain. CC -!- SIMILARITY: Contains 1 PHD-type zinc finger. CC -!- SEQUENCE CAUTION: CC Sequence=CAM17163.1; Type=Erroneous gene model prediction; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK036609; BAC29505.1; -; mRNA. DR EMBL; AK040943; BAC30755.2; -; mRNA. DR EMBL; AK040969; BAC30763.1; -; mRNA. DR EMBL; AL662922; CAM17161.1; -; Genomic_DNA. DR EMBL; AL840642; CAM15464.1; -; Genomic_DNA. DR EMBL; AL662922; CAM15464.1; JOINED; Genomic_DNA. DR EMBL; AL662922; CAM17159.1; -; Genomic_DNA. DR EMBL; AL840642; CAM17159.1; JOINED; Genomic_DNA. DR EMBL; AL662922; CAM17163.1; ALT_SEQ; Genomic_DNA. DR EMBL; AK122447; BAC65729.1; -; mRNA. DR EMBL; AF528164; AAO17385.1; ALT_SEQ; Genomic_DNA. DR RefSeq; NP_001009544.1; NM_001009544.2. DR RefSeq; NP_001106825.1; NM_001113354.1. DR RefSeq; NP_796175.1; NM_177201.5. DR RefSeq; XP_006528938.1; XM_006528875.1. DR RefSeq; XP_006528939.1; XM_006528876.1. DR RefSeq; XP_006528940.1; XM_006528877.1. DR RefSeq; XP_006528943.1; XM_006528880.1. DR UniGene; Mm.17156; -. DR UniGene; Mm.84774; -. DR PDB; 1WEP; NMR; -; A=1-63. DR PDBsum; 1WEP; -. DR ProteinModelPortal; Q80TJ7; -. DR SMR; Q80TJ7; 3-447. DR PhosphoSite; Q80TJ7; -. DR PaxDb; Q80TJ7; -. DR PRIDE; Q80TJ7; -. DR Ensembl; ENSMUST00000024121; ENSMUSP00000024121; ENSMUSG00000023350. DR Ensembl; ENSMUST00000046950; ENSMUSP00000040765; ENSMUSG00000041229. [Q80TJ7-1] DR Ensembl; ENSMUST00000046962; ENSMUSP00000041312; ENSMUSG00000041229. [Q80TJ7-2] DR Ensembl; ENSMUST00000112662; ENSMUSP00000108281; ENSMUSG00000041229. [Q80TJ7-2] DR Ensembl; ENSMUST00000112666; ENSMUSP00000108285; ENSMUSG00000041229. [Q80TJ7-3] DR Ensembl; ENSMUST00000168501; ENSMUSP00000127653; ENSMUSG00000041229. [Q80TJ7-1] DR GeneID; 320595; -. DR GeneID; 74042; -. DR KEGG; mmu:320595; -. DR KEGG; mmu:74042; -. DR UCSC; uc009upd.1; mouse. [Q80TJ7-3] DR UCSC; uc009upe.1; mouse. [Q80TJ7-1] DR CTD; 23133; -. DR MGI; MGI:2444341; Phf8. DR eggNOG; NOG290496; -. DR GeneTree; ENSGT00550000074396; -. DR HOVERGEN; HBG045631; -. DR InParanoid; A2ABU8; -. DR KO; K11445; -. DR OMA; EIDLYHC; -. DR OrthoDB; EOG73JKV9; -. DR TreeFam; TF106480; -. DR EvolutionaryTrace; Q80TJ7; -. DR NextBio; 339610; -. DR PRO; PR:Q80TJ7; -. DR ArrayExpress; Q80TJ7; -. DR Bgee; Q80TJ7; -. DR CleanEx; MM_PHF8; -. DR Genevestigator; Q80TJ7; -. DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB. DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB. DR GO; GO:0071558; F:histone demethylase activity (H3-K27 specific); ISS:UniProtKB. DR GO; GO:0051864; F:histone demethylase activity (H3-K36 specific); ISS:UniProtKB. DR GO; GO:0032454; F:histone demethylase activity (H3-K9 specific); ISS:UniProtKB. DR GO; GO:0035575; F:histone demethylase activity (H4-K20 specific); ISS:UniProtKB. DR GO; GO:0005506; F:iron ion binding; ISS:UniProtKB. DR GO; GO:0035064; F:methylated histone residue binding; ISS:UniProtKB. DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB. DR GO; GO:0007420; P:brain development; ISS:UniProtKB. DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; ISS:UniProtKB. DR GO; GO:0061188; P:negative regulation of chromatin silencing at rDNA; ISS:UniProtKB. DR GO; GO:0045943; P:positive regulation of transcription from RNA polymerase I promoter; ISS:UniProtKB. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 3.30.40.10; -; 1. DR InterPro; IPR003347; JmjC_dom. DR InterPro; IPR019786; Zinc_finger_PHD-type_CS. DR InterPro; IPR011011; Znf_FYVE_PHD. DR InterPro; IPR001965; Znf_PHD. DR InterPro; IPR019787; Znf_PHD-finger. DR InterPro; IPR013083; Znf_RING/FYVE/PHD. DR Pfam; PF02373; JmjC; 1. DR Pfam; PF00628; PHD; 1. DR SMART; SM00558; JmjC; 1. DR SMART; SM00249; PHD; 1. DR SUPFAM; SSF57903; SSF57903; 1. DR PROSITE; PS51184; JMJC; 1. DR PROSITE; PS01359; ZF_PHD_1; 1. DR PROSITE; PS50016; ZF_PHD_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Activator; Alternative splicing; Cell cycle; KW Chromatin regulator; Complete proteome; Dioxygenase; Iron; KW Metal-binding; Nucleus; Oxidoreductase; Phosphoprotein; KW Reference proteome; Transcription; Transcription regulation; Zinc; KW Zinc-finger. FT CHAIN 1 1023 Histone lysine demethylase PHF8. FT /FTId=PRO_0000059296. FT DOMAIN 195 351 JmjC. FT ZN_FING 5 56 PHD-type. FT REGION 65 79 Linker (By similarity). FT COMPBIAS 733 771 Ser-rich. FT METAL 247 247 Iron; catalytic (By similarity). FT METAL 249 249 Iron; catalytic (By similarity). FT METAL 319 319 Iron; catalytic (By similarity). FT BINDING 244 244 Substrate (By similarity). FT BINDING 264 264 Substrate (By similarity). FT MOD_RES 33 33 Phosphoserine; by CDK1 (By similarity). FT MOD_RES 84 84 Phosphoserine; by CDK1 (By similarity). FT MOD_RES 615 615 Phosphoserine. FT MOD_RES 669 669 Phosphothreonine (By similarity). FT MOD_RES 670 670 Phosphothreonine (By similarity). FT MOD_RES 768 768 Phosphoserine (By similarity). FT MOD_RES 817 817 Phosphoserine (By similarity). FT MOD_RES 820 820 Phosphoserine. FT MOD_RES 843 843 Phosphoserine (By similarity). FT VAR_SEQ 442 542 Missing (in isoform 2). FT /FTId=VSP_014966. FT VAR_SEQ 442 464 DIFQQNVGKTSNIFGLQRIFPAG -> VRSMGEGKAFGKGW FT RLKWQVRTL (in isoform 3). FT /FTId=VSP_014967. FT VAR_SEQ 465 1023 Missing (in isoform 3). FT /FTId=VSP_014968. FT VAR_SEQ 883 896 ELQKAQKKKYIKKK -> VRVDTQLVALLLMT (in FT isoform 2). FT /FTId=VSP_014969. FT VAR_SEQ 897 1023 Missing (in isoform 2). FT /FTId=VSP_014970. FT STRAND 16 18 FT STRAND 20 23 FT TURN 24 26 FT STRAND 29 31 FT HELIX 32 35 FT HELIX 39 42 FT STRAND 46 48 FT TURN 51 56 SQ SEQUENCE 1023 AA; 113553 MW; 7B9351944C000487 CRC64; MASVPVYCLC RLPYDVTRFM IECDMCQDWF HGSCVGVEEE KAADIDLYHC PNCEVLHGPS IMKKRRGSSK GHDNHKGKPL KTGSSMFIRE LRGRTFDSSD EVILKPTGSQ LTVEFLEENS FSVPILVLKK DGLGMTLPSP SFTVRDVEHY VGSDKEIDVI DVARQADCKM KLGDFVKYYY SGKREKVLNV ISLEFSDTRL SNLVETPRIV RKLSWVENLW PEECVFERPN VQKYCLMSVR DSYTDFHIDF GGTSVWYHVL KGEKIFYLIR PTNANLTLFE CWSSSSNQNE MFFGDQVEKC YKCSVKQGQT LFIPTGWIHA VLTPVDCLAF GGNFLHSLNI EMQLKAYEIE KRLSTADLFK FPNFETICWY VGKHILDIFR GLRENRRHPA SYLVHGGKAL NLAFRAWTKK EALPDHEDEI PETVRTVQLI KDLAREIRLV EDIFQQNVGK TSNIFGLQRI FPAGSIPLTK PAHSTSVSMS KLSLPSKNGS KKKGLKPKDI FKKAERKGKQ SSALGPAGQL SYNLMDPYSH QALKTGPSQK AKFNMSGTSL NDSDDDSADM DLDGSENPLA LLMANGSTKR MKSVSKSRRA KIAKKVDSAR LVAEQVMGDE FDLDSDDELQ IDERLGKEKA NLLIRSKFPR KLPRAKPCSD PNRIREPGEV EFDIEEDYTT DEDMVEGVES KLGNGSGAGG ILDLLKASRQ VGGPDYAALT EAPASPSTQE AIQGMLCMAN LQSSSSSPAT SSLQAWWTGG QERSSGSSSS GLGTVSSSPA SQRTPGKRPI KRPAYWKNES EEEENASLDE QDSLGACFKD AEYIYPSLES DDDDPALKSR PKKKKNSDDA PWSPKARVTP TLPKQDRPVR EGTRVASIET GLAAAAAKLA QQELQKAQKK KYIKKKPLLK EVEQPRPQDS NPIMTMPAPT VATTPQPDTS SSPQPPPEPK QEALSGSLAD HEYTARPNAF GMAQANRSTT PMAPGVFLTQ RRPSVGSQSS QAGQGKRPKK GLATAKQRLG RILKIHRNGK LLL // ID PHF2_MOUSE Reviewed; 1096 AA. AC Q9WTU0; Q6A023; Q80WA8; DT 15-AUG-2003, integrated into UniProtKB/Swiss-Prot. DT 15-AUG-2003, sequence version 2. DT 19-MAR-2014, entry version 98. DE RecName: Full=Lysine-specific demethylase PHF2; DE EC=1.14.11.-; DE AltName: Full=GRC5; DE AltName: Full=PHD finger protein 2; GN Name=Phf2; Synonyms=Kiaa0662; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=10051327; DOI=10.1007/s003359900989; RA Hasenpusch-Theil K., Chadwick B.P., Theil T., Heath S.K., RA Wilkinson D.G., Frischauf A.M.; RT "PHF2, a novel PHD finger gene located on human chromosome 9q22."; RL Mamm. Genome 10:294-298(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Limb; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 59-1096. RX PubMed=15368895; DOI=10.1093/dnares/11.3.205; RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H., RA Nagase T., Ohara O., Koga H.; RT "Prediction of the coding sequences of mouse homologues of KIAA gene: RT IV. The complete nucleotide sequences of 500 mouse KIAA-homologous RT cDNAs identified by screening of terminal sequences of cDNA clones RT randomly sampled from size-fractionated libraries."; RL DNA Res. 11:205-218(2004). RN [5] RP CATALYTIC ACTIVITY. RX PubMed=20129925; DOI=10.1074/jbc.C109.097667; RA Wen H., Li J., Song T., Lu M., Kan P.Y., Lee M.G., Sha B., Shi X.; RT "Recognition of histone H3K4 trimethylation by the plant homeodomain RT of PHF2 modulates histone demethylation."; RL J. Biol. Chem. 285:9322-9326(2010). RN [6] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-716, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic fibroblast; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., RA Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). CC -!- FUNCTION: Lysine demethylase that demethylates both histones and CC non-histone proteins. Enzymatically inactive by itself, and CC becomes active following phosphorylation by PKA: forms a complex CC with ARID5B and mediates demethylation of methylated ARID5B. CC Demethylation of ARID5B leads to target the PHF2-ARID5B complex to CC target promoters, where PHF2 mediates demethylation of CC dimethylated 'Lys-9' of histone H3 (H3K9me2), followed by CC transcription activation of target genes. The PHF2-ARID5B complex CC acts as a coactivator of HNF4A in liver. PHF2 is recruited to CC trimethylated 'Lys-4' of histone H3 (H3K4me3) at rDNA promoters CC and promotes expression of rDNA (By similarity). CC -!- ENZYME REGULATION: Enzymatically inactive by itself, and become CC active following phosphorylation by PKA (By similarity). CC -!- SUBUNIT: Component of the PHF2-ARID5B complex, at least composed CC of PHF2 and ARID5B. Interacts with HNF4A and NR1H4 (By CC similarity). CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus (By similarity). CC -!- DOMAIN: The PHD-type zinc finger mediates the binding to H3K4me2 CC and H3K4me3 (By similarity). CC -!- PTM: Phosphorylated by PKA on specific serine residues, leading to CC the formation of an active lysine demethylase complex (By CC similarity). CC -!- SIMILARITY: Belongs to the JHDM1 histone demethylase family. CC JHDM1D subfamily. CC -!- SIMILARITY: Contains 1 JmjC domain. CC -!- SIMILARITY: Contains 1 PHD-type zinc finger. CC -!- CAUTION: In contrast to the related histone demethylases JHDM1D CC and PHF8, the conserved active His in position 321 is replaced by CC a Tyr. However, the presence of a Tyr residue neither affects CC binding to the catalytic iron nor abolishes demethylase activity. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF043726; AAD21792.1; -; mRNA. DR EMBL; AC109249; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC051633; AAH51633.1; -; mRNA. DR EMBL; AK172995; BAD32273.1; -; mRNA. DR RefSeq; NP_035208.2; NM_011078.3. DR UniGene; Mm.486213; -. DR ProteinModelPortal; Q9WTU0; -. DR SMR; Q9WTU0; 1-444. DR BioGrid; 202144; 4. DR IntAct; Q9WTU0; 1. DR MINT; MINT-4107441; -. DR PhosphoSite; Q9WTU0; -. DR PaxDb; Q9WTU0; -. DR PRIDE; Q9WTU0; -. DR Ensembl; ENSMUST00000035540; ENSMUSP00000047308; ENSMUSG00000038025. DR GeneID; 18676; -. DR KEGG; mmu:18676; -. DR UCSC; uc007qim.1; mouse. DR CTD; 5253; -. DR MGI; MGI:1338034; Phf2. DR eggNOG; NOG290496; -. DR GeneTree; ENSGT00550000074396; -. DR HOGENOM; HOG000231232; -. DR HOVERGEN; HBG045631; -. DR InParanoid; Q6A023; -. DR KO; K11445; -. DR OMA; KYKNSKP; -. DR OrthoDB; EOG73JKV9; -. DR TreeFam; TF106480; -. DR NextBio; 294702; -. DR PRO; PR:Q9WTU0; -. DR Bgee; Q9WTU0; -. DR CleanEx; MM_PHF2; -. DR Genevestigator; Q9WTU0; -. DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB. DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW. DR GO; GO:0032454; F:histone demethylase activity (H3-K9 specific); ISS:UniProtKB. DR GO; GO:0005506; F:iron ion binding; ISS:UniProtKB. DR GO; GO:0035064; F:methylated histone residue binding; ISS:UniProtKB. DR GO; GO:0003713; F:transcription coactivator activity; IEA:Ensembl. DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB. DR GO; GO:0061188; P:negative regulation of chromatin silencing at rDNA; ISS:UniProtKB. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 3.30.40.10; -; 1. DR InterPro; IPR003347; JmjC_dom. DR InterPro; IPR019786; Zinc_finger_PHD-type_CS. DR InterPro; IPR011011; Znf_FYVE_PHD. DR InterPro; IPR001965; Znf_PHD. DR InterPro; IPR019787; Znf_PHD-finger. DR InterPro; IPR013083; Znf_RING/FYVE/PHD. DR Pfam; PF02373; JmjC; 1. DR Pfam; PF00628; PHD; 1. DR SMART; SM00558; JmjC; 1. DR SMART; SM00249; PHD; 1. DR SUPFAM; SSF57903; SSF57903; 1. DR PROSITE; PS51184; JMJC; 1. DR PROSITE; PS01359; ZF_PHD_1; 1. DR PROSITE; PS50016; ZF_PHD_2; 1. PE 1: Evidence at protein level; KW Acetylation; Activator; Chromatin regulator; Complete proteome; KW Dioxygenase; Iron; Metal-binding; Nucleus; Oxidoreductase; KW Phosphoprotein; Reference proteome; Transcription; KW Transcription regulation; Zinc; Zinc-finger. FT CHAIN 1 1096 Lysine-specific demethylase PHF2. FT /FTId=PRO_0000059291. FT DOMAIN 197 353 JmjC. FT ZN_FING 5 56 PHD-type. FT COMPBIAS 487 606 Lys-rich. FT COMPBIAS 959 1021 Ser-rich. FT METAL 249 249 Iron; catalytic (By similarity). FT METAL 251 251 Iron; catalytic (By similarity). FT METAL 321 321 Iron; catalytic (By similarity). FT BINDING 193 193 Alpha-ketoglutarate (By similarity). FT BINDING 246 246 Alpha-ketoglutarate (By similarity). FT BINDING 259 259 Alpha-ketoglutarate (By similarity). FT BINDING 266 266 Alpha-ketoglutarate (By similarity). FT BINDING 323 323 Alpha-ketoglutarate (By similarity). FT MOD_RES 474 474 Phosphoserine (By similarity). FT MOD_RES 479 479 Phosphothreonine (By similarity). FT MOD_RES 536 536 Phosphoserine (By similarity). FT MOD_RES 701 701 Phosphoserine (By similarity). FT MOD_RES 716 716 N6-acetyllysine. FT MOD_RES 876 876 Phosphoserine (By similarity). FT MOD_RES 1057 1057 Phosphoserine; by PKA (By similarity). FT CONFLICT 938 938 Q -> L (in Ref. 1; AAD21792). FT CONFLICT 955 955 P -> S (in Ref. 4; BAD32273). SQ SEQUENCE 1096 AA; 120814 MW; 778B822C007D8860 CRC64; MATVPVYCVC RLPYDVTRFM IECDACKDWF HGSCVGVEEE EAPDIDIYHC PNCEKTHGKS TLKKKRTWHK HGPGPTPDVK PVQNGSQLFI KELRSRTFPS AEDVVSRVPG SQLTVGYMEE HGFTEPILVP KKDGLGLAVP APTFYVSDVE NYVGPERSVD VTDVTKQKDC KMKLKEFVDY YYSTNRKRVL NVTNLEFSDT RMSSFVEPPD IVKKLSWVEN YWPDDALLAK PKVTKYCLIC VKDSYTDFHI DSGGASAWYH VLKGEKIFYL IRPASANISL YERWRSASNH SEMFFADQVD RCYKCTVKQG QTLFIPSGWI YATLTPVDCL AFAGHFLHSL SVEMQMRAYE VERRLKLGSL TQFPNFETAC WYMGKHLLEA FKGSHKSGKQ LPPHLVQGAK ILNGAFRSWT KKQALAEHED ELPEHFRPSQ LIKDLAKEIR LSENASKTVR PEVNAAASSD EVCDGDREKE EPPSPVETTP PRSLLEKVSK KKTSKTVKMP KPSKIPKPPK SPKPPKTLKL KDGSKKKGKK CKESASPTIP NLDLLEAHTK EALTKMEPPK KGKTPKSVLS VPNKDTVHTQ NDMERLEIRE QTKSKSEAKW KYKNSKPDSL LKMEEEQRLE KSPLAGNKDK FSFSFSNRKL LGSKALRPPS SPGVFGALQS FKEDKAKPVR DEYEYVSDDG ELKIDEFPIR RKKSAPKRDL SFLLDKKEAL LMPTSKPKLD SAVYKSDDSS DEGSLHIDTD TKPGRNAKVK KESGSSAAGI LDLLQASEEV GALEYNPNSQ PPASPSTQEA IQGMLSMANL QASDSCLQTT WGTGQAKGGS LAAHGARKIG GGNKGTGKRL LKRTAKNSVD LEDYEEQDHL DACFKDSDYV YPSLESDEDN PVFKSRSKKR KGSDDAPYSP TARVGPSVPR QDRPVREGTR VASIETGLAA AAAKLSQQEE QKNRKKKNTK RKPAPNTASP SISTSASAST GTTSASTTPA STTPASTTPA STTPASTSTA SSQASQEGSS PEPPPESHSS SLADHEYTAA GTFSGSQAGR ASQPMAPGVF LTQRRPSASS PNNTAAKGKR TKKGMATAKQ RLGKILKIHR NGKLLL // ID PHYD1_MOUSE Reviewed; 291 AA. AC Q9DB26; A2AQZ4; Q80V68; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 15-JAN-2008, sequence version 2. DT 19-FEB-2014, entry version 80. DE RecName: Full=Phytanoyl-CoA dioxygenase domain-containing protein 1; DE EC=1.-.-.-; GN Name=Phyhd1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Cerebellum, and Spinal cord; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Brain, and Mammary tumor; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: Has alpha-ketoglutarate-dependent dioxygenase activity. CC Does not show detectable activity towards fatty acid CoA CC thioesters. Is not expected to be active with phytanoyl CoA (By CC similarity). CC -!- COFACTOR: Iron (By similarity). CC -!- SIMILARITY: Belongs to the PhyH family. PHYHD1 subfamily. CC -!- SEQUENCE CAUTION: CC Sequence=AAI32272.1; Type=Erroneous initiation; CC Sequence=AAI32274.1; Type=Erroneous initiation; CC Sequence=BAB23937.1; Type=Erroneous initiation; CC Sequence=BAE23715.1; Type=Erroneous initiation; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK005293; BAB23937.1; ALT_INIT; mRNA. DR EMBL; AK138607; BAE23715.1; ALT_INIT; mRNA. DR EMBL; AL845258; CAM20569.2; -; Genomic_DNA. DR EMBL; AL954388; CAM20569.2; JOINED; Genomic_DNA. DR EMBL; AL845258; CAM20572.1; -; Genomic_DNA. DR EMBL; AL954388; CAM20572.1; JOINED; Genomic_DNA. DR EMBL; AL954388; CAM23174.2; -; Genomic_DNA. DR EMBL; AL845258; CAM23174.2; JOINED; Genomic_DNA. DR EMBL; AL954388; CAM23177.1; -; Genomic_DNA. DR EMBL; AL845258; CAM23177.1; JOINED; Genomic_DNA. DR EMBL; BC039982; AAH39982.1; -; mRNA. DR EMBL; BC132271; AAI32272.1; ALT_INIT; mRNA. DR EMBL; BC132273; AAI32274.1; ALT_INIT; mRNA. DR RefSeq; NP_001239497.1; NM_001252568.2. DR RefSeq; NP_001239499.1; NM_001252570.1. DR RefSeq; NP_001268758.1; NM_001281829.1. DR RefSeq; NP_758471.1; NM_172267.4. DR UniGene; Mm.297949; -. DR ProteinModelPortal; Q9DB26; -. DR SMR; Q9DB26; 2-291. DR IntAct; Q9DB26; 2. DR MINT; MINT-4128063; -. DR PhosphoSite; Q9DB26; -. DR PaxDb; Q9DB26; -. DR PRIDE; Q9DB26; -. DR Ensembl; ENSMUST00000091132; ENSMUSP00000088663; ENSMUSG00000079484. DR Ensembl; ENSMUST00000113645; ENSMUSP00000109275; ENSMUSG00000079484. DR Ensembl; ENSMUST00000154647; ENSMUSP00000121371; ENSMUSG00000079484. DR GeneID; 227696; -. DR KEGG; mmu:227696; -. DR UCSC; uc008jbv.2; mouse. DR CTD; 254295; -. DR MGI; MGI:3612860; Phyhd1. DR eggNOG; NOG74982; -. DR GeneTree; ENSGT00390000006287; -. DR HOGENOM; HOG000185005; -. DR HOVERGEN; HBG054973; -. DR InParanoid; Q9DB26; -. DR OrthoDB; EOG7JHM5W; -. DR TreeFam; TF300011; -. DR NextBio; 378756; -. DR PRO; PR:Q9DB26; -. DR ArrayExpress; Q9DB26; -. DR Bgee; Q9DB26; -. DR Genevestigator; Q9DB26; -. DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR InterPro; IPR008775; Phytyl_CoA_dOase. DR Pfam; PF05721; PhyH; 1. PE 2: Evidence at transcript level; KW Complete proteome; Dioxygenase; Iron; Metal-binding; Oxidoreductase; KW Phosphoprotein; Reference proteome. FT CHAIN 1 291 Phytanoyl-CoA dioxygenase domain- FT containing protein 1. FT /FTId=PRO_0000313634. FT REGION 156 158 Alpha-ketoglutarate binding (By FT similarity). FT METAL 156 156 Iron (By similarity). FT METAL 158 158 Iron (By similarity). FT METAL 246 246 Iron (By similarity). FT BINDING 102 102 Alpha-ketoglutarate (By similarity). FT BINDING 141 141 Alpha-ketoglutarate (By similarity). FT BINDING 174 174 Alpha-ketoglutarate (By similarity). FT BINDING 248 248 Alpha-ketoglutarate (By similarity). FT BINDING 257 257 Alpha-ketoglutarate (By similarity). FT MOD_RES 55 55 Phosphothreonine (By similarity). SQ SEQUENCE 291 AA; 32517 MW; 7CA9823E4E6BF8B3 CRC64; MACLSPSQLK KFQEDGFLLL EGFFTADECV AMQQRIGEIV AEMDVPLHCR TEFSTQEDEQ LQTQGKTDYF LSSGDKIRFF FEKGVFDEKG NFLVPPEKSI NKIGHALHAH DPVFRSITHS PKVQALVRSL GLQMPVVVQS MYIFKQPHFG GEVSPHQDAT FLYTEPLGRV LGLWIAMEDA MLENGCLWFI PGSHTRGVSR RMIRAPSDSG PGTSFLGSDP AWASNLFVPL PVRRGGLVLI HGEVVHKSEQ NHSDHSRQAY TVHLMEAAGT VWSPGNWLQP TPELPFPPLY S // ID PIR_MOUSE Reviewed; 290 AA. AC Q9D711; A2AIH9; Q3UAN0; Q8CIE9; DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 19-MAR-2014, entry version 95. DE RecName: Full=Pirin; DE EC=1.13.11.24; DE AltName: Full=Probable quercetin 2,3-dioxygenase PIR; DE Short=Probable quercetinase; GN Name=Pir; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Bone marrow, Hypothalamus, and Tongue; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Czech II; TISSUE=Mammary tumor; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 255-290. RC STRAIN=ICR; RA Teng X., Li D., Johns R.A.; RT "Hypoxia upregulates VEGF-D promoter in pulmonary vascular smooth RT muscle cells."; RL Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases. RN [6] RP FUNCTION, TISSUE SPECIFICITY, AND INDUCTION. RC STRAIN=129/SvEv; RX PubMed=20010624; DOI=10.1038/leu.2009.247; RA Licciulli S., Cambiaghi V., Scafetta G., Gruszka A.M., Alcalay M.; RT "Pirin downregulation is a feature of AML and leads to impairment of RT terminal myeloid differentiation."; RL Leukemia 24:429-437(2010). CC -!- FUNCTION: Transcriptional coregulator of NF-kappa-B which CC facilitates binding of NF-kappa-B proteins to target kappa-B genes CC in a redox-state-dependent manner. May be required for efficient CC terminal myeloid maturation of hematopoietic cells. Has quercetin CC 2,3-dioxygenase activity (in vitro) (By similarity). CC -!- CATALYTIC ACTIVITY: Quercetin + O(2) = 2-(3,4- CC dihydroxybenzoyloxy)-4,6-dihydroxybenzoate + CO + H(+). CC -!- COFACTOR: Binds 1 iron ion per subunit (By similarity). CC -!- PATHWAY: Flavonoid metabolism; quercetin degradation. CC -!- SUBUNIT: May interact with NF1/CTF1. Interacts with BCL3. CC Identified in a complex comprised of PIR, BLC3, NFKB1 and target CC DNA (By similarity). CC -!- SUBCELLULAR LOCATION: Nucleus (By similarity). Cytoplasm (By CC similarity). Note=Predominantly localized in dot-like subnuclear CC structures (By similarity). CC -!- TISSUE SPECIFICITY: Weakly expressed in bone marrow. CC -!- INDUCTION: Down-regulated in mice with acute myeloid leukemias CC induced by either PML-RAR or AML1-ETO fusion oncoproteins. CC -!- SIMILARITY: Belongs to the pirin family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK009757; BAB26481.1; -; mRNA. DR EMBL; AK138314; BAE23621.1; -; mRNA. DR EMBL; AK151301; BAE30284.1; -; mRNA. DR EMBL; AL671706; CAM21159.1; -; Genomic_DNA. DR EMBL; AL732475; CAM21159.1; JOINED; Genomic_DNA. DR EMBL; AL732475; CAM17376.1; -; Genomic_DNA. DR EMBL; AL671706; CAM17376.1; JOINED; Genomic_DNA. DR EMBL; CH466571; EDL40759.1; -; Genomic_DNA. DR EMBL; BC024062; AAH24062.1; -; mRNA. DR EMBL; AF345635; AAK54068.1; -; Genomic_DNA. DR RefSeq; NP_081429.1; NM_027153.3. DR RefSeq; XP_006529040.1; XM_006528977.1. DR UniGene; Mm.293463; -. DR ProteinModelPortal; Q9D711; -. DR SMR; Q9D711; 3-290. DR IntAct; Q9D711; 1. DR MINT; MINT-4107667; -. DR STRING; 10090.ENSMUSP00000033749; -. DR PhosphoSite; Q9D711; -. DR PaxDb; Q9D711; -. DR PRIDE; Q9D711; -. DR Ensembl; ENSMUST00000033749; ENSMUSP00000033749; ENSMUSG00000031379. DR GeneID; 69656; -. DR KEGG; mmu:69656; -. DR UCSC; uc009uvl.2; mouse. DR CTD; 8544; -. DR MGI; MGI:1916906; Pir. DR eggNOG; COG1741; -. DR GeneTree; ENSGT00390000008044; -. DR HOGENOM; HOG000248360; -. DR HOVERGEN; HBG019151; -. DR InParanoid; A2AIH9; -. DR KO; K06911; -. DR OMA; DPFVHMD; -. DR TreeFam; TF300002; -. DR UniPathway; UPA00724; -. DR NextBio; 329994; -. DR PRO; PR:Q9D711; -. DR ArrayExpress; Q9D711; -. DR Bgee; Q9D711; -. DR CleanEx; MM_PIR; -. DR Genevestigator; Q9D711; -. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. DR GO; GO:0005634; C:nucleus; ISS:UniProtKB. DR GO; GO:0046872; F:metal ion binding; ISS:UniProtKB. DR GO; GO:0008127; F:quercetin 2,3-dioxygenase activity; IDA:UniProtKB. DR GO; GO:0003712; F:transcription cofactor activity; ISS:UniProtKB. DR GO; GO:0030224; P:monocyte differentiation; ISO:MGI. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 2.60.120.10; -; 1. DR InterPro; IPR012093; Pirin. DR InterPro; IPR008778; Pirin_C_dom. DR InterPro; IPR003829; Pirin_N_dom. DR InterPro; IPR014710; RmlC-like_jellyroll. DR InterPro; IPR011051; RmlC_Cupin. DR PANTHER; PTHR13903; PTHR13903; 1. DR Pfam; PF02678; Pirin; 1. DR Pfam; PF05726; Pirin_C; 1. DR PIRSF; PIRSF006232; Pirin; 1. DR SUPFAM; SSF51182; SSF51182; 1. PE 2: Evidence at transcript level; KW Complete proteome; Cytoplasm; Dioxygenase; Iron; Metal-binding; KW Nucleus; Oxidoreductase; Reference proteome; Transcription; KW Transcription regulation. FT CHAIN 1 290 Pirin. FT /FTId=PRO_0000214052. FT METAL 56 56 Iron (By similarity). FT METAL 58 58 Iron (By similarity). FT METAL 101 101 Iron (By similarity). FT METAL 103 103 Iron (By similarity). FT CONFLICT 49 49 K -> R (in Ref. 2; AAH24062). SQ SEQUENCE 290 AA; 32066 MW; B95915522F62EC5F CRC64; MASSKKVTLS VLSREQSEGV GARVRRSIGR PELKNLDPFL LFDEFKGGKP GGFPDHPHRG FETVSYLLEG GSMAHEDFCG HVGKMNPGDL QWMTAGRGIL HAEMPCSEEP AHGLQLWVNL RRSEKMVAPQ YQELKSEEIP KPTKDGVTVA VISGEALGIK SKVYTRTPTL YLDFKLDQGA KHSQPIPKGW TSFIYTISGD VYIGPDDAQQ KIEPHHTAVL GEGDAVQLEN KDPKRSHFVL IAGEPLREPV VQHGPFVMNT NEEISQAILD FRNAKNGFEG ARTWKSKIGN // ID PLOD1_MOUSE Reviewed; 728 AA. AC Q9R0E2; DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 19-MAR-2014, entry version 107. DE RecName: Full=Procollagen-lysine,2-oxoglutarate 5-dioxygenase 1; DE EC=1.14.11.4; DE AltName: Full=Lysyl hydroxylase 1; DE Short=LH1; DE Flags: Precursor; GN Name=Plod1; Synonyms=Plod; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY. RX PubMed=10429951; DOI=10.1016/S0945-053X(99)00016-5; RA Ruotsalainen H., Sipila L., Kerkela E., Pospiech H., Myllylae R.; RT "Characterization of cDNAs for mouse lysyl hydroxylase 1, 2 and 3, RT their phylogenetic analysis and tissue-specific expression in the RT mouse."; RL Matrix Biol. 18:325-329(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-198. RX PubMed=19349973; DOI=10.1038/nbt.1532; RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., RA Schiess R., Aebersold R., Watts J.D.; RT "Mass-spectrometric identification and relative quantification of N- RT linked cell surface glycoproteins."; RL Nat. Biotechnol. 27:378-386(2009). CC -!- FUNCTION: Forms hydroxylysine residues in -Xaa-Lys-Gly- sequences CC in collagens. These hydroxylysines serve as sites of attachment CC for carbohydrate units and are essential for the stability of the CC intermolecular collagen cross-links. CC -!- CATALYTIC ACTIVITY: L-lysine-[procollagen] + 2-oxoglutarate + O(2) CC = (2S,5R)-5-hydroxy-L-lysine-[procollagen] + succinate + CO(2). CC -!- COFACTOR: Iron (By similarity). CC -!- COFACTOR: Ascorbate (By similarity). CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SUBCELLULAR LOCATION: Rough endoplasmic reticulum membrane; CC Peripheral membrane protein; Lumenal side. CC -!- TISSUE SPECIFICITY: Highly expressed in the liver, heart, lung, CC skeletal muscle and kidney. CC -!- SIMILARITY: Contains 1 Fe2OG dioxygenase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF046782; AAD54617.1; -; mRNA. DR EMBL; BC006599; AAH06599.1; -; mRNA. DR RefSeq; NP_035252.1; NM_011122.3. DR UniGene; Mm.37371; -. DR ProteinModelPortal; Q9R0E2; -. DR SMR; Q9R0E2; 552-726. DR IntAct; Q9R0E2; 1. DR MINT; MINT-4107945; -. DR PhosphoSite; Q9R0E2; -. DR PaxDb; Q9R0E2; -. DR PRIDE; Q9R0E2; -. DR Ensembl; ENSMUST00000019199; ENSMUSP00000019199; ENSMUSG00000019055. DR GeneID; 18822; -. DR KEGG; mmu:18822; -. DR UCSC; uc008vtk.2; mouse. DR CTD; 5351; -. DR MGI; MGI:99907; Plod1. DR eggNOG; NOG311199; -. DR GeneTree; ENSGT00550000074427; -. DR HOGENOM; HOG000231099; -. DR HOVERGEN; HBG053618; -. DR InParanoid; Q9R0E2; -. DR KO; K00473; -. DR OMA; KFEMGHV; -. DR OrthoDB; EOG79PJNP; -. DR TreeFam; TF313826; -. DR ChiTaRS; PLOD1; mouse. DR NextBio; 295184; -. DR PRO; PR:Q9R0E2; -. DR ArrayExpress; Q9R0E2; -. DR Bgee; Q9R0E2; -. DR Genevestigator; Q9R0E2; -. DR GO; GO:0030867; C:rough endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0031418; F:L-ascorbic acid binding; IEA:UniProtKB-KW. DR GO; GO:0008475; F:procollagen-lysine 5-dioxygenase activity; IEA:UniProtKB-EC. DR GO; GO:0001666; P:response to hypoxia; IEA:Ensembl. DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase. DR InterPro; IPR006620; Pro_4_hyd_alph. DR InterPro; IPR001006; Procol_lys_dOase. DR Pfam; PF03171; 2OG-FeII_Oxy; 1. DR SMART; SM00702; P4Hc; 1. DR PROSITE; PS51471; FE2OG_OXY; 1. DR PROSITE; PS01325; LYS_HYDROXYLASE; 1. PE 1: Evidence at protein level; KW Complete proteome; Dioxygenase; Endoplasmic reticulum; Glycoprotein; KW Iron; Membrane; Metal-binding; Oxidoreductase; Reference proteome; KW Signal; Vitamin C. FT SIGNAL 1 18 By similarity. FT CHAIN 19 728 Procollagen-lysine,2-oxoglutarate 5- FT dioxygenase 1. FT /FTId=PRO_0000024679. FT DOMAIN 637 728 Fe2OG dioxygenase. FT ACT_SITE 719 719 Potential. FT METAL 657 657 Iron (By similarity). FT METAL 659 659 Iron (By similarity). FT METAL 709 709 Iron (By similarity). FT CARBOHYD 198 198 N-linked (GlcNAc...). FT CARBOHYD 539 539 N-linked (GlcNAc...) (Potential). FT CARBOHYD 687 687 N-linked (GlcNAc...) (Potential). SQ SEQUENCE 728 AA; 83595 MW; 339C2D71976ED985 CRC64; MRSLLLLAPL AWLLLVQAKD DAKLEDNLLV LTVATKETEG FRRFKRSAQF FNYKIQSLGL GEDWSVDGGP AAAGGGQKVR LLKKALEKHA DKEDLVILFV DSYDVVFASG PRELLKKFQQ AKSQVVFSAE EHIYPDRRLE AKYPTVPDGK RFLGSGGFIG YAPSLSKLVA EWEGQDSDSD QLFYTKIFLN PEKREQINIS LDHRCRIFQN LDGALDEVVL KFEMGHVRAR NLAYDTLPVV VHGNGPTKLQ LNYLGNYIPR FWTFETGCTV CDEGLRSLKG IGDEALPTVL VGVFIEQPTP FLSLFFLRLL RLRYPQKQMR LFIHNQERHH KLQVEQFLAE HGSEYQSVKL VGPEVRMANA DARNMGADLC RQDQTCTYYF SVDADVALTE PNSLRLLIEQ NKNVIAPLMT RHGRLWSNFW GGLSADGYYA RSEDYVDIVQ GRRVGVWNVP YISNIYLIKG SALRAELQNV DLFHYSKLDS DMSFCANVRQ QEVFMFLTNR HTFGHLLSLD NYQTTHLHND LWEVFSNPED WKEKYIHENY TKALAGKLVE TPCPDVYWFP IFTEAACDEL VEEMEHYGQW SLGDNKDNRI QGGYENVPTI DIHMNQITFE REWHKFLVEY IAPMTEKLYP GYYTRAQFDL AFVVRYKPDE QPSLMPHHDA STFTVNIALN RVGEDYEGGG CRFLRYNCSV RAPRKGWALL HPGRLTHYHE GLPTTKGTRY IAVSFVDP // ID PLOD2_MOUSE Reviewed; 737 AA. AC Q9R0B9; E9QM54; Q8VDT4; DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 2. DT 19-MAR-2014, entry version 99. DE RecName: Full=Procollagen-lysine,2-oxoglutarate 5-dioxygenase 2; DE EC=1.14.11.4; DE AltName: Full=Lysyl hydroxylase 2; DE Short=LH2; DE Flags: Precursor; GN Name=Plod2; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY. RX PubMed=10429951; DOI=10.1016/S0945-053X(99)00016-5; RA Ruotsalainen H., Sipila L., Kerkela E., Pospiech H., Myllylae R.; RT "Characterization of cDNAs for mouse lysyl hydroxylase 1, 2 and 3, RT their phylogenetic analysis and tissue-specific expression in the RT mouse."; RL Matrix Biol. 18:325-329(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-704, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic fibroblast; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., RA Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). CC -!- FUNCTION: Forms hydroxylysine residues in -Xaa-Lys-Gly- sequences CC in collagens. These hydroxylysines serve as sites of attachment CC for carbohydrate units and are essential for the stability of the CC intermolecular collagen cross-links. CC -!- CATALYTIC ACTIVITY: L-lysine-[procollagen] + 2-oxoglutarate + O(2) CC = (2S,5R)-5-hydroxy-L-lysine-[procollagen] + succinate + CO(2). CC -!- COFACTOR: Iron (By similarity). CC -!- COFACTOR: Ascorbate (By similarity). CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SUBCELLULAR LOCATION: Rough endoplasmic reticulum membrane; CC Peripheral membrane protein; Lumenal side. CC -!- TISSUE SPECIFICITY: Is highly expressed in the heart, lung, CC kidney, eye, ovary and placenta. CC -!- SIMILARITY: Contains 1 Fe2OG dioxygenase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF080572; AAD53987.1; -; mRNA. DR EMBL; AC165156; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC021352; AAH21352.1; -; mRNA. DR RefSeq; NP_001136388.1; NM_001142916.1. DR RefSeq; NP_036091.2; NM_011961.3. DR UniGene; Mm.79983; -. DR ProteinModelPortal; Q9R0B9; -. DR IntAct; Q9R0B9; 1. DR MINT; MINT-4107957; -. DR STRING; 10090.ENSMUSP00000068611; -. DR PhosphoSite; Q9R0B9; -. DR PaxDb; Q9R0B9; -. DR PRIDE; Q9R0B9; -. DR Ensembl; ENSMUST00000070522; ENSMUSP00000068611; ENSMUSG00000032374. DR GeneID; 26432; -. DR KEGG; mmu:26432; -. DR UCSC; uc009rau.2; mouse. DR CTD; 5352; -. DR MGI; MGI:1347007; Plod2. DR eggNOG; NOG311199; -. DR GeneTree; ENSGT00550000074427; -. DR HOGENOM; HOG000231099; -. DR HOVERGEN; HBG053618; -. DR InParanoid; Q9R0B9; -. DR KO; K13645; -. DR OrthoDB; EOG79PJNP; -. DR NextBio; 304489; -. DR PRO; PR:Q9R0B9; -. DR ArrayExpress; Q9R0B9; -. DR Bgee; Q9R0B9; -. DR Genevestigator; Q9R0B9; -. DR GO; GO:0030867; C:rough endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0031418; F:L-ascorbic acid binding; IEA:UniProtKB-KW. DR GO; GO:0008475; F:procollagen-lysine 5-dioxygenase activity; IEA:UniProtKB-EC. DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase. DR InterPro; IPR006620; Pro_4_hyd_alph. DR InterPro; IPR001006; Procol_lys_dOase. DR Pfam; PF03171; 2OG-FeII_Oxy; 1. DR SMART; SM00702; P4Hc; 1. DR PROSITE; PS51471; FE2OG_OXY; 1. DR PROSITE; PS01325; LYS_HYDROXYLASE; 1. PE 1: Evidence at protein level; KW Complete proteome; Dioxygenase; Endoplasmic reticulum; Glycoprotein; KW Iron; Membrane; Metal-binding; Oxidoreductase; Phosphoprotein; KW Reference proteome; Signal; Vitamin C. FT SIGNAL 1 25 Potential. FT CHAIN 26 737 Procollagen-lysine,2-oxoglutarate 5- FT dioxygenase 2. FT /FTId=PRO_0000024684. FT DOMAIN 644 737 Fe2OG dioxygenase. FT ACT_SITE 728 728 Potential. FT METAL 666 666 Iron (By similarity). FT METAL 668 668 Iron (By similarity). FT METAL 718 718 Iron (By similarity). FT MOD_RES 320 320 Phosphothreonine (By similarity). FT MOD_RES 323 323 Phosphotyrosine (By similarity). FT MOD_RES 704 704 N6-succinyllysine. FT CARBOHYD 63 63 N-linked (GlcNAc...) (Potential). FT CARBOHYD 209 209 N-linked (GlcNAc...) (Potential). FT CARBOHYD 365 365 N-linked (GlcNAc...) (Potential). FT CARBOHYD 522 522 N-linked (GlcNAc...) (Potential). FT CARBOHYD 696 696 N-linked (GlcNAc...) (Potential). FT CARBOHYD 725 725 N-linked (GlcNAc...) (Potential). FT CONFLICT 2 2 G -> E (in Ref. 1; AAD53987). FT CONFLICT 405 405 F -> I (in Ref. 3; AAH21352). FT CONFLICT 611 611 I -> T (in Ref. 1; AAD53987 and 3; FT AAH21352). SQ SEQUENCE 737 AA; 84488 MW; 0FF2880E5FEEA084 CRC64; MGDRGARPGR LMPMLALLSW AAGLGVAEET PGRIPADKLL VITVATKEND GFHRFMNSAK YFNYTVKVLG QGQEWRGGDG MNSIGGGQKV RLLKEAMEHY ASQEDLVILF TECFDVVFAG GPEEVLKKFQ KTNHKIVFAA DGLLWPDKRL ADKYPVVHIG KRYLNSGGFI GYAPYISRLV QQWNLQDNDD DQLFYTKVYI DPLKREAFNI TLDHKCKIFQ ALNGATDEVV LKFENGKSRV KNTFYETLPV AINGNGPTKI LLNYFGNYVP NSWTQENGCA LCDVDTIDLS TVDVPPKVTL GVFIEQPTPF LPRFLNLLLT LDYPKEALQL FIHNKEVYHE KDIKVFVDKA KHDISSIKIV GPEENLSQAE ARNMGMDFCR QDEKCDYYFS VDADVVLTNP RTLKFLIEQN RKIIAPLVTR HGKLWSNFWG ALSPDGYYAR SEDYVDIVQG NRVGIWNVPY MANVYLIQGK TLRSEMNERN YFVRDKLDPD MALCRNARDM GVFMYISNRH EFGRLISTAN YNTSHLNNDF WQIFENPVDW KEKYINRDYS KIFTENIVEQ PCPDVFWFPI FSERACDELV EEMEHYGKWS GGKHHDSRIS GGYENVPTDD IHMKQIGLEN VWLHFIREFI APVTLKVFAG YYTKGFALLN FVVKYSPERQ RSLRPHHDAS TFTINIALNN VGEDFQGGGC KFLRYNCSIE SPRKGWSFMH PGRLTHLHEG LPVKNGTRYI AVSFIDP // ID PLOD3_MOUSE Reviewed; 741 AA. AC Q9R0E1; Q542E0; Q9CYY9; DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 19-MAR-2014, entry version 105. DE RecName: Full=Procollagen-lysine,2-oxoglutarate 5-dioxygenase 3; DE EC=1.14.11.4; DE AltName: Full=Lysyl hydroxylase 3; DE Short=LH3; DE Flags: Precursor; GN Name=Plod3; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY. RX PubMed=10429951; DOI=10.1016/S0945-053X(99)00016-5; RA Ruotsalainen H., Sipila L., Kerkela E., Pospiech H., Myllylae R.; RT "Characterization of cDNAs for mouse lysyl hydroxylase 1, 2 and 3, RT their phylogenetic analysis and tissue-specific expression in the RT mouse."; RL Matrix Biol. 18:325-329(1999). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=129/SvJ; RX PubMed=11334715; DOI=10.1016/S0945-053X(01)00130-5; RA Ruotsalainen H., Vanhatupa S., Tampio M., Sipila L., Valtavaara M., RA Myllylae R.; RT "Complete genomic structure of mouse lysyl hydroxylase 2 and lysyl RT hydroxylase 3/collagen glucosyltransferase."; RL Matrix Biol. 20:137-146(2001). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J, and NOD; TISSUE=Embryo, Lung, and Thymus; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6; TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-66. RX PubMed=19349973; DOI=10.1038/nbt.1532; RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., RA Schiess R., Aebersold R., Watts J.D.; RT "Mass-spectrometric identification and relative quantification of N- RT linked cell surface glycoproteins."; RL Nat. Biotechnol. 27:378-386(2009). CC -!- FUNCTION: Forms hydroxylysine residues in -Xaa-Lys-Gly- sequences CC in collagens. These hydroxylysines serve as sites of attachment CC for carbohydrate units and are essential for the stability of the CC intermolecular collagen cross-links. CC -!- CATALYTIC ACTIVITY: L-lysine-[procollagen] + 2-oxoglutarate + O(2) CC = (2S,5R)-5-hydroxy-L-lysine-[procollagen] + succinate + CO(2). CC -!- COFACTOR: Iron. CC -!- COFACTOR: Ascorbate. CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SUBCELLULAR LOCATION: Rough endoplasmic reticulum membrane; CC Peripheral membrane protein; Lumenal side. CC -!- TISSUE SPECIFICITY: Highly expressed in the heart, lung, liver and CC testis. CC -!- SIMILARITY: Contains 1 Fe2OG dioxygenase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF046783; AAD54618.1; -; mRNA. DR EMBL; AY014830; AAK00576.1; -; Genomic_DNA. DR EMBL; AK013195; BAB28704.1; -; mRNA. DR EMBL; AK033360; BAC28246.1; -; mRNA. DR EMBL; AK088948; BAC40669.1; -; mRNA. DR EMBL; BC043047; AAH43047.1; -; mRNA. DR EMBL; BC054734; AAH54734.1; -; mRNA. DR RefSeq; NP_036092.1; NM_011962.3. DR UniGene; Mm.251003; -. DR ProteinModelPortal; Q9R0E1; -. DR IntAct; Q9R0E1; 2. DR MINT; MINT-4107969; -. DR PhosphoSite; Q9R0E1; -. DR PaxDb; Q9R0E1; -. DR PRIDE; Q9R0E1; -. DR Ensembl; ENSMUST00000004968; ENSMUSP00000004968; ENSMUSG00000004846. DR GeneID; 26433; -. DR KEGG; mmu:26433; -. DR UCSC; uc009abj.2; mouse. DR CTD; 8985; -. DR MGI; MGI:1347008; Plod3. DR eggNOG; NOG311199; -. DR GeneTree; ENSGT00550000074427; -. DR HOGENOM; HOG000231099; -. DR HOVERGEN; HBG053618; -. DR InParanoid; Q9R0E1; -. DR KO; K13646; -. DR OMA; LRYDCVI; -. DR OrthoDB; EOG79PJNP; -. DR TreeFam; TF313826; -. DR BRENDA; 2.4.1.66; 3474. DR ChiTaRS; PLOD3; mouse. DR NextBio; 304493; -. DR PRO; PR:Q9R0E1; -. DR Bgee; Q9R0E1; -. DR Genevestigator; Q9R0E1; -. DR GO; GO:0030867; C:rough endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0031418; F:L-ascorbic acid binding; IEA:UniProtKB-KW. DR GO; GO:0033823; F:procollagen glucosyltransferase activity; IDA:MGI. DR GO; GO:0008475; F:procollagen-lysine 5-dioxygenase activity; IDA:MGI. DR GO; GO:0070831; P:basement membrane assembly; IMP:MGI. DR GO; GO:0032870; P:cellular response to hormone stimulus; IEA:Ensembl. DR GO; GO:0030199; P:collagen fibril organization; IMP:MGI. DR GO; GO:0001886; P:endothelial cell morphogenesis; IMP:MGI. DR GO; GO:0048730; P:epidermis morphogenesis; IMP:MGI. DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI. DR GO; GO:0060425; P:lung morphogenesis; IMP:MGI. DR GO; GO:0021915; P:neural tube development; IMP:MGI. DR GO; GO:0008104; P:protein localization; IMP:MGI. DR GO; GO:0042311; P:vasodilation; IMP:MGI. DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase. DR InterPro; IPR006620; Pro_4_hyd_alph. DR InterPro; IPR001006; Procol_lys_dOase. DR Pfam; PF03171; 2OG-FeII_Oxy; 1. DR SMART; SM00702; P4Hc; 1. DR PROSITE; PS51471; FE2OG_OXY; 1. DR PROSITE; PS01325; LYS_HYDROXYLASE; 1. PE 1: Evidence at protein level; KW Complete proteome; Dioxygenase; Endoplasmic reticulum; Glycoprotein; KW Iron; Membrane; Metal-binding; Oxidoreductase; Reference proteome; KW Signal; Vitamin C. FT SIGNAL 1 27 Potential. FT CHAIN 28 741 Procollagen-lysine,2-oxoglutarate 5- FT dioxygenase 3. FT /FTId=PRO_0000024687. FT DOMAIN 650 741 Fe2OG dioxygenase. FT ACT_SITE 732 732 Potential. FT METAL 670 670 Iron (By similarity). FT METAL 672 672 Iron (By similarity). FT METAL 722 722 Iron (By similarity). FT CARBOHYD 66 66 N-linked (GlcNAc...). FT CARBOHYD 286 286 N-linked (GlcNAc...) (Potential). FT CARBOHYD 551 551 N-linked (GlcNAc...) (Potential). FT CONFLICT 8 8 P -> H (in Ref. 3; BAB28704). SQ SEQUENCE 741 AA; 84922 MW; D1B79B386339D9F4 CRC64; MAAAGPEPRL LLLLLLLLPP LPPVTSASDR PRGANAVNPD KLLVITVATA ETEGYRRFLQ SAEFFNYTVR TLGLGQEWRG GDVARTVGGG QKVRWLKKEM EKYADQKDMI IMFVDSYDVI LASSPTELLK KFVQSGSHLL FSAESFCWPE WGLAEQYPEV GMGKRFLNSG GFIGFAPTIH QIVRQWNYKD DDDDQLFYTQ LYLDPGLREK LKLSLDHKSR IFQNLNGALD EVILKFDQNR VRIRNVAYDT LPVVVHGNGP TKLQLNYLGN YVPNGWTPQG GCGFCNQTLR TLPGGQPPPR VLLAVFVEQP TPFLPRFLQR LLLLDYPPDR ISLFLHNSEV YHEPHIADAW PQLQDHFSAV KLVGPEEALS AGEARDMAMD SCRQNPECEF YFSLDADAVL TNPETLRVLI EQNRKVIAPM LSRHGKLWSN FWGALSPNEY YARSEDYVEL VQRKRVGVWN VPYISQAYVI RGETLRTELP QKEVFSSSDT DPDMAFCKSV RDKGIFLHLS NQHEFGRLLA TSRYDTDHLH PDLWQIFDNP VDWREQYIHE NYSRALDGEG LVEQPCPDVY WFPLLTEQMC DELVEEMEHY GQWSGGRHED SRLAGGYENV PTVDIHMKQV GYEDQWLQLL RTYVGPMTEY LFPGYHTKTR AVMNFVVRYR PDEQPSLRPH HDSSTFTLNV ALNHKGVDYE GGGCRFLRYD CRISSPRKGW ALLHPGRLTH YHEGLPTTRG TRYIMVSFVD P // ID PNPO_MOUSE Reviewed; 261 AA. AC Q91XF0; Q3TP70; Q3U445; Q3U4X1; DT 26-SEP-2003, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 19-FEB-2014, entry version 102. DE RecName: Full=Pyridoxine-5'-phosphate oxidase; DE EC=1.4.3.5; DE AltName: Full=Pyridoxamine-phosphate oxidase; GN Name=Pnpo; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J, and NOD; TISSUE=Stomach, and Thymus; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Kidney, and Liver; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP PROTEIN SEQUENCE OF 120-138, AND MASS SPECTROMETRY. RC TISSUE=Hippocampus; RA Lubec G., Klug S.; RL Submitted (MAR-2007) to UniProtKB. RN [5] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=17242355; DOI=10.1073/pnas.0609836104; RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; RT "Large-scale phosphorylation analysis of mouse liver."; RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). CC -!- FUNCTION: Catalyzes the oxidation of either pyridoxine 5'- CC phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal CC 5'-phosphate (PLP) (By similarity). CC -!- CATALYTIC ACTIVITY: Pyridoxamine 5'-phosphate + H(2)O + O(2) = CC pyridoxal 5'-phosphate + NH(3) + H(2)O(2). CC -!- CATALYTIC ACTIVITY: Pyridoxine 5'-phosphate + O(2) = pyridoxal 5'- CC phosphate + H(2)O(2). CC -!- COFACTOR: Binds 1 FMN per subunit. CC -!- PATHWAY: Cofactor biosynthesis; B6 vitamer interconversion; CC pyridoxal 5'-phosphate from pyridoxamine 5'-phosphate: step 1/1. CC -!- PATHWAY: Cofactor biosynthesis; B6 vitamer interconversion; CC pyridoxal 5'-phosphate from pyridoxine 5'-phosphate: step 1/1. CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SIMILARITY: Belongs to the pyridoxamine 5'-phosphate oxidase CC family. CC -!- SEQUENCE CAUTION: CC Sequence=BAE32590.1; Type=Erroneous initiation; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK154004; BAE32309.1; -; mRNA. DR EMBL; AK154443; BAE32590.1; ALT_INIT; mRNA. DR EMBL; AK164667; BAE37867.1; -; mRNA. DR EMBL; AL596384; CAM21902.1; -; Genomic_DNA. DR EMBL; BC010785; AAH10785.1; -; mRNA. DR EMBL; BC026564; AAH26564.1; -; mRNA. DR RefSeq; NP_598782.1; NM_134021.2. DR UniGene; Mm.254704; -. DR ProteinModelPortal; Q91XF0; -. DR SMR; Q91XF0; 49-261. DR MINT; MINT-1869143; -. DR STRING; 10090.ENSMUSP00000018803; -. DR PhosphoSite; Q91XF0; -. DR PaxDb; Q91XF0; -. DR PRIDE; Q91XF0; -. DR Ensembl; ENSMUST00000018803; ENSMUSP00000018803; ENSMUSG00000018659. DR GeneID; 103711; -. DR KEGG; mmu:103711; -. DR UCSC; uc007ldc.1; mouse. DR CTD; 55163; -. DR MGI; MGI:2144151; Pnpo. DR eggNOG; COG0259; -. DR GeneTree; ENSGT00390000011219; -. DR HOGENOM; HOG000242755; -. DR HOVERGEN; HBG045634; -. DR InParanoid; Q91XF0; -. DR KO; K00275; -. DR OMA; PEHWGGY; -. DR OrthoDB; EOG7B8S4P; -. DR TreeFam; TF313411; -. DR UniPathway; UPA00190; UER00304. DR UniPathway; UPA00190; UER00305. DR NextBio; 356069; -. DR PRO; PR:Q91XF0; -. DR ArrayExpress; Q91XF0; -. DR Bgee; Q91XF0; -. DR CleanEx; MM_PNPO; -. DR Genevestigator; Q91XF0; -. DR GO; GO:0010181; F:FMN binding; IEA:InterPro. DR GO; GO:0004733; F:pyridoxamine-phosphate oxidase activity; IEA:UniProtKB-EC. DR GO; GO:0008615; P:pyridoxine biosynthetic process; IEA:UniProtKB-KW. DR Gene3D; 2.30.110.10; -; 1. DR HAMAP; MF_01629; PdxH; 1. DR InterPro; IPR000659; Pyridox_Oxase. DR InterPro; IPR019740; Pyridox_Oxase_CS. DR InterPro; IPR011576; Pyridox_Oxase_FMN-bd. DR InterPro; IPR019576; Pyridoxamine_oxidase_dimer_C. DR InterPro; IPR012349; Split_barrel_FMN-bd. DR PANTHER; PTHR10851; PTHR10851; 1. DR Pfam; PF10590; PNPOx_C; 1. DR Pfam; PF01243; Pyridox_oxidase; 1. DR PIRSF; PIRSF000190; Pyd_amn-ph_oxd; 1. DR SUPFAM; SSF50475; SSF50475; 1. DR TIGRFAMs; TIGR00558; pdxH; 1. DR PROSITE; PS01064; PYRIDOX_OXIDASE; 1. PE 1: Evidence at protein level; KW Complete proteome; Direct protein sequencing; Flavoprotein; FMN; KW Oxidoreductase; Pyridoxal phosphate; Pyridoxine biosynthesis; KW Reference proteome. FT CHAIN 1 261 Pyridoxine-5'-phosphate oxidase. FT /FTId=PRO_0000167784. FT NP_BIND 110 111 FMN (By similarity). FT NP_BIND 174 175 FMN (By similarity). FT REGION 225 227 Substrate binding (By similarity). FT BINDING 95 95 FMN (By similarity). FT BINDING 98 98 FMN; via amide nitrogen (By similarity). FT BINDING 100 100 Substrate (By similarity). FT BINDING 117 117 FMN (By similarity). FT BINDING 157 157 Substrate (By similarity). FT BINDING 161 161 Substrate (By similarity). FT BINDING 165 165 Substrate (By similarity). SQ SEQUENCE 261 AA; 30114 MW; D83A54883B4BC0EC CRC64; MTCGLLSVTV TFRRPAKWTG YLRHLCCRGA VMDLGPMRKS YRGDREAFEE THLTSLDPMK QFASWFDEAV QCPDIGEANA MCVATCTRDG KPSARMLLLK GFGKDGFRFF TNYESRKGKE LDSNPFASLV FYWEPLNRQV RVEGPVKKLP EKEAENYFHS RPKSSQIGAV VSRQSSVIPD REYLRKKNEE LGQLYQDQEV PKPEYWGGYI LYPQVMEFWQ GQTNRLHDRI VFRRGLATGD SPLGPMTHHG EEDWVYERLA P // ID PORED_MOUSE Reviewed; 330 AA. AC Q9WUP4; D3YZB6; D3Z3J5; Q3UU82; Q8BGE3; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 05-OCT-2010, sequence version 2. DT 19-MAR-2014, entry version 81. DE RecName: Full=Polyprenol reductase; DE EC=1.3.1.94; DE AltName: Full=3-oxo-5-alpha-steroid 4-dehydrogenase 3; DE EC=1.3.1.22; DE AltName: Full=Steroid 5-alpha-reductase 2-like; DE AltName: Full=Steroid 5-alpha-reductase 3; DE Short=S5AR 3; DE Short=SR type 3; GN Name=Srd5a3; Synonyms=Srd5a2l; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=129/Sv; RX PubMed=11116088; DOI=10.1101/gr.10.12.1928; RA Wilsbacher L.D., Sangoram A.M., Antoch M.P., Takahashi J.S.; RT "The mouse Clock locus: sequence and comparative analysis of 204 kb RT from mouse chromosome 5."; RL Genome Res. 10:1928-1940(2000). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC STRAIN=C57BL/6J; TISSUE=Cerebellum, Thymus, and Urinary bladder; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP FUNCTION, PATHWAY, AND DISRUPTION PHENOTYPE. RX PubMed=20637498; DOI=10.1016/j.cell.2010.06.001; RA Cantagrel V., Lefeber D.J., Ng B.G., Guan Z., Silhavy J.L., RA Bielas S.L., Lehle L., Hombauer H., Adamowicz M., Swiezewska E., RA De Brouwer A.P., Blumel P., Sykut-Cegielska J., Houliston S., RA Swistun D., Ali B.R., Dobyns W.B., Babovic-Vuksanovic D., RA van Bokhoven H., Wevers R.A., Raetz C.R., Freeze H.H., Morava E., RA Al-Gazali L., Gleeson J.G.; RT "SRD5A3 is required for converting polyprenol to dolichol and is RT mutated in a congenital glycosylation disorder."; RL Cell 142:203-217(2010). CC -!- FUNCTION: Plays a key role in early steps of protein N-linked CC glycosylation by being required for the conversion of polyprenol CC into dolichol. Dolichols are required for the synthesis of CC dolichol-linked monosaccharides and the oligosaccharide precursor CC used for N-glycosylation. Acts as a polyprenol reductase that CC promotes the reduction of the alpha-isoprene unit of polyprenols CC into dolichols in a NADP-dependent mechanism. Also able to convert CC testosterone (T) into 5-alpha-dihydrotestosterone (DHT). CC -!- CATALYTIC ACTIVITY: Ditrans,polycis-dolichol + NADP(+) = CC ditrans,polycis-polyprenol + NADPH. CC -!- CATALYTIC ACTIVITY: A 3-oxo-5-alpha-steroid + NADP(+) = a 3-oxo- CC Delta(4)-steroid + NADPH. CC -!- PATHWAY: Protein modification; protein glycosylation. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass CC membrane protein (By similarity). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9WUP4-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9WUP4-2; Sequence=VSP_039779; CC Note=No experimental confirmation available; CC -!- DISRUPTION PHENOTYPE: Death by E12.5. At E10.5, embryos are CC smaller and fail to undergo axial rotation observed at E8.5 in CC wild-types and present dilated hearts and open neural tubes. CC -!- SIMILARITY: Belongs to the steroid 5-alpha reductase family. CC Polyprenol reductase subfamily. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF146793; AAD30567.1; -; Genomic_DNA. DR EMBL; AK040198; BAC30537.1; -; mRNA. DR EMBL; AK075635; BAC35871.1; -; mRNA. DR EMBL; AK138681; BAE23745.1; -; mRNA. DR EMBL; AK139290; BAE23944.1; -; mRNA. DR EMBL; AK162527; BAE36955.1; -; mRNA. DR EMBL; AC147239; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC145647; AAI45648.1; -; mRNA. DR RefSeq; NP_065636.2; NM_020611.4. DR UniGene; Mm.289446; -. DR ProteinModelPortal; Q9WUP4; -. DR PhosphoSite; Q9WUP4; -. DR PaxDb; Q9WUP4; -. DR PRIDE; Q9WUP4; -. DR Ensembl; ENSMUST00000031143; ENSMUSP00000031143; ENSMUSG00000029233. [Q9WUP4-1] DR GeneID; 57357; -. DR KEGG; mmu:57357; -. DR UCSC; uc008xun.2; mouse. [Q9WUP4-2] DR UCSC; uc008xuo.2; mouse. [Q9WUP4-1] DR CTD; 79644; -. DR MGI; MGI:1930252; Srd5a3. DR eggNOG; NOG330066; -. DR GeneTree; ENSGT00500000044920; -. DR HOGENOM; HOG000018885; -. DR HOVERGEN; HBG057797; -. DR InParanoid; Q3UU82; -. DR KO; K12345; -. DR OMA; NQVAEFI; -. DR OrthoDB; EOG72ZCFT; -. DR TreeFam; TF315011; -. DR UniPathway; UPA00378; -. DR NextBio; 313740; -. DR PRO; PR:Q9WUP4; -. DR ArrayExpress; Q9WUP4; -. DR Bgee; Q9WUP4; -. DR CleanEx; MM_SRD5A3; -. DR Genevestigator; Q9WUP4; -. DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0003865; F:3-oxo-5-alpha-steroid 4-dehydrogenase activity; ISS:UniProtKB. DR GO; GO:0047751; F:cholestenone 5-alpha-reductase activity; IEA:UniProtKB-EC. DR GO; GO:0016628; F:oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor; ISS:UniProtKB. DR GO; GO:0019348; P:dolichol metabolic process; IMP:UniProtKB. DR GO; GO:0006488; P:dolichol-linked oligosaccharide biosynthetic process; IMP:UniProtKB. DR GO; GO:0016095; P:polyprenol catabolic process; IMP:UniProtKB. DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway. DR InterPro; IPR001104; 3-oxo-5_a-steroid_4-DH_C. DR Pfam; PF02544; Steroid_dh; 1. DR PROSITE; PS50244; S5A_REDUCTASE; 1. PE 2: Evidence at transcript level; KW Alternative splicing; Complete proteome; Endoplasmic reticulum; KW Membrane; NADP; Oxidoreductase; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 330 Polyprenol reductase. FT /FTId=PRO_0000317704. FT TOPO_DOM 1 16 Cytoplasmic (Potential). FT TRANSMEM 17 37 Helical; (Potential). FT TOPO_DOM 38 80 Lumenal (Potential). FT TRANSMEM 81 101 Helical; (Potential). FT TOPO_DOM 102 132 Cytoplasmic (Potential). FT TRANSMEM 133 153 Helical; (Potential). FT TOPO_DOM 154 169 Lumenal (Potential). FT TRANSMEM 170 190 Helical; (Potential). FT TOPO_DOM 191 206 Cytoplasmic (Potential). FT TRANSMEM 207 227 Helical; (Potential). FT TOPO_DOM 228 277 Lumenal (Potential). FT TRANSMEM 278 298 Helical; (Potential). FT TOPO_DOM 299 330 Cytoplasmic (Potential). FT VAR_SEQ 200 330 VYVLGKNLLIQARWFHILGMVMFFWSSAHQYKCHVILSNLR FT RNKKGVVIHCQHRIPFGDWFEYVSSANYLAELMIYISMAVT FT FGLHNLTWWLVVTYVFSSQALSAFFNHKFYRSTFVSYPKHR FT KAFLPFLF -> GKWPCQ (in isoform 2). FT /FTId=VSP_039779. FT CONFLICT 109 109 S -> G (in Ref. 1; AAD30567 and 4; FT AAI45648). FT CONFLICT 298 298 S -> F (in Ref. 1; AAD30567 and 4; FT AAI45648). SQ SEQUENCE 330 AA; 37936 MW; A26CAB23B295D75C CRC64; MAGWAGFELS ALNPLRTLWL ALAAAFLFAL LLQLAPARLL PSCALFQDLL RYGKTKQSGS RRPAVCRAFD VPKRYFSHFY VISVVWNGSL LWLLSQSLFL GAPFPNWLSA LLRTLGATQF QALEMESKAS RMPAAELALS AFLVLVFLWV HSLRRLFECF YVSVFSNAAI HVVQYCFGLV YYVLVGLTVL SQVPMDDKNV YVLGKNLLIQ ARWFHILGMV MFFWSSAHQY KCHVILSNLR RNKKGVVIHC QHRIPFGDWF EYVSSANYLA ELMIYISMAV TFGLHNLTWW LVVTYVFSSQ ALSAFFNHKF YRSTFVSYPK HRKAFLPFLF // ID PPOX_MOUSE Reviewed; 477 AA. AC P51175; P97344; Q99M34; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 19-MAR-2014, entry version 114. DE RecName: Full=Protoporphyrinogen oxidase; DE Short=PPO; DE EC=1.3.3.4; GN Name=Ppox; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND ENZYME RP REGULATION. RX PubMed=8554330; DOI=10.1006/abbi.1995.0051; RA Dailey T.A., Dailey H.A., Meissner P., Prasad A.R.; RT "Cloning, sequence, and expression of mouse protoporphyrinogen RT oxidase."; RL Arch. Biochem. Biophys. 324:379-384(1995). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION. RC TISSUE=Erythroleukemia; RX PubMed=7607249; DOI=10.1111/j.1432-1033.1995.0760h.x; RA Taketani S., Yoshinaga T., Furukawa T., Kohno H., Tokunaga R., RA Nishimura K., Inokuchi H.; RT "Induction of terminal enzymes for heme biosynthesis during RT differentiation of mouse erythroleukemia cells."; RL Eur. J. Biochem. 230:760-765(1995). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Mammary gland; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP SUBCELLULAR LOCATION. RC TISSUE=Liver; RX PubMed=3346226; RA Ferreira G.C., Andrew T.L., Karr S.W., Dailey H.A.; RT "Organization of the terminal two enzymes of the heme biosynthetic RT pathway. Orientation of protoporphyrinogen oxidase and evidence for a RT membrane complex."; RL J. Biol. Chem. 263:3835-3839(1988). CC -!- FUNCTION: Catalyzes the 6-electron oxidation of CC protoporphyrinogen-IX to form protoporphyrin-IX. CC -!- CATALYTIC ACTIVITY: Protoporphyrinogen-IX + 3 O(2) = CC protoporphyrin-IX + 3 H(2)O(2). CC -!- COFACTOR: Binds 1 FAD per subunit (By similarity). CC -!- ENZYME REGULATION: Inhibited by acifluorfen. CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin- CC IX biosynthesis; protoporphyrin-IX from protoporphyrinogen-IX: CC step 1/1. CC -!- SUBUNIT: Monomer. Homodimer (By similarity). CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral CC membrane protein; Intermembrane side. CC -!- INDUCTION: During erythroid differentiation. CC -!- SIMILARITY: Belongs to the protoporphyrinogen oxidase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U25114; AAA96003.1; -; mRNA. DR EMBL; D45185; BAA08126.1; -; mRNA. DR EMBL; BC002047; AAH02047.1; -; mRNA. DR PIR; S65684; S65684. DR PIR; S68367; S68367. DR RefSeq; NP_032937.1; NM_008911.2. DR RefSeq; XP_006496770.1; XM_006496707.1. DR UniGene; Mm.266888; -. DR ProteinModelPortal; P51175; -. DR SMR; P51175; 2-474. DR PhosphoSite; P51175; -. DR PaxDb; P51175; -. DR PRIDE; P51175; -. DR Ensembl; ENSMUST00000073120; ENSMUSP00000072863; ENSMUSG00000062729. DR GeneID; 19044; -. DR KEGG; mmu:19044; -. DR UCSC; uc007dns.1; mouse. DR CTD; 5498; -. DR MGI; MGI:104968; Ppox. DR eggNOG; COG1232; -. DR GeneTree; ENSGT00390000008744; -. DR HOGENOM; HOG000269479; -. DR HOVERGEN; HBG001709; -. DR InParanoid; P51175; -. DR KO; K00231; -. DR OMA; PNGFLDS; -. DR OrthoDB; EOG7DJSMB; -. DR TreeFam; TF323479; -. DR UniPathway; UPA00251; UER00324. DR ChiTaRS; PPOX; mouse. DR NextBio; 295501; -. DR PRO; PR:P51175; -. DR ArrayExpress; P51175; -. DR Bgee; P51175; -. DR CleanEx; MM_PPOX; -. DR Genevestigator; P51175; -. DR GO; GO:0031305; C:integral component of mitochondrial inner membrane; IEA:Ensembl. DR GO; GO:0031304; C:intrinsic component of mitochondrial inner membrane; IDA:UniProtKB. DR GO; GO:0004729; F:oxygen-dependent protoporphyrinogen oxidase activity; IDA:UniProtKB. DR GO; GO:0006783; P:heme biosynthetic process; ISS:UniProtKB. DR GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0042493; P:response to drug; IEA:Ensembl. DR Gene3D; 3.40.50.720; -; 1. DR Gene3D; 3.90.660.20; -; 1. DR InterPro; IPR002937; Amino_oxidase. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR004572; Protoporphyrinogen_oxidase. DR InterPro; IPR027418; Protoporphyrinogen_oxidase_C. DR Pfam; PF01593; Amino_oxidase; 1. DR TIGRFAMs; TIGR00562; proto_IX_ox; 1. PE 1: Evidence at protein level; KW Complete proteome; FAD; Flavoprotein; Heme biosynthesis; Membrane; KW Mitochondrion; Mitochondrion inner membrane; Oxidoreductase; KW Porphyrin biosynthesis; Reference proteome. FT CHAIN 1 477 Protoporphyrinogen oxidase. FT /FTId=PRO_0000135272. FT NP_BIND 9 14 FAD (By similarity). FT NP_BIND 34 35 FAD (By similarity). FT NP_BIND 57 60 FAD (By similarity). FT NP_BIND 454 456 FAD (By similarity). FT BINDING 42 42 FAD; via amide nitrogen (By similarity). FT BINDING 257 257 FAD; via amide nitrogen and carbonyl FT oxygen (By similarity). FT BINDING 449 449 FAD; via amide nitrogen (By similarity). FT CONFLICT 64 64 A -> T (in Ref. 2). FT CONFLICT 66 66 A -> P (in Ref. 2). FT CONFLICT 108 108 L -> S (in Ref. 2; BAA08126). FT CONFLICT 176 176 R -> Q (in Ref. 3; AAH02047). FT CONFLICT 427 427 W -> C (in Ref. 2; BAA08126). SQ SEQUENCE 477 AA; 50871 MW; 8CFB48120728DE6F CRC64; MGRTVIVLGG GISGLAASYH LIRGPSPPKV ILVEGSKRLG GWIRSIRGSD GAIFELGPRG IRPAGALGAR TLLLVSELGL ESEVLPVRGD HPAAQNRFLY VGGTLHPLPS GLRGLLRPSP PFSKPLFWAG LRELLKPRGK EPDETVHSFA QRRLGPEVAS LAMDSLCRGV FAGNSRELSI RSCFPSLFQA EQTHRSILLG LLLGAGQSPQ PDSSLIRQAR AERWSQWSLR GGLEVLPQAL HNHLASKGVT VLSGQPVCGL SLQPEGRWKV SLGDSSLEAD HIISAIPASE LSKLLPAEAA PLARILSTIK AVSVAVVNLQ YRGACLPVQG FGHLVPSSED PTVLGIVYDS VAFPEQDGNP PSLRVTVMLG GYWLQKLKAA GHQLSPELFQ QQAQEAAATQ LGLKEPPSHC LVHLHKNCIP QYTIGHWQKL DSAMQFLTAQ RLPLTLAGAS YEGVAVNDCI ESGRQAAVAV LGTESNS // ID PRDX1_MOUSE Reviewed; 199 AA. AC P35700; Q3UBV4; Q9CWI2; DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1994, sequence version 1. DT 19-MAR-2014, entry version 143. DE RecName: Full=Peroxiredoxin-1; DE EC=1.11.1.15; DE AltName: Full=Macrophage 23 kDa stress protein; DE AltName: Full=Osteoblast-specific factor 3; DE Short=OSF-3; DE AltName: Full=Thioredoxin peroxidase 2; DE AltName: Full=Thioredoxin-dependent peroxide reductase 2; GN Name=Prdx1; Synonyms=Msp23, Paga, Tdpx2; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Peritoneal macrophage; RX PubMed=8360158; RA Ishii T., Yamada M., Sato H., Matsue M., Taketani S., Nakayama K., RA Sugita Y., Bannai S.; RT "Cloning and characterization of a 23-kDa stress-induced mouse RT peritoneal macrophage protein."; RL J. Biol. Chem. 268:18633-18636(1993). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=C57BL/6; TISSUE=Osteoblast; RX PubMed=8089076; RA Kawai S., Takeshita S., Okazaki M., Kikuno R., Kudo A., Amann E.; RT "Cloning and characterization of OSF-3, a new member of the MER5 RT family, expressed in mouse osteoblastic cells."; RL J. Biochem. 115:641-643(1994). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. RC STRAIN=129/SvJ; RX PubMed=10548725; DOI=10.1016/S0378-1119(99)00413-8; RA Lee T.-H., Yu S.-L., Kim S.-U., Lee K.-K., Rhee S.G., Yu D.-Y.; RT "Characterization of mouse peroxiredoxin I genomic DNA and its RT expression."; RL Gene 239:243-250(1999). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=129/SvJ; TISSUE=Liver; RA Hino K., Sato H., Bannai S.; RT "Characterization of mouse type I peroxiredoxin gene and RT pseudogenes."; RL Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; RC TISSUE=Bone marrow, Hippocampus, Kidney, Liver, Mammary gland, and RC Stomach; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6; TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [7] RP PROTEIN SEQUENCE OF 17-27; 94-109; 111-120; 141-151; 159-168 AND RP 173-190, AND MASS SPECTROMETRY. RC STRAIN=C57BL/6; TISSUE=Brain, and Hippocampus; RA Lubec G., Kang S.U., Klug S., Yang J.W., Zigmond M.; RL Submitted (JUL-2007) to UniProtKB. RN [8] RP FUNCTION, AND DISRUPTION PHENOTYPE. RX PubMed=19766572; DOI=10.1016/j.cell.2009.06.042; RA Yan Y., Sabharwal P., Rao M., Sockanathan S.; RT "The antioxidant enzyme Prdx1 controls neuronal differentiation by RT thiol-redox-dependent activation of GDE2."; RL Cell 138:1209-1221(2009). RN [9] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-136, SUCCINYLATION [LARGE RP SCALE ANALYSIS] AT LYS-35, AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic fibroblast, and Liver; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., RA Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). CC -!- FUNCTION: Involved in redox regulation of the cell. Reduces CC peroxides with reducing equivalents provided through the CC thioredoxin system but not from glutaredoxin. May play an CC important role in eliminating peroxides generated during CC metabolism. Might participate in the signaling cascades of growth CC factors and tumor necrosis factor-alpha by regulating the CC intracellular concentrations of H(2)O(2). Regulates GDPD5 function CC by reducing an intramolecular disulfide bond (By similarity). CC Cooperates with GDPD5 to drive postmitotic motor neuron CC differentiation. CC -!- CATALYTIC ACTIVITY: 2 R'-SH + ROOH = R'-S-S-R' + H(2)O + ROH. CC -!- SUBUNIT: Homodimer; disulfide-linked, upon oxidation (By CC similarity). May form heterodimers with AOP2. Interacts with CC GDPD5; forms a mixed-disulfide with GDPD5 (By similarity). CC -!- INTERACTION: CC Self; NbExp=2; IntAct=EBI-444948, EBI-444948; CC Q13043:STK4 (xeno); NbExp=3; IntAct=EBI-444948, EBI-367376; CC -!- SUBCELLULAR LOCATION: Cytoplasm. Melanosome (By similarity). CC -!- TISSUE SPECIFICITY: Found in various tissues; high concentration CC in liver. CC -!- INDUCTION: By oxidative and sulfhydryl-reactive agents. CC -!- PTM: Phosphorylated on Thr-90 during the M-phase, which leads to a CC more than 80% decrease in enzymatic activity (By similarity). CC -!- DISRUPTION PHENOTYPE: Mice embryos loss approximately 50% of CC Islet1/Islet2+ and HB9+ motor neurons, whereas dorsal-ventral CC patterning events and the numbers of Olig2+ progenitors are CC normal. Toward the end of the cell death phase they have CC equivalent numbers of motor neurons as wild type embryos. CC -!- MISCELLANEOUS: The active site is the redox-active Cys-52 oxidized CC to Cys-SOH. Cys-SOH rapidly reacts with Cys-173-SH of the other CC subunit to form an intermolecular disulfide with a concomitant CC homodimer formation. The enzyme may be subsequently regenerated by CC reduction of the disulfide by thioredoxin (By similarity). CC -!- MISCELLANEOUS: Inactivated upon oxidative stress by overoxidation CC of Cys-52 to Cys-SO(2)H and Cys-SO(3)H. Cys-SO(2)H is retroreduced CC to Cys-SOH after removal of H(2)O(2), while Cys-SO(3)H may be CC irreversibly oxidized (By similarity). CC -!- SIMILARITY: Belongs to the AhpC/TSA family. CC -!- SIMILARITY: Contains 1 thioredoxin domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; D16142; BAA03713.1; -; mRNA. DR EMBL; D21252; BAA04796.1; -; mRNA. DR EMBL; AF157331; AAD45323.1; -; Genomic_DNA. DR EMBL; AF157329; AAD45323.1; JOINED; Genomic_DNA. DR EMBL; AF157330; AAD45323.1; JOINED; Genomic_DNA. DR EMBL; AB023564; BAA86992.1; -; Genomic_DNA. DR EMBL; AK002287; BAB21990.1; -; mRNA. DR EMBL; AK008711; BAB25847.1; -; mRNA. DR EMBL; AK010688; BAB27120.1; -; mRNA. DR EMBL; AK083243; BAC38827.1; -; mRNA. DR EMBL; AK145138; BAE26255.1; -; mRNA. DR EMBL; AK150797; BAE29860.1; -; mRNA. DR EMBL; AK151459; BAE30417.1; -; mRNA. DR EMBL; AK167624; BAE39676.1; -; mRNA. DR EMBL; AK169154; BAE40933.1; -; mRNA. DR EMBL; BC083348; AAH83348.1; -; mRNA. DR EMBL; BC086648; AAH86648.1; -; mRNA. DR PIR; A48513; A48513. DR RefSeq; NP_035164.1; NM_011034.4. DR UniGene; Mm.30929; -. DR ProteinModelPortal; P35700; -. DR SMR; P35700; 3-199. DR BioGrid; 202018; 3. DR IntAct; P35700; 18. DR MINT; MINT-1863043; -. DR PeroxiBase; 4555; Mm2CysPrx01-1. DR PhosphoSite; P35700; -. DR REPRODUCTION-2DPAGE; P35700; -. DR SWISS-2DPAGE; P35700; -. DR PaxDb; P35700; -. DR PRIDE; P35700; -. DR Ensembl; ENSMUST00000106470; ENSMUSP00000102078; ENSMUSG00000028691. DR Ensembl; ENSMUST00000135573; ENSMUSP00000114159; ENSMUSG00000028691. DR GeneID; 18477; -. DR KEGG; mmu:18477; -. DR UCSC; uc008uhd.1; mouse. DR CTD; 5052; -. DR MGI; MGI:99523; Prdx1. DR eggNOG; COG0450; -. DR GeneTree; ENSGT00390000004653; -. DR HOGENOM; HOG000022343; -. DR HOVERGEN; HBG000286; -. DR InParanoid; P35700; -. DR KO; K13279; -. DR OMA; EFKKINC; -. DR OrthoDB; EOG7T1RCD; -. DR TreeFam; TF105181; -. DR NextBio; 294178; -. DR PRO; PR:P35700; -. DR ArrayExpress; P35700; -. DR Bgee; P35700; -. DR CleanEx; MM_PRDX1; -. DR Genevestigator; P35700; -. DR GO; GO:0005829; C:cytosol; IEA:Ensembl. DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell. DR GO; GO:0005759; C:mitochondrial matrix; IEA:Ensembl. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR GO; GO:0005719; C:nuclear euchromatin; IEA:Ensembl. DR GO; GO:0005730; C:nucleolus; IEA:Ensembl. DR GO; GO:0005782; C:peroxisomal matrix; IEA:Ensembl. DR GO; GO:0020037; F:heme binding; IEA:Ensembl. DR GO; GO:0008379; F:thioredoxin peroxidase activity; IEA:Ensembl. DR GO; GO:0008283; P:cell proliferation; IMP:MGI. DR GO; GO:0034101; P:erythrocyte homeostasis; IMP:MGI. DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:Ensembl. DR GO; GO:0042267; P:natural killer cell mediated cytotoxicity; IMP:MGI. DR GO; GO:0042345; P:regulation of NF-kappaB import into nucleus; IMP:MGI. DR GO; GO:0032872; P:regulation of stress-activated MAPK cascade; IMP:MGI. DR GO; GO:0019430; P:removal of superoxide radicals; IMP:MGI. DR Gene3D; 3.40.30.10; -; 1. DR InterPro; IPR000866; AhpC/TSA. DR InterPro; IPR024706; Peroxiredoxin_AhpC-typ. DR InterPro; IPR019479; Peroxiredoxin_C. DR InterPro; IPR012336; Thioredoxin-like_fold. DR Pfam; PF10417; 1-cysPrx_C; 1. DR Pfam; PF00578; AhpC-TSA; 1. DR PIRSF; PIRSF000239; AHPC; 1. DR SUPFAM; SSF52833; SSF52833; 1. DR PROSITE; PS51352; THIOREDOXIN_2; 1. PE 1: Evidence at protein level; KW Acetylation; Antioxidant; Complete proteome; Cytoplasm; KW Direct protein sequencing; Disulfide bond; Oxidoreductase; Peroxidase; KW Phosphoprotein; Redox-active center; Reference proteome. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 199 Peroxiredoxin-1. FT /FTId=PRO_0000135077. FT DOMAIN 6 165 Thioredoxin. FT ACT_SITE 52 52 Cysteine sulfenic acid (-SOH) FT intermediate (By similarity). FT MOD_RES 2 2 N-acetylserine (By similarity). FT MOD_RES 7 7 N6-acetyllysine (By similarity). FT MOD_RES 16 16 N6-acetyllysine (By similarity). FT MOD_RES 27 27 N6-acetyllysine (By similarity). FT MOD_RES 35 35 N6-acetyllysine; alternate (By FT similarity). FT MOD_RES 35 35 N6-succinyllysine; alternate. FT MOD_RES 90 90 Phosphothreonine (By similarity). FT MOD_RES 136 136 N6-acetyllysine. FT DISULFID 52 52 Interchain (with C-173); in linked form FT (By similarity). FT DISULFID 173 173 Interchain (with C-52); in linked form FT (By similarity). FT CONFLICT 196 196 S -> F (in Ref. 5; BAB27120). SQ SEQUENCE 199 AA; 22176 MW; BEF5C995A86124D1 CRC64; MSSGNAKIGY PAPNFKATAV MPDGQFKDIS LSEYKGKYVV FFFYPLDFTF VCPTEIIAFS DRADEFKKLN CQVIGASVDS HFCHLAWINT PKKQGGLGPM NIPLISDPKR TIAQDYGVLK ADEGISFRGL FIIDDKGILR QITINDLPVG RSVDEIIRLV QAFQFTDKHG EVCPAGWKPG SDTIKPDVNK SKEYFSKQK // ID PRDX3_MOUSE Reviewed; 257 AA. AC P20108; DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1991, sequence version 1. DT 19-MAR-2014, entry version 140. DE RecName: Full=Thioredoxin-dependent peroxide reductase, mitochondrial; DE EC=1.11.1.15; DE AltName: Full=Antioxidant protein 1; DE Short=AOP-1; DE AltName: Full=PRX III; DE AltName: Full=Perioredoxin-3; DE AltName: Full=Protein MER5; DE Flags: Precursor; GN Name=Prdx3; Synonyms=Aop1, Mer5; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=2583515; DOI=10.1016/0378-1119(89)90297-7; RA Yamamoto T., Matsui Y., Natori S., Obinata M.; RT "Cloning of a housekeeping-type gene (MER5) preferentially expressed RT in murine erythroleukemia cells."; RL Gene 80:337-343(1989). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. RA Lee T.-H., Rhee S.G., Lee K.-K., Yu D.-Y.; RT "Characterization of mouse peroxiredoxin III genomic DNA and its RT expression."; RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Kidney; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Mammary gland; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP PROTEIN SEQUENCE OF 85-92; 151-167 AND 172-215, AND MASS SPECTROMETRY. RC STRAIN=C57BL/6; TISSUE=Brain, and Hippocampus; RA Lubec G., Kang S.U., Klug S., Yang J.W., Zigmond M.; RL Submitted (JUL-2007) to UniProtKB. RN [6] RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-84 AND LYS-92, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., RA Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). RN [7] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-92, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23576753; DOI=10.1073/pnas.1302961110; RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., RA Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.; RT "Label-free quantitative proteomics of the lysine acetylome in RT mitochondria identifies substrates of SIRT3 in metabolic pathways."; RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013). CC -!- FUNCTION: Involved in redox regulation of the cell. Protects CC radical-sensitive enzymes from oxidative damage by a radical- CC generating system. CC -!- CATALYTIC ACTIVITY: 2 R'-SH + ROOH = R'-S-S-R' + H(2)O + ROH. CC -!- SUBUNIT: Dodecameric ring assembled from homodimeric units; CC disulfide-linked, upon oxidation. The rings have an approximate CC diameter of 150 A and a central hole of 70 A. 3-5% of the rings CC are interlocked by pairs. Binds MAP3K13 (By similarity). Interacts CC with NEK6 (By similarity). Interacts with LRRK2 (By similarity). CC -!- SUBCELLULAR LOCATION: Mitochondrion (By similarity). CC -!- TISSUE SPECIFICITY: Housekeeping-type gene preferentially CC expressed in murine erythroleukemia (MEL) cells. CC -!- INDUCTION: Expression is increased after induction of MEL cells to CC differentiation by DMSO. CC -!- PTM: Phosphorylated by LRRK2; phosphorylation reduces perodixase CC activity (By similarity). CC -!- MISCELLANEOUS: The active site is the redox-active Cys-109 CC oxidized to Cys-SOH. Cys-SOH rapidly reacts with Cys-230-SH of the CC other subunit to form an intermolecular disulfide with a CC concomitant homodimer formation. The enzyme may be subsequently CC regenerated by reduction of the disulfide by thioredoxin (By CC similarity). CC -!- MISCELLANEOUS: Irreversibly inactivated by overoxidation of Cys- CC 109 (to Cys-SO(3)H) upon oxidative stress (By similarity). CC -!- SIMILARITY: Belongs to the AhpC/TSA family. CC -!- SIMILARITY: Contains 1 thioredoxin domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M28723; AAA39524.1; -; mRNA. DR EMBL; AF211938; AAF63705.1; -; Genomic_DNA. DR EMBL; AF211933; AAF63705.1; JOINED; Genomic_DNA. DR EMBL; AF211934; AAF63705.1; JOINED; Genomic_DNA. DR EMBL; AF211935; AAF63705.1; JOINED; Genomic_DNA. DR EMBL; AF211936; AAF63705.1; JOINED; Genomic_DNA. DR EMBL; AF211937; AAF63705.1; JOINED; Genomic_DNA. DR EMBL; AK002448; BAB22108.1; -; mRNA. DR EMBL; BC005626; AAH05626.1; -; mRNA. DR PIR; JQ0064; JQ0064. DR RefSeq; NP_031478.1; NM_007452.2. DR UniGene; Mm.29821; -. DR ProteinModelPortal; P20108; -. DR SMR; P20108; 64-254. DR IntAct; P20108; 4. DR MINT; MINT-217585; -. DR STRING; 10090.ENSMUSP00000025961; -. DR PeroxiBase; 4499; Mm2CysPrx03. DR PhosphoSite; P20108; -. DR REPRODUCTION-2DPAGE; IPI00116192; -. DR REPRODUCTION-2DPAGE; P20108; -. DR PaxDb; P20108; -. DR PRIDE; P20108; -. DR Ensembl; ENSMUST00000025961; ENSMUSP00000025961; ENSMUSG00000024997. DR GeneID; 11757; -. DR KEGG; mmu:11757; -. DR UCSC; uc008icd.1; mouse. DR CTD; 10935; -. DR MGI; MGI:88034; Prdx3. DR eggNOG; COG0450; -. DR GeneTree; ENSGT00390000004653; -. DR HOGENOM; HOG000022343; -. DR HOVERGEN; HBG000286; -. DR InParanoid; P20108; -. DR KO; K03386; -. DR OMA; TAVHNGE; -. DR OrthoDB; EOG7T1RCD; -. DR TreeFam; TF105181; -. DR NextBio; 279507; -. DR PRO; PR:P20108; -. DR ArrayExpress; P20108; -. DR Bgee; P20108; -. DR CleanEx; MM_PRDX3; -. DR Genevestigator; P20108; -. DR GO; GO:0005769; C:early endosome; IEA:Ensembl. DR GO; GO:0008385; C:IkappaB kinase complex; IEA:Ensembl. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR GO; GO:0043027; F:cysteine-type endopeptidase inhibitor activity involved in apoptotic process; IEA:Ensembl. DR GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW. DR GO; GO:0051920; F:peroxiredoxin activity; IEA:UniProtKB-EC. DR GO; GO:0042744; P:hydrogen peroxide catabolic process; ISO:MGI. DR GO; GO:0001893; P:maternal placenta development; IMP:MGI. DR GO; GO:0007005; P:mitochondrion organization; IEA:Ensembl. DR GO; GO:0030099; P:myeloid cell differentiation; IMP:MGI. DR GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl. DR GO; GO:0033673; P:negative regulation of kinase activity; IEA:Ensembl. DR GO; GO:0008284; P:positive regulation of cell proliferation; IEA:Ensembl. DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IEA:Ensembl. DR GO; GO:0051881; P:regulation of mitochondrial membrane potential; IEA:Ensembl. DR GO; GO:0032496; P:response to lipopolysaccharide; IMP:MGI. DR Gene3D; 3.40.30.10; -; 1. DR InterPro; IPR000866; AhpC/TSA. DR InterPro; IPR024706; Peroxiredoxin_AhpC-typ. DR InterPro; IPR019479; Peroxiredoxin_C. DR InterPro; IPR012336; Thioredoxin-like_fold. DR Pfam; PF10417; 1-cysPrx_C; 1. DR Pfam; PF00578; AhpC-TSA; 1. DR PIRSF; PIRSF000239; AHPC; 1. DR SUPFAM; SSF52833; SSF52833; 1. DR PROSITE; PS51352; THIOREDOXIN_2; 1. PE 1: Evidence at protein level; KW Acetylation; Antioxidant; Complete proteome; KW Direct protein sequencing; Disulfide bond; Mitochondrion; KW Oxidoreductase; Peroxidase; Phosphoprotein; Redox-active center; KW Reference proteome; Transit peptide. FT TRANSIT 1 63 Mitochondrion (By similarity). FT CHAIN 64 257 Thioredoxin-dependent peroxide reductase, FT mitochondrial. FT /FTId=PRO_0000023783. FT DOMAIN 64 222 Thioredoxin. FT ACT_SITE 109 109 Cysteine sulfenic acid (-SOH) FT intermediate (By similarity). FT MOD_RES 84 84 N6-succinyllysine. FT MOD_RES 92 92 N6-acetyllysine; alternate. FT MOD_RES 92 92 N6-succinyllysine; alternate. FT DISULFID 109 109 Interchain (with C-230); in linked form FT (By similarity). FT DISULFID 230 230 Interchain (with C-109); in linked form FT (By similarity). SQ SEQUENCE 257 AA; 28127 MW; 66513F2C5F1D56C0 CRC64; MAAAAGRLLW SSVARHASAI SRSISASTVL RPVASRRTCL TDILWSASAQ GKSAFSTSSS FHTPAVTQHA PYFKGTAVVN GEFKELSLDD FKGKYLVLFF YPLDFTFVCP TEIVAFSDKA NEFHDVNCEV VAVSVDSHFS HLAWINTPRK NGGLGHMNIT LLSDITKQIS RDYGVLLESA GIALRGLFII DPNGVVKHLS VNDLPVGRSV EETLRLVKAF QFVETHGEVC PANWTPESPT IKPSPTASKE YFEKVHQ // ID PRDX4_MOUSE Reviewed; 274 AA. AC O08807; B1AZS7; Q3U8E4; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1997, sequence version 1. DT 19-MAR-2014, entry version 129. DE RecName: Full=Peroxiredoxin-4; DE EC=1.11.1.15; DE AltName: Full=Antioxidant enzyme AOE372; DE AltName: Full=Peroxiredoxin IV; DE Short=Prx-IV; DE AltName: Full=Thioredoxin peroxidase AO372; DE AltName: Full=Thioredoxin-dependent peroxide reductase A0372; DE Flags: Precursor; GN Name=Prdx4; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=C57BL/6J; RX PubMed=11229364; DOI=10.1089/15230860050192288; RA Wong C.M., Chun A.C., Kok K.H., Zhou Y., Fung P.C., Kung H.F., RA Jeang K.-T., Jin D.-Y.; RT "Characterization of human and mouse peroxiredoxin IV: evidence for RT inhibition by Prx-IV of epidermal growth factor- and p53-induced RT reactive oxygen species."; RL Antioxid. Redox Signal. 2:507-518(2000). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J, and DBA/2; TISSUE=Bone marrow, and Liver; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J, and NMRI; TISSUE=Mammary gland, and Mammary tumor; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP PROTEIN SEQUENCE OF 190-203 AND 216-226. RC STRAIN=C57BL/6; TISSUE=Brain; RA Lubec G., Kang S.U., Yang J.W., Zigmond M.; RL Submitted (JUL-2007) to UniProtKB. CC -!- FUNCTION: Probably involved in redox regulation of the cell. CC Regulates the activation of NF-kappa-B in the cytosol by a CC modulation of I-kappa-B-alpha phosphorylation. CC -!- CATALYTIC ACTIVITY: 2 R'-SH + ROOH = R'-S-S-R' + H(2)O + ROH. CC -!- SUBUNIT: Homodimer or heterodimer with PRDX1; disulfide-linked, CC upon oxidation. CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Secreted (By CC similarity). CC -!- MISCELLANEOUS: The active site is the redox-active Cys-127 CC oxidized to Cys-SOH. Cys-SOH rapidly reacts with Cys-248-SH of the CC other subunit to form an intermolecular disulfide with a CC concomitant homodimer formation. The enzyme may be subsequently CC regenerated by reduction of the disulfide by thioredoxin (By CC similarity). CC -!- MISCELLANEOUS: Irreversibly inactivated by overoxidation of Cys- CC 127 (to Cys-SO(3)H) upon oxidative stress (By similarity). CC -!- SIMILARITY: Belongs to the AhpC/TSA family. CC -!- SIMILARITY: Contains 1 thioredoxin domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U96746; AAB57846.1; -; mRNA. DR EMBL; AK005031; BAB23758.1; -; mRNA. DR EMBL; AK146402; BAE27143.1; -; mRNA. DR EMBL; AK152255; BAE31074.1; -; mRNA. DR EMBL; BX005263; CAM23139.1; -; Genomic_DNA. DR EMBL; BC003349; AAH03349.1; -; mRNA. DR EMBL; BC019578; AAH19578.1; -; mRNA. DR RefSeq; NP_058044.1; NM_016764.4. DR UniGene; Mm.247542; -. DR PDB; 3VWU; X-ray; 3.30 A; A/B/C/D/E/F/G/H/I/J=41-274. DR PDB; 3VWV; X-ray; 1.80 A; A/B=87-274. DR PDB; 3W8J; X-ray; 2.10 A; C/D=244-263. DR PDBsum; 3VWU; -. DR PDBsum; 3VWV; -. DR PDBsum; 3W8J; -. DR ProteinModelPortal; O08807; -. DR SMR; O08807; 78-272. DR BioGrid; 207303; 1. DR IntAct; O08807; 5. DR MINT; MINT-1862981; -. DR STRING; 10090.ENSMUSP00000026328; -. DR PeroxiBase; 4532; Mm2CysPrx04. DR PhosphoSite; O08807; -. DR REPRODUCTION-2DPAGE; O08807; -. DR PaxDb; O08807; -. DR PRIDE; O08807; -. DR Ensembl; ENSMUST00000026328; ENSMUSP00000026328; ENSMUSG00000025289. DR GeneID; 53381; -. DR KEGG; mmu:53381; -. DR UCSC; uc009uru.1; mouse. DR CTD; 10549; -. DR MGI; MGI:1859815; Prdx4. DR eggNOG; COG0450; -. DR GeneTree; ENSGT00390000004653; -. DR HOGENOM; HOG000022343; -. DR HOVERGEN; HBG000286; -. DR InParanoid; B1AZS7; -. DR KO; K03386; -. DR OrthoDB; EOG7T1RCD; -. DR TreeFam; TF105181; -. DR NextBio; 310209; -. DR PRO; PR:O08807; -. DR ArrayExpress; O08807; -. DR Bgee; O08807; -. DR CleanEx; MM_PRDX4; -. DR Genevestigator; O08807; -. DR GO; GO:0005829; C:cytosol; IDA:MGI. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI. DR GO; GO:0005615; C:extracellular space; IEA:Ensembl. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW. DR GO; GO:0051920; F:peroxiredoxin activity; IEA:UniProtKB-EC. DR GO; GO:0042803; F:protein homodimerization activity; IDA:MGI. DR GO; GO:0019471; P:4-hydroxyproline metabolic process; IGI:MGI. DR GO; GO:0045454; P:cell redox homeostasis; IGI:MGI. DR GO; GO:0030198; P:extracellular matrix organization; IGI:MGI. DR GO; GO:0008584; P:male gonad development; IMP:MGI. DR GO; GO:2000255; P:negative regulation of male germ cell proliferation; IMP:MGI. DR GO; GO:0055114; P:oxidation-reduction process; IMP:MGI. DR GO; GO:0022417; P:protein maturation by protein folding; IGI:MGI. DR GO; GO:0072593; P:reactive oxygen species metabolic process; IDA:MGI. DR GO; GO:0007283; P:spermatogenesis; IMP:MGI. DR Gene3D; 3.40.30.10; -; 1. DR InterPro; IPR000866; AhpC/TSA. DR InterPro; IPR024706; Peroxiredoxin_AhpC-typ. DR InterPro; IPR019479; Peroxiredoxin_C. DR InterPro; IPR012336; Thioredoxin-like_fold. DR Pfam; PF10417; 1-cysPrx_C; 1. DR Pfam; PF00578; AhpC-TSA; 1. DR PIRSF; PIRSF000239; AHPC; 1. DR SUPFAM; SSF52833; SSF52833; 1. DR PROSITE; PS51352; THIOREDOXIN_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Antioxidant; Complete proteome; Cytoplasm; KW Direct protein sequencing; Disulfide bond; Oxidoreductase; Peroxidase; KW Redox-active center; Reference proteome; Secreted; Signal. FT SIGNAL 1 40 By similarity. FT CHAIN 41 274 Peroxiredoxin-4. FT /FTId=PRO_0000135099. FT DOMAIN 82 240 Thioredoxin. FT ACT_SITE 127 127 Cysteine sulfenic acid (-SOH) FT intermediate (By similarity). FT DISULFID 127 127 Interchain (with C-248); in linked form FT (By similarity). FT DISULFID 248 248 Interchain (with C-127); in linked form FT (By similarity). FT STRAND 92 97 FT STRAND 100 105 FT HELIX 106 109 FT STRAND 112 118 FT STRAND 122 126 FT HELIX 129 136 FT HELIX 138 143 FT STRAND 146 154 FT HELIX 156 163 FT HELIX 167 169 FT STRAND 179 181 FT HELIX 186 190 FT TURN 196 199 FT STRAND 204 208 FT STRAND 212 219 FT HELIX 226 244 SQ SEQUENCE 274 AA; 31053 MW; 73DB5374EC46241C CRC64; MEARSKLLDG TTASRRWTRK LVLLLPPLLL FLLRTESLQG LESDERFRTR ENECHFYAGG QVYPGEASRV SVADHSLHLS KAKISKPAPY WEGTAVINGE FKELKLTDYR GKYLVFFFYP LDFTFVCPTE IIAFGDRIEE FKSINTEVVA CSVDSQFTHL AWINTPRRQG GLGPIRIPLL SDLNHQISKD YGVYLEDSGH TLRGLFIIDD KGVLRQITLN DLPVGRSVDE TLRLVQAFQY TDKHGEVCPA GWKPGSETII PDPAGKLKYF DKLN // ID PRDX2_MOUSE Reviewed; 198 AA. AC Q61171; O88376; Q60796; Q9CWJ4; Q9DB49; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 19-MAR-2014, entry version 141. DE RecName: Full=Peroxiredoxin-2; DE EC=1.11.1.15; DE AltName: Full=Thiol-specific antioxidant protein; DE Short=TSA; DE AltName: Full=Thioredoxin peroxidase 1; DE AltName: Full=Thioredoxin-dependent peroxide reductase 1; GN Name=Prdx2; Synonyms=Tdpx1, Tpx; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=BALB/c; TISSUE=Brain; RX PubMed=9115640; RA Ichimiya S., Davis J.G., O'Rourke D.M., Katsumata M., Greene M.I.; RT "Murine thioredoxin peroxidase delays neuronal apoptosis and is RT expressed in areas of the brain most susceptible to hypoxic and RT ischemic injury."; RL DNA Cell Biol. 16:311-321(1997). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=129; RA Oberbaeumer I.; RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=C57BL/6; RA Chae H.Z., Kim H., Rhee S.; RL Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. RC STRAIN=129/SvJ; RX PubMed=9714804; DOI=10.1016/S0378-1119(98)00290-X; RA Lim M.J., Chae H.Z., Rhee S.G., Yu D.-Y., Lee K.-K., Yeom Y.I.; RT "The type II peroxiredoxin gene family of the mouse: molecular RT structure, expression and evolution."; RL Gene 216:197-205(1998). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=NOD; TISSUE=Cerebellum, Small intestine, and Thymus; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Brain, and Mammary gland; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [7] RP PROTEIN SEQUENCE OF 2-10 AND 120-135, CLEAVAGE OF INITIATOR RP METHIONINE, ACETYLATION AT ALA-2, AND MASS SPECTROMETRY. RC STRAIN=C57BL/6; TISSUE=Liver; RA Bienvenut W.V.; RL Submitted (JUL-2005) to UniProtKB. RN [8] RP PROTEIN SEQUENCE OF 11-26; 92-109; 120-127 AND 140-150, AND MASS RP SPECTROMETRY. RC STRAIN=C57BL/6; TISSUE=Brain, and Hippocampus; RA Lubec G., Kang S.U., Klug S., Yang J.W., Zigmond M.; RL Submitted (JUL-2007) to UniProtKB. RN [9] RP INTERACTION WITH TIPIN. RX PubMed=17141802; DOI=10.1016/j.jmb.2006.10.097; RA Gotter A.L., Suppa C., Emanuel B.S.; RT "Mammalian TIMELESS and Tipin are evolutionarily conserved replication RT fork-associated factors."; RL J. Mol. Biol. 366:36-52(2007). CC -!- FUNCTION: Involved in redox regulation of the cell. Reduces CC peroxides with reducing equivalents provided through the CC thioredoxin system. It is not able to receive electrons from CC glutaredoxin. May play an important role in eliminating peroxides CC generated during metabolism. Might participate in the signaling CC cascades of growth factors and tumor necrosis factor-alpha by CC regulating the intracellular concentrations of H(2)O(2). CC -!- CATALYTIC ACTIVITY: 2 R'-SH + ROOH = R'-S-S-R' + H(2)O + ROH. CC -!- SUBUNIT: Homodimer; disulfide-linked, upon oxidation (By CC similarity). Interacts with TIPIN. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- TISSUE SPECIFICITY: Widely expressed with highest levels in bone CC marrow. High levels also found in heart, brain, kidney and CC skeletal muscle. Lower levels in liver, lung and thymus. CC -!- MISCELLANEOUS: The active site is the redox-active Cys-51 oxidized CC to Cys-SOH. Cys-SOH rapidly reacts with Cys-172-SH of the other CC subunit to form an intermolecular disulfide with a concomitant CC homodimer formation. The enzyme may be subsequently regenerated by CC reduction of the disulfide by thioredoxin (By similarity). CC -!- MISCELLANEOUS: Inactivated upon oxidative stress by overoxidation CC of Cys-51 to Cys-SO(2)H and Cys-SO(3)H. Cys-SO(2)H is retroreduced CC to Cys-SOH after removal of H(2)O(2), while Cys-SO(3)H may be CC irreversibly oxidized (By similarity). CC -!- SIMILARITY: Belongs to the AhpC/TSA family. CC -!- SIMILARITY: Contains 1 thioredoxin domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U51679; AAB01941.1; -; mRNA. DR EMBL; X82067; CAA57566.1; -; mRNA. DR EMBL; U20611; AAA69475.1; -; mRNA. DR EMBL; AF032722; AAC35744.1; -; Genomic_DNA. DR EMBL; AF032718; AAC35744.1; JOINED; Genomic_DNA. DR EMBL; AF032719; AAC35744.1; JOINED; Genomic_DNA. DR EMBL; AF032720; AAC35744.1; JOINED; Genomic_DNA. DR EMBL; AF032721; AAC35744.1; JOINED; Genomic_DNA. DR EMBL; AK005225; BAB23893.1; -; mRNA. DR EMBL; AK008433; BAB25666.1; -; mRNA. DR EMBL; AK010653; BAB27093.1; -; mRNA. DR EMBL; AK088280; BAC40255.1; -; mRNA. DR EMBL; BC002034; AAH02034.1; -; mRNA. DR EMBL; BC081454; AAH81454.1; -; mRNA. DR RefSeq; NP_035693.3; NM_011563.5. DR RefSeq; XP_006530898.1; XM_006530835.1. DR UniGene; Mm.347009; -. DR UniGene; Mm.393373; -. DR ProteinModelPortal; Q61171; -. DR SMR; Q61171; 3-198. DR BioGrid; 204094; 1. DR IntAct; Q61171; 13. DR MINT; MINT-1862390; -. DR PeroxiBase; 4474; Mm2CysPrx02. DR PhosphoSite; Q61171; -. DR REPRODUCTION-2DPAGE; Q61171; -. DR SWISS-2DPAGE; Q61171; -. DR UCD-2DPAGE; Q61171; -. DR PaxDb; Q61171; -. DR PRIDE; Q61171; -. DR Ensembl; ENSMUST00000005292; ENSMUSP00000005292; ENSMUSG00000005161. DR Ensembl; ENSMUST00000109733; ENSMUSP00000105355; ENSMUSG00000005161. DR Ensembl; ENSMUST00000109734; ENSMUSP00000105356; ENSMUSG00000005161. DR Ensembl; ENSMUST00000164807; ENSMUSP00000126451; ENSMUSG00000005161. DR GeneID; 21672; -. DR KEGG; mmu:21672; -. DR UCSC; uc009mom.1; mouse. DR CTD; 7001; -. DR MGI; MGI:109486; Prdx2. DR eggNOG; COG0450; -. DR GeneTree; ENSGT00390000004653; -. DR HOGENOM; HOG000022343; -. DR HOVERGEN; HBG000286; -. DR InParanoid; Q61171; -. DR KO; K03386; -. DR OMA; LQFTEEF; -. DR OrthoDB; EOG7T1RCD; -. DR TreeFam; TF105181; -. DR ChiTaRS; PRDX2; mouse. DR NextBio; 300952; -. DR PRO; PR:Q61171; -. DR ArrayExpress; Q61171; -. DR Bgee; Q61171; -. DR CleanEx; MM_PRDX2; -. DR Genevestigator; Q61171; -. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR GO; GO:0008430; F:selenium binding; TAS:MGI. DR GO; GO:0008379; F:thioredoxin peroxidase activity; ISS:MGI. DR GO; GO:0000187; P:activation of MAPK activity; IMP:MGI. DR GO; GO:0048872; P:homeostasis of number of cells; IMP:MGI. DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IMP:MGI. DR GO; GO:2001240; P:negative regulation of extrinsic apoptotic signaling pathway in absence of ligand; IDA:MGI. DR GO; GO:0031665; P:negative regulation of lipopolysaccharide-mediated signaling pathway; IMP:MGI. DR GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; IMP:MGI. DR GO; GO:2000378; P:negative regulation of reactive oxygen species metabolic process; IMP:MGI. DR GO; GO:0045581; P:negative regulation of T cell differentiation; IMP:MGI. DR GO; GO:0030194; P:positive regulation of blood coagulation; IMP:BHF-UCL. DR GO; GO:0010310; P:regulation of hydrogen peroxide metabolic process; IMP:MGI. DR GO; GO:0019430; P:removal of superoxide radicals; IMP:BHF-UCL. DR GO; GO:0002536; P:respiratory burst involved in inflammatory response; IMP:MGI. DR GO; GO:0032496; P:response to lipopolysaccharide; IMP:MGI. DR GO; GO:0042098; P:T cell proliferation; IMP:MGI. DR GO; GO:0048538; P:thymus development; IMP:MGI. DR Gene3D; 3.40.30.10; -; 1. DR InterPro; IPR000866; AhpC/TSA. DR InterPro; IPR024706; Peroxiredoxin_AhpC-typ. DR InterPro; IPR019479; Peroxiredoxin_C. DR InterPro; IPR012336; Thioredoxin-like_fold. DR Pfam; PF10417; 1-cysPrx_C; 1. DR Pfam; PF00578; AhpC-TSA; 1. DR PIRSF; PIRSF000239; AHPC; 1. DR SUPFAM; SSF52833; SSF52833; 1. DR PROSITE; PS51352; THIOREDOXIN_2; 1. PE 1: Evidence at protein level; KW Acetylation; Antioxidant; Complete proteome; Cytoplasm; KW Direct protein sequencing; Disulfide bond; Oxidoreductase; Peroxidase; KW Redox-active center; Reference proteome. FT INIT_MET 1 1 Removed. FT CHAIN 2 198 Peroxiredoxin-2. FT /FTId=PRO_0000135081. FT DOMAIN 6 164 Thioredoxin. FT ACT_SITE 51 51 Cysteine sulfenic acid (-SOH) FT intermediate (By similarity). FT MOD_RES 2 2 N-acetylalanine. FT DISULFID 51 51 Interchain (with C-172); in linked form FT (By similarity). FT DISULFID 172 172 Interchain (with C-51); in linked form FT (By similarity). FT CONFLICT 38 38 V -> M (in Ref. 5; BAB27093). FT CONFLICT 39 39 V -> D (in Ref. 5; BAB23893). FT CONFLICT 69 69 G -> R (in Ref. 5; BAB23893). FT CONFLICT 97 97 G -> A (in Ref. 3; AAA69475). FT CONFLICT 113 113 Q -> H (in Ref. 5; BAB23893). FT CONFLICT 124 124 I -> V (in Ref. 5; BAB23893). FT CONFLICT 135 135 K -> S (in Ref. 5; BAB23893). FT CONFLICT 182 182 T -> N (in Ref. 3 and 4). SQ SEQUENCE 198 AA; 21779 MW; FE216F5426F7174D CRC64; MASGNAQIGK SAPDFTATAV VDGAFKEIKL SDYRGKYVVL FFYPLDFTFV CPTEIIAFSD HAEDFRKLGC EVLGVSVDSQ FTHLAWINTP RKEGGLGPLN IPLLADVTKS LSQNYGVLKN DEGIAYRGLF IIDAKGVLRQ ITVNDLPVGR SVDEALRLVQ AFQYTDEHGE VCPAGWKPGS DTIKPNVDDS KEYFSKHN // ID PRDX5_MOUSE Reviewed; 210 AA. AC P99029; Q9QX45; Q9QZ75; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 21-FEB-2002, sequence version 2. DT 19-MAR-2014, entry version 129. DE RecName: Full=Peroxiredoxin-5, mitochondrial; DE EC=1.11.1.15; DE AltName: Full=Antioxidant enzyme B166; DE Short=AOEB166; DE AltName: Full=Liver tissue 2D-page spot 2D-0014IV; DE AltName: Full=PLP; DE AltName: Full=Peroxiredoxin V; DE Short=Prx-V; DE AltName: Full=Peroxisomal antioxidant enzyme; DE AltName: Full=Thioredoxin peroxidase PMP20; DE AltName: Full=Thioredoxin reductase; DE Flags: Precursor; GN Name=Prdx5; Synonyms=Prdx6; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION. RX PubMed=10679306; DOI=10.1006/bbrc.2000.2231; RA Zhou Y., Kok K.H., Chun A.C.S., Wong C.M., Wu H.W., Lin M.C.M., RA Fung P.C.W., Kung H.-F., Jin D.-Y.; RT "Mouse peroxiredoxin V is a thioredoxin peroxidase that inhibits p53- RT induced apoptosis."; RL Biochem. Biophys. Res. Commun. 268:921-927(2000). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION. RX PubMed=10514471; DOI=10.1074/jbc.274.42.29897; RA Yamashita H., Avraham S., Jiang S., London R., Van Veldhoven P.P., RA Subramani S., Rogers R.A., Avraham H.; RT "Characterization of human and murine PMP20 peroxisomal proteins that RT exhibit antioxidant activity in vitro."; RL J. Biol. Chem. 274:29897-29904(1999). RN [3] RP NUCLEOTIDE SEQUENCE, AND CHARACTERIZATION. RC STRAIN=C3H/HeJ; TISSUE=Lung; RX PubMed=10521424; DOI=10.1074/jbc.274.43.30451; RA Knoops B., Clippe A., Bogard C., Arsalane K., Wattiez R., Hermans C., RA Duconseille E., Falmagne P., Bernard A.; RT "Cloning and characterization of AOEB166, a novel mammalian RT antioxidant enzyme of the peroxiredoxin family."; RL J. Biol. Chem. 274:30451-30458(1999). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=10753630; DOI=10.1006/bbrc.2000.2430; RA Lee T.H., Kim S.J., Kang S.W., Lee K.K., Rhee S.G., Yu D.Y.; RT "Molecular cloning and characterization of the mouse Peroxiredoxin V RT gene."; RL Biochem. Biophys. Res. Commun. 270:356-362(2000). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Kidney; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Mammary tumor; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [7] RP PROTEIN SEQUENCE OF 50-61. RC TISSUE=Liver; RA Sanchez J.-C., Rouge V., Frutiger S., Hughes G.J., Yan J.X., RA Hoogland C., Appel R.D., Binz P.-A., Hochstrasser D.F., Cowthorne M.; RL Submitted (AUG-1998) to UniProtKB. RN [8] RP PROTEIN SEQUENCE OF 72-79; 83-112 AND 145-172, AND MASS SPECTROMETRY. RC STRAIN=C57BL/6; TISSUE=Brain, and Hippocampus; RA Lubec G., Klug S., Kang S.U.; RL Submitted (APR-2007) to UniProtKB. RN [9] RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-70; LYS-79 AND LYS-112, RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., RA Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). RN [10] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-70; LYS-71 AND LYS-79, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23576753; DOI=10.1073/pnas.1302961110; RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., RA Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.; RT "Label-free quantitative proteomics of the lysine acetylome in RT mitochondria identifies substrates of SIRT3 in metabolic pathways."; RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013). CC -!- FUNCTION: Reduces hydrogen peroxide and alkyl hydroperoxides with CC reducing equivalents provided through the thioredoxin system. CC Involved in intracellular redox signaling. CC -!- CATALYTIC ACTIVITY: 2 R'-SH + ROOH = R'-S-S-R' + H(2)O + ROH. CC -!- SUBUNIT: Monomer. CC -!- SUBCELLULAR LOCATION: Mitochondrion. Cytoplasm. Peroxisome. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative initiation; Named isoforms=2; CC Name=Mitochondrial; CC IsoId=P99029-1; Sequence=Displayed; CC Name=Cytoplasmic+peroxisomal; CC IsoId=P99029-2; Sequence=VSP_018830; CC -!- TISSUE SPECIFICITY: Widely expressed. CC -!- SIMILARITY: Belongs to the peroxiredoxin 2 family. CC -!- SIMILARITY: Contains 1 thioredoxin domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF197951; AAF04855.1; -; mRNA. DR EMBL; AF124994; AAF27532.1; -; mRNA. DR EMBL; AF110733; AAG13450.1; -; mRNA. DR EMBL; AF208730; AAF21016.1; -; Genomic_DNA. DR EMBL; AF208729; AAF21016.1; JOINED; Genomic_DNA. DR EMBL; AK002383; BAB22058.1; -; mRNA. DR EMBL; AK003332; BAB22720.1; -; mRNA. DR EMBL; BC008174; AAH08174.1; -; mRNA. DR PIR; JC7239; JC7239. DR RefSeq; NP_036151.1; NM_012021.2. DR UniGene; Mm.279782; -. DR ProteinModelPortal; P99029; -. DR SMR; P99029; 50-210. DR BioGrid; 207718; 2. DR IntAct; P99029; 4. DR MINT; MINT-1859227; -. DR PeroxiBase; 4453; MmPrxV. DR PhosphoSite; P99029; -. DR REPRODUCTION-2DPAGE; P99029; -. DR SWISS-2DPAGE; P99029; -. DR PaxDb; P99029; -. DR PRIDE; P99029; -. DR Ensembl; ENSMUST00000025904; ENSMUSP00000025904; ENSMUSG00000024953. [P99029-1] DR GeneID; 54683; -. DR KEGG; mmu:54683; -. DR UCSC; uc008gjc.1; mouse. [P99029-1] DR CTD; 25824; -. DR MGI; MGI:1859821; Prdx5. DR eggNOG; COG0678; -. DR GeneTree; ENSGT00390000018173; -. DR HOGENOM; HOG000255884; -. DR HOVERGEN; HBG053675; -. DR InParanoid; P99029; -. DR KO; K11187; -. DR OMA; MSAWGKQ; -. DR OrthoDB; EOG77Q4XX; -. DR TreeFam; TF105182; -. DR NextBio; 311536; -. DR PRO; PR:P99029; -. DR ArrayExpress; P99029; -. DR Bgee; P99029; -. DR CleanEx; MM_PRDX5; -. DR CleanEx; MM_PRDX6; -. DR Genevestigator; P99029; -. DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:Ensembl. DR GO; GO:0005829; C:cytosol; IEA:Ensembl. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR GO; GO:0005634; C:nucleus; IEA:Ensembl. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl. DR GO; GO:0005782; C:peroxisomal matrix; ISS:UniProtKB. DR GO; GO:0016209; F:antioxidant activity; ISS:UniProtKB. DR GO; GO:0043027; F:cysteine-type endopeptidase inhibitor activity involved in apoptotic process; IEA:Ensembl. DR GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW. DR GO; GO:0072541; F:peroxynitrite reductase activity; IEA:Ensembl. DR GO; GO:0005102; F:receptor binding; ISS:UniProtKB. DR GO; GO:0001016; F:RNA polymerase III regulatory region DNA binding; IEA:Ensembl. DR GO; GO:0042744; P:hydrogen peroxide catabolic process; ISS:UniProtKB. DR GO; GO:0070995; P:NADPH oxidation; IEA:Ensembl. DR GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl. DR GO; GO:0051354; P:negative regulation of oxidoreductase activity; IEA:Ensembl. DR GO; GO:0016480; P:negative regulation of transcription from RNA polymerase III promoter; IEA:Ensembl. DR GO; GO:0032967; P:positive regulation of collagen biosynthetic process; IEA:Ensembl. DR GO; GO:2001057; P:reactive nitrogen species metabolic process; IEA:Ensembl. DR GO; GO:0060785; P:regulation of apoptosis involved in tissue homeostasis; IEA:Ensembl. DR Gene3D; 3.40.30.10; -; 1. DR InterPro; IPR013740; Redoxin. DR InterPro; IPR012336; Thioredoxin-like_fold. DR Pfam; PF08534; Redoxin; 1. DR SUPFAM; SSF52833; SSF52833; 1. DR PROSITE; PS51352; THIOREDOXIN_2; 1. PE 1: Evidence at protein level; KW Acetylation; Alternative initiation; Antioxidant; Complete proteome; KW Cytoplasm; Direct protein sequencing; Disulfide bond; Mitochondrion; KW Oxidoreductase; Peroxidase; Peroxisome; Redox-active center; KW Reference proteome; Transit peptide. FT TRANSIT 1 48 Mitochondrion (Potential). FT CHAIN 49 210 Peroxiredoxin-5, mitochondrial. FT /FTId=PRO_0000023795. FT DOMAIN 52 210 Thioredoxin. FT MOTIF 208 210 Microbody targeting signal (By FT similarity). FT ACT_SITE 96 96 Cysteine sulfenic acid (-SOH) FT intermediate (Potential). FT MOD_RES 70 70 N6-acetyllysine; alternate. FT MOD_RES 70 70 N6-succinyllysine; alternate. FT MOD_RES 71 71 N6-acetyllysine. FT MOD_RES 79 79 N6-acetyllysine; alternate. FT MOD_RES 79 79 N6-succinyllysine; alternate. FT MOD_RES 112 112 N6-succinyllysine. FT DISULFID 96 200 Redox-active (By similarity). FT VAR_SEQ 1 48 Missing (in isoform FT Cytoplasmic+peroxisomal). FT /FTId=VSP_018830. FT CONFLICT 55 55 G -> D (in Ref. 7; AA sequence). FT CONFLICT 83 102 GVLFGVPGAFTPGCSKTHLP -> VFCLESLGHLHLAVLRP FT TA (in Ref. 4; AAF21016). SQ SEQUENCE 210 AA; 21897 MW; E944104CC468BDD8 CRC64; MLQLGLRVLG CKASSVLRAS TCLAGRAGRK EAGWECGGAR SFSSSAVTMA PIKVGDAIPS VEVFEGEPGK KVNLAELFKG KKGVLFGVPG AFTPGCSKTH LPGFVEQAGA LKAKGAQVVA CLSVNDVFVI EEWGRAHQAE GKVRLLADPT GAFGKATDLL LDDSLVSLFG NRRLKRFSMV IDNGIVKALN VEPDGTGLTC SLAPNILSQL // ID PRDX6_MOUSE Reviewed; 224 AA. AC O08709; Q91WT2; Q9QWP4; Q9QWW0; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 19-MAR-2014, entry version 131. DE RecName: Full=Peroxiredoxin-6; DE EC=1.11.1.15; DE AltName: Full=1-Cys peroxiredoxin; DE Short=1-Cys PRX; DE AltName: Full=Acidic calcium-independent phospholipase A2; DE Short=aiPLA2; DE EC=3.1.1.-; DE AltName: Full=Antioxidant protein 2; DE AltName: Full=Non-selenium glutathione peroxidase; DE Short=NSGPx; DE EC=1.11.1.9; GN Name=Prdx6; Synonyms=Aop2, Ltw4, Prdx5; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 2-26. RC STRAIN=C3H/FEJ, C57BL/6J, and DBA/2J; TISSUE=Kidney, and Liver; RX PubMed=9205120; DOI=10.1006/geno.1997.4762; RA Iakoubova O.A., Pacella L.A., Her H., Beier D.R.; RT "LTW4 protein on mouse chromosome 1 is a member of a family of RT antioxidant proteins."; RL Genomics 42:474-478(1997). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=BALB/c; TISSUE=Skin; RX PubMed=9291135; RA Munz B., Frank S., Huebner G., Olsen E., Werner S.; RT "A novel type of glutathione peroxidase: expression and regulation RT during wound repair."; RL Biochem. J. 326:579-585(1997). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=129/SvJ, and C57BL/6; TISSUE=Brain; RX PubMed=10395907; DOI=10.1016/S0378-1119(99)00190-0; RA Lee T.-H., Yu S.-L., Kim S.-U., Kim Y.-M., Choi I., Kang S.W., RA Rhee S.G., Yu D.-Y.; RT "Characterization of the murine gene encoding 1-Cys peroxiredoxin and RT identification of highly homologous genes."; RL Gene 234:337-344(1999). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Pituitary; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Colon; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP PROTEIN SEQUENCE OF 2-22; 25-53; 98-106; 109-122; 145-155 AND 163-182, RP AND MASS SPECTROMETRY. RC STRAIN=C57BL/6; TISSUE=Brain, and Hippocampus; RA Lubec G., Kang S.U., Klug S., Yang J.W., Zigmond M.; RL Submitted (APR-2007) to UniProtKB. RN [7] RP INTERACTION WITH HTR2A. RX PubMed=14988405; DOI=10.1074/jbc.M312106200; RA Becamel C., Gavarini S., Chanrion B., Alonso G., Galeotti N., RA Dumuis A., Bockaert J., Marin P.; RT "The serotonin 5-HT2A and 5-HT2C receptors interact with specific sets RT of PDZ proteins."; RL J. Biol. Chem. 279:20257-20266(2004). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-89, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain; RX PubMed=18034455; DOI=10.1021/pr0701254; RA Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.; RT "Large-scale identification and evolution indexing of tyrosine RT phosphorylation sites from murine brain."; RL J. Proteome Res. 7:311-318(2008). RN [9] RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-209, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., RA Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). CC -!- FUNCTION: Involved in redox regulation of the cell. Can reduce CC H(2)O(2) and short chain organic, fatty acid, and phospholipid CC hydroperoxides. May play a role in the regulation of phospholipid CC turnover as well as in protection against oxidative injury (By CC similarity). CC -!- CATALYTIC ACTIVITY: 2 R'-SH + ROOH = R'-S-S-R' + H(2)O + ROH. CC -!- CATALYTIC ACTIVITY: 2 glutathione + H(2)O(2) = glutathione CC disulfide + 2 H(2)O. CC -!- SUBUNIT: Homodimer. Interacts with GSTP1; mediates PRDX6 CC glutathionylation and regeneration. Interacts with APEX1 and STH CC (By similarity). May interact with FAM168B (By similarity). May CC interact with HTR2A. CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Lysosome (By CC similarity). Cytoplasmic vesicle (By similarity). Note=Also found CC in lung secretory organelles (By similarity). CC -!- TISSUE SPECIFICITY: Highly expressed in heart, kidney and liver. CC Moderate expression in brain and stomach. Very low levels in CC intestine. CC -!- MISCELLANEOUS: The active site is the redox-active Cys-47 oxidized CC to Cys-SOH. Unlike 2-Cys peroxiredoxins, PRDX6 conserves only this CC peroxidatic cysteine. To regenerate and activate the enzyme, the CC oxidized form is directly reduced to cysteine by glutathione and CC not thioredoxin (By similarity). CC -!- MISCELLANEOUS: Irreversibly inactivated by overoxidation of Cys-47 CC (to Cys-SO(3)H) upon oxidative stress (By similarity). CC -!- SIMILARITY: Belongs to the AhpC/TSA family. Rehydrin subfamily. CC -!- SIMILARITY: Contains 1 thioredoxin domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF004670; AAC53277.1; -; mRNA. DR EMBL; Y12883; CAA73383.1; -; mRNA. DR EMBL; AF093852; AAC63376.1; -; mRNA. DR EMBL; AF093853; AAC67553.1; -; Genomic_DNA. DR EMBL; AF093857; AAD03716.1; -; Genomic_DNA. DR EMBL; AF093854; AAD03716.1; JOINED; Genomic_DNA. DR EMBL; AF093855; AAD03716.1; JOINED; Genomic_DNA. DR EMBL; AF093856; AAD03716.1; JOINED; Genomic_DNA. DR EMBL; AK030413; BAC26952.1; -; mRNA. DR EMBL; BC013489; AAH13489.1; -; mRNA. DR RefSeq; NP_031479.1; NM_007453.3. DR RefSeq; XP_006544594.1; XM_006544531.1. DR UniGene; Mm.186185; -. DR ProteinModelPortal; O08709; -. DR SMR; O08709; 5-224. DR BioGrid; 198118; 1. DR IntAct; O08709; 7. DR MINT; MINT-1869428; -. DR PhosphoSite; O08709; -. DR COMPLUYEAST-2DPAGE; O08709; -. DR REPRODUCTION-2DPAGE; O08709; -. DR SWISS-2DPAGE; O08709; -. DR UCD-2DPAGE; O08709; -. DR PaxDb; O08709; -. DR PRIDE; O08709; -. DR GeneID; 102642619; -. DR GeneID; 11758; -. DR KEGG; mmu:11758; -. DR CTD; 9588; -. DR MGI; MGI:894320; Prdx6. DR eggNOG; COG0450; -. DR HOVERGEN; HBG105234; -. DR InParanoid; O08709; -. DR KO; K11188; -. DR BRENDA; 1.11.1.15; 3474. DR ChiTaRS; PRDX6; mouse. DR NextBio; 279511; -. DR PRO; PR:O08709; -. DR CleanEx; MM_PRDX5; -. DR CleanEx; MM_PRDX6; -. DR Genevestigator; O08709; -. DR GO; GO:0016023; C:cytoplasmic membrane-bounded vesicle; IEA:UniProtKB-SubCell. DR GO; GO:0005829; C:cytosol; IDA:MGI. DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR GO; GO:0004602; F:glutathione peroxidase activity; IEA:UniProtKB-EC. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0004601; F:peroxidase activity; IMP:MGI. DR GO; GO:0051920; F:peroxiredoxin activity; IEA:UniProtKB-EC. DR GO; GO:0032060; P:bleb assembly; IMP:MGI. DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW. DR GO; GO:0000302; P:response to reactive oxygen species; IMP:MGI. DR Gene3D; 3.40.30.10; -; 1. DR InterPro; IPR000866; AhpC/TSA. DR InterPro; IPR024706; Peroxiredoxin_AhpC-typ. DR InterPro; IPR019479; Peroxiredoxin_C. DR InterPro; IPR012336; Thioredoxin-like_fold. DR Pfam; PF10417; 1-cysPrx_C; 1. DR Pfam; PF00578; AhpC-TSA; 1. DR PIRSF; PIRSF000239; AHPC; 1. DR SUPFAM; SSF52833; SSF52833; 1. DR PROSITE; PS51352; THIOREDOXIN_2; 1. PE 1: Evidence at protein level; KW Acetylation; Antioxidant; Complete proteome; Cytoplasm; KW Cytoplasmic vesicle; Direct protein sequencing; Disulfide bond; KW Hydrolase; Lipid degradation; Lipid metabolism; Lysosome; KW Multifunctional enzyme; Oxidoreductase; Peroxidase; Phosphoprotein; KW Redox-active center; Reference proteome. FT INIT_MET 1 1 Removed. FT CHAIN 2 224 Peroxiredoxin-6. FT /FTId=PRO_0000135103. FT DOMAIN 5 169 Thioredoxin. FT ACT_SITE 32 32 For phospholipase activity (By FT similarity). FT ACT_SITE 47 47 Cysteine sulfenic acid (-SOH) FT intermediate (By similarity). FT MOD_RES 44 44 Phosphothreonine (By similarity). FT MOD_RES 63 63 N6-acetyllysine (By similarity). FT MOD_RES 89 89 Phosphotyrosine. FT MOD_RES 209 209 N6-acetyllysine; alternate (By FT similarity). FT MOD_RES 209 209 N6-succinyllysine; alternate. FT DISULFID 47 47 Interchain; in linked form (By FT similarity). FT VARIANT 124 124 D -> A (in strain: C57BL/6, C57BL/6J and FT FVB/N). FT CONFLICT 154 154 G -> S (in Ref. 3; AAC67553). FT CONFLICT 181 181 W -> R (in Ref. 3; AAD03716). SQ SEQUENCE 224 AA; 24871 MW; AECDEDD332858B8F CRC64; MPGGLLLGDE APNFEANTTI GRIRFHDFLG DSWGILFSHP RDFTPVCTTE LGRAAKLAPE FAKRNVKLIA LSIDSVEDHL AWSKDINAYN GETPTEKLPF PIIDDKGRDL AILLGMLDPV EKDDNNMPVT ARVVFIFGPD KKLKLSILYP ATTGRNFDEI LRVVDSLQLT GTKPVATPVD WKKGESVMVV PTLSEEEAKQ CFPKGVFTKE LPSGKKYLRY TPQP // ID PROD2_MOUSE Reviewed; 456 AA. AC Q8VCZ9; Q2V058; Q9QX62; DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2002, sequence version 1. DT 19-MAR-2014, entry version 81. DE RecName: Full=Probable proline dehydrogenase 2; DE EC=1.5.5.2; DE AltName: Full=Kidney and liver proline oxidase 1; DE AltName: Full=MmPOX1; DE AltName: Full=Probable proline oxidase 2; DE AltName: Full=Proline oxidase-like protein; DE Short=PO; DE Short=Proline oxidase; GN Name=Prodh2; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Lin W.-W., Hu C.A., Valle D.; RL Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Yang Q., Tian Y., Wallner E.I., Kanwar Y.S.; RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Liver; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Liver; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP INDUCTION BY TCF1 AND HNF4A, AND DEVELOPMENTAL STAGE. RX PubMed=15581617; DOI=10.1016/j.febslet.2004.10.070; RA Kamiya A., Inoue Y., Kodama T., Gonzalez F.J.; RT "Hepatocyte nuclear factors 1alpha and 4alpha control expression of RT proline oxidase in adult liver."; RL FEBS Lett. 578:63-68(2004). RN [6] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-310 AND LYS-320, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23576753; DOI=10.1073/pnas.1302961110; RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., RA Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.; RT "Label-free quantitative proteomics of the lysine acetylome in RT mitochondria identifies substrates of SIRT3 in metabolic pathways."; RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013). CC -!- FUNCTION: Converts proline to delta-1-pyrroline-5-carboxylate CC (Probable). CC -!- CATALYTIC ACTIVITY: L-proline + a quinone = (S)-1-pyrroline-5- CC carboxylate + a quinol. CC -!- COFACTOR: FAD (By similarity). CC -!- PATHWAY: Amino-acid degradation; L-proline degradation into L- CC glutamate; L-glutamate from L-proline: step 1/2. CC -!- DEVELOPMENTAL STAGE: Expressed in liver at E14. Expression level CC increases at P5 and decreases after P21. CC -!- INDUCTION: In liver, by TCF1 and HNF4A. CC -!- SIMILARITY: Belongs to the proline oxidase family. CC -!- SEQUENCE CAUTION: CC Sequence=AAF21466.1; Type=Erroneous initiation; CC Sequence=AAQ13907.1; Type=Erroneous initiation; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U80019; AAF21466.1; ALT_INIT; mRNA. DR EMBL; AF222851; AAQ13907.1; ALT_INIT; mRNA. DR EMBL; AK050141; BAC34090.1; -; mRNA. DR EMBL; BC018182; AAH18182.1; -; mRNA. DR RefSeq; NP_062419.2; NM_019546.5. DR UniGene; Mm.270525; -. DR ProteinModelPortal; Q8VCZ9; -. DR IntAct; Q8VCZ9; 1. DR MINT; MINT-4119643; -. DR STRING; 10090.ENSMUSP00000062214; -. DR PhosphoSite; Q8VCZ9; -. DR PaxDb; Q8VCZ9; -. DR PRIDE; Q8VCZ9; -. DR DNASU; 56189; -. DR Ensembl; ENSMUST00000058280; ENSMUSP00000062214; ENSMUSG00000036892. DR GeneID; 56189; -. DR KEGG; mmu:56189; -. DR UCSC; uc009geo.1; mouse. DR CTD; 58510; -. DR MGI; MGI:1929093; Prodh2. DR eggNOG; COG0506; -. DR GeneTree; ENSGT00390000006265; -. DR HOGENOM; HOG000233406; -. DR HOVERGEN; HBG108294; -. DR InParanoid; Q8VCZ9; -. DR KO; K11394; -. DR OMA; SAMLRCV; -. DR OrthoDB; EOG7RZ5Q2; -. DR TreeFam; TF313544; -. DR UniPathway; UPA00261; UER00373. DR NextBio; 311988; -. DR PRO; PR:Q8VCZ9; -. DR ArrayExpress; Q8VCZ9; -. DR Bgee; Q8VCZ9; -. DR CleanEx; MM_PRODH2; -. DR Genevestigator; Q8VCZ9; -. DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:MGI. DR GO; GO:0004657; F:proline dehydrogenase activity; IEA:InterPro. DR GO; GO:0006537; P:glutamate biosynthetic process; IEA:InterPro. DR GO; GO:0010133; P:proline catabolic process to glutamate; IEA:UniProtKB-UniPathway. DR InterPro; IPR002872; Proline_DH. DR InterPro; IPR015659; Proline_oxidase. DR PANTHER; PTHR13914; PTHR13914; 1. DR Pfam; PF01619; Pro_dh; 1. PE 1: Evidence at protein level; KW Acetylation; Complete proteome; FAD; Flavoprotein; Oxidoreductase; KW Proline metabolism; Reference proteome. FT CHAIN 1 456 Probable proline dehydrogenase 2. FT /FTId=PRO_0000308624. FT MOD_RES 310 310 N6-acetyllysine. FT MOD_RES 320 320 N6-acetyllysine. FT CONFLICT 337 337 R -> H (in Ref. 1; AAF21466). FT CONFLICT 416 416 E -> K (in Ref. 1; AAF21466). SQ SEQUENCE 456 AA; 50723 MW; CD02C1474AADBD56 CRC64; MIWTRLPLYG PSKPSTGGWQ PLRFDGGAFH VKGTAELARA LLVLRLCAWP PLVTHGLAFQ AWSQRLLGSR LSGALLRASI YGQFVAGETA EEVRNCVGQL QALGLQPLLA VPTEEEPDST AKTSEVWYEE NLSAMLRCVD LSRALVDAHG PARNSLMQLK VTALASTRLC KELSAWIQRP RGSSELSPER LAEAMDSGRN LQLSCLSTEQ NQHLQASLSR LHRVAQHARA KCVRLLVDAE YTFINPALSL LVAALAVRWN SPEEGGPWVW NTYQAYLKDT HQRLEQDAEA AHKAGLAFGV KLVRGAYLDK ERSMTQLQGK EDCTQPDYEA TSRSYSRCLE LMLRCVSNHG PPCHLMVASH NEESVRQATK RMWELGIPLD GPVCFGQLLG MCDHVSLALG QAGYMVYKSI PYGCLEEVIP YLIRRAQENR SVLQGARREQ ALLSQELWRR LLGRTA // ID PROD_MOUSE Reviewed; 599 AA. AC Q9WU79; A0JLW6; Q3UNR4; Q9QX61; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 05-APR-2011, sequence version 2. DT 19-MAR-2014, entry version 94. DE RecName: Full=Proline dehydrogenase 1, mitochondrial; DE EC=1.5.5.2; DE AltName: Full=Proline oxidase; DE Flags: Precursor; GN Name=Prodh; Synonyms=Pro1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Kidney; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] OF 5-599. RC STRAIN=C57BL/6, and PRO/Re; TISSUE=Cerebellum; RX PubMed=10192398; DOI=10.1038/7777; RA Gogos J.A., Santha M., Takacs Z., Beck K.D., Luine V., Lucas L.R., RA Nadler J.V., Karayiorgou M.; RT "The gene encoding proline dehydrogenase modulates sensorimotor gating RT in mice."; RL Nat. Genet. 21:434-439(1999). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 7-599. RA Lin W.-W., Hu C.A., Valle D.; RL Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 56-599. RC TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [7] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-356; LYS-367 AND LYS-485, RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23576753; DOI=10.1073/pnas.1302961110; RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., RA Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.; RT "Label-free quantitative proteomics of the lysine acetylome in RT mitochondria identifies substrates of SIRT3 in metabolic pathways."; RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013). CC -!- FUNCTION: Converts proline to delta-1-pyrroline-5-carboxylate. CC -!- CATALYTIC ACTIVITY: L-proline + a quinone = (S)-1-pyrroline-5- CC carboxylate + a quinol. CC -!- COFACTOR: FAD. CC -!- PATHWAY: Amino-acid degradation; L-proline degradation into L- CC glutamate; L-glutamate from L-proline: step 1/2. CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix. CC -!- TISSUE SPECIFICITY: Expressed in liver, kidney, heart and to a CC lesser extent in brain, lung and muscle. CC -!- DISEASE: Note=Pro/re mice that have a premature termination on CC Prodh are sluggish in their movement. CC -!- SIMILARITY: Belongs to the proline oxidase family. CC -!- SEQUENCE CAUTION: CC Sequence=AAD24776.1; Type=Erroneous initiation; Note=Translation N-terminally extended; CC Sequence=AAI25328.1; Type=Erroneous initiation; Note=Translation N-terminally extended; CC Sequence=EDK97501.1; Type=Erroneous gene model prediction; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK144068; BAE25683.1; -; mRNA. DR EMBL; AC087064; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH466521; EDK97501.1; ALT_SEQ; Genomic_DNA. DR EMBL; AF120279; AAD24776.1; ALT_INIT; mRNA. DR EMBL; U80020; AAF21467.1; -; mRNA. DR EMBL; BC125327; AAI25328.1; ALT_INIT; mRNA. DR RefSeq; NP_035302.2; NM_011172.2. DR UniGene; Mm.28456; -. DR ProteinModelPortal; Q9WU79; -. DR SMR; Q9WU79; 349-580. DR IntAct; Q9WU79; 3. DR MINT; MINT-4130517; -. DR STRING; 10090.ENSMUSP00000003620; -. DR PhosphoSite; Q9WU79; -. DR PaxDb; Q9WU79; -. DR PRIDE; Q9WU79; -. DR Ensembl; ENSMUST00000003620; ENSMUSP00000003620; ENSMUSG00000003526. DR Ensembl; ENSMUST00000136776; ENSMUSP00000117597; ENSMUSG00000003526. DR GeneID; 19125; -. DR KEGG; mmu:19125; -. DR UCSC; uc007ymu.1; mouse. DR CTD; 5625; -. DR MGI; MGI:97770; Prodh. DR eggNOG; COG0506; -. DR GeneTree; ENSGT00390000006265; -. DR HOGENOM; HOG000233406; -. DR HOVERGEN; HBG008262; -. DR InParanoid; A0JLW6; -. DR KO; K00318; -. DR OMA; PLIRHNK; -. DR OrthoDB; EOG7K9K2J; -. DR TreeFam; TF313544; -. DR UniPathway; UPA00261; UER00373. DR NextBio; 295730; -. DR PRO; PR:Q9WU79; -. DR ArrayExpress; Q9WU79; -. DR Bgee; Q9WU79; -. DR CleanEx; MM_PRODH; -. DR Genevestigator; Q9WU79; -. DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:MGI. DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell. DR GO; GO:0016597; F:amino acid binding; IEA:Ensembl. DR GO; GO:0071949; F:FAD binding; ISS:UniProtKB. DR GO; GO:0004657; F:proline dehydrogenase activity; ISS:UniProtKB. DR GO; GO:0006537; P:glutamate biosynthetic process; IEA:InterPro. DR GO; GO:0010133; P:proline catabolic process to glutamate; IEA:UniProtKB-UniPathway. DR InterPro; IPR002872; Proline_DH. DR InterPro; IPR015659; Proline_oxidase. DR PANTHER; PTHR13914; PTHR13914; 1. DR Pfam; PF01619; Pro_dh; 1. PE 1: Evidence at protein level; KW Acetylation; Complete proteome; FAD; Flavoprotein; Mitochondrion; KW Oxidoreductase; Proline metabolism; Reference proteome; KW Transit peptide. FT TRANSIT 1 ? Mitochondrion (Potential). FT CHAIN ? 599 Proline dehydrogenase 1, mitochondrial. FT /FTId=PRO_0000025801. FT MOD_RES 356 356 N6-acetyllysine. FT MOD_RES 367 367 N6-acetyllysine. FT MOD_RES 485 485 N6-acetyllysine. FT CONFLICT 7 8 FL -> HE (in Ref. 5; AAF21467). FT CONFLICT 303 303 E -> V (in Ref. 1; BAE25683). FT CONFLICT 379 379 D -> G (in Ref. 1; BAE25683). FT CONFLICT 436 436 F -> S (in Ref. 4; AAD24776). FT CONFLICT 443 443 G -> R (in Ref. 4; AAD24776). SQ SEQUENCE 599 AA; 68036 MW; 528AA436920CE5DD CRC64; MALKRVFLLR SVAPRVAALS TKPQAQEQPP ASPEALRGCG AAKAVRPPVP AVDFTNTQEA YRSRRSWELV RNLLVLRLCA SPVLLAHHEQ LFQVARKLLG QRMFERLMKM TFYGHFVAGE DQESIRPLIR HNKAFGVGFI LDYGVEEDLS PEEAERKEME SCTSEAERDG SGANKREKQY QVHPAFGDRR DGVISARTYF YANEAKCDNY MENLLQCIKA SGGASDGGFS AIKLTALGRP QFLLQFSDVL TRWRRFFHQM AAEQGQAGRA AVDTKLEVAV LQDSIAKMGI ASRAEIEGWF TPETLGVSGT VDLLDWNSLI DSRTRLSRHL VVPNVQTGQL EPLLSRFTEE EEQQMKRMLQ RMDVLAKKAK EAGVRLMIDA EQSYFQPAIS RLTLEMQRRF NVDKPFIFNT FQCYLKDAYD NVTLDMELAR REGWCFGAKL VRGAYMAQER VRAAEIGYED PINPTYEATN AMYHRCLNYV LEELKHSTKA EVMVASHNED TVHFTLCRMK EIGLHPADGQ VCFGQLLGMC DQISFPLGQA GFPVYKYVPY GPVMEVLPYL SRRALENSSI MKGAQRERQL LWQELRRRLR TGSLFHHPA // ID PTGR1_MOUSE Reviewed; 329 AA. AC Q91YR9; Q3TKT6; Q9CPS1; DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot. DT 16-AUG-2005, sequence version 2. DT 19-MAR-2014, entry version 98. DE RecName: Full=Prostaglandin reductase 1; DE Short=PRG-1; DE EC=1.3.1.-; DE AltName: Full=15-oxoprostaglandin 13-reductase; DE EC=1.3.1.48; DE AltName: Full=NADP-dependent leukotriene B4 12-hydroxydehydrogenase; DE EC=1.3.1.74; GN Name=Ptgr1; Synonyms=Ltb4dh; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Embryo, Liver, Testis, and Urinary bladder; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Mammary tumor; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-178, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic fibroblast; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., RA Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). CC -!- FUNCTION: Functions as 15-oxo-prostaglandin 13-reductase and acts CC on 15-oxo-PGE1, 15-oxo-PGE2 and 15-oxo-PGE2-alpha. Has no activity CC towards PGE1, PGE2 and PGE2-alpha. Catalyzes the conversion of CC leukotriene B4 into its biologically less active metabolite, 12- CC oxo-leukotriene B4. This is an initial and key step of metabolic CC inactivation of leukotriene B4 (By similarity). CC -!- CATALYTIC ACTIVITY: n-alkanal + NAD(P)(+) = alk-2-enal + NAD(P)H. CC -!- CATALYTIC ACTIVITY: 11-alpha-hydroxy-9,15-dioxoprost-5-enoate + CC NAD(P)(+) = (5Z)-(13E)-11-alpha-hydroxy-9,15-dioxoprosta-5,13- CC dienoate + NAD(P)H. CC -!- SUBUNIT: Monomer or homodimer (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the NADP-dependent oxidoreductase L4BD CC family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK010888; BAB27248.1; -; mRNA. DR EMBL; AK011962; BAB27941.1; -; mRNA. DR EMBL; AK035425; BAC29060.1; -; mRNA. DR EMBL; AK134440; BAE22145.1; -; mRNA. DR EMBL; AK166835; BAE39057.1; -; mRNA. DR EMBL; BC014865; AAH14865.1; -; mRNA. DR RefSeq; NP_080244.1; NM_025968.3. DR UniGene; Mm.34497; -. DR ProteinModelPortal; Q91YR9; -. DR SMR; Q91YR9; 5-329. DR IntAct; Q91YR9; 1. DR MINT; MINT-4122050; -. DR PhosphoSite; Q91YR9; -. DR REPRODUCTION-2DPAGE; Q91YR9; -. DR PaxDb; Q91YR9; -. DR PRIDE; Q91YR9; -. DR Ensembl; ENSMUST00000030069; ENSMUSP00000030069; ENSMUSG00000028378. DR GeneID; 67103; -. DR KEGG; mmu:67103; -. DR UCSC; uc008szm.1; mouse. DR CTD; 22949; -. DR MGI; MGI:1914353; Ptgr1. DR eggNOG; COG2130; -. DR GeneTree; ENSGT00390000009335; -. DR HOGENOM; HOG000294663; -. DR HOVERGEN; HBG055024; -. DR InParanoid; Q91YR9; -. DR KO; K13948; -. DR OMA; IDVYYEN; -. DR OrthoDB; EOG7JT6WX; -. DR TreeFam; TF324201; -. DR NextBio; 323584; -. DR PRO; PR:Q91YR9; -. DR Bgee; Q91YR9; -. DR Genevestigator; Q91YR9; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0036132; F:13-prostaglandin reductase activity; IEA:UniProtKB-EC. DR GO; GO:0047522; F:15-oxoprostaglandin 13-oxidase activity; IEA:UniProtKB-EC. DR GO; GO:0032440; F:2-alkenal reductase [NAD(P)] activity; IEA:UniProtKB-EC. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0006693; P:prostaglandin metabolic process; IEA:GOC. DR GO; GO:0009636; P:response to toxic substance; IEA:Ensembl. DR Gene3D; 3.40.50.720; -; 1. DR Gene3D; 3.90.180.10; -; 1. DR InterPro; IPR013149; ADH_C. DR InterPro; IPR002085; ADH_SF_Zn-type. DR InterPro; IPR014190; B4_12hDH. DR InterPro; IPR011032; GroES-like. DR InterPro; IPR016040; NAD(P)-bd_dom. DR PANTHER; PTHR11695; PTHR11695; 1. DR Pfam; PF00107; ADH_zinc_N; 1. DR SUPFAM; SSF50129; SSF50129; 2. DR TIGRFAMs; TIGR02825; B4_12hDH; 1. PE 1: Evidence at protein level; KW Acetylation; Complete proteome; Cytoplasm; NADP; Oxidoreductase; KW Reference proteome. FT CHAIN 1 329 Prostaglandin reductase 1. FT /FTId=PRO_0000218066. FT NP_BIND 152 155 NADP (By similarity). FT NP_BIND 239 245 NADP (By similarity). FT NP_BIND 270 272 NADP (By similarity). FT BINDING 178 178 NADP (By similarity). FT BINDING 193 193 NADP (By similarity). FT BINDING 217 217 NADP (By similarity). FT BINDING 321 321 NADP (By similarity). FT MOD_RES 178 178 N6-acetyllysine. FT CONFLICT 298 298 C -> Y (in Ref. 2; AAH14865). FT CONFLICT 301 301 Y -> H (in Ref. 2; AAH14865). SQ SEQUENCE 329 AA; 35560 MW; FD0CA4682DB493D8 CRC64; MVQAKSWTLK KHFEGFPTDG NFELKTTELP PLNNGEVLLE ALFLSVDPYM RVAAKKLKEG DRMMGEQVAR VVESKNSAFP KGTIVAALLG WTSHSISDGN GLTKLPVEWP DKLPLSLALG TVGMPGLTAY FGLLDICGVK GGETVMVSAA AGAVGSVVGQ IAKLKGCKVV GTAGSDEKVA YLKKLGFDVA FNYKTVKSLE EALRTASPDG YDCYFDNVGG EFSNAVILQM KTFGRIAICG AISQYNRTGP CPQGPAPEVV IYQQLRMEGF IVNRWQGEVR QKALTELMNW VSEGKVQCHE YVTEGFEKMP AAFMGMLKGE NLGKTIVKA // ID PTGR2_MOUSE Reviewed; 351 AA. AC Q8VDQ1; Q3TG36; Q3ULY3; Q8BZA2; Q9D1W8; DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot. DT 22-JUL-2008, sequence version 2. DT 19-MAR-2014, entry version 96. DE RecName: Full=Prostaglandin reductase 2; DE Short=PRG-2; DE EC=1.3.1.48; DE AltName: Full=15-oxoprostaglandin 13-reductase; DE AltName: Full=Zinc-binding alcohol dehydrogenase domain-containing protein 1; GN Name=Ptgr2; Synonyms=Zadh1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC STRAIN=C57BL/6J; RC TISSUE=Cerebellum, Embryonic heart, Mammary gland, and RC Medulla oblongata; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC STRAIN=Czech II; TISSUE=Mammary tumor; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE RP SPECIFICITY, DEVELOPMENTAL STAGE, AND MUTAGENESIS OF TYR-259. RX PubMed=17449869; DOI=10.1074/jbc.M702289200; RA Chou W.-L., Chuang L.-M., Chou C.-C., Wang A.H.-J., Lawson J.A., RA FitzGerald G.A., Chang Z.-F.; RT "Identification of a novel prostaglandin reductase reveals the RT involvement of prostaglandin E2 catabolism in regulation of peroxisome RT proliferator-activated receptor gamma activation."; RL J. Biol. Chem. 282:18162-18172(2007). RN [4] RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS), AND SUBUNIT. RX PubMed=15229897; DOI=10.1002/prot.20163; RA Levin I., Schwarzenbacher R., McMullan D., Abdubek P., Ambing E., RA Biorac T., Cambell J., Canaves J.M., Chiu H.-J., Dai X., Deacon A.M., RA DiDonato M., Elsliger M.-A., Godzik A., Grittini C., Grzechnik S.K., RA Hampton E., Jaroszewski L., Karlak C., Klock H.E., Koesema E., RA Kreusch A., Kuhn P., Lesley S.A., McPhillips T.M., Miller M.D., RA Morse A., Moy K., Ouyang J., Page R., Quijano K., Reyes R., Robb A., RA Sims E., Spraggon G., Stevens R.C., van den Bedem H., Velasquez J., RA Vincent J., von Delft F., Wang X., West B., Wolf G., Xu Q., RA Hodgson K.O., Wooley J., Wilson I.A.; RT "Crystal structure of a putative NADPH-dependent oxidoreductase (GI: RT 18204011) from mouse at 2.10 A resolution."; RL Proteins 56:629-633(2004). RN [5] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH NADPH. RX PubMed=19000823; DOI=10.1016/j.str.2008.09.007; RA Wu Y.H., Ko T.P., Guo R.T., Hu S.M., Chuang L.M., Wang A.H.; RT "Structural basis for catalytic and inhibitory mechanisms of human RT prostaglandin reductase PTGR2."; RL Structure 16:1714-1723(2008). CC -!- FUNCTION: Functions as 15-oxo-prostaglandin 13-reductase and acts CC on 15-keto-PGE1, 15-keto-PGE2, 15-keto-PGE1-alpha and 15-keto- CC PGE2-alpha with highest activity towards 15-keto-PGE2. CC Overexpression represses transcriptional activity of PPARG and CC inhibits adipocyte differentiation. CC -!- CATALYTIC ACTIVITY: 11-alpha-hydroxy-9,15-dioxoprost-5-enoate + CC NAD(P)(+) = (5Z)-(13E)-11-alpha-hydroxy-9,15-dioxoprosta-5,13- CC dienoate + NAD(P)H. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=49.6 uM for 15-keto-PGE2; CC KM=34.4 uM for 15-keto-PGE1; CC KM=108.8 uM for 15-keto-PGF2-alpha; CC KM=59.2 uM for 15-keto-PGF2-beta; CC KM=94.6 uM for NADPH; CC Vmax=178.4 umol/min/mg enzyme for 15-keto-PGE2; CC Vmax=115.0 umol/min/mg enzyme for 15-keto-PGE1; CC Vmax=230.9 umol/min/mg enzyme for 15-keto-PGF2-alpha; CC Vmax=206.4 umol/min/mg enzyme for 15-keto-PGF2-beta; CC Vmax=144.7 umol/min/mg enzyme for NADPH; CC -!- SUBUNIT: Monomer. CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q8VDQ1-1; Sequence=Displayed; CC Name=2; CC IsoId=Q8VDQ1-2; Sequence=VSP_013528, VSP_013529; CC Note=No experimental confirmation available; CC -!- TISSUE SPECIFICITY: Widely expressed with highest levels in CC adipose tissues. CC -!- DEVELOPMENTAL STAGE: Highly expressed in the late phase of CC adipocyte differentiation (at protein level). CC -!- SIMILARITY: Belongs to the NADP-dependent oxidoreductase L4BD CC family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK036168; BAC29329.1; -; mRNA. DR EMBL; AK021033; BAB32284.1; -; mRNA. DR EMBL; AK145232; BAE26315.1; -; mRNA. DR EMBL; AK159932; BAE35493.1; -; mRNA. DR EMBL; AK168895; BAE40712.1; -; mRNA. DR EMBL; BC021466; AAH21466.1; -; mRNA. DR RefSeq; NP_001239554.1; NM_001252625.1. DR RefSeq; NP_001239555.1; NM_001252626.1. DR RefSeq; NP_084156.2; NM_029880.3. DR UniGene; Mm.246127; -. DR PDB; 1VJ1; X-ray; 2.10 A; A=1-351. DR PDB; 2ZB3; X-ray; 2.00 A; A=1-351. DR PDBsum; 1VJ1; -. DR PDBsum; 2ZB3; -. DR ProteinModelPortal; Q8VDQ1; -. DR SMR; Q8VDQ1; 2-346. DR BioGrid; 218562; 1. DR IntAct; Q8VDQ1; 1. DR MINT; MINT-4126675; -. DR STRING; 10090.ENSMUSP00000119981; -. DR PhosphoSite; Q8VDQ1; -. DR PaxDb; Q8VDQ1; -. DR PRIDE; Q8VDQ1; -. DR DNASU; 77219; -. DR Ensembl; ENSMUST00000123614; ENSMUSP00000115704; ENSMUSG00000072946. [Q8VDQ1-1] DR Ensembl; ENSMUST00000146377; ENSMUSP00000119981; ENSMUSG00000072946. [Q8VDQ1-1] DR Ensembl; ENSMUST00000147363; ENSMUSP00000114766; ENSMUSG00000072946. [Q8VDQ1-2] DR GeneID; 77219; -. DR KEGG; mmu:77219; -. DR UCSC; uc007oep.2; mouse. [Q8VDQ1-1] DR CTD; 145482; -. DR MGI; MGI:1916372; Ptgr2. DR eggNOG; COG2130; -. DR GeneTree; ENSGT00390000009335; -. DR HOGENOM; HOG000294663; -. DR HOVERGEN; HBG055024; -. DR InParanoid; Q8VDQ1; -. DR KO; K13949; -. DR OMA; GGASKCA; -. DR OrthoDB; EOG7B31N5; -. DR TreeFam; TF324201; -. DR Reactome; REACT_188937; Metabolism. DR SABIO-RK; Q8VDQ1; -. DR EvolutionaryTrace; Q8VDQ1; -. DR NextBio; 346608; -. DR PRO; PR:Q8VDQ1; -. DR ArrayExpress; Q8VDQ1; -. DR Bgee; Q8VDQ1; -. DR Genevestigator; Q8VDQ1; -. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR GO; GO:0036132; F:13-prostaglandin reductase activity; IEA:UniProtKB-EC. DR GO; GO:0047522; F:15-oxoprostaglandin 13-oxidase activity; ISS:UniProtKB. DR GO; GO:0006693; P:prostaglandin metabolic process; ISS:UniProtKB. DR Gene3D; 3.40.50.720; -; 1. DR Gene3D; 3.90.180.10; -; 1. DR InterPro; IPR013149; ADH_C. DR InterPro; IPR002085; ADH_SF_Zn-type. DR InterPro; IPR011032; GroES-like. DR InterPro; IPR016040; NAD(P)-bd_dom. DR PANTHER; PTHR11695; PTHR11695; 1. DR Pfam; PF00107; ADH_zinc_N; 1. DR SUPFAM; SSF50129; SSF50129; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Complete proteome; Cytoplasm; KW NADP; Oxidoreductase; Reference proteome. FT CHAIN 1 351 Prostaglandin reductase 2. FT /FTId=PRO_0000218071. FT NP_BIND 165 168 NADP. FT NP_BIND 253 259 NADP. FT NP_BIND 287 289 NADP. FT REGION 99 100 Substrate binding (By similarity). FT REGION 288 290 Substrate binding (By similarity). FT BINDING 192 192 NADP. FT BINDING 208 208 NADP. FT BINDING 231 231 NADP. FT BINDING 337 337 NADP. FT VAR_SEQ 314 316 VKE -> FLF (in isoform 2). FT /FTId=VSP_013528. FT VAR_SEQ 317 351 Missing (in isoform 2). FT /FTId=VSP_013529. FT MUTAGEN 259 259 Y->F: Significant reduction in catalytic FT efficiency. FT CONFLICT 18 18 P -> T (in Ref. 1; BAB32284). FT CONFLICT 31 31 P -> L (in Ref. 2; AAH21466). FT CONFLICT 81 81 V -> I (in Ref. 1; BAE26315 and 2; FT AAH21466). FT CONFLICT 91 91 T -> A (in Ref. 1; BAE26315 and 2; FT AAH21466). FT CONFLICT 239 239 A -> T (in Ref. 1; BAE26315 and 2; FT AAH21466). FT CONFLICT 260 261 SN -> NK (in Ref. 1; BAE26315 and 2; FT AAH21466). FT CONFLICT 318 318 M -> V (in Ref. 1; BAE26315 and 2; FT AAH21466). FT STRAND 3 8 FT HELIX 20 22 FT STRAND 23 28 FT STRAND 38 47 FT HELIX 51 55 FT STRAND 57 59 FT STRAND 75 85 FT STRAND 95 110 FT HELIX 111 113 FT STRAND 115 117 FT HELIX 119 122 FT HELIX 126 130 FT TURN 131 133 FT HELIX 135 147 FT STRAND 157 162 FT HELIX 166 177 FT STRAND 181 189 FT HELIX 190 198 FT STRAND 203 207 FT HELIX 208 210 FT HELIX 213 220 FT STRAND 225 232 FT HELIX 234 242 FT STRAND 244 252 FT HELIX 256 258 FT HELIX 271 280 FT STRAND 283 286 FT HELIX 289 291 FT HELIX 293 295 FT HELIX 296 308 FT STRAND 316 320 FT HELIX 322 324 FT HELIX 325 333 FT STRAND 338 344 SQ SEQUENCE 351 AA; 38015 MW; 2766871577A8022F CRC64; MIIQRVVLNS RPGKNGNPVA ENFRVEEFSL PDALNEGQVQ VRTLYLSVDP YMRCKMNEDT GTDYLAPWQL AQVADGGGIG VVEESKHQKL TKGDFVTSFY WPWQTKAILD GNGLEKVDPQ LVDGHLSYFL GAIGMPGLTS LIGVQEKGHI SAGSNQTMVV SGAAGACGSL AGQIGHLLGC SRVVGICGTQ EKCLFLTSEL GFDAAVNYKT GNVAEQLREA CPGGVDVYFD NVGGDISNAV ISQMNENSHI ILCGQISQYS NDVPYPPPLP PAVEAIRKER NITRERFTVL NYKDKFEPGI LQLSQWFKEG KLKVKETMAK GLENMGVAFQ SMMTGGNVGK QIVCISEDSS L // ID PXDN_MOUSE Reviewed; 1475 AA. AC Q3UQ28; A4FU83; E9QNQ9; DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 2. DT 19-MAR-2014, entry version 87. DE RecName: Full=Peroxidasin homolog; DE EC=1.11.1.7; DE Flags: Precursor; GN Name=Pxdn; Synonyms=Kiaa0230; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Head; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 370-1475. RC STRAIN=C57BL/6; TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE. RX PubMed=18929642; DOI=10.1016/j.freeradbiomed.2008.09.009; RA Cheng G., Salerno J.C., Cao Z., Pagano P.J., Lambeth J.D.; RT "Identification and characterization of VPO1, a new animal heme- RT containing peroxidase."; RL Free Radic. Biol. Med. 45:1682-1694(2008). RN [5] RP SUBCELLULAR LOCATION. RX PubMed=19590037; DOI=10.2353/ajpath.2009.080693; RA Peterfi Z., Donko A., Orient A., Sum A., Prokai A., Molnar B., RA Vereb Z., Rajnavolgyi E., Kovacs K.J., Muller V., Szabo A.J., RA Geiszt M.; RT "Peroxidasin is secreted and incorporated into the extracellular RT matrix of myofibroblasts and fibrotic kidney."; RL Am. J. Pathol. 175:725-735(2009). RN [6] RP DEVELOPMENTAL STAGE. RX PubMed=18848646; DOI=10.1016/j.gep.2008.09.004; RA Homma S., Shimada T., Hikake T., Yaginuma H.; RT "Expression pattern of LRR and Ig domain-containing protein (LRRIG RT protein) in the early mouse embryo."; RL Gene Expr. Patterns 9:1-26(2009). CC -!- FUNCTION: Displays low peroxidase activity and is likely to CC participate in H(2)O(2) metabolism and peroxidative reactions in CC the cardiovascular system (By similarity). Plays a role in CC extracellular matrix formation. CC -!- CATALYTIC ACTIVITY: 2 phenolic donor + H(2)O(2) = 2 phenoxyl CC radical of the donor + 2 H(2)O. CC -!- COFACTOR: Binds 1 calcium ion per subunit (By similarity). CC -!- COFACTOR: Binds 1 heme B (iron-protoporphyrin IX) group covalently CC per subunit (By similarity). CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular CC matrix. Note=Enriched in the peritubular space of fibrotic CC kidneys. CC -!- TISSUE SPECIFICITY: Highly expressed in the cardiovascular system. CC -!- DEVELOPMENTAL STAGE: Expressed in all embryonic tissues at 10 dpc. CC Detected at 7 dpc. CC -!- SIMILARITY: Belongs to the peroxidase family. XPO subfamily. CC -!- SIMILARITY: Contains 4 Ig-like C2-type (immunoglobulin-like) CC domains. CC -!- SIMILARITY: Contains 4 LRR (leucine-rich) repeats. CC -!- SIMILARITY: Contains 1 LRRCT domain. CC -!- SIMILARITY: Contains 1 LRRNT domain. CC -!- SIMILARITY: Contains 1 VWFC domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK142872; BAE25216.1; -; mRNA. DR EMBL; AC159626; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC165078; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC112913; AAI12914.1; -; mRNA. DR RefSeq; NP_852060.2; NM_181395.2. DR UniGene; Mm.251774; -. DR ProteinModelPortal; Q3UQ28; -. DR SMR; Q3UQ28; 30-673, 735-1311. DR PhosphoSite; Q3UQ28; -. DR PaxDb; Q3UQ28; -. DR PRIDE; Q3UQ28; -. DR Ensembl; ENSMUST00000122328; ENSMUSP00000113703; ENSMUSG00000020674. DR GeneID; 69675; -. DR KEGG; mmu:69675; -. DR UCSC; uc007ngl.2; mouse. DR CTD; 7837; -. DR MGI; MGI:1916925; Pxdn. DR eggNOG; NOG262194; -. DR GeneTree; ENSGT00550000074325; -. DR HOGENOM; HOG000016084; -. DR HOVERGEN; HBG108312; -. DR InParanoid; Q3UQ28; -. DR OMA; EPVITWN; -. DR OrthoDB; EOG7D2FD6; -. DR TreeFam; TF314316; -. DR NextBio; 330062; -. DR PRO; PR:Q3UQ28; -. DR ArrayExpress; Q3UQ28; -. DR Bgee; Q3UQ28; -. DR CleanEx; MM_PXDN; -. DR Genevestigator; Q3UQ28; -. DR GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl. DR GO; GO:0031012; C:extracellular matrix; IDA:UniProtKB. DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB. DR GO; GO:0005578; C:proteinaceous extracellular matrix; IEA:UniProtKB-SubCell. DR GO; GO:0005201; F:extracellular matrix structural constituent; IEA:Ensembl. DR GO; GO:0020037; F:heme binding; ISS:UniProtKB. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004601; F:peroxidase activity; ISS:UniProtKB. DR GO; GO:0030198; P:extracellular matrix organization; IDA:UniProtKB. DR GO; GO:0042744; P:hydrogen peroxide catabolic process; ISS:UniProtKB. DR Gene3D; 1.10.640.10; -; 2. DR Gene3D; 2.60.40.10; -; 4. DR InterPro; IPR000483; Cys-rich_flank_reg_C. DR InterPro; IPR010255; Haem_peroxidase. DR InterPro; IPR002007; Haem_peroxidase_animal. DR InterPro; IPR019791; Haem_peroxidase_animal_subgr. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR013098; Ig_I-set. DR InterPro; IPR003598; Ig_sub2. DR InterPro; IPR001611; Leu-rich_rpt. DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp. DR InterPro; IPR000372; LRR-contain_N. DR InterPro; IPR001007; VWF_C. DR Pfam; PF03098; An_peroxidase; 1. DR Pfam; PF07679; I-set; 4. DR Pfam; PF00560; LRR_1; 1. DR Pfam; PF00093; VWC; 1. DR PRINTS; PR00457; ANPEROXIDASE. DR SMART; SM00408; IGc2; 4. DR SMART; SM00369; LRR_TYP; 4. DR SMART; SM00082; LRRCT; 1. DR SMART; SM00013; LRRNT; 1. DR SMART; SM00214; VWC; 1. DR SUPFAM; SSF48113; SSF48113; 1. DR PROSITE; PS50835; IG_LIKE; 4. DR PROSITE; PS51450; LRR; 5. DR PROSITE; PS50292; PEROXIDASE_3; 1. DR PROSITE; PS01208; VWFC_1; 1. DR PROSITE; PS50184; VWFC_2; 1. PE 2: Evidence at transcript level; KW Calcium; Complete proteome; Disulfide bond; Extracellular matrix; KW Glycoprotein; Heme; Hydrogen peroxide; Immunoglobulin domain; Iron; KW Leucine-rich repeat; Metal-binding; Oxidoreductase; Peroxidase; KW Phosphoprotein; Reference proteome; Repeat; Secreted; Signal. FT SIGNAL 1 23 Potential. FT CHAIN 24 1475 Peroxidasin homolog. FT /FTId=PRO_0000319620. FT DOMAIN 24 60 LRRNT. FT REPEAT 84 105 LRR 1. FT REPEAT 108 129 LRR 2. FT REPEAT 132 153 LRR 3. FT REPEAT 156 177 LRR 4. FT DOMAIN 189 242 LRRCT. FT DOMAIN 243 329 Ig-like C2-type 1. FT DOMAIN 339 425 Ig-like C2-type 2. FT DOMAIN 430 517 Ig-like C2-type 3. FT DOMAIN 518 607 Ig-like C2-type 4. FT DOMAIN 1409 1467 VWFC. FT ACT_SITE 824 824 Proton acceptor (By similarity). FT METAL 825 825 Calcium (By similarity). FT METAL 904 904 Calcium (By similarity). FT METAL 906 906 Calcium; via carbonyl oxygen (By FT similarity). FT METAL 908 908 Calcium (By similarity). FT METAL 910 910 Calcium (By similarity). FT METAL 1071 1071 Iron (heme axial ligand) (By similarity). FT BINDING 823 823 Heme (covalent; via 2 links) (By FT similarity). FT BINDING 977 977 Heme (covalent; via 2 links) (By FT similarity). FT SITE 974 974 Transition state stabilizer (By FT similarity). FT MOD_RES 1173 1173 Phosphotyrosine (By similarity). FT MOD_RES 1177 1177 Phosphoserine (By similarity). FT CARBOHYD 637 637 N-linked (GlcNAc...) (Potential). FT CARBOHYD 696 696 N-linked (GlcNAc...) (Potential). FT CARBOHYD 716 716 N-linked (GlcNAc...) (Potential). FT CARBOHYD 728 728 N-linked (GlcNAc...) (Potential). FT CARBOHYD 1175 1175 N-linked (GlcNAc...) (Potential). FT CARBOHYD 1277 1277 N-linked (GlcNAc...) (Potential). FT CARBOHYD 1364 1364 N-linked (GlcNAc...) (Potential). FT DISULFID 264 314 By similarity. FT DISULFID 360 409 By similarity. FT DISULFID 451 499 By similarity. FT DISULFID 543 591 By similarity. FT DISULFID 729 745 By similarity. FT DISULFID 844 854 By similarity. FT DISULFID 848 872 By similarity. FT DISULFID 956 967 By similarity. FT DISULFID 1174 1231 By similarity. FT DISULFID 1272 1298 By similarity. FT CONFLICT 549 549 P -> Q (in Ref. 1; BAE25216). FT CONFLICT 1298 1298 C -> R (in Ref. 3; AAI12914). SQ SEQUENCE 1475 AA; 165103 MW; 7F49A5B0D4CDBEB6 CRC64; MAVRPTRRCL LALLLCFAWW AMAVVASKQG AGCPSRCLCF RTTVRCMHLL LEAVPAVAPQ TSILDLRFNR IREIQPGAFR RLRSLNTLLL NNNQIKKIPN GAFEDLENLK YLYLYKNEIQ SIDRQAFKGL ASLEQLYLHF NQIETLDPES FQHLPKLERL FLHNNRITHL VPGTFSQLES MKRLRLDSNA LHCDCEILWL ADLLKTYAQS GNAQAAATCE YPRRIQGRSV ATITPEELNC ERPRITSEPQ DADVTSGNTV YFTCRAEGNP KPEIIWLRNN NELSMKTDSR LNLLDDGTLM IQNTQEADEG VYQCMAKNVA GEAKTQEVTL RYLGSPARPT FVIQPQNTEV LVGESVTLEC SATGHPLPQI TWTRGDRTPL PIDPRVNITP SGGLYIQNVA QSDSGEYTCF ASNSVDSIHA TAFIIVQALP QFTVTPQSRV VIEGQTVDFQ CAAKGHPQPV IAWTKGGSQL SVDRRHLVLS SGTLRISGVA LHDQGQYECQ AVNIIGSQKV VAHLTVQPRV TPVFASIPSD MTVEVGTNVQ LPCSSQGEPE PAITWNKDGV QVTESGKFHI SPEGFLTIND VGTADAGRYE CVARNTIGYA SVSMVLSVNV PDVSRNGDPY VATSIVEAIA TVDRAINSTR THLFDSRPRS PNDLLALFRY PRDPYTVGQA RAGEIFERTL QLIQEHVQHG LMVDLNGTSY HYNDLVSPQY LSLIANLSGC TAHRRVNNCS DMCFHQKYRT HDGTCNNLQH PMWGASLTAF ERLLKAVYEN GFNTPRGINS QRQYNGHVLP MPRLVSTTLI GTEVITPDEQ FTHMLMQWGQ FLDHDLDSTV VALSQARFSD GQHCSSVCSN DPPCFSVMIP PNDPRVRSGA RCMFFVRSSP VCGSGMTSLL MNSVYPREQI NQLTSYIDAS NVYGSTDHEA RSIRDLASHR GLLRQGIVQR SGKPLLPFAT GPPTECMRDE NESPIPCFLA GDHRANEQLG LTSMHTLWFR EHNRIAAELL KLNPHWDGDT VYHETRKIVG AEIQHITYRH WLPKILGEVG MKMLGEYRGY DPSVNAGIFN AFATAAFRFG HTLINPLLYR LDENFEPIPQ GHVPLHKAFF SPFRIVNEGG IDPLLRGLFG VAGKMRIPSQ LLNTELTERL FSMAHTVALD LAAINIQRGR DHGIPPYHDY RVYCNLSAAY TFEDLKNEIK SPVIREKLQR LYGSTLNIDL FPALMVEDLV PGSRLGPTLM CLLSTQFRRL RDGDRLWYEN PGVFSPAQLT QLKQTSLARI LCDNSDNITR VQQDVFRVAE FPHGYSSCED IPRVDLRVWQ DCCEDCRTRG QFNAFSYHFR GRRSLEFSYE DDKPTKRARW RKALSVKHGK HLSNATSATH EHLEGPATND LKEFVLEMQK IITDLRKQIN SLESRLSTTE CVDDSGESHG GNTKWKKDPC TVCECKNGQI TCFVEACQPA ACPQPVKVEG ACCPVCLKNT AEEKP // ID PYRD1_MOUSE Reviewed; 498 AA. AC Q3TMV7; Q3UFM2; Q8R2X5; DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2005, sequence version 1. DT 19-MAR-2014, entry version 72. DE RecName: Full=Pyridine nucleotide-disulfide oxidoreductase domain-containing protein 1; DE EC=1.8.1.-; GN Name=Pyroxd1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Bone marrow; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Mammary tumor; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- COFACTOR: Binds 1 FAD per subunit (By similarity). CC -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide CC oxidoreductase family. PYROXD1 subfamily. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK148411; BAE28538.1; -; mRNA. DR EMBL; AK165677; BAE38333.1; -; mRNA. DR EMBL; BC027061; AAH27061.1; -; mRNA. DR RefSeq; NP_898988.2; NM_183165.3. DR UniGene; Mm.490474; -. DR ProteinModelPortal; Q3TMV7; -. DR SMR; Q3TMV7; 8-40, 298-421. DR PhosphoSite; Q3TMV7; -. DR PRIDE; Q3TMV7; -. DR Ensembl; ENSMUST00000041852; ENSMUSP00000036394; ENSMUSG00000041671. DR GeneID; 232491; -. DR KEGG; mmu:232491; -. DR UCSC; uc009epc.1; mouse. DR CTD; 79912; -. DR MGI; MGI:2676395; Pyroxd1. DR eggNOG; COG0446; -. DR GeneTree; ENSGT00390000014894; -. DR HOGENOM; HOG000265662; -. DR HOVERGEN; HBG108313; -. DR InParanoid; Q3TMV7; -. DR OMA; CEVIWAI; -. DR OrthoDB; EOG71P29Z; -. DR TreeFam; TF105963; -. DR ChiTaRS; PYROXD1; mouse. DR NextBio; 381131; -. DR PRO; PR:Q3TMV7; -. DR Bgee; Q3TMV7; -. DR Genevestigator; Q3TMV7; -. DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW. DR InterPro; IPR013027; FAD_pyr_nucl-diS_OxRdtase. DR InterPro; IPR023753; Pyr_nucl-diS_OxRdtase_FAD/NAD. DR Pfam; PF07992; Pyr_redox_2; 1. DR PRINTS; PR00368; FADPNR. PE 2: Evidence at transcript level; KW Acetylation; Complete proteome; FAD; Flavoprotein; NADP; KW Oxidoreductase; Reference proteome. FT CHAIN 1 498 Pyridine nucleotide-disulfide FT oxidoreductase domain-containing protein FT 1. FT /FTId=PRO_0000327420. FT MOD_RES 1 1 N-acetylmethionine (By similarity). FT CONFLICT 68 68 T -> I (in Ref. 1; BAE28538 and 2; FT AAH27061). FT CONFLICT 203 203 I -> T (in Ref. 1; BAE28538 and 2; FT AAH27061). FT CONFLICT 277 277 L -> F (in Ref. 1; BAE28538). FT CONFLICT 304 304 T -> K (in Ref. 1; BAE28538 and 2; FT AAH27061). SQ SEQUENCE 498 AA; 55592 MW; ABD67D55D64F82F5 CRC64; MEAPRPAGTF VVVGGGIAGV TCAEQLAVSF PEEDILLVTA SPVIKAVTNF RQVSKVLEEF DVEEQPGTML ESRFPNIKVI ESGVKQLKSE DHCIFTEDGR EFVYKKLCLC AGAKPKLIYE GNPRVLGIRD TDSAQEFQKE LAKARRIMIV GNGGIALELA YEIEGCEVVW AIKDNAIGNT FFDAGAAEFL TSKLMSEKSE AKIAHKRTIY TVEEAKKETR TKSKADYVGS ALGPDWHGGL ALKGTEEFSH SVHIETRCEV KKIYLEEEFK IMKKKSLAFP KDHHKSVTAD KEMWPVYVEL TNGTIYGCDF LVSATGVTPN VHPFLHRNNF ALGEDGGLRV DDQMRTSLPD IYAAGDICTA CWQPSPVWQQ MRLWTQARQM GYYAAKCMAA ASMGHPIDMD FSFELFAHVT KFFNYKVVLL GKYNAQGLGA DHELMLRCTR GQEYVKVVMQ NGRMMGAVLI GETDLEETFE NLILNQMDLS SYGEDLLDPN IDIEDYFD // ID PYRD2_MOUSE Reviewed; 581 AA. AC Q3U4I7; E9QPD2; Q8CAN2; Q9D630; DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot. DT 18-SEP-2013, sequence version 3. DT 19-MAR-2014, entry version 65. DE RecName: Full=Pyridine nucleotide-disulfide oxidoreductase domain-containing protein 2; DE EC=1.-.-.-; GN Name=Pyroxd2; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J, and NOD; TISSUE=Head, and Hypothalamus; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). CC -!- FUNCTION: Probable oxidoreductase (By similarity). CC -!- SIMILARITY: Belongs to the carotenoid/retinoid oxidoreductase CC family. CC -!- SEQUENCE CAUTION: CC Sequence=BAE32444.1; Type=Miscellaneous discrepancy; Note=Intron retention between positions 50 and 165; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK014668; BAB29495.1; -; mRNA. DR EMBL; AK038414; BAC29991.1; -; mRNA. DR EMBL; AK154222; BAE32444.1; ALT_SEQ; mRNA. DR EMBL; AC125458; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; NP_083287.2; NM_029011.2. DR UniGene; Mm.329858; -. DR ProteinModelPortal; Q3U4I7; -. DR STRING; 10090.ENSMUSP00000075825; -. DR PhosphoSite; Q3U4I7; -. DR PaxDb; Q3U4I7; -. DR PRIDE; Q3U4I7; -. DR Ensembl; ENSMUST00000076505; ENSMUSP00000075825; ENSMUSG00000060224. DR GeneID; 74580; -. DR KEGG; mmu:74580; -. DR CTD; 84795; -. DR MGI; MGI:1921830; Pyroxd2. DR eggNOG; COG1233; -. DR GeneTree; ENSGT00390000011684; -. DR InParanoid; Q3U4I7; -. DR OMA; NYASPYA; -. DR OrthoDB; EOG7PP568; -. DR TreeFam; TF315188; -. DR ChiTaRS; PYROXD2; mouse. DR NextBio; 341153; -. DR PRO; PR:Q3U4I7; -. DR CleanEx; MM_4833409A17RIK; -. DR Genevestigator; Q3U4I7; -. DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW. PE 2: Evidence at transcript level; KW Complete proteome; FAD; Flavoprotein; Oxidoreductase; KW Reference proteome. FT CHAIN 1 581 Pyridine nucleotide-disulfide FT oxidoreductase domain-containing protein FT 2. FT /FTId=PRO_0000244072. FT NP_BIND 38 71 FAD (Potential). FT CONFLICT 19 19 T -> A (in Ref. 1; BAE32444). FT CONFLICT 73 73 A -> R (in Ref. 1; BAB29495). FT CONFLICT 106 115 KHGLKLHLRD -> VDRLAWPGGW (in Ref. 1; FT BAC29991). SQ SEQUENCE 581 AA; 62940 MW; 8BC394516E5AB468 CRC64; MAAGGRGLIR ALHSSPCPTW KRAQSGANGR LKPEYDAVVI GAGHNGLVAA AYLQRLGVNT AVFERRHVIG GAAVTEEIIP GFKFSRASYL LSLLRPQICT DLELKKHGLK LHLRDPYSFT PMLEEGTLNR LPRSLLLGTD MAANQKEISQ FSRKDAQAFP RYEEFMKRLV LAIDPLLDAA PVDTTAFQHG SLLQRLRALS TLKPLLKAGR TLGAQLPQYY EVLTAPISKV LDQRFESEPL KATLATDAVI GAMTSPHTPG SGYVLLHHVM GSLEGTQGAW SYVQGGMGAL SDAIASSAAT RGASIFTEKT VAKVQVNSEG RAQGVTLQDG EEVRSRVVLS CASPQVTFLE LTPQEWLPGA FVKRISQLDT QSPVTKINVA VDRLPNFQAA PNAPGDQPQG HHQCSIHLNC EDTLLLHQAF EDAKGGLPSQ KPMIELCIPS SLDPTLAPPG CHVVSLFTQY TPYTLAGGKV WNEQEKNTYA DKVFDCIEAY APGFKRSVLA RDILTPPDLE RIFRLPGGNI FHGAMSLDQL YFARPVPQHS DYRCPVQGLY LCGSGAHPGG GVMGAAGRNA AHVVFRDLKN M // ID PYRD_MOUSE Reviewed; 395 AA. AC O35435; DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 2. DT 19-FEB-2014, entry version 111. DE RecName: Full=Dihydroorotate dehydrogenase (quinone), mitochondrial; DE Short=DHOdehase; DE EC=1.3.5.2; DE AltName: Full=Dihydroorotate oxidase; DE Flags: Precursor; GN Name=Dhodh; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Knecht W., Ullrich A., Loeffler M.; RT "Cloning of murine dihydroorotate dehydrogenase."; RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Mammary gland; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: Catalyzes the conversion of dihydroorotate to orotate CC with quinone as electron acceptor. CC -!- CATALYTIC ACTIVITY: (S)-dihydroorotate + a quinone = orotate + a CC quinol. CC -!- COFACTOR: Binds 1 FMN per subunit (By similarity). CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo CC pathway; orotate from (S)-dihydroorotate (quinone route): step CC 1/1. CC -!- SUBUNIT: Monomer (By similarity). CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Single-pass CC membrane protein (By similarity). CC -!- PTM: The uncleaved transit peptide is required for mitochondrial CC targeting and proper membrane integration (By similarity). CC -!- SIMILARITY: Belongs to the dihydroorotate dehydrogenase family. CC Type 2 subfamily. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF029667; AAB82948.2; -; mRNA. DR EMBL; BC019542; AAH19542.1; -; mRNA. DR EMBL; BC027829; AAH27829.1; -; mRNA. DR EMBL; BC045206; AAH45206.1; -; mRNA. DR RefSeq; NP_064430.1; NM_020046.3. DR UniGene; Mm.23894; -. DR ProteinModelPortal; O35435; -. DR SMR; O35435; 37-395. DR BioGrid; 208162; 1. DR IntAct; O35435; 1. DR STRING; 10090.ENSMUSP00000070303; -. DR BindingDB; O35435; -. DR ChEMBL; CHEMBL2991; -. DR PhosphoSite; O35435; -. DR PaxDb; O35435; -. DR PRIDE; O35435; -. DR Ensembl; ENSMUST00000069058; ENSMUSP00000070303; ENSMUSG00000031730. DR Ensembl; ENSMUST00000123605; ENSMUSP00000115934; ENSMUSG00000031730. DR GeneID; 56749; -. DR KEGG; mmu:56749; -. DR UCSC; uc009nip.1; mouse. DR CTD; 1723; -. DR MGI; MGI:1928378; Dhodh. DR eggNOG; COG0167; -. DR GeneTree; ENSGT00500000044924; -. DR HOGENOM; HOG000225103; -. DR HOVERGEN; HBG006898; -. DR InParanoid; O35435; -. DR KO; K00254; -. DR OMA; VYEGPGL; -. DR TreeFam; TF105973; -. DR UniPathway; UPA00070; UER00946. DR NextBio; 313274; -. DR PRO; PR:O35435; -. DR ArrayExpress; O35435; -. DR Bgee; O35435; -. DR CleanEx; MM_DHODH; -. DR Genevestigator; O35435; -. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl. DR GO; GO:0004158; F:dihydroorotate oxidase activity; IEA:Ensembl. DR GO; GO:0008144; F:drug binding; IEA:Ensembl. DR GO; GO:0010181; F:FMN binding; IEA:Ensembl. DR GO; GO:0048039; F:ubiquinone binding; IEA:Ensembl. DR GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:Ensembl. DR GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0007565; P:female pregnancy; IEA:Ensembl. DR GO; GO:0007595; P:lactation; IEA:Ensembl. DR GO; GO:0043065; P:positive regulation of apoptotic process; IEA:Ensembl. DR GO; GO:0090140; P:regulation of mitochondrial fission; IEA:Ensembl. DR GO; GO:0031000; P:response to caffeine; IEA:Ensembl. DR GO; GO:0042493; P:response to drug; IEA:Ensembl. DR GO; GO:0042594; P:response to starvation; IEA:Ensembl. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00225; DHO_dh_type2; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR012135; Dihydroorotate_DH_1_2. DR InterPro; IPR005719; Dihydroorotate_DH_2. DR InterPro; IPR001295; Dihydroorotate_DH_CS. DR Pfam; PF01180; DHO_dh; 1. DR PIRSF; PIRSF000164; DHO_oxidase; 1. DR TIGRFAMs; TIGR01036; pyrD_sub2; 1. DR PROSITE; PS00911; DHODEHASE_1; 1. DR PROSITE; PS00912; DHODEHASE_2; 1. PE 2: Evidence at transcript level; KW Complete proteome; Flavoprotein; FMN; Membrane; Mitochondrion; KW Mitochondrion inner membrane; Oxidoreductase; Pyrimidine biosynthesis; KW Reference proteome; Transit peptide; Transmembrane; KW Transmembrane helix. FT CHAIN 1 395 Dihydroorotate dehydrogenase (quinone), FT mitochondrial. FT /FTId=PRO_0000029885. FT TRANSIT 1 10 Mitochondrion; not cleaved (By FT similarity). FT TOPO_DOM 1 10 Mitochondrial matrix (Potential). FT TRANSMEM 11 30 Helical; (Potential). FT TOPO_DOM 31 395 Mitochondrial intermembrane (Potential). FT NP_BIND 95 99 FMN (By similarity). FT NP_BIND 355 356 FMN (By similarity). FT REGION 144 148 Substrate binding (By similarity). FT REGION 211 216 Substrate binding (By similarity). FT REGION 283 284 Substrate binding (By similarity). FT ACT_SITE 214 214 Nucleophile (By similarity). FT BINDING 99 99 Substrate (By similarity). FT BINDING 119 119 FMN (By similarity). FT BINDING 180 180 FMN (By similarity). FT BINDING 211 211 FMN (By similarity). FT BINDING 254 254 FMN (By similarity). FT BINDING 282 282 FMN; via carbonyl oxygen (By similarity). FT BINDING 305 305 FMN; via amide nitrogen (By similarity). FT BINDING 334 334 FMN; via amide nitrogen (By similarity). SQ SEQUENCE 395 AA; 42700 MW; 84F2D93D0646E39D CRC64; MAWRQLRKRA LDAAIILGGG GLLFTSYLTA TGDDHFYAEY LMPALQRLLD PESAHRLAVR VISLGLLPRA TFQDSNMLEV RVLGHKFRNP VGIAAGFDKH GEAVDGLYKL GFGFVEVGSV TPQPQEGNPR PRVFRLPEDQ AVINRYGFNS HGLSAVEHRL RARQQKQTQL TTDGLPLGIN LGKNKTSVDA AADYVEGVRI LGPLADYLVV NVSSPNTAGL RSLQGKTELR RLLSKVLQER DALKGPQKPA VLVKIAPDLT AQDKEDIASV ARELGIDGLI ITNTTVSRPV GLQGALRSET GGLSGKPLRD LSTQTIREMY ALTQGTIPII GVGGVSSGQD ALEKIQAGAS LVQLYTALTF LGPPVVARVK RELEALLKER GFNTVTDAIG VDHRR // ID QORL2_MOUSE Reviewed; 350 AA. AC Q3UNZ8; Q3UAM2; DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2005, sequence version 1. DT 19-MAR-2014, entry version 70. DE RecName: Full=Quinone oxidoreductase-like protein 2; DE EC=1.-.-.-; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC STRAIN=C57BL/6J; TISSUE=Bone marrow, and Kidney; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC STRAIN=FVB/N; TISSUE=Kidney; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-201, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., RA Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). RN [4] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-36; LYS-302 AND LYS-328, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23576753; DOI=10.1073/pnas.1302961110; RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., RA Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.; RT "Label-free quantitative proteomics of the lysine acetylome in RT mitochondria identifies substrates of SIRT3 in metabolic pathways."; RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q3UNZ8-1; Sequence=Displayed; CC Name=2; CC IsoId=Q3UNZ8-2; Sequence=VSP_034229, VSP_034230; CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase CC family. Quinone oxidoreductase subfamily. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK143913; BAE25599.1; -; mRNA. DR EMBL; AK151310; BAE30292.1; -; mRNA. DR EMBL; BC045198; AAH45198.1; -; mRNA. DR RefSeq; NP_001028456.1; NM_001033284.1. DR UniGene; Mm.215960; -. DR ProteinModelPortal; Q3UNZ8; -. DR SMR; Q3UNZ8; 28-349. DR PhosphoSite; Q3UNZ8; -. DR PaxDb; Q3UNZ8; -. DR PRIDE; Q3UNZ8; -. DR Ensembl; ENSMUST00000046743; ENSMUSP00000044945; ENSMUSG00000033488. [Q3UNZ8-1] DR Ensembl; ENSMUST00000119891; ENSMUSP00000113664; ENSMUSG00000033488. [Q3UNZ8-2] DR GeneID; 226527; -. DR KEGG; mmu:226527; -. DR UCSC; uc007ddj.1; mouse. [Q3UNZ8-1] DR UCSC; uc007ddk.1; mouse. [Q3UNZ8-2] DR MGI; MGI:2448516; BC026585. DR eggNOG; COG0604; -. DR GeneTree; ENSGT00550000074483; -. DR HOGENOM; HOG000294672; -. DR HOVERGEN; HBG108388; -. DR InParanoid; Q3UNZ8; -. DR OMA; FWGEFAR; -. DR OrthoDB; EOG7N63NM; -. DR TreeFam; TF314255; -. DR NextBio; 378210; -. DR ArrayExpress; Q3UNZ8; -. DR Bgee; Q3UNZ8; -. DR Genevestigator; Q3UNZ8; -. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR Gene3D; 3.40.50.720; -; 1. DR Gene3D; 3.90.180.10; -; 1. DR InterPro; IPR013149; ADH_C. DR InterPro; IPR013154; ADH_GroES-like. DR InterPro; IPR002085; ADH_SF_Zn-type. DR InterPro; IPR011032; GroES-like. DR InterPro; IPR016040; NAD(P)-bd_dom. DR PANTHER; PTHR11695; PTHR11695; 1. DR Pfam; PF08240; ADH_N; 1. DR Pfam; PF00107; ADH_zinc_N; 1. DR SUPFAM; SSF50129; SSF50129; 1. PE 1: Evidence at protein level; KW Acetylation; Alternative splicing; Complete proteome; Oxidoreductase; KW Reference proteome. FT CHAIN 1 350 Quinone oxidoreductase-like protein 2. FT /FTId=PRO_0000341239. FT MOD_RES 36 36 N6-acetyllysine. FT MOD_RES 201 201 N6-succinyllysine. FT MOD_RES 302 302 N6-acetyllysine. FT MOD_RES 328 328 N6-acetyllysine. FT VAR_SEQ 165 171 ETVLVTA -> STMPSFM (in isoform 2). FT /FTId=VSP_034229. FT VAR_SEQ 172 350 Missing (in isoform 2). FT /FTId=VSP_034230. SQ SEQUENCE 350 AA; 37809 MW; 1F36FB378727C9F3 CRC64; MAARLCTRCL PPVWLCRQAW QGQGRHYRAA LCTELKQPLT IQEVAPRPVG PQEVRVDVHF CGVNFADILA CRGQYQEKPP LPFTPGMEFS GAVLETGTDV STVKKGDRVI GVSSFHAMAE QCITDQKTLW RIPENVSLQD AAVLPVSYGT AILAVDHRAR IQPGETVLVT AAAGATGLAV IDVATNVFRA KVIAATGSDE KCKLAVQRGA QFSVNYSQGS LRDAVKKLAG SGGVNVAIDM VGGDVFLESL RSLAWEGRIV VLGFAGGNIA SVPSNLLLLK NISAMGLYWG RYQHQDFAVF SKSMSTAMQY CQQGLIHPHT GAVFKLEKIN DAFLHVMQRK STGKVLLSLK // ID QORL1_MOUSE Reviewed; 348 AA. AC Q921W4; Q3UKX2; Q8VCS1; Q9CWR9; DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 19-MAR-2014, entry version 101. DE RecName: Full=Quinone oxidoreductase-like protein 1; DE EC=1.-.-.-; DE AltName: Full=Quinone oxidoreductase homolog 1; DE Short=QOH-1; DE AltName: Full=Zeta-crystallin homolog; GN Name=Cryzl1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC STRAIN=C57BL/6J; TISSUE=Embryonic stem cell, and Placenta; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Mammary tumor, and Salivary gland; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q921W4-1; Sequence=Displayed; CC Name=2; CC IsoId=Q921W4-2; Sequence=VSP_000209, VSP_000210; CC Note=No experimental confirmation available; CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase CC family. Quinone oxidoreductase subfamily. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK010433; BAB26935.1; -; mRNA. DR EMBL; AK145827; BAE26679.1; -; mRNA. DR EMBL; BC010479; AAH10479.1; -; mRNA. DR EMBL; BC019387; AAH19387.1; -; mRNA. DR RefSeq; NP_598440.1; NM_133679.2. DR RefSeq; XP_006523136.1; XM_006523073.1. DR UniGene; Mm.109823; -. DR UniGene; Mm.468265; -. DR ProteinModelPortal; Q921W4; -. DR SMR; Q921W4; 1-348. DR IntAct; Q921W4; 2. DR MINT; MINT-4131456; -. DR STRING; 10090.ENSMUSP00000073171; -. DR PhosphoSite; Q921W4; -. DR PaxDb; Q921W4; -. DR PRIDE; Q921W4; -. DR Ensembl; ENSMUST00000073466; ENSMUSP00000073171; ENSMUSG00000058240. [Q921W4-1] DR Ensembl; ENSMUST00000114023; ENSMUSP00000109656; ENSMUSG00000058240. [Q921W4-2] DR GeneID; 66609; -. DR KEGG; mmu:66609; -. DR UCSC; uc007zyf.2; mouse. [Q921W4-1] DR CTD; 9946; -. DR MGI; MGI:1913859; Cryzl1. DR eggNOG; COG0604; -. DR GeneTree; ENSGT00390000013113; -. DR HOGENOM; HOG000293267; -. DR HOVERGEN; HBG009484; -. DR InParanoid; Q921W4; -. DR KO; K00540; -. DR OMA; SNGKAHV; -. DR OrthoDB; EOG7K0ZDM; -. DR TreeFam; TF328922; -. DR NextBio; 322156; -. DR PRO; PR:Q921W4; -. DR ArrayExpress; Q921W4; -. DR Bgee; Q921W4; -. DR CleanEx; MM_CRYZL1; -. DR Genevestigator; Q921W4; -. DR GO; GO:0005829; C:cytosol; IEA:Ensembl. DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR Gene3D; 3.40.50.720; -; 1. DR Gene3D; 3.90.180.10; -; 1. DR InterPro; IPR013149; ADH_C. DR InterPro; IPR013154; ADH_GroES-like. DR InterPro; IPR002085; ADH_SF_Zn-type. DR InterPro; IPR011032; GroES-like. DR InterPro; IPR016040; NAD(P)-bd_dom. DR PANTHER; PTHR11695; PTHR11695; 1. DR Pfam; PF08240; ADH_N; 1. DR Pfam; PF00107; ADH_zinc_N; 1. DR SUPFAM; SSF50129; SSF50129; 1. PE 2: Evidence at transcript level; KW Alternative splicing; Complete proteome; NADP; Oxidoreductase; KW Reference proteome. FT CHAIN 1 348 Quinone oxidoreductase-like protein 1. FT /FTId=PRO_0000160914. FT VAR_SEQ 226 231 VRLYSK -> GLEADV (in isoform 2). FT /FTId=VSP_000209. FT VAR_SEQ 232 348 Missing (in isoform 2). FT /FTId=VSP_000210. FT CONFLICT 154 155 Missing (in Ref. 2; AAH19387). SQ SEQUENCE 348 AA; 38725 MW; 0EED796E6AF7CB42 CRC64; MKGLYFQQSS TNEEVTFVFQ EKENVPVTED NFVRVQVKAC ALSHINTKLL AEMKMEKDFF PVGREVSGIV LEVGRKVTFF QPDDEVVGIL PLDSEDPGLC EVIRVHEHYL VHKPEKVSWT EAAGVIRDGV RACTALYYLS QLSPGKSVLI MDGASAFGTI AIQLAHHRGA KVISTAHSLE DKQHLERLRP SIARVIDVSN GKVHVAESCL EETGGLGVDI VIDAGVRLYS KDDEPAVKLH LPHKHDIITL LGVGGHWVTT EENLQLDPPD SHCLFLKGAT VAFLNDEVWN LSNAQQGKYL CILKDVMEKL SAGVFRPLLD EPIPLYEAKV SMEVVQKNQE RKKQVVQF // ID QOR_MOUSE Reviewed; 331 AA. AC P47199; Q62508; Q99L63; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 19-MAR-2014, entry version 118. DE RecName: Full=Quinone oxidoreductase; DE EC=1.6.5.5; DE AltName: Full=NADPH:quinone reductase; DE AltName: Full=Zeta-crystallin; GN Name=Cryz; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Liver; RX PubMed=8170370; RA Gonzalez P., Hernandez-Calzadilla C., Rao P.V., Rodriguez I.R., RA Zigler J.S. Jr., Borras T.; RT "Comparative analysis of the zeta-crystallin/quinone reductase gene in RT guinea pig and mouse."; RL Mol. Biol. Evol. 11:305-315(1994). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Mammary tumor; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] OF 130-331. RC STRAIN=C57BL/6J; TISSUE=Brain cortex; RX PubMed=8645260; DOI=10.1006/bbrc.1996.0313; RA Kajiwara K., Nagawawa H., Shimizu-Nishikawa K., Ookura T., Kimura M., RA Sugaya E.; RT "Molecular characterization of seizure-related genes isolated by RT differential screening."; RL Biochem. Biophys. Res. Commun. 219:795-799(1996). RN [4] RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-298, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., RA Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). RN [5] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-186, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23576753; DOI=10.1073/pnas.1302961110; RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., RA Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.; RT "Label-free quantitative proteomics of the lysine acetylome in RT mitochondria identifies substrates of SIRT3 in metabolic pathways."; RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013). CC -!- FUNCTION: Does not have alcohol dehydrogenase activity. Binds NADP CC and acts through a one-electron transfer process. Orthoquinones, CC such as 1,2-naphthoquinone or 9,10-phenanthrenequinone, are the CC best substrates (in vitro). May act in the detoxification of CC xenobiotics. Interacts with (AU)-rich elements (ARE) in the 3'-UTR CC of target mRNA species and enhances their stability. NADPH binding CC interferes with mRNA binding (By similarity). CC -!- CATALYTIC ACTIVITY: NADPH + 2 quinone = NADP(+) + 2 semiquinone. CC -!- SUBUNIT: Homotetramer (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase CC family. Quinone oxidoreductase subfamily. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; S70056; AAB30620.2; -; mRNA. DR EMBL; BC003800; AAH03800.1; -; mRNA. DR EMBL; D78646; BAA11463.1; -; mRNA. DR PIR; A54932; A54932. DR RefSeq; NP_034098.1; NM_009968.3. DR RefSeq; XP_006501036.1; XM_006500973.1. DR UniGene; Mm.374855; -. DR ProteinModelPortal; P47199; -. DR SMR; P47199; 6-331. DR IntAct; P47199; 4. DR MINT; MINT-1862605; -. DR BindingDB; P47199; -. DR ChEMBL; CHEMBL4332; -. DR PhosphoSite; P47199; -. DR REPRODUCTION-2DPAGE; IPI00134704; -. DR REPRODUCTION-2DPAGE; P47199; -. DR PaxDb; P47199; -. DR PRIDE; P47199; -. DR Ensembl; ENSMUST00000029850; ENSMUSP00000029850; ENSMUSG00000028199. DR GeneID; 12972; -. DR KEGG; mmu:12972; -. DR UCSC; uc008rup.3; mouse. DR CTD; 1429; -. DR MGI; MGI:88527; Cryz. DR eggNOG; COG0604; -. DR GeneTree; ENSGT00550000074483; -. DR HOGENOM; HOG000294672; -. DR HOVERGEN; HBG002466; -. DR InParanoid; P47199; -. DR KO; K00344; -. DR OMA; IPYFTAC; -. DR TreeFam; TF314255; -. DR NextBio; 282736; -. DR PRO; PR:P47199; -. DR ArrayExpress; P47199; -. DR Bgee; P47199; -. DR CleanEx; MM_CRYZ; -. DR Genevestigator; P47199; -. DR GO; GO:0005829; C:cytosol; ISS:UniProtKB. DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl. DR GO; GO:0003730; F:mRNA 3'-UTR binding; ISS:UniProtKB. DR GO; GO:0070402; F:NADPH binding; ISS:UniProtKB. DR GO; GO:0003960; F:NADPH:quinone reductase activity; ISS:UniProtKB. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0051289; P:protein homotetramerization; IEA:Ensembl. DR GO; GO:0042178; P:xenobiotic catabolic process; ISS:UniProtKB. DR Gene3D; 3.40.50.720; -; 1. DR Gene3D; 3.90.180.10; -; 1. DR InterPro; IPR013149; ADH_C. DR InterPro; IPR013154; ADH_GroES-like. DR InterPro; IPR002085; ADH_SF_Zn-type. DR InterPro; IPR011032; GroES-like. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR002364; Quin_OxRdtase/zeta-crystal_CS. DR PANTHER; PTHR11695; PTHR11695; 1. DR Pfam; PF08240; ADH_N; 1. DR Pfam; PF00107; ADH_zinc_N; 1. DR SUPFAM; SSF50129; SSF50129; 1. DR PROSITE; PS01162; QOR_ZETA_CRYSTAL; 1. PE 1: Evidence at protein level; KW Acetylation; Complete proteome; Cytoplasm; NADP; Oxidoreductase; KW Reference proteome; RNA-binding. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 331 Quinone oxidoreductase. FT /FTId=PRO_0000160908. FT NP_BIND 158 161 NADP (By similarity). FT NP_BIND 248 251 NADP (By similarity). FT NP_BIND 271 273 NADP (By similarity). FT BINDING 53 53 NADP (By similarity). FT BINDING 181 181 NADP; via amide nitrogen (By similarity). FT BINDING 200 200 NADP (By similarity). FT BINDING 231 231 NADP (By similarity). FT MOD_RES 2 2 N-acetylalanine (By similarity). FT MOD_RES 23 23 N6-acetyllysine (By similarity). FT MOD_RES 186 186 N6-acetyllysine. FT MOD_RES 298 298 N6-succinyllysine. FT CONFLICT 58 58 A -> T (in Ref. 2; AAH03800). FT CONFLICT 131 133 IPY -> TMD (in Ref. 3; BAA11463). SQ SEQUENCE 331 AA; 35269 MW; 35816C043EFE16A2 CRC64; MATGQKLMRA IRVFEFGGPE VLKLQSDVVV PVPQSHQVLI KVHACGVNPV ETYIRSGAYS RKPALPYTPG SDVAGIIESV GDKVSAFKKG DRVFCYSTVS GGYAEFALAA DDTIYPLPET LNFRQGAALG IPYFTACRAL FHSARARAGE SVLVHGASGG VGLATCQIAR AHGLKVLGTA GSEEGKKLVL QNGAHEVFNH KEANYIDKIK MSVGDKDKGV DVIIEMLANE NLSNDLKLLS HGGRVVVVGC RGPIEINPRD TMAKETSIIG VSLSSSTKEE FQQFAGLLQA GIEKGWVKPV IGSEYPLEKA AQAHEDIIHG SGKTGKMILL L // ID QSOX2_MOUSE Reviewed; 692 AA. AC Q3TMX7; A2ALE0; A2ALE1; Q3TZA5; Q8C9I4; Q8K0M2; DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2005, sequence version 1. DT 19-MAR-2014, entry version 78. DE RecName: Full=Sulfhydryl oxidase 2; DE EC=1.8.3.2; DE AltName: Full=Quiescin Q6-like protein 1; DE Flags: Precursor; GN Name=Qsox2; Synonyms=Qscn6l1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3). RC STRAIN=C57BL/6J; TISSUE=Adipose tissue, Inner ear, and Thymus; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC STRAIN=FVB/N; TISSUE=Salivary gland; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: Catalyzes the oxidation of sulfhydryl groups in peptide CC and protein thiols to disulfides with the reduction of oxygen to CC hydrogen peroxide. May contribute to disulfide bond formation in a CC variety of secreted proteins (By similarity). CC -!- CATALYTIC ACTIVITY: 2 R'C(R)SH + O(2) = R'C(R)S-S(R)CR' + CC H(2)O(2). CC -!- COFACTOR: Binds 1 FAD per subunit (Potential). CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein (By CC similarity). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q3TMX7-1; Sequence=Displayed; CC Name=2; CC IsoId=Q3TMX7-2; Sequence=VSP_020501, VSP_020502; CC Note=No experimental confirmation available; CC Name=3; CC IsoId=Q3TMX7-3; Sequence=VSP_020500; CC Note=No experimental confirmation available; CC -!- SIMILARITY: Belongs to the quiescin-sulfhydryl oxidase (QSOX) CC family. CC -!- SIMILARITY: Contains 1 ERV/ALR sulfhydryl oxidase domain. CC -!- SIMILARITY: Contains 1 thioredoxin domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK042036; BAC31140.1; ALT_SEQ; mRNA. DR EMBL; AK140324; BAE24335.1; -; mRNA. DR EMBL; AK157992; BAE34304.1; -; mRNA. DR EMBL; AK165642; BAE38312.1; -; mRNA. DR EMBL; AL773595; CAM20023.1; -; Genomic_DNA. DR EMBL; AL773595; CAM20024.1; -; Genomic_DNA. DR EMBL; BC030934; AAH30934.1; -; mRNA. DR RefSeq; NP_705787.1; NM_153559.2. DR RefSeq; XP_006497965.1; XM_006497902.1. DR UniGene; Mm.116769; -. DR ProteinModelPortal; Q3TMX7; -. DR SMR; Q3TMX7; 54-562. DR PhosphoSite; Q3TMX7; -. DR PaxDb; Q3TMX7; -. DR PRIDE; Q3TMX7; -. DR Ensembl; ENSMUST00000036187; ENSMUSP00000037128; ENSMUSG00000036327. [Q3TMX7-2] DR Ensembl; ENSMUST00000091263; ENSMUSP00000088807; ENSMUSG00000036327. [Q3TMX7-3] DR GeneID; 227638; -. DR KEGG; mmu:227638; -. DR UCSC; uc008iuj.1; mouse. [Q3TMX7-2] DR UCSC; uc008iuk.1; mouse. [Q3TMX7-1] DR CTD; 169714; -. DR MGI; MGI:2387194; Qsox2. DR eggNOG; NOG237986; -. DR GeneTree; ENSGT00390000008045; -. DR HOGENOM; HOG000231631; -. DR HOVERGEN; HBG080360; -. DR InParanoid; A2ALE0; -. DR KO; K10758; -. DR OMA; HCIGYAP; -. DR OrthoDB; EOG73RB9X; -. DR TreeFam; TF316749; -. DR ChiTaRS; QSOX2; mouse. DR NextBio; 378712; -. DR PRO; PR:Q3TMX7; -. DR Bgee; Q3TMX7; -. DR CleanEx; MM_QSOX2; -. DR Genevestigator; Q3TMX7; -. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0016972; F:thiol oxidase activity; IEA:UniProtKB-EC. DR GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro. DR Gene3D; 1.20.120.310; -; 1. DR Gene3D; 3.40.30.10; -; 1. DR InterPro; IPR017905; ERV/ALR_sulphydryl_oxidase. DR InterPro; IPR012336; Thioredoxin-like_fold. DR InterPro; IPR013766; Thioredoxin_domain. DR Pfam; PF04777; Evr1_Alr; 1. DR Pfam; PF00085; Thioredoxin; 1. DR SUPFAM; SSF52833; SSF52833; 1. DR SUPFAM; SSF69000; SSF69000; 1. DR PROSITE; PS51324; ERV_ALR; 1. DR PROSITE; PS51352; THIOREDOXIN_2; 1. PE 2: Evidence at transcript level; KW Alternative splicing; Complete proteome; Disulfide bond; FAD; KW Flavoprotein; Glycoprotein; Membrane; Oxidoreductase; KW Reference proteome; Signal; Transmembrane; Transmembrane helix. FT SIGNAL 1 38 Potential. FT CHAIN 39 692 Sulfhydryl oxidase 2. FT /FTId=PRO_0000249539. FT TRANSMEM 656 676 Helical; (Potential). FT DOMAIN 54 172 Thioredoxin. FT DOMAIN 415 524 ERV/ALR sulfhydryl oxidase. FT NP_BIND 499 506 FAD (By similarity). FT ACT_SITE 85 85 Nucleophile (By similarity). FT ACT_SITE 88 88 Nucleophile (By similarity). FT BINDING 420 420 FAD (By similarity). FT BINDING 427 427 FAD (By similarity). FT BINDING 431 431 FAD (By similarity). FT BINDING 472 472 FAD (By similarity). FT BINDING 476 476 FAD (By similarity). FT BINDING 521 521 FAD (By similarity). FT BINDING 524 524 FAD (By similarity). FT CARBOHYD 71 71 N-linked (GlcNAc...) (Potential). FT CARBOHYD 172 172 N-linked (GlcNAc...) (Potential). FT CARBOHYD 212 212 N-linked (GlcNAc...) (Potential). FT CARBOHYD 260 260 N-linked (GlcNAc...) (Potential). FT DISULFID 85 88 Redox-active (By similarity). FT DISULFID 412 424 By similarity. FT DISULFID 470 473 By similarity. FT DISULFID 530 533 By similarity. FT VAR_SEQ 1 165 Missing (in isoform 3). FT /FTId=VSP_020500. FT VAR_SEQ 574 666 EWEAQGREQEEGKGLNPSGKSWRHHDTGSLRPPHILGPRTD FT LSKSLHHRLDLRLQSPQGPQALKEAKAVVPFLGVGFSSLDM FT SLCVVLYVASS -> SVLRARPWLGQMARLSHVNLLPHFPV FT EEVSSLKPGVLCLKTNKPRSSLGVSKDEHSWSVSLRIGPI FT (in isoform 2). FT /FTId=VSP_020501. FT VAR_SEQ 667 692 Missing (in isoform 2). FT /FTId=VSP_020502. SQ SEQUENCE 692 AA; 77775 MW; 3BDC7058817484A1 CRC64; MAAARAVARD PGAYARQPPS LRAARLPRLL FLLAVVAAVG PREGGGARLY REGSDAVWLL DSGSVRSATG NSSAAWLVQF HSSWCGHCIG YAPTWRALAA DVRDWAAAIR VAALDCAEEK NQDVCRTYDI HFYPTFRYFK AFTKEFTTGE NFKGPDRELR TVRQTMIDFL QNHTEGTWPP ACPPLDPIQS SDILSFMDSH SGQYHAIVFE SNGSYVGREV ILDLIPYENI MVSRALDTDK AFLGTLGITS VPSCYLIYPN GSHGLVNVAK PLRSFFSSHL KSLPDVRKKS LFLPEKSNKE EKSEVVVWKE FDRAKLYTAD LESGLHYLLR VELAAHRSLA GAQLKTFRDF VTVVAKLFPG RPAVKKLLET LQEWLANLPL DKIPYNAILD LVNNKMQISG IFLTSHVKWV GCQGSRLELR GYPCSLWKLF HTLTVQASTH PEALAGTGFE GHPQAVLQAI RRYIRTFFGC KECGEHFEEM AKESMDSVKT PDQAVLWLWR KHNMVNSRLA GHLSEDPKFP KVPWPTPDLC PACHEEIKGL DSWNEGQVLL FLKQHYSRDN LVDAYSVDQG SPGEWEAQGR EQEEGKGLNP SGKSWRHHDT GSLRPPHILG PRTDLSKSLH HRLDLRLQSP QGPQALKEAK AVVPFLGVGF SSLDMSLCVV LYVASSLFLM IMYFFFRVRS KRWKVRLYHP AV // ID QSOX1_MOUSE Reviewed; 748 AA. AC Q8BND5; Q3TDY9; Q3TE19; Q3TR29; Q3UEL4; Q8K041; Q9DBL6; DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 19-MAR-2014, entry version 99. DE RecName: Full=Sulfhydryl oxidase 1; DE Short=mSOx; DE EC=1.8.3.2; DE AltName: Full=Quiescin Q6; DE AltName: Full=Skin sulfhydryl oxidase; DE Flags: Precursor; GN Name=Qsox1; Synonyms=Qscn6, Sox; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), SUBCELLULAR LOCATION, AND RP TISSUE SPECIFICITY. RX PubMed=12354420; DOI=10.1016/S0923-1811(02)00061-0; RA Matsuba S., Suga Y., Ishidoh K., Hashimoto Y., Takamori K., RA Kominami E., Wilhelm B., Seitz J., Ogawa H.; RT "Sulfhydryl oxidase (SOx) from mouse epidermis: molecular cloning, RT nucleotide sequence, and expression of recombinant protein in the RT cultured cells."; RL J. Dermatol. Sci. 30:50-62(2002). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3 AND 4). RC STRAIN=C57BL/6J, and NOD; RC TISSUE=Cerebellum, Liver, and Spinal ganglion; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE RP SEQUENCE [LARGE SCALE MRNA] OF 137-538 (ISOFORM 3). RC STRAIN=C57BL/6, and FVB/N; TISSUE=Eye, and Salivary gland; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: Catalyzes the oxidation of sulfhydryl groups in peptide CC and protein thiols to disulfides with the reduction of oxygen to CC hydrogen peroxide. May contribute to disulfide bond formation in a CC variety of secreted proteins (By similarity). CC -!- CATALYTIC ACTIVITY: 2 R'C(R)SH + O(2) = R'C(R)S-S(R)CR' + CC H(2)O(2). CC -!- COFACTOR: Binds 1 FAD per subunit (By similarity). CC -!- SUBUNIT: Monomer (By similarity). CC -!- SUBCELLULAR LOCATION: Isoform 1: Golgi apparatus membrane; Single- CC pass membrane protein (By similarity). CC -!- SUBCELLULAR LOCATION: Isoform 2: Secreted. Note=Found in the CC extracellular medium of quiescent cells but not in proliferating CC cells. CC -!- SUBCELLULAR LOCATION: Isoform 3: Secreted. Note=Found in the CC extracellular medium of quiescent cells but not in proliferating CC cells. CC -!- SUBCELLULAR LOCATION: Isoform 4: Secreted. Note=Found in the CC extracellular medium of quiescent cells but not in proliferating CC cells. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; CC IsoId=Q8BND5-1; Sequence=Displayed; CC Name=2; CC IsoId=Q8BND5-2; Sequence=VSP_020495, VSP_020496; CC Note=No experimental confirmation available; CC Name=3; CC IsoId=Q8BND5-3; Sequence=VSP_020493, VSP_020494; CC Name=4; CC IsoId=Q8BND5-4; Sequence=VSP_020491, VSP_020492; CC Note=No experimental confirmation available. Ref.2 (BAE37202) CC sequence is in conflict in position: 127:C->Y; CC -!- TISSUE SPECIFICITY: Expressed in the seminal vesicles and skin. CC -!- SIMILARITY: Belongs to the quiescin-sulfhydryl oxidase (QSOX) CC family. CC -!- SIMILARITY: Contains 1 ERV/ALR sulfhydryl oxidase domain. CC -!- SIMILARITY: Contains 1 thioredoxin domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AB044284; BAB21936.1; -; mRNA. DR EMBL; AK004880; BAB23638.1; -; mRNA. DR EMBL; AK083938; BAC39073.1; -; mRNA. DR EMBL; AK149465; BAE28897.1; -; mRNA. DR EMBL; AK163119; BAE37202.1; -; mRNA. DR EMBL; AK166839; BAE39061.1; -; mRNA. DR EMBL; AK169877; BAE41429.1; -; mRNA. DR EMBL; AK169920; BAE41459.1; -; mRNA. DR EMBL; AK170449; BAE41807.1; -; mRNA. DR EMBL; BC034131; AAH34131.1; -; mRNA. DR EMBL; BC076590; AAH76590.1; -; mRNA. DR RefSeq; NP_001020116.1; NM_001024945.1. DR RefSeq; NP_075757.1; NM_023268.2. DR UniGene; Mm.27035; -. DR PDB; 3T58; X-ray; 2.40 A; A/B/C/D=36-550. DR PDB; 3T59; X-ray; 2.80 A; A/B/C/D=36-550. DR PDBsum; 3T58; -. DR PDBsum; 3T59; -. DR ProteinModelPortal; Q8BND5; -. DR SMR; Q8BND5; 38-549. DR PhosphoSite; Q8BND5; -. DR PaxDb; Q8BND5; -. DR PRIDE; Q8BND5; -. DR Ensembl; ENSMUST00000035325; ENSMUSP00000035658; ENSMUSG00000033684. [Q8BND5-1] DR Ensembl; ENSMUST00000111764; ENSMUSP00000107394; ENSMUSG00000033684. [Q8BND5-2] DR GeneID; 104009; -. DR KEGG; mmu:104009; -. DR UCSC; uc007dbo.1; mouse. [Q8BND5-3] DR UCSC; uc007dbp.1; mouse. [Q8BND5-1] DR UCSC; uc007dbq.1; mouse. [Q8BND5-4] DR UCSC; uc011wtx.1; mouse. [Q8BND5-2] DR CTD; 5768; -. DR MGI; MGI:1330818; Qsox1. DR eggNOG; COG0526; -. DR GeneTree; ENSGT00390000008045; -. DR HOVERGEN; HBG080360; -. DR InParanoid; Q8BND5; -. DR KO; K10758; -. DR OMA; SHNRVNA; -. DR OrthoDB; EOG73RB9X; -. DR TreeFam; TF316749; -. DR NextBio; 356343; -. DR PRO; PR:Q8BND5; -. DR Bgee; Q8BND5; -. DR CleanEx; MM_QSOX1; -. DR Genevestigator; Q8BND5; -. DR GO; GO:0005783; C:endoplasmic reticulum; ISA:MGI. DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB. DR GO; GO:0030173; C:integral component of Golgi membrane; ISS:UniProtKB. DR GO; GO:0016971; F:flavin-linked sulfhydryl oxidase activity; ISS:UniProtKB. DR GO; GO:0003756; F:protein disulfide isomerase activity; ISS:UniProtKB. DR GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro. DR Gene3D; 1.20.120.310; -; 1. DR Gene3D; 3.40.30.10; -; 1. DR InterPro; IPR017905; ERV/ALR_sulphydryl_oxidase. DR InterPro; IPR012336; Thioredoxin-like_fold. DR InterPro; IPR013766; Thioredoxin_domain. DR Pfam; PF04777; Evr1_Alr; 1. DR Pfam; PF00085; Thioredoxin; 1. DR SUPFAM; SSF52833; SSF52833; 1. DR SUPFAM; SSF69000; SSF69000; 1. DR PROSITE; PS51324; ERV_ALR; 1. DR PROSITE; PS51352; THIOREDOXIN_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Complete proteome; Disulfide bond; KW FAD; Flavoprotein; Glycoprotein; Golgi apparatus; Membrane; KW Oxidoreductase; Reference proteome; Secreted; Signal; Transmembrane; KW Transmembrane helix. FT SIGNAL 1 32 Potential. FT CHAIN 33 748 Sulfhydryl oxidase 1. FT /FTId=PRO_0000249534. FT TRANSMEM 711 731 Helical; (Potential). FT DOMAIN 33 159 Thioredoxin. FT DOMAIN 399 506 ERV/ALR sulfhydryl oxidase. FT NP_BIND 481 488 FAD (By similarity). FT ACT_SITE 73 73 Nucleophile (By similarity). FT ACT_SITE 76 76 Nucleophile (By similarity). FT BINDING 404 404 FAD (By similarity). FT BINDING 411 411 FAD (By similarity). FT BINDING 415 415 FAD (By similarity). FT BINDING 454 454 FAD (By similarity). FT BINDING 458 458 FAD (By similarity). FT BINDING 503 503 FAD (By similarity). FT BINDING 506 506 FAD (By similarity). FT CARBOHYD 133 133 N-linked (GlcNAc...) (Potential). FT CARBOHYD 246 246 N-linked (GlcNAc...) (Potential). FT DISULFID 73 76 Redox-active (By similarity). FT DISULFID 396 408 By similarity. FT DISULFID 452 455 By similarity. FT DISULFID 512 515 By similarity. FT VAR_SEQ 126 154 FFQAFTKNGSGATLPGAGANVQTLRMRLI -> VCEGGATV FT EWFWPSTQSSVPHFPGTFLGC (in isoform 4). FT /FTId=VSP_020491. FT VAR_SEQ 155 748 Missing (in isoform 4). FT /FTId=VSP_020492. FT VAR_SEQ 567 568 VM -> LL (in isoform 3). FT /FTId=VSP_020493. FT VAR_SEQ 569 748 Missing (in isoform 3). FT /FTId=VSP_020494. FT VAR_SEQ 660 661 VN -> LL (in isoform 2). FT /FTId=VSP_020495. FT VAR_SEQ 662 748 Missing (in isoform 2). FT /FTId=VSP_020496. FT CONFLICT 637 637 M -> I (in Ref. 2; BAE41429). FT CONFLICT 656 656 F -> L (in Ref. 2; BAE41429). FT STRAND 43 48 FT TURN 50 52 FT HELIX 53 57 FT STRAND 61 69 FT HELIX 74 90 FT HELIX 91 93 FT TURN 94 96 FT STRAND 97 103 FT HELIX 107 109 FT HELIX 110 115 FT STRAND 120 127 FT STRAND 137 139 FT HELIX 146 157 FT HELIX 176 179 FT HELIX 182 184 FT STRAND 189 196 FT HELIX 202 209 FT TURN 210 212 FT STRAND 216 222 FT HELIX 226 232 FT STRAND 237 244 FT STRAND 249 251 FT HELIX 259 266 FT HELIX 293 296 FT STRAND 301 303 FT HELIX 304 316 FT HELIX 319 321 FT STRAND 323 326 FT HELIX 327 343 FT HELIX 348 363 FT STRAND 367 370 FT HELIX 371 380 FT HELIX 383 386 FT STRAND 403 405 FT HELIX 406 426 FT HELIX 437 449 FT HELIX 453 466 FT HELIX 467 469 FT HELIX 473 491 FT STRAND 505 507 FT TURN 509 511 FT HELIX 513 515 FT HELIX 528 538 FT HELIX 541 543 SQ SEQUENCE 748 AA; 82785 MW; 0499F6B8DAB5A8D1 CRC64; MRRCGRLSGP PSLLLLLLLL SPLLFSGPGA YAARLSVLYS SSDPLTLLDA DSVRPTVLGS SSAWAVEFFA SWCGHCIAFA PTWKELANDV KDWRPALNLA VLDCAEETNS AVCREFNIAG FPTVRFFQAF TKNGSGATLP GAGANVQTLR MRLIDALESH RDTWPPACPP LEPAKLNDID GFFTRNKADY LALVFEREDS YLGREVTLDL SQYHAVAVRR VLNTESDLVN KFGVTDFPSC YLLLRNGSVS RVPVLVESRS FYTSYLRGLP GLTRDAPPTT ATPVTADKIA PTVWKFADRS KIYMADLESA LHYILRVEVG KFSVLEGQRL VALKKFVAVL AKYFPGQPLV QNFLHSINDW LQKQQKKRIP YSFFKAALDS RKEDAVLTEK VNWVGCQGSE PHFRGFPCSL WVLFHFLTVQ ANRYSEAHPQ EPADGQEVLQ AMRSYVQFFF GCRDCADHFE QMAAASMHQV RSPSNAILWL WTSHNRVNAR LSGALSEDPH FPKVQWPPRE LCSACHNELN GQVPLWDLGA TLNFLKAHFS PANIVIDSSA SRHTGRRGSP EATPELVMDT LKLESRNSVL GHEQAASAES PGATALDVPA EKPEASGPQE LYTGLRMGGA SPGQGPPERM EDHQRDMQEN APGQQHLSKR DTEALFLPEV NHLQGPLELR RGGRSPKQLA PILEEEPEAL AIQGQGQWLQ VLGGGISHLD ISLCVGLYSV SFMGLLAMYT YFRARLRTPK GHASYPTA // ID RDH10_MOUSE Reviewed; 341 AA. AC Q8VCH7; Q8CJ68; DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2004, sequence version 2. DT 19-FEB-2014, entry version 92. DE RecName: Full=Retinol dehydrogenase 10; DE EC=1.1.1.300; GN Name=Rdh10; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY. RC STRAIN=C57BL/6; TISSUE=Eye; RX PubMed=12407145; RA Wu B.X., Chen Y., Chen Y., Fan J., Rohrer B., Crouch R.K., Ma J.-X.; RT "Cloning and characterization of a novel all-trans retinol short-chain RT dehydrogenase/reductase from the RPE."; RL Invest. Ophthalmol. Vis. Sci. 43:3365-3372(2002). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Salivary gland; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP TISSUE SPECIFICITY. RX PubMed=15505029; DOI=10.1167/iovs.03-1302; RA Wu B.X., Moiseyev G., Chen Y., Rohrer B., Crouch R.K., Ma J.-X.; RT "Identification of RDH10, an all-trans retinol dehydrogenase, in RT retinal Mueller cells."; RL Invest. Ophthalmol. Vis. Sci. 45:3857-3862(2004). RN [4] RP FUNCTION, DEVELOPMENTAL STAGE, AND SUBCELLULAR LOCATION. RX PubMed=17473173; DOI=10.1101/gad.1533407; RA Sandell L.L., Sanderson B.W., Moiseyev G., Johnson T., Mushegian A., RA Young K., Rey J.-P., Ma J.-X., Staehling-Hampton K., Trainor P.A.; RT "RDH10 is essential for synthesis of embryonic retinoic acid and is RT required for limb, craniofacial, and organ development."; RL Genes Dev. 21:1113-1124(2007). CC -!- FUNCTION: Retinol dehydrogenase with a clear preference for NADP. CC Converts all-trans-retinol to all-trans-retinal. Has no detectable CC activity towards 11-cis-retinol, 9-cis-retinol and 13-cis-retinol CC (By similarity). Required for normal embryonic development. CC -!- CATALYTIC ACTIVITY: All-trans-retinol + NADP(+) = all-trans- CC retinal + NADPH. CC -!- PATHWAY: Cofactor metabolism; retinol metabolism. CC -!- SUBCELLULAR LOCATION: Microsome membrane; Single-pass membrane CC protein (Potential). Endoplasmic reticulum membrane; Single-pass CC membrane protein (Potential). CC -!- TISSUE SPECIFICITY: Detected in retinal pigment epithelium (at CC protein level). CC -!- DEVELOPMENTAL STAGE: First detected in the neural groove at E8.0. CC At E8.5, detected in lateral plate mesoderm, the dorsal region of CC the somites, the floor plate of the neural tube and in head CC mesenchyme. At E9.5, detected in dorsal paraxial mesoderm, lateral CC plate mesoderm and in nephrogenic cord tissues. At E10.5, detected CC in lung buds, developing mesonephros, mesodermal tissue CC surrounding dorsal root ganglia and adjacent to the forlimb buds. CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases CC (SDR) family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF456767; AAN64749.1; -; mRNA. DR EMBL; BC019796; AAH19796.2; -; mRNA. DR RefSeq; NP_598593.1; NM_133832.3. DR UniGene; Mm.274376; -. DR ProteinModelPortal; Q8VCH7; -. DR SMR; Q8VCH7; 30-303. DR IntAct; Q8VCH7; 1. DR MINT; MINT-4119572; -. DR PhosphoSite; Q8VCH7; -. DR PaxDb; Q8VCH7; -. DR PRIDE; Q8VCH7; -. DR Ensembl; ENSMUST00000027053; ENSMUSP00000027053; ENSMUSG00000025921. DR GeneID; 98711; -. DR KEGG; mmu:98711; -. DR UCSC; uc007ajm.1; mouse. DR CTD; 157506; -. DR MGI; MGI:1924238; Rdh10. DR eggNOG; COG1028; -. DR GeneTree; ENSGT00540000069900; -. DR HOVERGEN; HBG051352; -. DR InParanoid; Q8VCH7; -. DR KO; K11151; -. DR OMA; MNNNEAK; -. DR OrthoDB; EOG7Z3F50; -. DR TreeFam; TF312837; -. DR BRENDA; 1.1.1.105; 3474. DR UniPathway; UPA00912; -. DR NextBio; 353589; -. DR PRO; PR:Q8VCH7; -. DR Bgee; Q8VCH7; -. DR CleanEx; MM_RDH10; -. DR Genevestigator; Q8VCH7; -. DR GO; GO:0044297; C:cell body; IEA:Ensembl. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0016020; C:membrane; IDA:MGI. DR GO; GO:0052650; F:NADP-retinol dehydrogenase activity; IEA:UniProtKB-EC. DR GO; GO:0004745; F:retinol dehydrogenase activity; IMP:MGI. DR GO; GO:0060449; P:bud elongation involved in lung branching; IMP:MGI. DR GO; GO:0043583; P:ear development; IMP:MGI. DR GO; GO:0031076; P:embryonic camera-type eye development; IMP:MGI. DR GO; GO:0035115; P:embryonic forelimb morphogenesis; IMP:MGI. DR GO; GO:0048703; P:embryonic viscerocranium morphogenesis; IMP:MGI. DR GO; GO:0008406; P:gonad development; IMP:MGI. DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI. DR GO; GO:0001656; P:metanephros development; IMP:MGI. DR GO; GO:0014032; P:neural crest cell development; IMP:MGI. DR GO; GO:0043584; P:nose development; IMP:MGI. DR GO; GO:0060431; P:primary lung bud formation; IMP:MGI. DR GO; GO:0042574; P:retinal metabolic process; IEA:Ensembl. DR GO; GO:0002138; P:retinoic acid biosynthetic process; IMP:MGI. DR GO; GO:0007601; P:visual perception; ISA:MGI. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR002198; DH_sc/Rdtase_SDR. DR InterPro; IPR002347; Glc/ribitol_DH. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR020904; Sc_DH/Rdtase_CS. DR Pfam; PF00106; adh_short; 1. DR PIRSF; PIRSF000126; 11-beta-HSD1; 1. DR PRINTS; PR00081; GDHRDH. DR PRINTS; PR00080; SDRFAMILY. DR PROSITE; PS00061; ADH_SHORT; 1. PE 1: Evidence at protein level; KW Complete proteome; Endoplasmic reticulum; Membrane; Microsome; NADP; KW Oxidoreductase; Reference proteome; Signal-anchor; Transmembrane; KW Transmembrane helix. FT CHAIN 1 341 Retinol dehydrogenase 10. FT /FTId=PRO_0000307683. FT TRANSMEM 3 23 Helical; Signal-anchor; (Potential). FT NP_BIND 40 64 NADP (By similarity). FT ACT_SITE 210 210 Proton acceptor (By similarity). FT BINDING 197 197 Substrate (By similarity). SQ SEQUENCE 341 AA; 38075 MW; D0FEDDBE9915EA89 CRC64; MNIVVEFFVV TFKVLWAFVL AAARWLVRPK EKSVAGQVCL ITGAGSGLGR LFALEFARRR ALLVLWDINT QSNEETAGMV RHIYRDLEAA DAAALQAGKG EEEILPPCNL QVFTYTCDVG KRENVYLTAE RVRKEVGEVS VLVNNAGVVS GHHLLECPDE LIERTMMVNC HAHFWTTKAF LPTMLEINHG HIVTVASSLG LFSTAGVEDY CASKFGVVGF HESLSHELKA AEKDGIKTTL VCPYLVDTGM FRGCRIRKEI EPFLPPLKPD YCVKQAMRAI LTDQPMVCTP RLMYIVTFMK SILPFEAVVC MYRFLGADKC MYPFIAQRKQ ATNNNEAKNG I // ID RDH14_MOUSE Reviewed; 334 AA. AC Q9ERI6; DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2001, sequence version 1. DT 19-FEB-2014, entry version 94. DE RecName: Full=Retinol dehydrogenase 14; DE EC=1.1.1.-; DE AltName: Full=Alcohol dehydrogenase PAN2; GN Name=Rdh14; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=C57BL/6J; TISSUE=Fetus; RA Li K.X., Brereton P.S., Obeyesekere V.R., Krozowski Z.S.; RT "Cloning of the mouse Pan2 cDNA: a novel member of the short chain RT alcohol dehydrogenase superfamily."; RL Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Mammary tumor; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: Exhibits an oxidoreductive catalytic activity towards CC retinoids. Most efficient as an NADPH-dependent retinal reductase. CC Displays high activity toward 9-cis and all-trans-retinol. No CC steroid dehydrogenase activity detected (By similarity). CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases CC (SDR) family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF303831; AAG30904.1; -; mRNA. DR EMBL; BC020094; AAH20094.1; -; mRNA. DR RefSeq; NP_076186.1; NM_023697.2. DR UniGene; Mm.119343; -. DR ProteinModelPortal; Q9ERI6; -. DR SMR; Q9ERI6; 45-327. DR PhosphoSite; Q9ERI6; -. DR PaxDb; Q9ERI6; -. DR PRIDE; Q9ERI6; -. DR Ensembl; ENSMUST00000020947; ENSMUSP00000020947; ENSMUSG00000020621. DR GeneID; 105014; -. DR KEGG; mmu:105014; -. DR UCSC; uc007nar.2; mouse. DR CTD; 57665; -. DR MGI; MGI:1920402; Rdh14. DR eggNOG; COG1028; -. DR GeneTree; ENSGT00570000078988; -. DR HOVERGEN; HBG078800; -. DR InParanoid; Q9ERI6; -. DR KO; K11162; -. DR OMA; RAFCQEM; -. DR OrthoDB; EOG73Z2TK; -. DR TreeFam; TF105429; -. DR BRENDA; 1.1.1.105; 3474. DR NextBio; 357402; -. DR PRO; PR:Q9ERI6; -. DR Bgee; Q9ERI6; -. DR CleanEx; MM_RDH14; -. DR Genevestigator; Q9ERI6; -. DR GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR002198; DH_sc/Rdtase_SDR. DR InterPro; IPR002347; Glc/ribitol_DH. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Pfam; PF00106; adh_short; 1. DR PRINTS; PR00081; GDHRDH. DR PRINTS; PR00080; SDRFAMILY. PE 2: Evidence at transcript level; KW Complete proteome; NADP; Oxidoreductase; Reference proteome. FT CHAIN 1 334 Retinol dehydrogenase 14. FT /FTId=PRO_0000054771. FT NP_BIND 51 57 NADP (By similarity). FT ACT_SITE 215 215 Proton acceptor (By similarity). FT BINDING 190 190 Substrate (By similarity). SQ SEQUENCE 334 AA; 36366 MW; A05653655E70802D CRC64; MAVASVAAAL LAALGGALWL AARRFSGPRN QRQQGGGDPG LMHGKTVLIT GANSGLGRAT AAELLRLGAR VIMGCRDRAR AEEAAGQLRQ ELCQAGGAGP DGTDGQLVVK ELDLASLRSV RAFCQELLQE EPRLDVLINN AGVFHCPYTK TEDGFEMQFG VNHLGHFLLT NLLLGLLKSS APSRIVVVSS KLYKYGEINF EDLNSEQSYN KSFCYSRSKL ANILFTRELA RRLEGTNVTV NVLHPGIVRT NLGRHIHIPL LARPLFNLVS WAFFKTPLEG AQTSIYLACS PDVEGVSGRY FGDCKEEELL PKAMDESVAR KLWDISEVMV GILK // ID RDH11_MOUSE Reviewed; 316 AA. AC Q9QYF1; Q3UXM9; Q9D0U5; DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot. DT 29-AUG-2003, sequence version 2. DT 19-MAR-2014, entry version 114. DE RecName: Full=Retinol dehydrogenase 11; DE EC=1.1.1.300; DE AltName: Full=Androgen-regulated short-chain dehydrogenase/reductase 1; DE AltName: Full=Cell line MC/9.IL4-derived protein 1; DE AltName: Full=M42C60; DE AltName: Full=Prostate short-chain dehydrogenase/reductase 1; DE AltName: Full=Retinal reductase 1; DE Short=RalR1; DE AltName: Full=Short-chain aldehyde dehydrogenase; DE Short=SCALD; GN Name=Rdh11; Synonyms=Arsdr1, Mdt1, Psdr1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND ALTERNATIVE SPLICING. RC TISSUE=Mast cell; RX PubMed=8018917; RA Hara T., Harada N., Mitsui H., Miura T., Ishizaka T., Miyajima A.; RT "Characterization of cell phenotype by a novel cDNA library RT subtraction system: expression of CD8 alpha in a mast cell-derived RT interleukin-4-dependent cell line."; RL Blood 84:189-199(1994). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Testis; RX PubMed=12137953; DOI=10.1016/S0378-1119(02)00718-7; RA Moore S., Pritchard C., Lin B., Ferguson C., Nelson P.S.; RT "Isolation and characterization of the murine prostate short-chain RT dehydrogenase/reductase 1 (Psdr1) gene, a new member of the short- RT chain steroid dehydrogenase/reductase family."; RL Gene 293:149-160(2002). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=12807874; DOI=10.1074/jbc.M304969200; RA Kasus-Jacobi A., Ou J., Bashmakov Y.K., Shelton J.M., Richardson J.A., RA Goldstein J.L., Brown M.S.; RT "Characterization of mouse short-chain aldehyde reductase (SCALD), an RT enzyme regulated by sterol regulatory element-binding proteins."; RL J. Biol. Chem. 278:32380-32389(2003). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Embryo, and Muellerian duct; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Mammary tumor; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: Exhibits an oxidoreductive catalytic activity towards CC retinoids. Most efficient as an NADPH-dependent all-trans-retinal CC reductase. Also involved in the metabolism of short-chain CC aldehydes. CC -!- CATALYTIC ACTIVITY: All-trans-retinol + NADP(+) = all-trans- CC retinal + NADPH. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass CC type II membrane protein (By similarity). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=1; CC Comment=A number of isoforms are produced; CC Name=1; CC IsoId=Q9QYF1-1; Sequence=Displayed; CC -!- TISSUE SPECIFICITY: Expressed at higher level in liver and testis. CC Expressed at lower levels in smooth muscle, thymus, submaxillary CC gland and epididymis. In testis, expression is restricted to CC pachytene spermatocytes. Also expressed in four layers of the CC retina, including the outer segment of rods and cones. CC -!- PTM: Not glycosylated (By similarity). CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases CC (SDR) family. CC -!- SEQUENCE CAUTION: CC Sequence=BAA88521.1; Type=Frameshift; Positions=311; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AB035959; BAA88521.1; ALT_FRAME; mRNA. DR EMBL; AY039032; AAK91516.1; -; mRNA. DR EMBL; AF474027; AAL79910.1; -; mRNA. DR EMBL; AK004413; BAB23296.1; -; mRNA. DR EMBL; AK135443; BAE22534.1; -; mRNA. DR EMBL; BC018261; AAH18261.1; -; mRNA. DR RefSeq; NP_067532.2; NM_021557.5. DR UniGene; Mm.291799; -. DR ProteinModelPortal; Q9QYF1; -. DR SMR; Q9QYF1; 28-315. DR IntAct; Q9QYF1; 2. DR MINT; MINT-1865554; -. DR PhosphoSite; Q9QYF1; -. DR PaxDb; Q9QYF1; -. DR PRIDE; Q9QYF1; -. DR Ensembl; ENSMUST00000161204; ENSMUSP00000124066; ENSMUSG00000066441. [Q9QYF1-1] DR GeneID; 17252; -. DR KEGG; mmu:17252; -. DR UCSC; uc007oaa.1; mouse. [Q9QYF1-1] DR CTD; 51109; -. DR MGI; MGI:102581; Rdh11. DR eggNOG; COG1028; -. DR GeneTree; ENSGT00570000078988; -. DR HOVERGEN; HBG078800; -. DR InParanoid; Q9QYF1; -. DR KO; K11152; -. DR OMA; CMWWLFS; -. DR OrthoDB; EOG73Z2TK; -. DR TreeFam; TF105429; -. DR BRENDA; 1.1.1.105; 3474. DR NextBio; 291722; -. DR PRO; PR:Q9QYF1; -. DR ArrayExpress; Q9QYF1; -. DR Bgee; Q9QYF1; -. DR CleanEx; MM_RDH11; -. DR Genevestigator; Q9QYF1; -. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005622; C:intracellular; ISS:UniProtKB. DR GO; GO:0001917; C:photoreceptor inner segment; IDA:MGI. DR GO; GO:0052650; F:NADP-retinol dehydrogenase activity; ISO:MGI. DR GO; GO:0004745; F:retinol dehydrogenase activity; ISS:UniProtKB. DR GO; GO:0016062; P:adaptation of rhodopsin mediated signaling; IMP:MGI. DR GO; GO:0042574; P:retinal metabolic process; ISO:MGI. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR002198; DH_sc/Rdtase_SDR. DR InterPro; IPR002347; Glc/ribitol_DH. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Pfam; PF00106; adh_short; 1. DR PRINTS; PR00081; GDHRDH. DR PRINTS; PR00080; SDRFAMILY. PE 2: Evidence at transcript level; KW Acetylation; Alternative splicing; Complete proteome; KW Endoplasmic reticulum; Membrane; NADP; Oxidoreductase; KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix. FT CHAIN 1 316 Retinol dehydrogenase 11. FT /FTId=PRO_0000054764. FT TRANSMEM 1 21 Helical; Signal-anchor for type II FT membrane protein; (Potential). FT TOPO_DOM 22 316 Cytoplasmic (Potential). FT NP_BIND 45 51 NADP (By similarity). FT ACT_SITE 199 199 Proton acceptor (By similarity). FT BINDING 174 174 Substrate (By similarity). FT MOD_RES 109 109 N6-acetyllysine (By similarity). FT CONFLICT 238 238 R -> G (in Ref. 1; BAA88521). FT CONFLICT 279 279 S -> R (in Ref. 1; BAA88521). SQ SEQUENCE 316 AA; 35148 MW; 62FAE25585CC05FE CRC64; MFGFLLLLSL PFILYLVTPK IRKMLSSGVC TSNVQLPGKV AIVTGANTGI GKETAKDLAQ RGARVYLACR DVDKGELAAR EIQAVTGNSQ VFVRKLDLAD TKSIRAFAKD FLAEEKHLHL LINNAGVMMC PYSKTADGFE MHIGVNHLGH FLLTHLLLEK LKESAPSRIV NLSSLGHHLG RIHFHNLQGE KFYSAGLAYC HSKLANILFT KELAKRLKGS GVTTYSVHPG TVHSELTRYS SIMRWLWQLF FVFIKTPQEG AQTSLYCALT EGLESLSGSH FSDCQLAWVS YQGRNEIIAR RLWDVSCDLL GLPVDW // ID RDH1_MOUSE Reviewed; 318 AA. AC O55240; DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1998, sequence version 1. DT 19-MAR-2014, entry version 119. DE RecName: Full=11-cis retinol dehydrogenase; DE Short=11-cis RDH; DE Short=11-cis RoDH; DE EC=1.1.1.315; DE AltName: Full=9-cis retinol dehydrogenase; DE AltName: Full=Cis-retinol dehydrogenase; DE AltName: Full=Retinol dehydrogenase 5; DE Flags: Precursor; GN Name=Rdh5; Synonyms=cRDH, rdh, RDH4; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY. RC STRAIN=129/SvJ; TISSUE=Liver; RX PubMed=9654122; DOI=10.1016/S0014-5793(98)00473-6; RA Driessen C.A., Winkens H.J., Kuhlmann E.D., Janssen A.P., RA van Vugt A.H., Deutman A.F., Janssen J.J.; RT "The visual cycle retinol dehydrogenase: possible involvement in the RT 9-cis retinoic acid biosynthetic pathway."; RL FEBS Lett. 428:135-140(1998). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY, RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE. RC TISSUE=Liver; RX PubMed=9539749; DOI=10.1073/pnas.95.8.4404; RA Romert A., Tuvendal P., Simon A., Dencker L., Eriksson U.; RT "The identification of a 9-cis retinol dehydrogenase in the mouse RT embryo reveals a pathway for synthesis of 9-cis retinoic acid."; RL Proc. Natl. Acad. Sci. U.S.A. 95:4404-4409(1998). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, CATALYTIC RP ACTIVITY, ENZYME REGULATION, AND TISSUE SPECIFICITY. RC STRAIN=129/SvJ, BALB/c, and C57BL/6J; TISSUE=Kidney, and Liver; RX PubMed=10588954; RA Gamble M.V., Shang E., Zott R.P., Mertz J.R., Wolgemuth D.J., RA Blaner W.S.; RT "Biochemical properties, tissue expression, and gene structure of a RT short chain dehydrogenase/reductase able to catalyze cis-retinol RT oxidation."; RL J. Lipid Res. 40:2279-2292(1999). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Cerebellum; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Kidney; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [8] RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE. RX PubMed=10739682; DOI=10.1006/excr.2000.4817; RA Romert A., Tuvendal P., Tryggvason K., Dencker L., Eriksson U.; RT "Gene structure, expression analysis, and membrane topology of RDH4."; RL Exp. Cell Res. 256:338-345(2000). RN [9] RP DISRUPTION PHENOTYPE. RX PubMed=10825191; DOI=10.1128/MCB.20.12.4275-4287.2000; RA Driessen C.A., Winkens H.J., Hoffmann K., Kuhlmann L.D., Janssen B.P., RA Van Vugt A.H., Van Hooser J.P., Wieringa B.E., Deutman A.F., RA Palczewski K., Ruether K., Janssen J.J.; RT "Disruption of the 11-cis-retinol dehydrogenase gene leads to RT accumulation of cis-retinols and cis-retinyl esters."; RL Mol. Cell. Biol. 20:4275-4287(2000). CC -!- FUNCTION: Stereospecific 11-cis retinol dehydrogenase, which CC catalyzes the final step in the biosynthesis of 11-cis CC retinaldehyde, the universal chromophore of visual pigments. Also CC able to oxidize 9-cis-retinol and 13-cis-retinol, but not all- CC trans-retinol. Active in the presence of NAD as cofactor but not CC in the presence of NADP. CC -!- CATALYTIC ACTIVITY: 11-cis-retinol-[retinal-binding-protein] + CC NAD(+) = 11-cis-retinal-[retinol-binding-protein] + NADH. CC -!- ENZYME REGULATION: Inhibited by 9-cis-, 13-cis- and all-trans- CC retinoic acids, with the most potent inhibitor being 13-cis- CC retinoic acid. Weakly inhibited by oleic acid. CC -!- PATHWAY: Cofactor metabolism; retinol metabolism. CC -!- SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein (By CC similarity). Endoplasmic reticulum lumen. CC -!- TISSUE SPECIFICITY: Expressed in eye, liver, kidney, brain, CC intestine, placenta, epididymus and submaxillary gland. In eye, CC strongly expressed in the retinal pigment epithelium, with lower CC expression levels detected in the inner segment of the CC photoreceptor cells and in the outer plexiform layer. In kidney, CC strong expression detected in the distal tubules and the CC transitional epithelium in the renal pelvis, with weaker CC expression detected in the epithelium of the outer stripe of the CC outer zone of the medulla. In liver, detected in hepatocytes in CC the centrilobular area. In lung, present in Clara cells in the CC epithelium of the bronchiole, in parenchyma and in cartilage CC surrounding the secondary bronchi. In skin, expressed in CC epidermis, hair follicles and mast cells in the dermis. Expressed CC in heart (PubMed:10588954 and PubMed:10739682). Not detected in CC heart (PubMed:9539749). Not detected in lung, spleen, skeletal CC muscle and testis. CC -!- DEVELOPMENTAL STAGE: Abundantly expressed during embryonic CC development, especially in the developing central nervous system CC and sensory organs, cranial and spinal ganglia and endoderm of CC foregut and hindgut. At E10, detected along the entire neural CC tube, the mid- and hindbrain floor, the central canal of the brain CC vesicles, spinal cord, lung mesenchyme, the trabecular layer of CC the heart ventricles, endoderm and endodermally-derived structures CC such as tracheal epithelium and liver. At E11, expressed in the CC brain vesicles, along the spinal cord, myotome, migrating muscle CC progenitor cells in the body wall, cells of the genital ridge, CC spinal ganglion, liver, cerebellar primordium, basal cells of the CC neuroepithelium of the mesenchephalic flexure, collections of CC cells in the pons, Rathke's pouch, spinal and cranial ganglia and CC the floor plate, retina, lens, optic stalks and the neural crest- CC derived mesenchyme in the anterior eye segment. During eye CC development, expression restricted to the retinal pigment CC epithelium of the posterior hemisphere at E18, with expression CC levels increasing postnatally to P16. CC -!- DISRUPTION PHENOTYPE: Mutant mice develop normally and are CC fertile. No abnormalities can be found in the retinal structure, CC rhodopsin content and fundus appearance of their eyes. Mice CC display a mild visual phenotype of impaired dark adaptation and CC accumulation of 11-cis- and 13-cis-retinols and 11-cis- and 13- CC cis-retinyl esters in the eyes. CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases CC (SDR) family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X97752; CAA66347.1; -; Genomic_DNA. DR EMBL; AF013288; AAC25951.1; -; mRNA. DR EMBL; AF033195; AAC00491.1; -; mRNA. DR EMBL; AF033196; AAC00492.1; -; mRNA. DR EMBL; AK135139; BAE22435.1; -; mRNA. DR EMBL; AC122380; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH466578; EDL24632.1; -; Genomic_DNA. DR EMBL; BC021372; AAH21372.1; -; mRNA. DR RefSeq; NP_598767.1; NM_134006.4. DR RefSeq; XP_006513450.1; XM_006513387.1. DR UniGene; Mm.439856; -. DR ProteinModelPortal; O55240; -. DR SMR; O55240; 27-281. DR PRIDE; O55240; -. DR Ensembl; ENSMUST00000026406; ENSMUSP00000026406; ENSMUSG00000025350. DR GeneID; 19682; -. DR KEGG; mmu:19682; -. DR UCSC; uc007how.1; mouse. DR CTD; 5959; -. DR MGI; MGI:1201412; Rdh5. DR GeneTree; ENSGT00620000087655; -. DR HOVERGEN; HBG005482; -. DR InParanoid; O55240; -. DR KO; K00061; -. DR OMA; GPTPWLT; -. DR OrthoDB; EOG7FXZZX; -. DR TreeFam; TF325617; -. DR BRENDA; 1.1.1.105; 244. DR UniPathway; UPA00912; -. DR NextBio; 297004; -. DR PRO; PR:O55240; -. DR ArrayExpress; O55240; -. DR Bgee; O55240; -. DR Genevestigator; O55240; -. DR GO; GO:0044297; C:cell body; IEA:Ensembl. DR GO; GO:0005788; C:endoplasmic reticulum lumen; IDA:MGI. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW. DR GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW. DR GO; GO:0042572; P:retinol metabolic process; IEA:UniProtKB-UniPathway. DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR002198; DH_sc/Rdtase_SDR. DR InterPro; IPR002347; Glc/ribitol_DH. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Pfam; PF00106; adh_short; 1. DR PRINTS; PR00081; GDHRDH. DR PRINTS; PR00080; SDRFAMILY. PE 1: Evidence at protein level; KW Complete proteome; Endoplasmic reticulum; Glycoprotein; Membrane; NAD; KW Oxidoreductase; Reference proteome; Sensory transduction; Signal; KW Vision. FT SIGNAL 1 23 Potential. FT CHAIN 24 318 11-cis retinol dehydrogenase. FT /FTId=PRO_0000419633. FT NP_BIND 32 56 NADP (By similarity). FT ACT_SITE 175 175 Proton acceptor (By similarity). FT BINDING 163 163 Substrate (By similarity). FT CARBOHYD 160 160 N-linked (GlcNAc...) (Potential). SQ SEQUENCE 318 AA; 34826 MW; AA8DB76CD0BF7DFC CRC64; MWLPLLLGAL LWAVLWLLRD RQSLPASDAF IFITGCDSGF GRLLALQLDQ KGFQVLAGCL TPSGAEDLQQ MASSRLHTTL LDITDPQNVQ QVAKWVKTRV GETGLFGLVN NAGVAGIIGP TPWLTQDDFQ RVLSVNTLGP IGVTLALLPL LQQARGRVVN ITSVLGRIAA NGGGYCVSKF GLEAFSDSLR RDMAPFGVQV SIVEPGFFRT PVTNLESLES TLKACWARLP PAIQAHYGEA FLDTYLRVQR RIMNLICDPE LTKVTSCLEH ALTARHPRTR YSPGWDAKLL WLPASYLPAR VVDAVLTWIL PRPAQSVS // ID RDHE2_MOUSE Reviewed; 309 AA. AC Q7TQA3; DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2003, sequence version 1. DT 19-MAR-2014, entry version 89. DE RecName: Full=Epidermal retinol dehydrogenase 2; DE Short=EPHD-2; DE Short=RDH-E2; DE EC=1.1.1.105; DE AltName: Full=Retinal short-chain dehydrogenase reductase 2; DE Short=retSDR2; DE AltName: Full=Short-chain dehydrogenase reductase 9; DE AltName: Full=Short-chain dehydrogenase/reductase family 16C member 5; GN Name=Sdr16c5; Synonyms=Rdhe2, Scdr9; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Huang C.Q., Wu S.L., Cheng Z.; RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Cecum; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: Oxidoreductase with strong preference for NAD. Active in CC both the oxidative and reductive directions. Oxidizes all-trans- CC retinol in all-trans-retinaldehyde. No activity was detected with CC 11-cis-retinol or 11-cis-retinaldehyde as substrates with either CC NAD(+)/NADH or NADP(+)/NADPH (By similarity). CC -!- CATALYTIC ACTIVITY: All-trans-retinol-[cellular-retinol-binding- CC protein] + NAD(+) = all-trans-retinal-[cellular-retinol-binding- CC protein] + NADH. CC -!- PATHWAY: Cofactor metabolism; retinol metabolism. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass CC membrane protein (By similarity). CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases CC (SDR) family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AY277588; AAP41074.1; -; mRNA. DR EMBL; AK136508; BAE23016.1; -; mRNA. DR EMBL; AL807387; CAM18651.1; -; Genomic_DNA. DR EMBL; BC104134; AAI04135.1; -; mRNA. DR EMBL; BC104135; AAI04136.1; -; mRNA. DR RefSeq; NP_871789.1; NM_181989.1. DR UniGene; Mm.98096; -. DR ProteinModelPortal; Q7TQA3; -. DR SMR; Q7TQA3; 34-281. DR STRING; 10090.ENSMUSP00000046298; -. DR PhosphoSite; Q7TQA3; -. DR PRIDE; Q7TQA3; -. DR DNASU; 242285; -. DR Ensembl; ENSMUST00000040925; ENSMUSP00000046298; ENSMUSG00000028236. DR GeneID; 242285; -. DR KEGG; mmu:242285; -. DR UCSC; uc008rww.1; mouse. DR CTD; 195814; -. DR MGI; MGI:2668443; Sdr16c5. DR eggNOG; COG1028; -. DR GeneTree; ENSGT00540000069900; -. DR HOVERGEN; HBG051352; -. DR InParanoid; Q7TQA3; -. DR KO; K15734; -. DR OMA; NFLDCPD; -. DR OrthoDB; EOG7Z3F50; -. DR TreeFam; TF312837; -. DR UniPathway; UPA00912; -. DR NextBio; 385284; -. DR PRO; PR:Q7TQA3; -. DR Bgee; Q7TQA3; -. DR Genevestigator; Q7TQA3; -. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004745; F:retinol dehydrogenase activity; IEA:UniProtKB-EC. DR GO; GO:0043616; P:keratinocyte proliferation; IEA:Ensembl. DR GO; GO:0042574; P:retinal metabolic process; IEA:Ensembl. DR GO; GO:0042572; P:retinol metabolic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR002198; DH_sc/Rdtase_SDR. DR InterPro; IPR002347; Glc/ribitol_DH. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Pfam; PF00106; adh_short; 1. DR PRINTS; PR00081; GDHRDH. DR PRINTS; PR00080; SDRFAMILY. PE 2: Evidence at transcript level; KW Complete proteome; Endoplasmic reticulum; Membrane; NAD; NADP; KW Oxidoreductase; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 309 Epidermal retinol dehydrogenase 2. FT /FTId=PRO_0000305974. FT TRANSMEM 11 31 Helical; (Potential). FT TRANSMEM 270 290 Helical; (Potential). FT NP_BIND 44 68 NAD or NADP (By similarity). FT ACT_SITE 190 190 Proton acceptor (By similarity). FT BINDING 177 177 Substrate (Potential). SQ SEQUENCE 309 AA; 34193 MW; C5DE4B63AB35A665 CRC64; MSQNLESVKN LLVFLGKSLL SVLEALLFHV ISKPRKNVAG EIVLITGAGS GLGRLLALQF ARLGAVLVLW DVNKEANDET HQLAREAGAA RVHAYTCDCS RREEVYRVAD QVKKEVGDVS ILINNAGIVT GRNFLDCPDD LMEKSFDVNF KAHLWMYKAF LPAMIANNHG HLVCISSSAG LIGVNGLSDY CASKFAALGF AESMFIETLA KKQWGIKTTI VCPFFIKTGM FEGCTTKCPT LLPILDPEYA VRKIIDAILQ EQLYLYMPKF LYFIVFLKSI LPIKTGILIA DYLGVFHMTE GFTGQKKKT // ID RDH7_MOUSE Reviewed; 316 AA. AC O88451; DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1998, sequence version 1. DT 19-MAR-2014, entry version 107. DE RecName: Full=Retinol dehydrogenase 7; DE EC=1.1.1.105; DE AltName: Full=Cis-retinol/3alpha-hydroxysterol short-chain dehydrogenase isozyme 2; DE AltName: Full=Cis-retinol/androgen dehydrogenase type 2; DE Short=CRAD-2; GN Name=Rdh7; Synonyms=Crad2; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY. RX PubMed=9651397; DOI=10.1074/jbc.273.28.17910; RA Su J., Chai X., Kahn B., Napoli J.L.; RT "cDNA cloning, tissue distribution, and substrate characteristics of a RT cis-retinol/3alpha-hydroxysterol short-chain dehydrogenase isozyme."; RL J. Biol. Chem. 273:17910-17916(1998). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=129/Ola; TISSUE=Liver; RX PubMed=10876094; DOI=10.1016/S0378-1119(00)00194-3; RA Tomita K., Sato M., Kajiwara K., Tanaka M., Tamiya G., Makino S., RA Tomizawa M., Mizutani A., Kuwano Y., Shiina T., Ishii H., Kimura M.; RT "Gene structure and promoter for Crad2 encoding mouse cis-retinol/3- RT hydroxysterol short-chain dehydrogenase isozyme."; RL Gene 251:175-186(2000). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Liver; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: Acts on androgens and retinols, i.e. has steroid 3- CC alpha- and 17-beta-dehydrogenase and cis/trans-retinol catalytic CC activities. CC -!- CATALYTIC ACTIVITY: All-trans-retinol-[cellular-retinol-binding- CC protein] + NAD(+) = all-trans-retinal-[cellular-retinol-binding- CC protein] + NADH. CC -!- PATHWAY: Cofactor metabolism; retinol metabolism. CC -!- SUBCELLULAR LOCATION: Microsome (By similarity). Endoplasmic CC reticulum (By similarity). CC -!- TISSUE SPECIFICITY: Highly expressed in liver. Also expressed in CC lung, eye, kidney, and brain. CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases CC (SDR) family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF056194; AAC40159.1; -; mRNA. DR EMBL; AB015165; BAB03717.1; -; mRNA. DR EMBL; AB032058; BAB03718.1; -; mRNA. DR EMBL; AB032057; BAB03719.1; -; Genomic_DNA. DR EMBL; BC024603; AAH24603.1; -; mRNA. DR EMBL; BC092255; AAH92255.1; -; mRNA. DR EMBL; BC093514; AAH93514.1; -; mRNA. DR RefSeq; NP_001144221.1; NM_001150749.1. DR RefSeq; NP_059501.1; NM_017473.4. DR UniGene; Mm.6696; -. DR ProteinModelPortal; O88451; -. DR SMR; O88451; 25-284. DR IntAct; O88451; 1. DR MINT; MINT-1862586; -. DR STRING; 10090.ENSMUSP00000039252; -. DR PhosphoSite; O88451; -. DR PaxDb; O88451; -. DR PRIDE; O88451; -. DR Ensembl; ENSMUST00000047199; ENSMUSP00000039252; ENSMUSG00000040134. DR GeneID; 54150; -. DR KEGG; mmu:54150; -. DR UCSC; uc007hkv.2; mouse. DR CTD; 54150; -. DR MGI; MGI:1860517; Rdh7. DR eggNOG; COG1028; -. DR GeneTree; ENSGT00620000087655; -. DR HOVERGEN; HBG005482; -. DR InParanoid; O88451; -. DR OMA; VQVASIC; -. DR OrthoDB; EOG7FXZZX; -. DR TreeFam; TF325617; -. DR BRENDA; 1.1.1.105; 3474. DR UniPathway; UPA00912; -. DR ChiTaRS; Rdh7; mouse. DR NextBio; 310969; -. DR PRO; PR:O88451; -. DR Bgee; O88451; -. DR CleanEx; MM_RDH7; -. DR Genevestigator; O88451; -. DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell. DR GO; GO:0003824; F:catalytic activity; ISS:MGI. DR GO; GO:0004745; F:retinol dehydrogenase activity; IEA:UniProtKB-EC. DR GO; GO:0042572; P:retinol metabolic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR002198; DH_sc/Rdtase_SDR. DR InterPro; IPR002347; Glc/ribitol_DH. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR020904; Sc_DH/Rdtase_CS. DR Pfam; PF00106; adh_short; 1. DR PRINTS; PR00081; GDHRDH. DR PRINTS; PR00080; SDRFAMILY. DR PROSITE; PS00061; ADH_SHORT; 1. PE 2: Evidence at transcript level; KW Complete proteome; Endoplasmic reticulum; Microsome; NAD; NADP; KW Oxidoreductase; Reference proteome. FT CHAIN 1 316 Retinol dehydrogenase 7. FT /FTId=PRO_0000054761. FT NP_BIND 33 57 NADP (By similarity). FT ACT_SITE 175 175 Proton acceptor (By similarity). FT BINDING 163 163 Substrate (By similarity). SQ SEQUENCE 316 AA; 35660 MW; 0BFB9A1C2DDE3C17 CRC64; MWLYLVALVG LWTLLRFFRE RQVVSHLQDK YVFITGCDSG FGNLLARQLD RRGMRVLAAC LTEKGAEQLR NKTSDRLETV ILDVTKTESI VAATQWVKER VGNRGLWGLV NNAGICVFAI NEWLKKEDFA NILDVNLLGM IEVTLSMLPL VRKARGRVVN ISSSMGRVSL CGGGYCISKY GVEAFSDSLR REISYFGVKV AIIEPGGFRT NVSNYERLSH SIEKLWDQTS SEVKEVYDKN FLDSYIKAIQ SLTDTCSDDL SVVTDCMEHA LTACHPRTRY SAGWDAKLFY LPLSYMPTFL VDAMLYWSSV KPAQAL // ID RDH12_MOUSE Reviewed; 316 AA. AC Q8BYK4; Q91WA5; Q9D1Y4; DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 19-FEB-2014, entry version 89. DE RecName: Full=Retinol dehydrogenase 12; DE EC=1.1.1.-; GN Name=Rdh12; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Spinal cord; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Retina; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: Exhibits an oxidoreductive catalytic activity towards CC retinoids. Most efficient as an NADPH-dependent retinal reductase. CC Displays high activity toward 9-cis and all-trans-retinol. Also CC involved in the metabolism of short-chain aldehydes. No steroid CC dehydrogenase activity detected. Might be the key enzyme in the CC formation of 11-cis-retinal from 11-cis-retinol during CC regeneration of the cone visual pigments (By similarity). CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases CC (SDR) family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK020927; BAB32258.1; -; mRNA. DR EMBL; AK039233; BAC30288.1; -; mRNA. DR EMBL; BC016204; AAH16204.1; -; mRNA. DR RefSeq; NP_084293.1; NM_030017.3. DR UniGene; Mm.274373; -. DR ProteinModelPortal; Q8BYK4; -. DR SMR; Q8BYK4; 40-310. DR PhosphoSite; Q8BYK4; -. DR PaxDb; Q8BYK4; -. DR PRIDE; Q8BYK4; -. DR Ensembl; ENSMUST00000021548; ENSMUSP00000021548; ENSMUSG00000021123. DR Ensembl; ENSMUST00000122227; ENSMUSP00000112543; ENSMUSG00000021123. DR GeneID; 77974; -. DR KEGG; mmu:77974; -. DR UCSC; uc007oac.1; mouse. DR CTD; 145226; -. DR MGI; MGI:1925224; Rdh12. DR eggNOG; COG1028; -. DR GeneTree; ENSGT00570000078988; -. DR HOVERGEN; HBG078800; -. DR InParanoid; Q8BYK4; -. DR KO; K11153; -. DR OMA; LGVNHLX; -. DR OrthoDB; EOG73Z2TK; -. DR TreeFam; TF105429; -. DR BRENDA; 1.1.1.105; 3474. DR NextBio; 347915; -. DR PRO; PR:Q8BYK4; -. DR ArrayExpress; Q8BYK4; -. DR Bgee; Q8BYK4; -. DR CleanEx; MM_RDH12; -. DR Genevestigator; Q8BYK4; -. DR GO; GO:0005622; C:intracellular; ISS:UniProtKB. DR GO; GO:0004745; F:retinol dehydrogenase activity; ISS:UniProtKB. DR GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW. DR GO; GO:0042572; P:retinol metabolic process; ISS:UniProtKB. DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR002198; DH_sc/Rdtase_SDR. DR InterPro; IPR002347; Glc/ribitol_DH. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Pfam; PF00106; adh_short; 1. DR PRINTS; PR00081; GDHRDH. DR PRINTS; PR00080; SDRFAMILY. PE 2: Evidence at transcript level; KW Complete proteome; NADP; Oxidoreductase; Reference proteome; KW Sensory transduction; Vision. FT CHAIN 1 316 Retinol dehydrogenase 12. FT /FTId=PRO_0000054767. FT NP_BIND 46 52 NADP (By similarity). FT ACT_SITE 200 200 Proton acceptor (By similarity). FT BINDING 175 175 Substrate (By similarity). FT CONFLICT 114 125 Missing (in Ref. 2; AAH16204). FT CONFLICT 120 120 H -> D (in Ref. 1; BAB32258). SQ SEQUENCE 316 AA; 35292 MW; CF5745B6710A6148 CRC64; MLFILVLLTS FLSILYLTAP SIRKFFAGGV CTTNVQIPGK VVVITGANTG IGKETARELA RRGARVYIAC RDVLKGESAA SEIRADTKNS QVLVRKLDLS DTKSIRAFAE RFLAEEKKLH ILINNAGVMM CPYSKTTDGF ETHFGVNHLG HFLLTYLLLE RLKESAPARV VNLSSIAHLI GKIRFHDLQG QKRYCSAFAY GHSKLANLLF TRELAKRLQG TGVTAYAVHP GVVLSEITRN SYLLCLLWRL FSPFFKSTSQ GAQTSLHCAL AEDLEPLSGK YFSDCKRMWV SSRARNKKTA ERLWNVSCEL LGIQWE // ID RDH13_MOUSE Reviewed; 334 AA. AC Q8CEE7; Q8CC07; DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 19-MAR-2014, entry version 93. DE RecName: Full=Retinol dehydrogenase 13; DE EC=1.1.1.-; GN Name=Rdh13; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Diencephalon, and Liver; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6; TISSUE=Eye; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: Does not exhibit retinol dehydrogenase (RDH) activity in CC vitro (By similarity). CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases CC (SDR) family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK028434; BAC25950.1; -; mRNA. DR EMBL; AK034180; BAC28618.1; -; mRNA. DR EMBL; BC082583; AAH82583.1; -; mRNA. DR RefSeq; NP_780581.1; NM_175372.4. DR RefSeq; XP_006539525.1; XM_006539462.1. DR UniGene; Mm.413106; -. DR ProteinModelPortal; Q8CEE7; -. DR SMR; Q8CEE7; 30-322. DR PhosphoSite; Q8CEE7; -. DR PaxDb; Q8CEE7; -. DR PRIDE; Q8CEE7; -. DR Ensembl; ENSMUST00000008579; ENSMUSP00000008579; ENSMUSG00000008435. DR Ensembl; ENSMUST00000119485; ENSMUSP00000113433; ENSMUSG00000008435. DR GeneID; 108841; -. DR KEGG; mmu:108841; -. DR UCSC; uc009exm.2; mouse. DR CTD; 112724; -. DR MGI; MGI:1918732; Rdh13. DR eggNOG; COG1028; -. DR GeneTree; ENSGT00570000078988; -. DR HOVERGEN; HBG078800; -. DR InParanoid; Q8CEE7; -. DR KO; K11161; -. DR OMA; RHTGLHQ; -. DR OrthoDB; EOG73Z2TK; -. DR TreeFam; TF105429; -. DR NextBio; 361381; -. DR PRO; PR:Q8CEE7; -. DR ArrayExpress; Q8CEE7; -. DR Bgee; Q8CEE7; -. DR CleanEx; MM_RDH13; -. DR Genevestigator; Q8CEE7; -. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW. DR GO; GO:0042462; P:eye photoreceptor cell development; IMP:MGI. DR GO; GO:0009644; P:response to high light intensity; IMP:MGI. DR GO; GO:0010842; P:retina layer formation; IMP:MGI. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR002198; DH_sc/Rdtase_SDR. DR InterPro; IPR002347; Glc/ribitol_DH. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR020904; Sc_DH/Rdtase_CS. DR Pfam; PF00106; adh_short; 1. DR PRINTS; PR00081; GDHRDH. DR PRINTS; PR00080; SDRFAMILY. DR PROSITE; PS00061; ADH_SHORT; 1. PE 2: Evidence at transcript level; KW Complete proteome; NADP; Oxidoreductase; Reference proteome. FT CHAIN 1 334 Retinol dehydrogenase 13. FT /FTId=PRO_0000054769. FT NP_BIND 45 51 NAD or NADP (By similarity). FT ACT_SITE 200 200 Proton acceptor (By similarity). FT BINDING 174 174 Substrate (By similarity). FT CONFLICT 114 148 Missing (in Ref. 1; BAC28618). SQ SEQUENCE 334 AA; 36464 MW; 4EBBCE1643C1FECE CRC64; MSRFLLPVSV VGTVIGGTVL LKDYVAGGAC PSKATIPGKT VIVTGANTGI GKQTALELAK RGGNVILACR DMEKCEVAAK DIRGETLNPR VRAERLDLAS LKSIREFARK VIKEEERVDI LVNNAAVMRC PHWTTEDGFE MQFGVNYLGH FLLTNLLLDK LKASAPSRII NLSSLAHVAG HIDFEDLNWQ MKKYDTKAAY CQSKLAVVLF TKELSHRLQG SGVTVNALHP GVARTELGRH TGMHNSAFSG FMLGPFFWLL FKSPQLAAQP STYLAVAEEL ENVSGKYFDG LREKAPSPEA EDEEVARRLW TESARLVGLA MAHGSPGRGH AIPR // ID RETST_MOUSE Reviewed; 609 AA. AC Q64FW2; Q149J8; Q3UNN9; Q78JX8; Q8VHE7; Q9CW85; DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 3. DT 19-MAR-2014, entry version 79. DE RecName: Full=All-trans-retinol 13,14-reductase; DE EC=1.3.99.23; DE AltName: Full=All-trans-13,14-dihydroretinol saturase; DE Short=RetSat; DE AltName: Full=PPAR-alpha-regulated and starvation-induced gene protein; DE Flags: Precursor; GN Name=Retsat; Synonyms=Ppsig; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=A/J; RX PubMed=11753649; DOI=10.1038/sj.onc.1204941; RA Wang Y., Hu L., Yao R., Wang M., Crist K.A., Grubbs C.J., RA Johanning G.L., Lubet R.A., You M.; RT "Altered gene expression profile in chemically induced rat mammary RT adenocarcinomas and its modulation by an aromatase inhibitor."; RL Oncogene 20:7710-7721(2001). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR RP LOCATION, AND TISSUE SPECIFICITY. RC STRAIN=C57BL/6; TISSUE=Retina; RX PubMed=15358783; DOI=10.1074/jbc.M409130200; RA Moise A.R., Kuksa V., Imanishi Y., Palczewski K.; RT "Identification of all-trans-retinol: all-trans-13,14-dihydroretinol RT saturase."; RL J. Biol. Chem. 279:50230-50242(2004). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], TISSUE SPECIFICITY, AND RP INDUCTION. RC STRAIN=129S6/SvEvTac, and SV/129; TISSUE=Liver, and Spleen; RX PubMed=18289917; DOI=10.1016/j.biocel.2008.01.006; RA Sun Y., Ng L., Lam W., Lo C.K., Chan P.T., Yuen Y.L., Wong P.F., RA Tsang D.S., Cheung W.T., Lee S.S.; RT "Identification and characterization of a novel mouse peroxisome RT proliferator-activated receptor alpha-regulated and starvation-induced RT gene, Ppsig."; RL Int. J. Biochem. Cell Biol. 40:1775-1791(2008). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C3H, and C57BL/6J; TISSUE=Brain, and Kidney; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SV/129; TISSUE=Liver; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Salivary gland; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: Retinol saturase carrying out the saturation of the 13- CC 14 double bond of all-trans-retinol to produce all-trans-13,14- CC dihydroretinol. Has activity toward all-trans-retinol as CC substrate. Does not use all-trans-retinoic acid nor 9-cis, 11-cis CC or 13-cis-retinol isomers as substrates. May play a role in the CC metabolism of vitamin A. CC -!- CATALYTIC ACTIVITY: All-trans-13,14-dihydroretinol + acceptor = CC all-trans-retinol + reduced acceptor. CC -!- COFACTOR: NAD, NADP, or FAD (By similarity). CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral CC membrane protein. CC -!- TISSUE SPECIFICITY: Predominantly expressed in the liver and CC kidney. Also expressed in intestine, white fat and brown fat. CC Weakly expressed in heart, skeletal muscle and testis and barely CC detected in the lung, brain and spleen. CC -!- INDUCTION: Up-regulated during starvation. CC -!- SIMILARITY: Belongs to the carotenoid/retinoid oxidoreductase CC family. CrtISO subfamily. CC -!- SEQUENCE CAUTION: CC Sequence=BAB22406.2; Type=Erroneous initiation; Note=Translation N-terminally extended; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF466400; AAL73986.1; -; Genomic_DNA. DR EMBL; AY704159; AAU25836.1; -; mRNA. DR EMBL; EF620363; ABS17600.1; -; mRNA. DR EMBL; EF620364; ABS17601.1; -; mRNA. DR EMBL; EF620365; ABS17602.1; -; mRNA. DR EMBL; EF620366; ABS17603.1; -; Genomic_DNA. DR EMBL; AK002851; BAB22406.2; ALT_INIT; mRNA. DR EMBL; AK144115; BAE25708.1; -; mRNA. DR EMBL; AC125039; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH466523; EDK98989.1; -; Genomic_DNA. DR EMBL; BC011203; AAH11203.2; -; mRNA. DR EMBL; BC117751; AAI17752.1; -; mRNA. DR RefSeq; NP_080435.3; NM_026159.4. DR UniGene; Mm.305108; -. DR ProteinModelPortal; Q64FW2; -. DR SMR; Q64FW2; 28-138, 295-365. DR PhosphoSite; Q64FW2; -. DR PaxDb; Q64FW2; -. DR PRIDE; Q64FW2; -. DR Ensembl; ENSMUST00000070597; ENSMUSP00000068568; ENSMUSG00000056666. DR GeneID; 67442; -. DR KEGG; mmu:67442; -. DR UCSC; uc009cix.1; mouse. DR CTD; 54884; -. DR MGI; MGI:1914692; Retsat. DR eggNOG; COG1233; -. DR GeneTree; ENSGT00390000017613; -. DR HOGENOM; HOG000233930; -. DR HOVERGEN; HBG079484; -. DR InParanoid; Q149J8; -. DR KO; K09516; -. DR OMA; GQDIFTC; -. DR OrthoDB; EOG74J97V; -. DR TreeFam; TF328375; -. DR BioCyc; MetaCyc:MONOMER-16797; -. DR BRENDA; 1.3.99.23; 3474. DR NextBio; 324578; -. DR PRO; PR:Q64FW2; -. DR ArrayExpress; Q64FW2; -. DR Bgee; Q64FW2; -. DR Genevestigator; Q64FW2; -. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:HGNC. DR GO; GO:0005640; C:nuclear outer membrane; IDA:HGNC. DR GO; GO:0051786; F:all-trans-retinol 13,14-reductase activity; IDA:HGNC. PE 1: Evidence at protein level; KW Complete proteome; Endoplasmic reticulum; FAD; Flavoprotein; Membrane; KW NAD; NADP; Oxidoreductase; Reference proteome; Signal. FT SIGNAL 1 25 Potential. FT CHAIN 26 609 All-trans-retinol 13,14-reductase. FT /FTId=PRO_0000225667. FT NP_BIND 69 97 FAD or NAD or NADP (Potential). FT CONFLICT 273 273 A -> T (in Ref. 1; AAL73986 and 4; FT BAE25708). FT CONFLICT 293 293 G -> R (in Ref. 1; AAL73986 and 4; FT BAE25708). FT CONFLICT 306 306 I -> V (in Ref. 7; AAH11203). FT CONFLICT 451 451 E -> D (in Ref. 4; BAE25708). FT CONFLICT 495 495 A -> V (in Ref. 4; BAB22406). SQ SEQUENCE 609 AA; 67334 MW; 7BC21825B8A4ABD2 CRC64; MWITALLLAV LLLVILHRVY VGLYAASSPN PFAEDVKRPP EPLVTDKEAR KKVLKQAFSV SRVPEKLDAV VIGSGIGGLA SAAVLAKAGK RVLVLEQHTK AGGCCHTFGE NGLEFDTGIH YIGRMREGNI GRFILDQITE GQLDWAPMAS PFDLMILEGP NGRKEFPMYS GRKEYIQGLK KKFPKEEAVI DKYMELVKVV ARGVSHAVLL KFLPLPLTQL LSKFGLLTRF SPFCRASTQS LAEVLQQLGA SRELQAVLSY IFPTYGVTPS HTAFSLHALL VDHYIQGAYY PRGGSSEIAF HTIPLIQRAG GAVLTRATVQ SVLLDSAGRA CGVSVKKGQE LVNIYCPVVI SNAGMFNTYQ HLLPETVRHL PDVKKQLAMV RPGLSMLSIF ICLKGTKEDL KLQSTNYYVY FDTDMDKAME RYVSMPKEKA PEHIPLLFIA FPSSKDPTWE ERFPDRSTMT ALVPMAFEWF EEWQEEPKGK RGVDYETLKN AFVEASMSVI MKLFPQLEGK VESVTGGSPL TNQYYLAAPR GATYGADHDL ARLHPHAMAS IRAQTPIPNL YLTGQDIFTC GLMGALQGAL LCSSAILKRN LYSDLQALGS KVKAQKKKM // ID RIR1_MOUSE Reviewed; 792 AA. AC P07742; Q91YM8; DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 2. DT 19-FEB-2014, entry version 126. DE RecName: Full=Ribonucleoside-diphosphate reductase large subunit; DE EC=1.17.4.1; DE AltName: Full=Ribonucleoside-diphosphate reductase subunit M1; DE AltName: Full=Ribonucleotide reductase large subunit; GN Name=Rrm1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=2581962; RA Caras I.W., Levinson B.B., Fabry M., Williams S.R., Martin D.W. Jr.; RT "Cloned mouse ribonucleotide reductase subunit M1 cDNA reveals amino RT acid sequence homology with Escherichia coli and herpesvirus RT ribonucleotide reductases."; RL J. Biol. Chem. 260:7015-7022(1985). RN [2] RP SEQUENCE REVISION. RA Caras I.W.; RL Submitted (AUG-1985) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J, and NOD; TISSUE=Embryo, Embryonic liver, and Thymus; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Mammary tumor; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP CATALYTIC ACTIVITY, AND SUBUNIT. RX PubMed=19176520; DOI=10.1074/jbc.M809338200; RA Avval F.Z., Holmgren A.; RT "Molecular mechanisms of thioredoxin and glutaredoxin as hydrogen RT donors for mammalian S phase ribonucleotide reductase."; RL J. Biol. Chem. 284:8233-8240(2009). CC -!- FUNCTION: Provides the precursors necessary for DNA synthesis. CC Catalyzes the biosynthesis of deoxyribonucleotides from the CC corresponding ribonucleotides. CC -!- CATALYTIC ACTIVITY: 2'-deoxyribonucleoside diphosphate + CC thioredoxin disulfide + H(2)O = ribonucleoside diphosphate + CC thioredoxin. CC -!- ENZYME REGULATION: Under complex allosteric control mediated by CC deoxynucleoside triphosphates and ATP binding to separate CC specificity and activation sites on the M1 subunit. The type of CC nucleotide bound at the specificity site determines substrate CC preference. It seems probable that ATP makes the enzyme reduce CDP CC and UDP, dGTP favors ADP reduction and dTTP favors GDP reduction. CC Stimulated by ATP and inhibited by dATP binding to the activity CC site (By similarity). CC -!- PATHWAY: Genetic information processing; DNA replication. CC -!- SUBUNIT: Heterodimer of a large and a small subunit. Interacts CC with RRM2B (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- MISCELLANEOUS: Two distinct regulatory sites have been defined: CC the specificity site, which controls substrate specificity, and CC the activity site which regulates overall catalytic activity. A CC substrate-binding catalytic site, located on M1, is formed only in CC the presence of the second subunit M2. CC -!- MISCELLANEOUS: The level of the enzyme activity is closely CC correlated with the growth rate of a cell and appears to vary with CC the cell cycle. CC -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase CC large chain family. CC -!- SIMILARITY: Contains 1 ATP-cone domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; K02927; AAA40061.1; -; mRNA. DR EMBL; AK088043; BAC40112.1; -; mRNA. DR EMBL; AK137075; BAE23230.1; -; mRNA. DR EMBL; AK168586; BAE40455.1; -; mRNA. DR EMBL; CH466531; EDL16602.1; -; Genomic_DNA. DR EMBL; BC016450; AAH16450.1; -; mRNA. DR PIR; A24050; A24050. DR RefSeq; NP_033129.2; NM_009103.3. DR UniGene; Mm.197486; -. DR UniGene; Mm.415177; -. DR ProteinModelPortal; P07742; -. DR SMR; P07742; 14-742. DR BioGrid; 203022; 3. DR IntAct; P07742; 1. DR MINT; MINT-4121992; -. DR BindingDB; P07742; -. DR ChEMBL; CHEMBL3739; -. DR PhosphoSite; P07742; -. DR PaxDb; P07742; -. DR PRIDE; P07742; -. DR Ensembl; ENSMUST00000033283; ENSMUSP00000033283; ENSMUSG00000030978. DR GeneID; 20133; -. DR KEGG; mmu:20133; -. DR UCSC; uc009irp.2; mouse. DR CTD; 6240; -. DR MGI; MGI:98180; Rrm1. DR eggNOG; COG0209; -. DR GeneTree; ENSGT00390000001372; -. DR HOGENOM; HOG000057035; -. DR HOVERGEN; HBG003447; -. DR InParanoid; Q91YM8; -. DR KO; K10807; -. DR OMA; KSHIQFY; -. DR OrthoDB; EOG7BGHK2; -. DR TreeFam; TF300578; -. DR UniPathway; UPA00326; -. DR NextBio; 297643; -. DR PRO; PR:P07742; -. DR Bgee; P07742; -. DR CleanEx; MM_RRM1; -. DR Genevestigator; P07742; -. DR GO; GO:0042995; C:cell projection; IEA:Ensembl. DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl. DR GO; GO:0005635; C:nuclear envelope; IEA:Ensembl. DR GO; GO:0005971; C:ribonucleoside-diphosphate reductase complex; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0017076; F:purine nucleotide binding; IDA:MGI. DR GO; GO:0004748; F:ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor; IDA:UniProtKB. DR GO; GO:0021846; P:cell proliferation in forebrain; IEA:Ensembl. DR GO; GO:0009263; P:deoxyribonucleotide biosynthetic process; IDA:UniProtKB. DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniPathway. DR GO; GO:0008584; P:male gonad development; IEA:Ensembl. DR GO; GO:0000278; P:mitotic cell cycle; IEA:Ensembl. DR GO; GO:0051290; P:protein heterotetramerization; IPI:UniProtKB. DR GO; GO:0006206; P:pyrimidine nucleobase metabolic process; IEA:Ensembl. DR GO; GO:0010212; P:response to ionizing radiation; IEA:Ensembl. DR GO; GO:0060041; P:retina development in camera-type eye; IEA:Ensembl. DR InterPro; IPR005144; ATP-cone. DR InterPro; IPR013346; NrdE_NrdA. DR InterPro; IPR000788; RNR_lg_C. DR InterPro; IPR013509; RNR_lsu_N. DR InterPro; IPR008926; RNR_R1-su_N. DR Pfam; PF03477; ATP-cone; 1. DR Pfam; PF02867; Ribonuc_red_lgC; 1. DR Pfam; PF00317; Ribonuc_red_lgN; 1. DR PRINTS; PR01183; RIBORDTASEM1. DR SUPFAM; SSF48168; SSF48168; 1. DR TIGRFAMs; TIGR02506; NrdE_NrdA; 1. DR PROSITE; PS51161; ATP_CONE; 1. DR PROSITE; PS00089; RIBORED_LARGE; 1. PE 1: Evidence at protein level; KW Acetylation; Allosteric enzyme; ATP-binding; Complete proteome; KW Cytoplasm; Disulfide bond; DNA replication; Nucleotide-binding; KW Oxidoreductase; Reference proteome. FT CHAIN 1 792 Ribonucleoside-diphosphate reductase FT large subunit. FT /FTId=PRO_0000187191. FT DOMAIN 1 92 ATP-cone. FT REGION 11 17 Allosteric activator binding (By FT similarity). FT REGION 217 218 Substrate binding (By similarity). FT REGION 285 288 Allosteric effector binding, determines FT substrate specificity (By similarity). FT REGION 427 431 Substrate binding (By similarity). FT REGION 603 607 Substrate binding (By similarity). FT ACT_SITE 427 427 Proton acceptor (By similarity). FT ACT_SITE 429 429 Cysteine radical intermediate (By FT similarity). FT ACT_SITE 431 431 Proton acceptor (By similarity). FT BINDING 5 5 Allosteric activator (By similarity). FT BINDING 53 53 Allosteric activator (By similarity). FT BINDING 88 88 Allosteric activator (By similarity). FT BINDING 247 247 Substrate; via amide nitrogen (By FT similarity). FT SITE 218 218 Important for hydrogen atom transfer (By FT similarity). FT SITE 226 226 Allosteric effector binding, determines FT substrate specificity (By similarity). FT SITE 256 256 Allosteric effector binding, determines FT substrate specificity (By similarity). FT SITE 444 444 Important for hydrogen atom transfer (By FT similarity). FT SITE 737 737 Important for electron transfer (By FT similarity). FT SITE 738 738 Important for electron transfer (By FT similarity). FT SITE 787 787 Interacts with thioredoxin/glutaredoxin FT (By similarity). FT SITE 790 790 Interacts with thioredoxin/glutaredoxin FT (By similarity). FT MOD_RES 17 17 N6-acetyllysine (By similarity). FT MOD_RES 376 376 N6-acetyllysine (By similarity). FT DISULFID 218 444 Redox-active (By similarity). FT CONFLICT 202 202 S -> P (in Ref. 1; AAA40061). SQ SEQUENCE 792 AA; 90210 MW; 051C6CE407D24C69 CRC64; MHVIKRDGRQ ERVMFDKITS RIQKLCYGLN MDFVDPAQIT MKVIQGLYSG VTTVELDTLA AETAATLTTK HPDYAILAAR IAVSNLHKET KKVFSDVMED LYNYINPHNG RHSPMVASST LDIVMANKDR LNSAIIYDRD FSYNYFGFKT LERSYLLKIN GKVAERPQHM LMRVSVGIHK EDIDAAIETY NLLSEKWFTH ASPTLFNAGT NRPQLSSCFL LSMKDDSIEG IYDTLKQCAL ISKSAGGIGV AVSCIRATGS YIAGTNGNSN GLVPMLRVYN NTARYVDQGG NKRPGAFAIY LEPWHLDIFE FLDLKKNTGK EEQRARDLFF ALWIPDLFMK RVETNQDWSL MCPNECPGLD EVWGEEFEKL YESYEKQGRV RKVVKAQQLW YAIIESQTET GTPYMLYKDS CNRKSNQQNL GTIKCSNLCT EIVEYTSKDE VAVCNLASLA LNMYVTPEHT YDFEKLAEVT KVIVRNLNKI IDINYYPIPE AHLSNKRHRP IGIGVQGLAD AFILMRYPFE SPEAQLLNKQ IFETIYYGAL EASCELAKEY GPYETYEGSP VSKGILQYDM WNVAPTDLWD WKPLKEKIAK YGIRNSLLIA PMPTASTAQI LGNNESIEPY TSNIYTRRVL SGEFQIVNPH LLKDLTERGL WNEEMKNQII ACNGSIQSIP EIPDDLKQLY KTVWEISQKT VLKMAAERGA FIDQSQSLNI HIAEPNYGKL TSMHFYGWKQ GLKTGMYYLR TRPAANPIQF TLNKEKLKDK EKALKEEEEK ERNTAAMVCS LENREECLMC GS // ID RIR2B_MOUSE Reviewed; 351 AA. AC Q6PEE3; DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 19-FEB-2014, entry version 96. DE RecName: Full=Ribonucleoside-diphosphate reductase subunit M2 B; DE EC=1.17.4.1; DE AltName: Full=TP53-inducible ribonucleotide reductase M2 B; DE AltName: Full=p53-inducible ribonucleotide reductase small subunit 2-like protein; DE Short=p53R2; GN Name=Rrm2b; Synonyms=P53r2; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Thymus; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6; TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP FUNCTION, AND SUBUNIT. RX PubMed=11517226; DOI=10.1074/jbc.M106088200; RA Guittet O., Haakansson P., Voevodskaya N., Fridd S., Graeslund A., RA Arakawa H., Nakamura Y., Thelander L.; RT "Mammalian p53R2 protein forms an active ribonucleotide reductase in RT vitro with the R1 protein, which is expressed both in resting cells in RT response to DNA damage and in proliferating cells."; RL J. Biol. Chem. 276:40647-40651(2001). RN [4] RP FUNCTION, AND DISRUPTION PHENOTYPE. RX PubMed=12858174; DOI=10.1038/ng1212; RA Kimura T., Takeda S., Sagiya Y., Gotoh M., Nakamura Y., Arakawa H.; RT "Impaired function of p53R2 in Rrm2b-null mice causes severe renal RT failure through attenuation of dNTP pools."; RL Nat. Genet. 34:440-445(2003). CC -!- FUNCTION: Plays a pivotal role in cell survival by repairing CC damaged DNA in a p53/TP53-dependent manner. Supplies CC deoxyribonucleotides for DNA repair in cells arrested at G1 or G2. CC Contains an iron-tyrosyl free radical center required for CC catalysis. Forms an active ribonucleotide reductase (RNR) complex CC with RRM1 which is expressed both in resting and proliferating CC cells in response to DNA damage. CC -!- CATALYTIC ACTIVITY: 2'-deoxyribonucleoside diphosphate + CC thioredoxin disulfide + H(2)O = ribonucleoside diphosphate + CC thioredoxin. CC -!- COFACTOR: Binds 2 iron ions per subunit (By similarity). CC -!- PATHWAY: Genetic information processing; DNA replication. CC -!- SUBUNIT: Heterotetramer with large (RRM1) subunit. Interacts with CC p53/TP53. Interacts with RRM1 in response to DNA damage (By CC similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By CC similarity). Note=Translocates from cytoplasm to nucleus in CC response to DNA damage (By similarity). CC -!- DISRUPTION PHENOTYPE: Mice develop normally until they are weaned CC but from then on exhibit growth retardation and early mortality. CC Pathological examination indicates that multiple organs fail and CC that they die from severe renal failure by the age of 14 weeks. CC -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase CC small chain family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK138731; BAE23760.1; -; mRNA. DR EMBL; BC058103; AAH58103.1; -; mRNA. DR RefSeq; NP_955770.1; NM_199476.1. DR UniGene; Mm.24738; -. DR ProteinModelPortal; Q6PEE3; -. DR SMR; Q6PEE3; 28-314. DR STRING; 10090.ENSMUSP00000022901; -. DR PhosphoSite; Q6PEE3; -. DR PaxDb; Q6PEE3; -. DR PRIDE; Q6PEE3; -. DR Ensembl; ENSMUST00000022901; ENSMUSP00000022901; ENSMUSG00000022292. DR GeneID; 382985; -. DR KEGG; mmu:382985; -. DR UCSC; uc007vnl.1; mouse. DR CTD; 50484; -. DR MGI; MGI:2155865; Rrm2b. DR eggNOG; COG0208; -. DR GeneTree; ENSGT00390000013305; -. DR HOGENOM; HOG000255975; -. DR HOVERGEN; HBG001647; -. DR InParanoid; Q6PEE3; -. DR KO; K10808; -. DR OMA; KIFNTEA; -. DR OrthoDB; EOG7VMP5N; -. DR TreeFam; TF300465; -. DR UniPathway; UPA00326; -. DR NextBio; 403612; -. DR PRO; PR:Q6PEE3; -. DR ArrayExpress; Q6PEE3; -. DR Bgee; Q6PEE3; -. DR CleanEx; MM_RRM2B; -. DR Genevestigator; Q6PEE3; -. DR GO; GO:0005739; C:mitochondrion; IC:MGI. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004748; F:ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor; IDA:MGI. DR GO; GO:0009186; P:deoxyribonucleoside diphosphate metabolic process; IEA:InterPro. DR GO; GO:0009200; P:deoxyribonucleoside triphosphate metabolic process; IMP:MGI. DR GO; GO:0009263; P:deoxyribonucleotide biosynthetic process; IDA:MGI. DR GO; GO:0006281; P:DNA repair; IMP:MGI. DR GO; GO:0001822; P:kidney development; IMP:MGI. DR GO; GO:0006264; P:mitochondrial DNA replication; IMP:MGI. DR GO; GO:1902254; P:negative regulation of intrinsic apoptotic signaling pathway by p53 class mediator; IMP:MGI. DR GO; GO:0003014; P:renal system process; IMP:MGI. DR GO; GO:0006979; P:response to oxidative stress; IMP:MGI. DR Gene3D; 1.10.620.20; -; 1. DR InterPro; IPR009078; Ferritin-like_SF. DR InterPro; IPR012348; RNR-rel. DR InterPro; IPR000358; RNR_small. DR PANTHER; PTHR23409; PTHR23409; 1. DR Pfam; PF00268; Ribonuc_red_sm; 1. DR SUPFAM; SSF47240; SSF47240; 1. DR PROSITE; PS00368; RIBORED_SMALL; 1. PE 1: Evidence at protein level; KW Complete proteome; Cytoplasm; DNA damage; DNA repair; DNA replication; KW Iron; Metal-binding; Nucleus; Oxidoreductase; Reference proteome. FT CHAIN 1 351 Ribonucleoside-diphosphate reductase FT subunit M2 B. FT /FTId=PRO_0000228152. FT ACT_SITE 138 138 By similarity. FT METAL 100 100 Iron 1 (By similarity). FT METAL 131 131 Iron 1 (By similarity). FT METAL 131 131 Iron 2 (By similarity). FT METAL 134 134 Iron 1 (By similarity). FT METAL 194 194 Iron 2 (By similarity). FT METAL 228 228 Iron 2 (By similarity). FT METAL 231 231 Iron 2 (By similarity). SQ SEQUENCE 351 AA; 40804 MW; 4E1259233C9CC8A9 CRC64; MGDPERPEAA RPEKGEQLCS ETEENVVRSN EEPLLRKSSR RFVIFPIQYP DIWRMYKQAQ ASFWTAEEVD LSKDLPHWNK LKSDEKYFIS HILAFFAASD GIVNENLVER FSQEVQVPEA RCFYGFQILI ENVHSEMYSL LIDTYIRDPK KREFLFNAIE TMPYVKKKAD WALRWIADRK STFGERVVAF AAVEGIFFSG SFAAIFWLKK RGLMPGLTFS NELISRDEGL HCDFACLMFQ YLVNKPSEDR VREIIADAVQ IEQEFLTEAL PVGLIGMNCV LMKQYIEFVA DRLLGELGFS KIFQAENPFD FMENISLEGK TNFFEKRVSE YQRFAVMAET TDNVFTLDAD F // ID RIR2_MOUSE Reviewed; 390 AA. AC P11157; Q3UI23; Q542E2; DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1989, sequence version 1. DT 19-MAR-2014, entry version 144. DE RecName: Full=Ribonucleoside-diphosphate reductase subunit M2; DE EC=1.17.4.1; DE AltName: Full=Ribonucleotide reductase small chain; DE AltName: Full=Ribonucleotide reductase small subunit; GN Name=Rrm2; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=3025593; RA Thelander L., Berg P.; RT "Isolation and characterization of expressible cDNA clones encoding RT the M1 and M2 subunits of mouse ribonucleotide reductase."; RL Mol. Cell. Biol. 6:3433-3442(1986). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=2684652; RA Thelander M., Thelander L.; RT "Molecular cloning and expression of the functional gene encoding the RT M2 subunit of mouse ribonucleotide reductase: a new dominant marker RT gene."; RL EMBO J. 8:2475-2479(1989). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J, DBA/2, and NOD; RC TISSUE=Eye, Kidney, Liver, and Thymus; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6; TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=17242355; DOI=10.1073/pnas.0609836104; RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; RT "Large-scale phosphorylation analysis of mouse liver."; RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic fibroblast; RX PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200; RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.; RT "Large scale localization of protein phosphorylation by use of RT electron capture dissociation mass spectrometry."; RL Mol. Cell. Proteomics 8:904-912(2009). RN [7] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 65-352. RX PubMed=8876648; DOI=10.1006/jmbi.1996.0546; RA Kauppi B., Nielsen B.B., Ramaswamy S., Larsen I.K., Thelander M., RA Thelander L., Eklund H.; RT "The three-dimensional structure of mammalian ribonucleotide reductase RT protein R2 reveals a more-accessible iron-radical site than RT Escherichia coli R2."; RL J. Mol. Biol. 262:706-720(1996). RN [8] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 65-352. RX PubMed=12087093; DOI=10.1074/jbc.M203358200; RA Strand K.R., Karlsen S., Andersson K.K.; RT "Cobalt substitution of mouse R2 ribonucleotide reductase as a model RT for the reactive diferrous state. Spectroscopic and structural RT evidence for a ferromagnetically coupled dinuclear cobalt cluster."; RL J. Biol. Chem. 277:34229-34238(2002). RN [9] RP STRUCTURE BY NMR OF 384-390. RX PubMed=7583667; DOI=10.1038/nsb1195-951; RA Fisher A.L., Laub P.B., Cooperman B.S.; RT "NMR structure of an inhibitory R2 C-terminal peptide bound to mouse RT ribonucleotide reductase R1 subunit."; RL Nat. Struct. Biol. 2:951-955(1995). CC -!- FUNCTION: Provides the precursors necessary for DNA synthesis. CC Catalyzes the biosynthesis of deoxyribonucleotides from the CC corresponding ribonucleotides. Inhibits Wnt signaling (By CC similarity). CC -!- CATALYTIC ACTIVITY: 2'-deoxyribonucleoside diphosphate + CC thioredoxin disulfide + H(2)O = ribonucleoside diphosphate + CC thioredoxin. CC -!- COFACTOR: Binds 2 iron ions per subunit. CC -!- PATHWAY: Genetic information processing; DNA replication. CC -!- SUBUNIT: Heterodimer of a large and a small subunit. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- PTM: Phosphorylation on Ser-20 relieves the inhibitory effect on CC Wnt signaling (By similarity). CC -!- MISCELLANEOUS: Two distinct regulatory sites have been defined: CC the specificity site, which controls substrate specificity, and CC the activity site which regulates overall catalytic activity. A CC substrate-binding catalytic site, located on M1, is formed only in CC the presence of the second subunit M2. CC -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase CC small chain family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M14223; AAA40062.1; -; mRNA. DR EMBL; X15666; CAA33707.1; -; Genomic_DNA. DR EMBL; AK088907; BAC40647.1; -; mRNA. DR EMBL; AK142027; BAE24918.1; -; mRNA. DR EMBL; AK147111; BAE27683.1; -; mRNA. DR EMBL; AK161643; BAE36508.1; -; mRNA. DR EMBL; AK167078; BAE39238.1; -; mRNA. DR EMBL; AK167204; BAE39331.1; -; mRNA. DR EMBL; AK168205; BAE40165.1; -; mRNA. DR EMBL; AK168994; BAE40793.1; -; mRNA. DR EMBL; BC085136; AAH85136.1; -; mRNA. DR PIR; S06735; S06735. DR RefSeq; NP_033130.1; NM_009104.2. DR UniGene; Mm.471826; -. DR UniGene; Mm.99; -. DR PDB; 1AFT; NMR; -; A=384-390. DR PDB; 1H0N; X-ray; 2.40 A; A=1-390. DR PDB; 1H0O; X-ray; 2.20 A; A=1-390. DR PDB; 1W68; X-ray; 2.20 A; A=1-390. DR PDB; 1W69; X-ray; 2.20 A; A=1-390. DR PDB; 1XSM; X-ray; 2.30 A; A=1-390. DR PDBsum; 1AFT; -. DR PDBsum; 1H0N; -. DR PDBsum; 1H0O; -. DR PDBsum; 1W68; -. DR PDBsum; 1W69; -. DR PDBsum; 1XSM; -. DR DisProt; DP00462; -. DR ProteinModelPortal; P11157; -. DR SMR; P11157; 8-353. DR BioGrid; 203023; 4. DR IntAct; P11157; 1. DR MINT; MINT-1605522; -. DR BindingDB; P11157; -. DR ChEMBL; CHEMBL3527; -. DR PhosphoSite; P11157; -. DR PaxDb; P11157; -. DR PRIDE; P11157; -. DR Ensembl; ENSMUST00000020980; ENSMUSP00000020980; ENSMUSG00000020649. DR GeneID; 20135; -. DR KEGG; mmu:20135; -. DR UCSC; uc007ner.2; mouse. DR CTD; 6241; -. DR MGI; MGI:98181; Rrm2. DR eggNOG; COG0208; -. DR GeneTree; ENSGT00390000013305; -. DR HOGENOM; HOG000255975; -. DR HOVERGEN; HBG001647; -. DR InParanoid; P11157; -. DR KO; K10808; -. DR OMA; GMPEIEY; -. DR OrthoDB; EOG7VMP5N; -. DR TreeFam; TF300465; -. DR BRENDA; 1.17.4.1; 3474. DR UniPathway; UPA00326; -. DR ChiTaRS; RRM2; mouse. DR EvolutionaryTrace; P11157; -. DR NextBio; 297647; -. DR PRO; PR:P11157; -. DR ArrayExpress; P11157; -. DR Bgee; P11157; -. DR CleanEx; MM_RRM2; -. DR Genevestigator; P11157; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004748; F:ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor; IDA:UniProtKB. DR GO; GO:0009186; P:deoxyribonucleoside diphosphate metabolic process; IEA:InterPro. DR GO; GO:0009263; P:deoxyribonucleotide biosynthetic process; IDA:UniProtKB. DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniPathway. DR GO; GO:0051290; P:protein heterotetramerization; IPI:UniProtKB. DR Gene3D; 1.10.620.20; -; 1. DR InterPro; IPR009078; Ferritin-like_SF. DR InterPro; IPR012348; RNR-rel. DR InterPro; IPR000358; RNR_small. DR PANTHER; PTHR23409; PTHR23409; 1. DR Pfam; PF00268; Ribonuc_red_sm; 1. DR SUPFAM; SSF47240; SSF47240; 1. DR PROSITE; PS00368; RIBORED_SMALL; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Cytoplasm; DNA replication; Iron; KW Metal-binding; Oxidoreductase; Phosphoprotein; Reference proteome. FT CHAIN 1 390 Ribonucleoside-diphosphate reductase FT subunit M2. FT /FTId=PRO_0000190450. FT ACT_SITE 177 177 By similarity. FT METAL 139 139 Iron 1. FT METAL 170 170 Iron 1. FT METAL 170 170 Iron 2. FT METAL 173 173 Iron 1. FT METAL 233 233 Iron 2. FT METAL 267 267 Iron 1. FT METAL 267 267 Iron 2. FT METAL 270 270 Iron 2. FT MOD_RES 20 20 Phosphoserine. FT MOD_RES 33 33 Phosphothreonine (By similarity). FT HELIX 68 70 FT TURN 72 74 FT HELIX 78 81 FT STRAND 83 85 FT HELIX 89 100 FT HELIX 105 107 FT HELIX 113 119 FT HELIX 122 148 FT HELIX 150 153 FT HELIX 157 184 FT HELIX 188 195 FT HELIX 197 200 FT HELIX 202 216 FT STRAND 218 220 FT HELIX 222 249 FT HELIX 254 279 FT HELIX 287 306 FT HELIX 311 314 FT HELIX 318 335 FT HELIX 349 351 FT TURN 386 388 SQ SEQUENCE 390 AA; 45096 MW; AC7ACC4FAF8A4A2F CRC64; MLSVRTPLAT IADQQQLQLS PLKRLTLADK ENTPPTLSST RVLASKAARR IFQDSAELES KAPTNPSVED EPLLRENPRR FVVFPIEYHD IWQMYKKAEA SFWTAEEVDL SKDIQHWEAL KPDERHFISH VLAFFAASDG IVNENLVERF SQEVQVTEAR CFYGFQIAME NIHSEMYSLL IDTYIKDPKE REYLFNAIET MPCVKKKADW ALRWIGDKEA TYGERVVAFA AVEGIFFSGS FASIFWLKKR GLMPGLTFSN ELISRDEGLH CDFACLMFKH LVHKPAEQRV REIITNAVRI EQEFLTEALP VKLIGMNCTL MKQYIEFVAD RLMLELGFNK IFRVENPFDF MENISLEGKT NFFEKRVGEY QRMGVMSNST ENSFTLDADF // ID RNLS_MOUSE Reviewed; 342 AA. AC A7RDN6; Q3TD88; Q80W75; DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot. DT 16-JUN-2009, sequence version 2. DT 19-MAR-2014, entry version 46. DE RecName: Full=Renalase; DE EC=1.4.-.-; DE AltName: Full=Monoamine oxidase-C; DE Short=MAO-C; DE Short=mMAO-C; DE Flags: Precursor; GN Name=Rnls; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, AND RP TISSUE SPECIFICITY. RC STRAIN=Kunming; TISSUE=Kidney; RX PubMed=17846919; DOI=10.1007/s11033-007-9131-1; RA Wang J., Qi S., Cheng W., Li L., Wang F., Li Y.-Z., Zhang S.-P.; RT "Identification, expression and tissue distribution of a renalase RT homologue from mouse."; RL Mol. Biol. Rep. 35:613-620(2008). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC STRAIN=NOD; TISSUE=Dendritic cell; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Testis; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: Probable FAD-dependent amine oxidase secreted by the CC kidney, which circulates in blood and modulates cardiac function CC and systemic blood pressure. Degrades catecholamines such as CC dopamine, norepinephrine and epinephrine in vitro. Lowers blood CC pressure in vivo by decreasing cardiac contractility and heart CC rate and preventing a compensatory increase in peripheral vascular CC tone, suggesting a causal link to the increased plasma CC catecholamine and heightened cardiovascular risk. High CC concentrations of catecholamines activate plasma renalase and CC promotes its secretion and synthesis (By similarity). CC -!- COFACTOR: FAD (By similarity). CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=A7RDN6-1; Sequence=Displayed; CC Name=2; CC IsoId=A7RDN6-2; Sequence=VSP_053114; CC Note=No experimental confirmation available; CC -!- TISSUE SPECIFICITY: Expressed predominantly in kidney and testis CC with lower levels in liver, heart and embryo and weak expression CC in brain and skeletal muscle. CC -!- SIMILARITY: Belongs to the renalase family. CC -!- SEQUENCE CAUTION: CC Sequence=AAH52355.2; Type=Erroneous termination; Positions=33; Note=Translated as Trp; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DQ788834; ABG82016.1; -; mRNA. DR EMBL; AK170321; BAE41716.1; -; mRNA. DR EMBL; BC052355; AAH52355.2; ALT_SEQ; mRNA. DR RefSeq; NP_001139814.2; NM_001146342.2. DR RefSeq; NP_001161290.1; NM_001167818.1. DR UniGene; Mm.204591; -. DR ProteinModelPortal; A7RDN6; -. DR SMR; A7RDN6; 1-341. DR PhosphoSite; A7RDN6; -. DR PaxDb; A7RDN6; -. DR PRIDE; A7RDN6; -. DR Ensembl; ENSMUST00000096114; ENSMUSP00000093825; ENSMUSG00000071573. DR GeneID; 67795; -. DR KEGG; mmu:67795; -. DR UCSC; uc008hft.2; mouse. [A7RDN6-1] DR CTD; 55328; -. DR MGI; MGI:1915045; Rnls. DR eggNOG; NOG74071; -. DR GeneTree; ENSGT00390000016052; -. DR HOGENOM; HOG000007721; -. DR InParanoid; Q80W75; -. DR OrthoDB; EOG747PJ6; -. DR TreeFam; TF332799; -. DR NextBio; 325581; -. DR PRO; PR:A7RDN6; -. DR ArrayExpress; A7RDN6; -. DR Bgee; A7RDN6; -. DR Genevestigator; A7RDN6; -. DR GO; GO:0005615; C:extracellular space; IEA:Ensembl. DR GO; GO:0016491; F:oxidoreductase activity; IDA:MGI. DR GO; GO:0003214; P:cardiac left ventricle morphogenesis; IMP:MGI. DR GO; GO:0042417; P:dopamine metabolic process; IMP:MGI. DR GO; GO:0042414; P:epinephrine metabolic process; IMP:MGI. DR GO; GO:0060047; P:heart contraction; IMP:MGI. DR GO; GO:0042415; P:norepinephrine metabolic process; IMP:MGI. DR GO; GO:0055062; P:phosphate ion homeostasis; IMP:MGI. DR GO; GO:0003073; P:regulation of systemic arterial blood pressure; IMP:MGI. DR GO; GO:0071871; P:response to epinephrine; IEA:Ensembl. DR GO; GO:0002931; P:response to ischemia; IEA:Ensembl. DR GO; GO:0071873; P:response to norepinephrine; IMP:MGI. DR GO; GO:1902074; P:response to salt; IEA:Ensembl. DR InterPro; IPR002937; Amino_oxidase. DR Pfam; PF01593; Amino_oxidase; 1. PE 2: Evidence at transcript level; KW Alternative splicing; Complete proteome; FAD; Flavoprotein; KW Oxidoreductase; Reference proteome; Secreted; Signal. FT SIGNAL 1 17 Potential. FT CHAIN 18 342 Renalase. FT /FTId=PRO_0000376858. FT REGION 61 62 FAD-binding (By similarity). FT BINDING 12 12 FAD (By similarity). FT BINDING 42 42 FAD (By similarity). FT VAR_SEQ 41 123 Missing (in isoform 2). FT /FTId=VSP_053114. FT CONFLICT 31 31 G -> A (in Ref. 1; ABG82016 and 2; FT BAE41716). FT CONFLICT 36 36 G -> A (in Ref. 1; ABG82016 and 2; FT BAE41716). FT CONFLICT 138 138 K -> E (in Ref. 2; BAE41716). SQ SEQUENCE 342 AA; 37597 MW; 0445A137C6E1F981 CRC64; MSRVLVVGAG LTGSLCAALL RKEITAPLYL GLWDKGGDIG GRMITASSPH NPRCTADLGA QYITCSPHYV KEHQNFYEEL LAHGILKPLT SPIEGMKGKE GDCNFVAPQG FSSVIKYYLK KSGAEVSLKH CVTQIHLKDN KWEVSTDTGS AEQFDLVILT MPAPQILELQ GDIVNLISER QREQLKSVSY SSRYALGLFY EVGMKIGVPW SCRYLSSHPC ICFISIDNKK RNIESSECGP SVVIQTTVPF GVQHLEASEA DVQKLMIQQL ETILPGLPQP VATICHKWTY SQVTSSVSDR PGQMTLHLKP FLVCGGDGFT HSNFNGCISS ALSVMKVLKR YI // ID RSAD1_MOUSE Reviewed; 442 AA. AC Q5SUV1; B2RTE1; Q6PHM8; DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot. DT 21-DEC-2004, sequence version 1. DT 19-FEB-2014, entry version 69. DE RecName: Full=Radical S-adenosyl methionine domain-containing protein 1, mitochondrial; DE EC=1.3.99.-; DE AltName: Full=Oxygen-independent coproporphyrinogen-III oxidase-like protein RSAD1; DE Flags: Precursor; GN Name=Rsad1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6; TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: May be involved in porphyrin cofactor biosynthesis (By CC similarity). CC -!- COFACTOR: Binds 1 4Fe-4S cluster. The cluster is coordinated with CC 3 cysteines and an exchangeable S-adenosyl-L-methionine CC (Potential). CC -!- SUBCELLULAR LOCATION: Mitochondrion (Potential). CC -!- SIMILARITY: Belongs to the anaerobic coproporphyrinogen-III CC oxidase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AL645809; CAI25588.1; -; Genomic_DNA. DR EMBL; BC056485; AAH56485.1; -; mRNA. DR EMBL; BC139274; AAI39275.1; -; mRNA. DR EMBL; BC139276; AAI39277.1; -; mRNA. DR RefSeq; NP_001013399.1; NM_001013381.2. DR UniGene; Mm.342275; -. DR ProteinModelPortal; Q5SUV1; -. DR SMR; Q5SUV1; 41-279. DR STRING; 10090.ENSMUSP00000037361; -. DR PRIDE; Q5SUV1; -. DR Ensembl; ENSMUST00000040487; ENSMUSP00000037361; ENSMUSG00000039096. DR GeneID; 237926; -. DR KEGG; mmu:237926; -. DR UCSC; uc007kza.2; mouse. DR CTD; 55316; -. DR MGI; MGI:3039628; Rsad1. DR eggNOG; COG0635; -. DR GeneTree; ENSGT00390000011216; -. DR HOGENOM; HOG000015381; -. DR HOVERGEN; HBG108421; -. DR InParanoid; B2RTE1; -. DR OMA; WLGQLQE; -. DR OrthoDB; EOG7TJ3JG; -. DR TreeFam; TF332416; -. DR NextBio; 383574; -. DR PRO; PR:Q5SUV1; -. DR Bgee; Q5SUV1; -. DR CleanEx; MM_RSAD1; -. DR Genevestigator; Q5SUV1; -. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0004109; F:coproporphyrinogen oxidase activity; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006779; P:porphyrin-containing compound biosynthetic process; IEA:UniProtKB-KW. DR Gene3D; 3.80.30.20; -; 1. DR InterPro; IPR004559; Coprogen_oxidase_HemN-rel. DR InterPro; IPR006638; Elp3/MiaB/NifB. DR InterPro; IPR010723; HemN_C_dom. DR InterPro; IPR007197; rSAM. DR InterPro; IPR023404; rSAM_horseshoe. DR Pfam; PF06969; HemN_C; 1. DR Pfam; PF04055; Radical_SAM; 1. DR SMART; SM00729; Elp3; 1. DR TIGRFAMs; TIGR00539; hemN_rel; 1. PE 2: Evidence at transcript level; KW 4Fe-4S; Complete proteome; Iron; Iron-sulfur; Metal-binding; KW Mitochondrion; Oxidoreductase; Porphyrin biosynthesis; KW Reference proteome; S-adenosyl-L-methionine; Transit peptide. FT TRANSIT 1 17 Mitochondrion (Potential). FT CHAIN 18 442 Radical S-adenosyl methionine domain- FT containing protein 1, mitochondrial. FT /FTId=PRO_0000284610. FT REGION 99 100 S-adenosyl-L-methionine 2 binding (By FT similarity). FT METAL 49 49 Iron-sulfur (4Fe-4S-S-AdoMet) FT (Potential). FT METAL 53 53 Iron-sulfur (4Fe-4S-S-AdoMet) FT (Potential). FT METAL 56 56 Iron-sulfur (4Fe-4S-S-AdoMet) FT (Potential). FT BINDING 43 43 S-adenosyl-L-methionine 1 (By FT similarity). FT BINDING 55 55 S-adenosyl-L-methionine 2; via carbonyl FT oxygen (By similarity). FT BINDING 98 98 S-adenosyl-L-methionine 1; via amide FT nitrogen and carbonyl oxygen (By FT similarity). FT BINDING 131 131 S-adenosyl-L-methionine 1 (By FT similarity). FT BINDING 158 158 S-adenosyl-L-methionine 2 (By FT similarity). FT BINDING 170 170 S-adenosyl-L-methionine 2 (By FT similarity). FT BINDING 195 195 S-adenosyl-L-methionine 2 (By FT similarity). SQ SEQUENCE 442 AA; 48665 MW; 999B006D092D7FA3 CRC64; MVPSGVRTGR WVAAARAAQR RPRVDSLGQP PSPESASTRA ALYVHWPYCE KRCSYCNFNK YIPRGVEEGT VRNCLVTEAR TLLRLSGVQR VESVFFGGGT PSLASPHTVA AVLEAVAQEV YLPADSEVTL EANPTSAPGP RLAAFGAAGV NRLSIGLQSL DDAELQLLGR THSASDALRT LAEARLLFPG RVSVDLMLGL PAQKVEPWLQ QLQKLLYHCD DHLSLYQLTL ERGTSLFAQV QQGTLPAPDP DLAAEMYQEG RTVLRDAGFR QYEVSNFARN GALSTHNWTY WQCGQYLGIG PGAHGRFVPQ GTGGHTREAR IQTLEPDNWM KEVTLFGHGT RKCVRLGKLE LLEEVLAMGL RTDVGVTHQH WQQFEPQLTL WDVFGASKEV EELLAQGLLL LDYRGLRCSW EGLAVLDSLL LTLLPQLQEA WQHRPSSPVS GG // ID S16C6_MOUSE Reviewed; 316 AA. AC Q05A13; DT 13-OCT-2009, integrated into UniProtKB/Swiss-Prot. DT 14-NOV-2006, sequence version 1. DT 19-MAR-2014, entry version 63. DE RecName: Full=Short-chain dehydrogenase/reductase family 16C member 6; DE EC=1.1.1.-; GN Name=Sdr16c6; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases CC (SDR) family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AL807387; CAM18644.1; -; Genomic_DNA. DR EMBL; BX004841; CAM18644.1; JOINED; Genomic_DNA. DR EMBL; BX004841; CAM26881.1; -; Genomic_DNA. DR EMBL; AL807387; CAM26881.1; JOINED; Genomic_DNA. DR EMBL; CH466538; EDL05701.1; -; Genomic_DNA. DR EMBL; BC125450; AAI25451.1; -; mRNA. DR EMBL; BC125452; AAI25453.1; -; mRNA. DR RefSeq; NP_001074179.1; NM_001080710.2. DR UniGene; Mm.298546; -. DR ProteinModelPortal; Q05A13; -. DR SMR; Q05A13; 30-264. DR STRING; 10090.ENSMUSP00000104020; -. DR PRIDE; Q05A13; -. DR Ensembl; ENSMUST00000095151; ENSMUSP00000092773; ENSMUSG00000071019. DR Ensembl; ENSMUST00000108383; ENSMUSP00000104020; ENSMUSG00000071019. DR GeneID; 242286; -. DR KEGG; mmu:242286; -. DR UCSC; uc008rwy.1; mouse. DR CTD; 242286; -. DR MGI; MGI:2685269; Sdr16c6. DR eggNOG; COG1028; -. DR GeneTree; ENSGT00540000069900; -. DR InParanoid; Q05A13; -. DR OMA; LFLELTM; -. DR OrthoDB; EOG7Z3F50; -. DR TreeFam; TF312837; -. DR NextBio; 385288; -. DR PRO; PR:Q05A13; -. DR Bgee; Q05A13; -. DR Genevestigator; Q05A13; -. DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR002198; DH_sc/Rdtase_SDR. DR InterPro; IPR002347; Glc/ribitol_DH. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Pfam; PF00106; adh_short; 1. DR PIRSF; PIRSF000126; 11-beta-HSD1; 1. DR PRINTS; PR00081; GDHRDH. DR PRINTS; PR00080; SDRFAMILY. PE 2: Evidence at transcript level; KW Complete proteome; NAD; NADP; Oxidoreductase; Reference proteome. FT CHAIN 1 316 Short-chain dehydrogenase/reductase FT family 16C member 6. FT /FTId=PRO_0000386458. FT NP_BIND 40 64 NAD or NADP (By similarity). FT ACT_SITE 186 186 Proton acceptor (By similarity). FT BINDING 173 173 Substrate (Potential). SQ SEQUENCE 316 AA; 35158 MW; CEDB810B99CD39C9 CRC64; MNSVADTAIF FGKFLYYFLE SLVFKVIPKR KKDVSGEIVL ITGAGSGLGR LLAIHFASHG ATLVLWDINQ EGNMETCRLV KQKGDVKVFA YKCDCSSRIE VYRVADQVKE EVGDVTILIN NAGVVTGKSF LNTPDHLVEK SFLVNAISHF WTCKAFLPAM VKANHGHLVC ISSIAGLVGI NGLSDYSSSK FAAFGFAESL FLELTMIMKT KVKSTIVCPY FIKTGMFEGC TTKYPLLLPL LEQEYVAQKI FNAILEEQVY LIIPKFAYVA LFLKQIISPK MMIALGEYLG VDTCMTSFTG RVKAEELQME TKRKEQ // ID S5A2_MOUSE Reviewed; 254 AA. AC Q99N99; Q3UTZ9; DT 16-APR-2002, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 19-FEB-2014, entry version 91. DE RecName: Full=3-oxo-5-alpha-steroid 4-dehydrogenase 2; DE EC=1.3.1.22; DE AltName: Full=5 alpha-SR2; DE AltName: Full=SR type 2; DE AltName: Full=Steroid 5-alpha-reductase 2; DE Short=S5AR 2; GN Name=Srd5a2; Synonyms=5art2; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Kidney; RX PubMed=11884637; DOI=10.1093/nar/30.6.1387; RA Takeyama K., Kato S.; RT "Transcriptional regulation of the mouse steroid 5alpha-reductase type RT II gene by progesterone in brain."; RL Nucleic Acids Res. 30:1387-1393(2002). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Aorta, and Vein; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: Converts testosterone (T) into 5-alpha- CC dihydrotestosterone (DHT) and progesterone or corticosterone into CC their corresponding 5-alpha-3-oxosteroids. It plays a central role CC in sexual differentiation and androgen physiology (By similarity). CC -!- CATALYTIC ACTIVITY: A 3-oxo-5-alpha-steroid + NADP(+) = a 3-oxo- CC Delta(4)-steroid + NADPH. CC -!- SUBCELLULAR LOCATION: Microsome membrane; Multi-pass membrane CC protein (By similarity). Endoplasmic reticulum membrane; Multi- CC pass membrane protein (Potential). CC -!- SIMILARITY: Belongs to the steroid 5-alpha reductase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AB049456; BAB40179.1; -; mRNA. DR EMBL; AK138946; BAE23830.1; -; mRNA. DR EMBL; BC125510; AAI25511.1; -; mRNA. DR RefSeq; NP_444418.1; NM_053188.2. DR UniGene; Mm.38933; -. DR ProteinModelPortal; Q99N99; -. DR STRING; 10090.ENSMUSP00000048862; -. DR PhosphoSite; Q99N99; -. DR PRIDE; Q99N99; -. DR Ensembl; ENSMUST00000043458; ENSMUSP00000048862; ENSMUSG00000038541. DR GeneID; 94224; -. DR KEGG; mmu:94224; -. DR UCSC; uc008dnt.1; mouse. DR CTD; 6716; -. DR MGI; MGI:2150380; Srd5a2. DR eggNOG; NOG282706; -. DR GeneTree; ENSGT00510000046634; -. DR HOGENOM; HOG000050133; -. DR HOVERGEN; HBG003402; -. DR InParanoid; Q99N99; -. DR KO; K12344; -. DR OMA; GYGKYSE; -. DR OrthoDB; EOG75QR56; -. DR TreeFam; TF314668; -. DR NextBio; 352223; -. DR PRO; PR:Q99N99; -. DR ArrayExpress; Q99N99; -. DR Bgee; Q99N99; -. DR CleanEx; MM_SRD5A2; -. DR Genevestigator; Q99N99; -. DR GO; GO:0070852; C:cell body fiber; IEA:Ensembl. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl. DR GO; GO:0003865; F:3-oxo-5-alpha-steroid 4-dehydrogenase activity; IMP:MGI. DR GO; GO:0033218; F:amide binding; IEA:Ensembl. DR GO; GO:0047751; F:cholestenone 5-alpha-reductase activity; IEA:UniProtKB-EC. DR GO; GO:0006702; P:androgen biosynthetic process; IMP:MGI. DR GO; GO:0018879; P:biphenyl metabolic process; IEA:Ensembl. DR GO; GO:0060348; P:bone development; IEA:Ensembl. DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW. DR GO; GO:0018894; P:dibenzo-p-dioxin metabolic process; IEA:Ensembl. DR GO; GO:0030540; P:female genitalia development; IEA:Ensembl. DR GO; GO:0021766; P:hippocampus development; IEA:Ensembl. DR GO; GO:0021854; P:hypothalamus development; IEA:Ensembl. DR GO; GO:0030539; P:male genitalia development; IMP:MGI. DR GO; GO:0008584; P:male gonad development; IEA:Ensembl. DR GO; GO:0018963; P:phthalate metabolic process; IEA:Ensembl. DR GO; GO:0042493; P:response to drug; IEA:Ensembl. DR GO; GO:0032354; P:response to follicle-stimulating hormone; IEA:Ensembl. DR GO; GO:0031667; P:response to nutrient levels; IEA:Ensembl. DR GO; GO:0043434; P:response to peptide hormone; IEA:Ensembl. DR GO; GO:0033574; P:response to testosterone; IEA:Ensembl. DR GO; GO:0006706; P:steroid catabolic process; IEA:Ensembl. DR InterPro; IPR016636; 3-oxo-5-alpha-steroid_4-DH. DR InterPro; IPR001104; 3-oxo-5_a-steroid_4-DH_C. DR Pfam; PF02544; Steroid_dh; 1. DR PIRSF; PIRSF015596; 5_alpha-SR2; 1. DR PROSITE; PS50244; S5A_REDUCTASE; 1. PE 2: Evidence at transcript level; KW Complete proteome; Differentiation; Endoplasmic reticulum; Membrane; KW Microsome; NADP; Oxidoreductase; Reference proteome; KW Sexual differentiation; Transmembrane; Transmembrane helix. FT CHAIN 1 254 3-oxo-5-alpha-steroid 4-dehydrogenase 2. FT /FTId=PRO_0000213678. FT TRANSMEM 8 28 Helical; (Potential). FT TRANSMEM 72 92 Helical; (Potential). FT TRANSMEM 146 166 Helical; (Potential). FT TRANSMEM 206 226 Helical; (Potential). SQ SEQUENCE 254 AA; 28619 MW; 8D25019E8DC4DF47 CRC64; MPIVCHQVPV LAGSATLATM GTLILCFGKP ASYGKHSESV SSGVPLLPAR IAWFLQELPS FVVSVGMLAW QPRSLFGPPG NVLLGLFSAH YFHRTFIYSL LTRGRPLSAV IFLKATAFCI GNGLLQAYYL VYCAEYPEEW YTDMRFSVGV FFFILGMGIN IHSDCMLRQL RKPGEVIYRI PQGGLFTYVS GANFLGEIIE WMGYALATWS VPAFAFAFFT LCFLGMQAFY HHRFYLKMFK DYPKSRKALI PFIF // ID S5A1_MOUSE Reviewed; 255 AA. AC Q68FF9; Q505K7; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 05-FEB-2008, sequence version 2. DT 19-FEB-2014, entry version 72. DE RecName: Full=3-oxo-5-alpha-steroid 4-dehydrogenase 1; DE EC=1.3.1.22; DE AltName: Full=SR type 1; DE AltName: Full=Steroid 5-alpha-reductase 1; DE Short=S5AR 1; GN Name=Srd5a1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6, and FVB/N; TISSUE=Brain, and Liver; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: Converts testosterone into 5-alpha-dihydrotestosterone CC and progesterone or corticosterone into their corresponding 5- CC alpha-3-oxosteroids. It plays a central role in sexual CC differentiation and androgen physiology (By similarity). CC -!- CATALYTIC ACTIVITY: A 3-oxo-5-alpha-steroid + NADP(+) = a 3-oxo- CC Delta(4)-steroid + NADPH. CC -!- SUBCELLULAR LOCATION: Microsome membrane; Multi-pass membrane CC protein (By similarity). Endoplasmic reticulum membrane; Multi- CC pass membrane protein (Potential). CC -!- SIMILARITY: Belongs to the steroid 5-alpha reductase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BC079863; AAH79863.1; -; mRNA. DR EMBL; BC094503; AAH94503.1; -; mRNA. DR RefSeq; NP_780492.2; NM_175283.3. DR UniGene; Mm.451912; -. DR UniGene; Mm.483181; -. DR ProteinModelPortal; Q68FF9; -. DR PhosphoSite; Q68FF9; -. DR PaxDb; Q68FF9; -. DR PRIDE; Q68FF9; -. DR Ensembl; ENSMUST00000091514; ENSMUSP00000089097; ENSMUSG00000021594. DR GeneID; 78925; -. DR KEGG; mmu:78925; -. DR UCSC; uc007rck.1; mouse. DR CTD; 6715; -. DR MGI; MGI:98400; Srd5a1. DR eggNOG; NOG82739; -. DR GeneTree; ENSGT00510000046634; -. DR HOGENOM; HOG000050133; -. DR HOVERGEN; HBG003402; -. DR InParanoid; Q68FF9; -. DR KO; K12343; -. DR OrthoDB; EOG75QR56; -. DR TreeFam; TF314668; -. DR NextBio; 349772; -. DR PRO; PR:Q68FF9; -. DR Bgee; Q68FF9; -. DR CleanEx; MM_SRD5A1; -. DR Genevestigator; Q68FF9; -. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0003865; F:3-oxo-5-alpha-steroid 4-dehydrogenase activity; ISS:UniProtKB. DR GO; GO:0047751; F:cholestenone 5-alpha-reductase activity; IEA:UniProtKB-EC. DR GO; GO:0006702; P:androgen biosynthetic process; IMP:MGI. DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW. DR GO; GO:0007548; P:sex differentiation; IEA:UniProtKB-KW. DR InterPro; IPR016636; 3-oxo-5-alpha-steroid_4-DH. DR InterPro; IPR001104; 3-oxo-5_a-steroid_4-DH_C. DR Pfam; PF02544; Steroid_dh; 1. DR PIRSF; PIRSF015596; 5_alpha-SR2; 1. DR PROSITE; PS50244; S5A_REDUCTASE; 1. PE 2: Evidence at transcript level; KW Complete proteome; Differentiation; Endoplasmic reticulum; Membrane; KW Microsome; NADP; Oxidoreductase; Reference proteome; KW Sexual differentiation; Transmembrane; Transmembrane helix. FT CHAIN 1 255 3-oxo-5-alpha-steroid 4-dehydrogenase 1. FT /FTId=PRO_0000317711. FT TRANSMEM 6 26 Helical; (Potential). FT TRANSMEM 82 102 Helical; (Potential). FT TRANSMEM 107 127 Helical; (Potential). FT TRANSMEM 142 162 Helical; (Potential). FT TRANSMEM 205 225 Helical; (Potential). FT CONFLICT 7 7 C -> R (in Ref. 1; AAH79863). FT CONFLICT 142 142 V -> I (in Ref. 1; AAH94503). FT CONFLICT 176 176 E -> D (in Ref. 1; AAH94503). SQ SEQUENCE 255 AA; 29344 MW; 80A5624B25D46D1A CRC64; MELDELCLLD ALVYLEGFLA FVAFVGLQMV GSSYGRYSSQ WSGRRVPARP AWFLQELPSM AWPLYECIRP AAARLGNLPN RVLLAMFLIH YVQRTLVFPV LIRGGKPTLL FTFVLAFLFC TLNGYLQSRY LSQFAVYAED WVTHPCFLTG FALWLVGMVI NIHSDHILRN LRKPGETGYK IPRGGLFEYV SSANYFGELV EWCGFALASW SLQGVVFALF TLCALFTRAR QHHQWYLEKF EDYPKTRKIL IPFLL // ID SARDH_MOUSE Reviewed; 919 AA. AC Q99LB7; DT 13-SEP-2004, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 19-MAR-2014, entry version 92. DE RecName: Full=Sarcosine dehydrogenase, mitochondrial; DE Short=SarDH; DE EC=1.5.8.3; DE Flags: Precursor; GN Name=Sardh; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Mammary tumor; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [2] RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-38; LYS-174; LYS-278; RP LYS-378; LYS-392; LYS-535; LYS-803; LYS-885 AND LYS-905, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., RA Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). RN [3] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-174; LYS-560; LYS-776; RP LYS-803; LYS-885 AND LYS-905, AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23576753; DOI=10.1073/pnas.1302961110; RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., RA Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.; RT "Label-free quantitative proteomics of the lysine acetylome in RT mitochondria identifies substrates of SIRT3 in metabolic pathways."; RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013). CC -!- CATALYTIC ACTIVITY: Sarcosine + H(2)O + electron-transfer CC flavoprotein = glycine + formaldehyde + reduced electron-transfer CC flavoprotein. CC -!- COFACTOR: Binds 1 FAD covalently per monomer (By similarity). CC -!- PATHWAY: Amine and polyamine degradation; sarcosine degradation; CC formaldehyde and glycine from sarcosine: step 1/1. CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix (By similarity). CC -!- SIMILARITY: Belongs to the GcvT family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BC003456; AAH03456.1; -; mRNA. DR RefSeq; NP_619606.1; NM_138665.2. DR RefSeq; XP_006497851.1; XM_006497788.1. DR RefSeq; XP_006497852.1; XM_006497789.1. DR UniGene; Mm.278467; -. DR ProteinModelPortal; Q99LB7; -. DR SMR; Q99LB7; 66-917. DR BioGrid; 228656; 1. DR IntAct; Q99LB7; 3. DR MINT; MINT-1839313; -. DR PhosphoSite; Q99LB7; -. DR PaxDb; Q99LB7; -. DR PRIDE; Q99LB7; -. DR Ensembl; ENSMUST00000102886; ENSMUSP00000099950; ENSMUSG00000009614. DR GeneID; 192166; -. DR KEGG; mmu:192166; -. DR UCSC; uc008ixg.2; mouse. DR CTD; 1757; -. DR MGI; MGI:2183102; Sardh. DR eggNOG; COG0665; -. DR GeneTree; ENSGT00530000063120; -. DR HOGENOM; HOG000251716; -. DR HOVERGEN; HBG002326; -. DR InParanoid; Q99LB7; -. DR KO; K00314; -. DR OMA; AIWRNGQ; -. DR OrthoDB; EOG7W1533; -. DR TreeFam; TF314735; -. DR UniPathway; UPA00292; UER00398. DR NextBio; 371164; -. DR PRO; PR:Q99LB7; -. DR ArrayExpress; Q99LB7; -. DR Bgee; Q99LB7; -. DR CleanEx; MM_SARDH; -. DR Genevestigator; Q99LB7; -. DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell. DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB. DR GO; GO:0004047; F:aminomethyltransferase activity; IEA:InterPro. DR GO; GO:0008480; F:sarcosine dehydrogenase activity; IEA:UniProtKB-EC. DR GO; GO:0006546; P:glycine catabolic process; IEA:InterPro. DR GO; GO:0032259; P:methylation; IEA:GOC. DR Gene3D; 3.30.1360.120; -; 3. DR InterPro; IPR006076; FAD-dep_OxRdtase. DR InterPro; IPR013977; GCV_T_C. DR InterPro; IPR006222; GCV_T_N. DR InterPro; IPR027266; TrmE/GcvT_dom1. DR Pfam; PF01266; DAO; 1. DR Pfam; PF01571; GCV_T; 1. DR Pfam; PF08669; GCV_T_C; 1. PE 1: Evidence at protein level; KW Acetylation; Complete proteome; FAD; Flavoprotein; Mitochondrion; KW Oxidoreductase; Phosphoprotein; Reference proteome; Transit peptide. FT TRANSIT 1 22 Mitochondrion (Potential). FT CHAIN 23 919 Sarcosine dehydrogenase, mitochondrial. FT /FTId=PRO_0000010771. FT MOD_RES 38 38 N6-succinyllysine. FT MOD_RES 109 109 Tele-8alpha-FAD histidine (By FT similarity). FT MOD_RES 174 174 N6-acetyllysine; alternate. FT MOD_RES 174 174 N6-succinyllysine; alternate. FT MOD_RES 278 278 N6-succinyllysine. FT MOD_RES 378 378 N6-succinyllysine. FT MOD_RES 392 392 N6-succinyllysine. FT MOD_RES 535 535 N6-succinyllysine. FT MOD_RES 560 560 N6-acetyllysine. FT MOD_RES 776 776 N6-acetyllysine. FT MOD_RES 778 778 Phosphotyrosine (By similarity). FT MOD_RES 803 803 N6-acetyllysine; alternate. FT MOD_RES 803 803 N6-succinyllysine; alternate. FT MOD_RES 885 885 N6-acetyllysine; alternate. FT MOD_RES 885 885 N6-succinyllysine; alternate. FT MOD_RES 905 905 N6-acetyllysine; alternate. FT MOD_RES 905 905 N6-succinyllysine; alternate. SQ SEQUENCE 919 AA; 101682 MW; 4908ACB540C9D305 CRC64; MASLSRVLRV AATCPRGRAA WNLGLQPLAT EARPTTEKSV PYQRTLKEEA QGASVVPQGP SQPLPSTANV VVIGGGSLGC QTLYHLAKLG VGGAVLLERE RLTSGTTWHT AGLLWQLRPS DVEVELLAHT RQVVSRDLEE ETGLHTGWIQ NGGLFIASNQ QRLNEYKRLM SLGKAYGIES HVLSPAETKS LYPLMNVDDL YGTLYVPQDG TMDPAGTCTT LTRAAVARGA QVIENCAVTG IRVRTDDFGV RRVAAVETEH GSIQTPCVVN CAGVWASKVG RMAGVKVPLV AMHHAYVVTE RIEGIQNMPN VRDHDASVYL RLQGDALSVG GYEANPIFWE EVSDKFAFGL FDLDWDVFTQ HIEGAINRVP VLEKTGIKST VCGPESFTPD HKPLMGEAPE LRGFFLGCGF NSAGMMLGGG CGQELAHWIV HGRPEKDMYS YDIRRFHHSL TDHTRWIRER SHESYAKNYS VVFPHDEPLA GRNMRRDPLH EELLGQGCVF QERQGWERPG WFNPQETAQV LDYDYYGAYG NQAHKDYTYS RLLGDEYTFD FPPHHHMIQK ECLACRGAAA VFNMSYFGKF YLLGVDARKA ADWLFSADVN RPPGSTVYTC MLNQRGGTES DLTVSRLAPG TQASPLVPAF EGDCYYLAVG GAVAQHNWSH INTVLQDQEF RCQLMDSSED LGMLSIQGPA SRDILQDVLD ADLSNEAFPF STHQLVRAAG HLVRAIRLSF VGELGWELHV PRASCLPVYR AVMAAGARHG LVNAGYRAID SLSIEKGYRH WHADLRPDDS PLEAGLAFTC KLKTSVPFLG REALEKQRAT GLRRRLICLT VEEEVPMFGL EAIWRNGQVV GHVRRADFGF TVNKTIAYGY IRDPSGGPVS LDFVKNGEYA LERMGVTYAA QVHLKSPFDP DNKRVKGIY // ID SC5D_MOUSE Reviewed; 299 AA. AC O88822; Q8BGI0; DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot. DT 18-SEP-2013, sequence version 2. DT 19-MAR-2014, entry version 100. DE RecName: Full=Lathosterol oxidase; DE EC=1.14.21.6; DE AltName: Full=C-5 sterol desaturase; DE AltName: Full=Delta(7)-sterol 5-desaturase; DE AltName: Full=Lathosterol 5-desaturase; DE AltName: Full=Sterol-C5-desaturase; GN Name=Sc5d; Synonyms=Sc5dl; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=BALB/c; RX PubMed=10786622; DOI=10.1016/S0167-4781(99)00248-1; RA Nishi S., Nishino H., Ishibashi T.; RT "cDNA cloning of the mammalian sterol C5-desaturase and the expression RT in yeast mutant."; RL Biochim. Biophys. Acta 1490:106-108(2000). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Brain cortex; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). CC -!- FUNCTION: Catalyzes a dehydrogenation to introduce C5-6 double CC bond into lathosterol. CC -!- CATALYTIC ACTIVITY: 5-alpha-cholest-7-en-3-beta-ol + NAD(P)H + CC O(2) = cholesta-5,7-dien-3-beta-ol + NAD(P)(+) + 2 H(2)O. CC -!- COFACTOR: Iron (By similarity). CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass CC membrane protein (Probable). CC -!- DOMAIN: The histidine box domains may contain the active site CC and/or be involved in metal ion binding. CC -!- SIMILARITY: Belongs to the sterol desaturase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AB016248; BAA33730.1; -; mRNA. DR EMBL; AK043825; BAC31666.1; -; mRNA. DR EMBL; AK077670; BAC36944.1; -; mRNA. DR EMBL; AC160051; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; NP_766357.1; NM_172769.2. DR RefSeq; XP_006510316.1; XM_006510253.1. DR UniGene; Mm.32700; -. DR UniGene; Mm.392107; -. DR UniGene; Mm.470142; -. DR STRING; 10090.ENSMUSP00000057354; -. DR PhosphoSite; O88822; -. DR PRIDE; O88822; -. DR Ensembl; ENSMUST00000052725; ENSMUSP00000057354; ENSMUSG00000032018. DR Ensembl; ENSMUST00000169609; ENSMUSP00000130438; ENSMUSG00000032018. DR GeneID; 235293; -. DR KEGG; mmu:235293; -. DR UCSC; uc009par.1; mouse. DR CTD; 6309; -. DR MGI; MGI:1353611; Sc5d. DR eggNOG; COG3000; -. DR GeneTree; ENSGT00550000075101; -. DR HOGENOM; HOG000200579; -. DR HOVERGEN; HBG012628; -. DR InParanoid; O88822; -. DR KO; K00227; -. DR OMA; FFCATLS; -. DR OrthoDB; EOG7NSB2T; -. DR TreeFam; TF300797; -. DR BRENDA; 1.14.21.6; 3474. DR NextBio; 382567; -. DR PRO; PR:O88822; -. DR Genevestigator; O88822; -. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0000248; F:C-5 sterol desaturase activity; IEA:Ensembl. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0050046; F:lathosterol oxidase activity; IEA:UniProtKB-EC. DR GO; GO:0033490; P:cholesterol biosynthetic process via lathosterol; IEA:Ensembl. DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro. DR InterPro; IPR006694; Fatty_acid_hydroxylase. DR Pfam; PF04116; FA_hydroxylase; 1. PE 2: Evidence at transcript level; KW Complete proteome; Endoplasmic reticulum; Iron; Lipid biosynthesis; KW Lipid metabolism; Membrane; NAD; NADP; Oxidoreductase; Phosphoprotein; KW Reference proteome; Steroid biosynthesis; Steroid metabolism; KW Sterol biosynthesis; Sterol metabolism; Transmembrane; KW Transmembrane helix. FT CHAIN 1 299 Lathosterol oxidase. FT /FTId=PRO_0000117029. FT TRANSMEM 32 52 Helical; (Potential). FT TRANSMEM 79 99 Helical; (Potential). FT TRANSMEM 117 137 Helical; (Potential). FT TRANSMEM 186 206 Helical; (Potential). FT MOTIF 138 143 Histidine box-1. FT MOTIF 151 155 Histidine box-2. FT MOTIF 228 233 Histidine box-3. FT MOD_RES 253 253 Phosphoserine (By similarity). FT CONFLICT 136 136 W -> R (in Ref. 1; BAA33730). FT CONFLICT 291 291 G -> S (in Ref. 1; BAA33730). SQ SEQUENCE 299 AA; 35062 MW; 96F3AFF61F7ED707 CRC64; MDLVLSAADY YFFTPYVYPA TWPEDNIIRQ TISLLIVTNL GAYILYFFCA TLSYYFVYDH SLMKHPQFLK NQVSREIVFT VKSLPWISIP TVSLFLLELR GYSKLYDDIG DFPNGWIHLM VSVVSFLFFT DMLIYWIHRG LHHRLVYKRI HKPHHIWKIP TPFASHAFHP VDGFLQSLPY HIYPFVFPLH KVVYLGLYVL VNVWTISIHD GDFRVPQILR PFINGSAHHT DHHMFFDYNY GQYFTLWDRI GGSFKHPSSF EGKGPHSYVK NMTEKESNSF AENGCKGKKV GNGEFTKNK // ID SCPDL_MOUSE Reviewed; 429 AA. AC Q8R127; Q3TMB9; DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2002, sequence version 1. DT 19-MAR-2014, entry version 89. DE RecName: Full=Saccharopine dehydrogenase-like oxidoreductase; DE EC=1.-.-.-; GN Name=Sccpdh; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Cerebellum, Corpora quadrigemina, and Lung; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Liver; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- SIMILARITY: Belongs to the saccharopine dehydrogenase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK042919; BAC31405.1; -; mRNA. DR EMBL; AK046033; BAC32578.1; -; mRNA. DR EMBL; AK077695; BAC36962.1; -; mRNA. DR EMBL; AK082803; BAC38628.1; -; mRNA. DR EMBL; AK166018; BAE38523.1; -; mRNA. DR EMBL; BC025803; AAH25803.1; -; mRNA. DR RefSeq; NP_848768.1; NM_178653.3. DR UniGene; Mm.136458; -. DR UniGene; Mm.491204; -. DR ProteinModelPortal; Q8R127; -. DR SMR; Q8R127; 10-102. DR IntAct; Q8R127; 1. DR MINT; MINT-4118497; -. DR PhosphoSite; Q8R127; -. DR PaxDb; Q8R127; -. DR PRIDE; Q8R127; -. DR Ensembl; ENSMUST00000040538; ENSMUSP00000040956; ENSMUSG00000038936. DR GeneID; 109232; -. DR KEGG; mmu:109232; -. DR UCSC; uc007dvp.1; mouse. DR CTD; 51097; -. DR MGI; MGI:1924486; Sccpdh. DR eggNOG; COG3268; -. DR GeneTree; ENSGT00390000004799; -. DR HOGENOM; HOG000251397; -. DR HOVERGEN; HBG057028; -. DR InParanoid; Q8R127; -. DR OMA; MTFFGQG; -. DR OrthoDB; EOG7B31MZ; -. DR TreeFam; TF314904; -. DR NextBio; 361807; -. DR PRO; PR:Q8R127; -. DR ArrayExpress; Q8R127; -. DR Bgee; Q8R127; -. DR CleanEx; MM_SCCPDH; -. DR Genevestigator; Q8R127; -. DR GO; GO:0005811; C:lipid particle; IEA:Ensembl. DR GO; GO:0030496; C:midbody; IEA:Ensembl. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR005097; Saccharopine_DH/HSpermid_syn. DR Pfam; PF03435; Saccharop_dh; 1. PE 2: Evidence at transcript level; KW Acetylation; Complete proteome; Oxidoreductase; Reference proteome. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 429 Saccharopine dehydrogenase-like FT oxidoreductase. FT /FTId=PRO_0000212841. FT MOD_RES 2 2 N-acetylalanine (By similarity). SQ SEQUENCE 429 AA; 47129 MW; FCC63118BFCEE7E4 CRC64; MATEQRPFHL VVFGASGFTG QFVTEEVARE QIASEQSSRL PWAVAGRSKE KLQQVLEKAA QKLGRPSLSS EVGVIICDIS NPASLDEMAK QAKLVLNCVG PYRFYGEPVV KACIENGTSC IDICGEPQFL ELMHAKYHEK AAEKGVYIIG SSGFDSIPAD LGVLYTRNQM NGTLTAVESF LTINTGPEGL CIHDGTWKSA IYGFGDKGSL RKLRSVSCLK PVPIVGTKLK RRWPVSYCRE LNSYSIPFLG SDISVVKRTQ RYLHENLEDS PVQYAAYVTV GGITSVIKLM FAGLFFLFFV KFSIGRQLLI KFPWLFSFGY FSKQGPTQKQ MDETSFTMTF FGQGYSHGTC VEKNKPNIRI CTQVKGPEAG YVATPIAMVQ AAMTFLSDAS DLPKGGGVFT PGAAFSRTKL IDRLNKHGIE FSVISSSEV // ID SDHA_MOUSE Reviewed; 664 AA. AC Q8K2B3; Q0QF19; Q3UH25; Q3UKP7; Q3V4B1; Q921P5; Q9Z1Z4; DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2002, sequence version 1. DT 19-MAR-2014, entry version 107. DE RecName: Full=Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial; DE EC=1.3.5.1; DE AltName: Full=Flavoprotein subunit of complex II; DE Short=Fp; DE Flags: Precursor; GN Name=Sdha; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Bone marrow, Egg, Heart, Pancreas, and Testis; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Czech II, and FVB/N; TISSUE=Mammary gland, and Mammary tumor; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP PROTEIN SEQUENCE OF 1-14; 47-92; 121-128; 196-207; 233-246; 251-282; RP 313-325; 362-418; 452-480; 486-498; 528-547; 601-615; 624-633 AND RP 637-647. RC STRAIN=C57BL/6; TISSUE=Brain, and Hippocampus; RA Lubec G., Klug S., Kang S.U.; RL Submitted (APR-2007) to UniProtKB. RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] OF 59-609. RC TISSUE=Liver; RX PubMed=16751257; DOI=10.1093/molbev/msl027; RA Kullberg M., Nilsson M.A., Arnason U., Harley E.H., Janke A.; RT "Housekeeping genes for phylogenetic analysis of eutherian RT relationships."; RL Mol. Biol. Evol. 23:1493-1503(2006). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 74-605. RC TISSUE=Heart; RA Weinreich D.M.; RT "OXPHOS genes in mammals and the molecular clock."; RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases. RN [6] RP ACETYLATION AT LYS-179; LYS-182; LYS-250; LYS-335; LYS-480; LYS-485; RP LYS-498; LYS-547; LYS-550; LYS-598; LYS-608; LYS-624 AND LYS-633, RP DEACETYLATION BY SIRT3, AND MUTAGENESIS OF LYS-. RX PubMed=21858060; DOI=10.1371/journal.pone.0023295; RA Finley L.W., Haas W., Desquiret-Dumas V., Wallace D.C., Procaccio V., RA Gygi S.P., Haigis M.C.; RT "Succinate dehydrogenase is a direct target of sirtuin 3 deacetylase RT activity."; RL PLoS ONE 6:E23295-E23295(2011). RN [7] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-179 AND LYS-547, RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-179; LYS-250; LYS-335; RP LYS-485; LYS-498; LYS-538; LYS-547 AND LYS-615, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic fibroblast, and Liver; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., RA Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). RN [8] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-167; LYS-179; LYS-182; RP LYS-335; LYS-423; LYS-498; LYS-517; LYS-538; LYS-547; LYS-608; LYS-636 RP AND LYS-647, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Liver; RX PubMed=23576753; DOI=10.1073/pnas.1302961110; RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., RA Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.; RT "Label-free quantitative proteomics of the lysine acetylome in RT mitochondria identifies substrates of SIRT3 in metabolic pathways."; RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013). CC -!- FUNCTION: Flavoprotein (FP) subunit of succinate dehydrogenase CC (SDH) that is involved in complex II of the mitochondrial electron CC transport chain and is responsible for transferring electrons from CC succinate to ubiquinone (coenzyme Q) (By similarity). Can act as a CC tumor suppressor (By similarity). CC -!- CATALYTIC ACTIVITY: Succinate + ubiquinone = fumarate + ubiquinol. CC -!- COFACTOR: FAD (By similarity). CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; CC fumarate from succinate (eukaryal route): step 1/1. CC -!- SUBUNIT: Component of complex II composed of four subunits: the CC flavoprotein (FP) SDHA, iron-sulfur protein (IP) SDHB, and a CC cytochrome b560 composed of SDHC and SDHD. Interacts with CC SDHAF2/SDH5; interaction is required for FAD attachment (By CC similarity). Interacts with TRAP1 (By similarity). CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral CC membrane protein; Matrix side (By similarity). CC -!- PTM: Acetylation of Lys-498 and Lys-538 is observed in liver CC mitochondria from fasted mice but not from fed mice. Deacetylated CC by SIRT3. CC -!- PTM: Phosphorylation at Tyr-215 is important for efficient CC electron transfer in complex II and the prevention of ROS CC generation (By similarity). CC -!- MISCELLANEOUS: The complex, present in mitochondria, can be CC degraded to form EC 1.3.99.1, which no longer reacts with CC ubiquinone. CC -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase 2 family. CC FRD/SDH subfamily. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK029520; BAC26491.1; -; mRNA. DR EMBL; AK034928; BAC28884.1; -; mRNA. DR EMBL; AK049590; BAC33831.1; -; mRNA. DR EMBL; AK050475; BAC34276.1; -; mRNA. DR EMBL; AK075990; BAC36101.1; -; mRNA. DR EMBL; AK145923; BAE26754.1; -; mRNA. DR EMBL; AK147286; BAE27822.1; -; mRNA. DR EMBL; AK147624; BAE28032.1; -; mRNA. DR EMBL; AK153085; BAE31710.1; -; mRNA. DR EMBL; AK162148; BAE36754.1; -; mRNA. DR EMBL; AK169254; BAE41018.1; -; mRNA. DR EMBL; AK004362; BAE43173.1; -; mRNA. DR EMBL; BC011301; AAH11301.1; -; mRNA. DR EMBL; BC031849; AAH31849.1; -; mRNA. DR EMBL; DQ402975; ABD77308.1; -; mRNA. DR EMBL; AF095938; AAC72373.1; -; mRNA. DR RefSeq; NP_075770.1; NM_023281.1. DR UniGene; Mm.158231; -. DR ProteinModelPortal; Q8K2B3; -. DR SMR; Q8K2B3; 52-664. DR IntAct; Q8K2B3; 7. DR MINT; MINT-4122544; -. DR PhosphoSite; Q8K2B3; -. DR REPRODUCTION-2DPAGE; Q8K2B3; -. DR PaxDb; Q8K2B3; -. DR PRIDE; Q8K2B3; -. DR Ensembl; ENSMUST00000022062; ENSMUSP00000022062; ENSMUSG00000021577. DR GeneID; 66945; -. DR KEGG; mmu:66945; -. DR UCSC; uc007rfa.1; mouse. DR CTD; 6389; -. DR MGI; MGI:1914195; Sdha. DR eggNOG; COG1053; -. DR GeneTree; ENSGT00390000010046; -. DR HOVERGEN; HBG001461; -. DR InParanoid; Q8K2B3; -. DR KO; K00234; -. DR OMA; INVFGKR; -. DR OrthoDB; EOG7MH0XJ; -. DR TreeFam; TF300763; -. DR UniPathway; UPA00223; UER01006. DR ChiTaRS; SdhA; mouse. DR NextBio; 323092; -. DR PRO; PR:Q8K2B3; -. DR ArrayExpress; Q8K2B3; -. DR Bgee; Q8K2B3; -. DR Genevestigator; Q8K2B3; -. DR GO; GO:0005749; C:mitochondrial respiratory chain complex II; ISS:UniProtKB. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. DR GO; GO:0008177; F:succinate dehydrogenase (ubiquinone) activity; IEA:UniProtKB-EC. DR GO; GO:0007399; P:nervous system development; IEA:Ensembl. DR GO; GO:0022904; P:respiratory electron transport chain; ISS:UniProtKB. DR GO; GO:0006105; P:succinate metabolic process; ISS:UniProtKB. DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway. DR Gene3D; 1.20.58.100; -; 1. DR Gene3D; 3.90.700.10; -; 1. DR InterPro; IPR003953; FAD_bind_dom. DR InterPro; IPR003952; FRD_SDH_FAD_BS. DR InterPro; IPR015939; Fum_Rdtase/Succ_DH_flav-like_C. DR InterPro; IPR027477; Succ_DH/fumarate_Rdtase_cat. DR InterPro; IPR011281; Succ_DH_flav_su_fwd. DR InterPro; IPR014006; Succ_Dhase_FrdA_Gneg. DR Pfam; PF00890; FAD_binding_2; 1. DR Pfam; PF02910; Succ_DH_flav_C; 1. DR SUPFAM; SSF46977; SSF46977; 1. DR SUPFAM; SSF56425; SSF56425; 1. DR TIGRFAMs; TIGR01816; sdhA_forward; 1. DR TIGRFAMs; TIGR01812; sdhA_frdA_Gneg; 1. DR PROSITE; PS00504; FRD_SDH_FAD_BINDING; 1. PE 1: Evidence at protein level; KW Acetylation; Complete proteome; Direct protein sequencing; KW Electron transport; FAD; Flavoprotein; Membrane; Mitochondrion; KW Mitochondrion inner membrane; Oxidoreductase; Phosphoprotein; KW Reference proteome; Transit peptide; Transport; KW Tricarboxylic acid cycle; Tumor suppressor. FT TRANSIT 1 43 Mitochondrion (By similarity). FT CHAIN 44 664 Succinate dehydrogenase [ubiquinone] FT flavoprotein subunit, mitochondrial. FT /FTId=PRO_0000010337. FT NP_BIND 68 73 FAD (By similarity). FT NP_BIND 91 106 FAD (By similarity). FT NP_BIND 456 457 FAD (By similarity). FT ACT_SITE 340 340 Proton acceptor (By similarity). FT BINDING 275 275 FAD (By similarity). FT BINDING 296 296 Substrate (By similarity). FT BINDING 308 308 Substrate (By similarity). FT BINDING 407 407 Substrate (By similarity). FT BINDING 440 440 FAD (By similarity). FT BINDING 451 451 Substrate (By similarity). FT MOD_RES 99 99 Tele-8alpha-FAD histidine (By FT similarity). FT MOD_RES 167 167 N6-acetyllysine. FT MOD_RES 179 179 N6-acetyllysine; alternate. FT MOD_RES 179 179 N6-succinyllysine; alternate. FT MOD_RES 182 182 N6-acetyllysine. FT MOD_RES 215 215 Phosphotyrosine; by SRC (By similarity). FT MOD_RES 250 250 N6-acetyllysine; alternate. FT MOD_RES 250 250 N6-succinyllysine; alternate. FT MOD_RES 335 335 N6-acetyllysine; alternate. FT MOD_RES 335 335 N6-succinyllysine; alternate. FT MOD_RES 423 423 N6-acetyllysine. FT MOD_RES 480 480 N6-acetyllysine. FT MOD_RES 485 485 N6-acetyllysine; alternate. FT MOD_RES 485 485 N6-succinyllysine; alternate. FT MOD_RES 498 498 N6-acetyllysine; alternate. FT MOD_RES 498 498 N6-succinyllysine; alternate. FT MOD_RES 517 517 N6-acetyllysine. FT MOD_RES 538 538 N6-acetyllysine; alternate. FT MOD_RES 538 538 N6-succinyllysine; alternate. FT MOD_RES 547 547 N6-acetyllysine; alternate. FT MOD_RES 547 547 N6-succinyllysine; alternate. FT MOD_RES 550 550 N6-acetyllysine. FT MOD_RES 598 598 N6-acetyllysine. FT MOD_RES 608 608 N6-acetyllysine. FT MOD_RES 615 615 N6-succinyllysine. FT MOD_RES 624 624 N6-acetyllysine. FT MOD_RES 633 633 N6-acetyllysine. FT MOD_RES 636 636 N6-acetyllysine. FT MOD_RES 647 647 N6-acetyllysine. FT CONFLICT 69 69 A -> V (in Ref. 1; BAE26754). FT CONFLICT 246 246 R -> Q (in Ref. 1; BAE26754). FT CONFLICT 428 428 Q -> R (in Ref. 1; BAE26754). FT CONFLICT 501 501 F -> L (in Ref. 4; ABD77308). FT CONFLICT 517 517 K -> M (in Ref. 4; ABD77308). FT CONFLICT 571 571 L -> M (in Ref. 4; ABD77308). SQ SEQUENCE 664 AA; 72585 MW; DDCE1535163C9449 CRC64; MAGVGAVSRL LRGRRLALTG AWPGTLQKQT CGFHFSVGEN KKASAKVSDA ISTQYPVVDH EFDAVVVGAG GAGLRAAFGL SEAGFNTACL TKLFPTRSHT VAAQGGINAA LGNMEEDNWR WHFYDTVKGS DWLGDQDAIH YMTEQAPASV VELENYGMPF SRTEDGKIYQ RAFGGQSLKF GKGGQAHRCC CVADRTGHSL LHTLYGRSLR YDTSYFVEYF ALDLLMENGE CRGVIALCIE DGSIHRIRAK NTVIATGGYG RTYFSCTSAH TSTGDGTAMV TRAGLPCQDL EFVQFHPTGI YGAGCLITEG CRGEGGILIN SQGERFMERY APVAKDLASR DVVSRSMTLE IREGRGCGPE KDHVYLQLHH LPPEQLATRL PGISETAMIF AGVDVTKEPI PVLPTVHYNM GGIPTNYKGQ VLKHVNGQDQ IVPGLYACGE AACASVHGAN RLGANSLLDL VVFGRACALS IAESCRPGDK VPSIKANAGE ESVMNLDKLR FADGSIRTSE LRLNMQKSMQ NHAAVFRVGS VLQEGCEKIS QLYGDLKHLK TFDRGMVWNT DLVETLELQN LMLCALQTIY GAEARKESRG AHAREDYKVR VDEYDYSKPI QGQQKKPFGE HWRKHTLSYV DIKTGKVTLE YRPVIDKTLN EADCATVPPA IRSY // ID SDHB_MOUSE Reviewed; 282 AA. AC Q9CQA3; Q3TF82; Q9DC91; DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 19-MAR-2014, entry version 107. DE RecName: Full=Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial; DE EC=1.3.5.1; DE AltName: Full=Iron-sulfur subunit of complex II; DE Short=Ip; DE Flags: Precursor; GN Name=Sdhb; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Amnion, Bone marrow, Brain, and Tongue; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6, and FVB/N; TISSUE=Brain, and Colon; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP PROTEIN SEQUENCE OF 49-92; 118-153; 170-179; 208-232 AND 245-257, AND RP MASS SPECTROMETRY. RC STRAIN=C57BL/6, and OF1; TISSUE=Brain, and Hippocampus; RA Lubec G., Kang S.U., Sunyer B., Chen W.-Q.; RL Submitted (JAN-2009) to UniProtKB. RN [4] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-53 AND LYS-57, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23576753; DOI=10.1073/pnas.1302961110; RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., RA Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.; RT "Label-free quantitative proteomics of the lysine acetylome in RT mitochondria identifies substrates of SIRT3 in metabolic pathways."; RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013). CC -!- FUNCTION: Iron-sulfur protein (IP) subunit of succinate CC dehydrogenase (SDH) that is involved in complex II of the CC mitochondrial electron transport chain and is responsible for CC transferring electrons from succinate to ubiquinone (coenzyme Q) CC (By similarity). CC -!- CATALYTIC ACTIVITY: Succinate + ubiquinone = fumarate + ubiquinol. CC -!- COFACTOR: Binds 1 2Fe-2S cluster (By similarity). CC -!- COFACTOR: Binds 1 3Fe-4S cluster (By similarity). CC -!- COFACTOR: Binds 1 4Fe-4S cluster (By similarity). CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; CC fumarate from succinate (eukaryal route): step 1/1. CC -!- SUBUNIT: Component of complex II composed of four subunits: the CC flavoprotein (FP) SDHA, iron-sulfur protein (IP) SDHB, and a CC cytochrome b560 composed of SDHC and SDHD (By similarity). CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral CC membrane protein; Matrix side (By similarity). CC -!- SIMILARITY: Belongs to the succinate dehydrogenase/fumarate CC reductase iron-sulfur protein family. CC -!- SIMILARITY: Contains 1 2Fe-2S ferredoxin-type domain. CC -!- SIMILARITY: Contains 1 4Fe-4S ferredoxin-type domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK003052; BAB22534.1; -; mRNA. DR EMBL; AK003533; BAB22842.1; -; mRNA. DR EMBL; AK009660; BAB26422.1; -; mRNA. DR EMBL; AK153045; BAE31674.1; -; mRNA. DR EMBL; AK169252; BAE41016.1; -; mRNA. DR EMBL; BC013509; AAH13509.1; -; mRNA. DR EMBL; BC051934; AAH51934.1; -; mRNA. DR PIR; PT0094; PT0094. DR RefSeq; NP_075863.2; NM_023374.3. DR UniGene; Mm.246965; -. DR ProteinModelPortal; Q9CQA3; -. DR SMR; Q9CQA3; 39-277. DR IntAct; Q9CQA3; 5. DR MINT; MINT-1860322; -. DR PhosphoSite; Q9CQA3; -. DR REPRODUCTION-2DPAGE; Q9CQA3; -. DR PaxDb; Q9CQA3; -. DR PRIDE; Q9CQA3; -. DR Ensembl; ENSMUST00000010007; ENSMUSP00000010007; ENSMUSG00000009863. DR GeneID; 67680; -. DR KEGG; mmu:67680; -. DR UCSC; uc008vnl.1; mouse. DR CTD; 6390; -. DR MGI; MGI:1914930; Sdhb. DR eggNOG; COG0479; -. DR GeneTree; ENSGT00390000013558; -. DR HOGENOM; HOG000160590; -. DR HOVERGEN; HBG005483; -. DR InParanoid; Q9CQA3; -. DR KO; K00235; -. DR OMA; DSHERML; -. DR OrthoDB; EOG7H4DTN; -. DR TreeFam; TF300754; -. DR UniPathway; UPA00223; UER01006. DR ChiTaRS; SDHB; mouse. DR NextBio; 325239; -. DR PRO; PR:Q9CQA3; -. DR ArrayExpress; Q9CQA3; -. DR Bgee; Q9CQA3; -. DR Genevestigator; Q9CQA3; -. DR GO; GO:0005749; C:mitochondrial respiratory chain complex II; ISS:UniProtKB. DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; ISS:UniProtKB. DR GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; ISS:UniProtKB. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; ISS:UniProtKB. DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008177; F:succinate dehydrogenase (ubiquinone) activity; IEA:UniProtKB-EC. DR GO; GO:0048039; F:ubiquinone binding; ISS:UniProtKB. DR GO; GO:0022904; P:respiratory electron transport chain; IEA:Ensembl. DR GO; GO:0006105; P:succinate metabolic process; IEA:Ensembl. DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway. DR Gene3D; 3.10.20.30; -; 1. DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type. DR InterPro; IPR006058; 2Fe2S_fd_BS. DR InterPro; IPR017896; 4Fe4S_Fe-S-bd. DR InterPro; IPR017900; 4Fe4S_Fe_S_CS. DR InterPro; IPR012675; Beta-grasp_dom. DR InterPro; IPR009051; Helical_ferredxn. DR InterPro; IPR004489; Succ_DH/fum_Rdtase_Fe-S. DR InterPro; IPR025192; Succ_DH/fum_Rdtase_N. DR Pfam; PF13085; Fer2_3; 1. DR SUPFAM; SSF46548; SSF46548; 1. DR SUPFAM; SSF54292; SSF54292; 1. DR TIGRFAMs; TIGR00384; dhsB; 1. DR PROSITE; PS00197; 2FE2S_FER_1; 1. DR PROSITE; PS51085; 2FE2S_FER_2; 1. DR PROSITE; PS00198; 4FE4S_FER_1; 1. DR PROSITE; PS51379; 4FE4S_FER_2; 1. PE 1: Evidence at protein level; KW 2Fe-2S; 3Fe-4S; 4Fe-4S; Acetylation; Complete proteome; KW Direct protein sequencing; Electron transport; Iron; Iron-sulfur; KW Membrane; Metal-binding; Mitochondrion; Mitochondrion inner membrane; KW Oxidoreductase; Reference proteome; Transit peptide; Transport; KW Tricarboxylic acid cycle. FT TRANSIT 1 30 Mitochondrion (By similarity). FT CHAIN 31 282 Succinate dehydrogenase [ubiquinone] FT iron-sulfur subunit, mitochondrial. FT /FTId=PRO_0000010356. FT DOMAIN 42 135 2Fe-2S ferredoxin-type. FT DOMAIN 178 208 4Fe-4S ferredoxin-type. FT METAL 95 95 Iron-sulfur 1 (2Fe-2S) (By similarity). FT METAL 100 100 Iron-sulfur 1 (2Fe-2S) (By similarity). FT METAL 103 103 Iron-sulfur 1 (2Fe-2S) (By similarity). FT METAL 115 115 Iron-sulfur 1 (2Fe-2S) (By similarity). FT METAL 188 188 Iron-sulfur 2 (4Fe-4S) (By similarity). FT METAL 191 191 Iron-sulfur 2 (4Fe-4S) (By similarity). FT METAL 194 194 Iron-sulfur 2 (4Fe-4S) (By similarity). FT METAL 198 198 Iron-sulfur 3 (3Fe-4S) (By similarity). FT METAL 245 245 Iron-sulfur 3 (3Fe-4S) (By similarity). FT METAL 251 251 Iron-sulfur 3 (3Fe-4S) (By similarity). FT METAL 255 255 Iron-sulfur 2 (4Fe-4S) (By similarity). FT BINDING 203 203 Ubiquinone; shared with DHSD (By FT similarity). FT MOD_RES 53 53 N6-acetyllysine. FT MOD_RES 57 57 N6-acetyllysine. FT CONFLICT 40 40 R -> K (in Ref. 1; BAB22534). SQ SEQUENCE 282 AA; 31814 MW; A8616A911427AF8E CRC64; MAATVGVSLK RGFPAAVLGR VGLQFQACRG AQTAAAAAPR IKKFAIYRWD PDKTGDKPRM QTYEVDLNKC GPMVLDALIK IKNEVDSTLT FRRSCREGIC GSCAMNINGG NTLACTRRID TDLSKVSKIY PLPHMYVIKD LVPDLSNFYA QYKSIEPYLK KKDESQEGKQ QYLQSIEDRE KLDGLYECIL CACCSTSCPS YWWNGDKYLG PAVLMQAYRW MIDSRDDFTE ERLAKLQDPF SVYRCHTIMN CTQTCPKGLN PGKAIAEIKK MMATYKEKRA LA // ID SERA_MOUSE Reviewed; 533 AA. AC Q61753; Q3TEE5; Q75SV9; Q8C603; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 19-MAR-2014, entry version 124. DE RecName: Full=D-3-phosphoglycerate dehydrogenase; DE Short=3-PGDH; DE EC=1.1.1.95; DE AltName: Full=A10; GN Name=Phgdh; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=129/SvJ; RX PubMed=14645240; DOI=10.1074/jbc.C300507200; RA Yoshida K., Furuya S., Osuka S., Mitoma J., Shinoda Y., Watanabe M., RA Azuma N., Tanaka H., Hashikawa T., Itohara S., Hirabayashi Y.; RT "Targeted disruption of the mouse 3-phosphoglycerate dehydrogenase RT gene causes severe neurodevelopmental defects and results in embryonic RT lethality."; RL J. Biol. Chem. 279:3573-3577(2004). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J, and NOD; TISSUE=Testis, and Thymus; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6; TISSUE=Brain, and Olfactory epithelium; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP PROTEIN SEQUENCE OF 39-54; 248-268; 365-380 AND 523-533, AND MASS RP SPECTROMETRY. RC TISSUE=Brain, and Hippocampus; RA Lubec G., Klug S., Yang J.W., Zigmond M.; RL Submitted (JUL-2007) to UniProtKB. RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 49-533. RA Miller I.J., Bieker J.J.; RT "Sequences and expression patterns of murine erythroleukemia cDNAs RT isolated by subtractive cloning."; RL Submitted (SEP-1993) to the EMBL/GenBank/DDBJ databases. RN [6] RP DISRUPTION PHENOTYPE. RX PubMed=19114063; DOI=10.1016/j.neures.2008.12.002; RA Kawakami Y., Yoshida K., Yang J.H., Suzuki T., Azuma N., Sakai K., RA Hashikawa T., Watanabe M., Yasuda K., Kuhara S., Hirabayashi Y., RA Furuya S.; RT "Impaired neurogenesis in embryonic spinal cord of Phgdh knockout RT mice, a serine deficiency disorder model."; RL Neurosci. Res. 63:184-193(2009). RN [7] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-21 AND LYS-58, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic fibroblast; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., RA Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). CC -!- CATALYTIC ACTIVITY: 3-phospho-D-glycerate + NAD(+) = 3- CC phosphonooxypyruvate + NADH. CC -!- CATALYTIC ACTIVITY: 2-hydroxyglutarate + NAD(+) = 2-oxoglutarate + CC NADH. CC -!- PATHWAY: Amino-acid biosynthesis; L-serine biosynthesis; L-serine CC from 3-phospho-D-glycerate: step 1/3. CC -!- SUBUNIT: Homotetramer (By similarity). CC -!- DISRUPTION PHENOTYPE: Decreased level of free serine, glycine, CC taurine, GABA, glutamine, and threonine in spinal cord and head. CC Impaired central nervous system (CNS) with shorter neural tube CC length and overall growth retardation. Severe atrophy at the CC thoracic level, particularly in the dorsal spinal cord. Poorly CC developed dorsal horn and adjacent mantle zone. Neurons fail to CC develop neurites, particularly commissural axonal fibers. CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid CC dehydrogenase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AB128936; BAD08449.1; -; Genomic_DNA. DR EMBL; AK076815; BAC36494.1; -; mRNA. DR EMBL; AK169684; BAE41303.1; -; mRNA. DR EMBL; BC086668; AAH86668.1; -; mRNA. DR EMBL; BC110673; AAI10674.1; -; mRNA. DR EMBL; L21027; AAB67986.1; -; mRNA. DR RefSeq; NP_058662.2; NM_016966.3. DR UniGene; Mm.16898; -. DR UniGene; Mm.371997; -. DR ProteinModelPortal; Q61753; -. DR SMR; Q61753; 5-503. DR BioGrid; 231770; 1. DR IntAct; Q61753; 4. DR MINT; MINT-4114515; -. DR PhosphoSite; Q61753; -. DR COMPLUYEAST-2DPAGE; Q61753; -. DR REPRODUCTION-2DPAGE; IPI00225961; -. DR REPRODUCTION-2DPAGE; Q61753; -. DR SWISS-2DPAGE; Q61753; -. DR PaxDb; Q61753; -. DR PRIDE; Q61753; -. DR Ensembl; ENSMUST00000065793; ENSMUSP00000064755; ENSMUSG00000053398. DR GeneID; 236539; -. DR KEGG; mmu:236539; -. DR UCSC; uc008qps.1; mouse. DR CTD; 26227; -. DR MGI; MGI:1355330; Phgdh. DR eggNOG; COG0111; -. DR GeneTree; ENSGT00530000063021; -. DR HOGENOM; HOG000136693; -. DR HOVERGEN; HBG054241; -. DR InParanoid; Q61753; -. DR KO; K00058; -. DR OMA; NDNTFAQ; -. DR OrthoDB; EOG7JT6WT; -. DR TreeFam; TF314548; -. DR UniPathway; UPA00135; UER00196. DR NextBio; 382995; -. DR PRO; PR:Q61753; -. DR Bgee; Q61753; -. DR CleanEx; MM_PHGDH; -. DR Genevestigator; Q61753; -. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR GO; GO:0004617; F:phosphoglycerate dehydrogenase activity; TAS:MGI. DR GO; GO:0070314; P:G1 to G0 transition; IMP:MGI. DR GO; GO:0009448; P:gamma-aminobutyric acid metabolic process; IMP:MGI. DR GO; GO:0021782; P:glial cell development; IMP:MGI. DR GO; GO:0006541; P:glutamine metabolic process; IMP:MGI. DR GO; GO:0006544; P:glycine metabolic process; IMP:MGI. DR GO; GO:0006564; P:L-serine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0006563; P:L-serine metabolic process; IMP:MGI. DR GO; GO:0021915; P:neural tube development; IMP:MGI. DR GO; GO:0031175; P:neuron projection development; IMP:MGI. DR GO; GO:0010468; P:regulation of gene expression; IMP:MGI. DR GO; GO:0021510; P:spinal cord development; IMP:MGI. DR GO; GO:0019530; P:taurine metabolic process; IMP:MGI. DR GO; GO:0006566; P:threonine metabolic process; IMP:MGI. DR Gene3D; 3.40.50.720; -; 2. DR InterPro; IPR006236; D-3-Phosphoglycerate_DH. DR InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom. DR InterPro; IPR006140; D-isomer_2_OHA_DH_NAD-bd. DR InterPro; IPR016040; NAD(P)-bd_dom. DR PANTHER; PTHR10996:SF20; PTHR10996:SF20; 1. DR Pfam; PF00389; 2-Hacid_dh; 1. DR Pfam; PF02826; 2-Hacid_dh_C; 1. DR TIGRFAMs; TIGR01327; PGDH; 1. DR PROSITE; PS00065; D_2_HYDROXYACID_DH_1; 1. DR PROSITE; PS00670; D_2_HYDROXYACID_DH_2; 1. DR PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1. PE 1: Evidence at protein level; KW Acetylation; Amino-acid biosynthesis; Complete proteome; KW Direct protein sequencing; NAD; Oxidoreductase; Reference proteome; KW Serine biosynthesis. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 533 D-3-phosphoglycerate dehydrogenase. FT /FTId=PRO_0000076014. FT NP_BIND 155 156 NAD (By similarity). FT NP_BIND 234 236 NAD (By similarity). FT NP_BIND 283 286 NAD (By similarity). FT ACT_SITE 236 236 By similarity. FT ACT_SITE 265 265 By similarity. FT ACT_SITE 283 283 Proton donor (By similarity). FT BINDING 78 78 NAD (By similarity). FT BINDING 175 175 NAD (By similarity). FT BINDING 207 207 NAD; via carbonyl oxygen (By similarity). FT BINDING 260 260 NAD (By similarity). FT MOD_RES 2 2 N-acetylalanine (By similarity). FT MOD_RES 21 21 N6-acetyllysine. FT MOD_RES 58 58 N6-acetyllysine. FT CONFLICT 77 77 G -> V (in Ref. 5; AAB67986). FT CONFLICT 87 88 AA -> PP (in Ref. 5; AAB67986). FT CONFLICT 124 124 A -> T (in Ref. 5; AAB67986). FT CONFLICT 369 369 C -> W (in Ref. 5; AAB67986). FT CONFLICT 377 377 G -> A (in Ref. 5; AAB67986). FT CONFLICT 447 447 M -> K (in Ref. 2; BAC36494). SQ SEQUENCE 533 AA; 56586 MW; 49CBF125AD6A12A5 CRC64; MAFANLRKVL ISDSLDPCCR KILQDGGLQV VEKQNLSKEE LIAELQDCEG LIVRSATKVT ADVINAAEKL QVVGRAGTGV DNVDLEAATR KGILVMNTPN GNSLSAAELT CGMIMCLARQ IPQATASMKD GKWDRKKFMG TELNGKTLGI LGLGRIGREV ATRMQSFGMK TVGYDPIISP EVAASFGVQQ LPLEEIWPLC DFITVHTPLL PSTTGLLNDS TFAQCKKGVR VVNCARGGIV DEGALLRALQ SGQCAGAALD VFTEEPPRDR ALVDHENVIS CPHLGASTKE AQSRCGEEIA VQFVDMVKGK SLTGVVNAQA LTSAFSPHTK PWIGLAEAMG TLMHAWAGSP KGTIQVVTQG TSLKNAGTCL SPAVIVGLLR EASKQADVNL VNAKLLVKEA GLNVTTSHNP GVPGEQGSGE CLLTVALAGA PYQAVGLVQG TTPMLQMLNG AVFRPEVPLR RGQPLLVFRA QPSDPGMLPT MIGLLAEAGV QLLSYQTSMV SDGEPWHVMG LSSLLPSLET WKQHVLEAFQ FCF // ID SMOX_MOUSE Reviewed; 555 AA. AC Q99K82; A2ANQ8; A2ANQ9; A2ANR0; A2ANR1; A2ANR2; Q70LA3; Q70LA4; AC Q70LA5; Q70LA7; Q70LA8; Q70LA9; Q70LB0; Q8CJ56; Q8CJ57; DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 19-MAR-2014, entry version 88. DE RecName: Full=Spermine oxidase; DE EC=1.5.3.16; DE AltName: Full=Polyamine oxidase 1; DE Short=PAO-1; DE Short=PAOh1; GN Name=Smox; Synonyms=Smo; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3; 4; 5; 6; 7 AND 10), TISSUE RP SPECIFICITY, AND SUBCELLULAR LOCATION. RC STRAIN=DBA/2; TISSUE=Brain; RX PubMed=14764092; DOI=10.1111/j.1432-1033.2004.03979.x; RA Cervelli M., Bellini A., Bianchi M., Marcocci L., Nocera S., RA Polticelli F., Federico R., Amendola R., Mariottini P.; RT "Mouse spermine oxidase gene splice variants. Nuclear subcellular RT localization of a novel active isoform."; RL Eur. J. Biochem. 271:760-770(2004). RN [2] RP NUCLEOTIDE SEQUENCE (ISOFORMS 1; 8 AND 9). RC TISSUE=Liver; RA Wang Y., Devereux W., Stewart T.M., Casero R.A. Jr.; RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC STRAIN=FVB/N; TISSUE=Mammary tumor; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP CHARACTERIZATION, AND MUTAGENESIS OF CYS-320. RX PubMed=12141946; DOI=10.1042/BJ20020720; RA Vujcic S., Diegelman P., Bacchi C.J., Kramer D.L., Porter C.W.; RT "Identification and characterization of a novel flavin-containing RT spermine oxidase of mammalian cell origin."; RL Biochem. J. 367:665-675(2002). CC -!- FUNCTION: Flavoenzyme which catalyzes the oxidation of spermine to CC spermidine. Can also use N(1)-acetylspermine and spermidine as CC substrates, with different affinity depending on the isoform CC (isozyme) and on the experimental conditions. Plays an important CC role in the regulation of polyamine intracellular concentration CC and has the potential to act as a determinant of cellular CC sensitivity to the antitumor polyamine analogs. May contribute to CC beta-alanine production via aldehyde dehydrogenase conversion of CC 3-amino-propanal. CC -!- CATALYTIC ACTIVITY: Spermine + O(2) + H(2)O = spermidine + 3- CC aminopropanal + H(2)O(2). CC -!- COFACTOR: Binds 1 FAD per subunit (By similarity). CC -!- PATHWAY: Amine and polyamine degradation; spermine degradation. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SUBCELLULAR LOCATION: Isoform 2: Cytoplasm. Nucleus. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=10; CC Name=1; Synonyms=Alpha, Polyamine oxidase-l; CC IsoId=Q99K82-1; Sequence=Displayed; CC Note=Major isoform; CC Name=2; Synonyms=Mu; CC IsoId=Q99K82-2; Sequence=VSP_011137; CC Note=Active. Nuclear and cytoplasmic; CC Name=3; Synonyms=Eta; CC IsoId=Q99K82-3; Sequence=VSP_011131; CC Name=4; Synonyms=Omega; CC IsoId=Q99K82-4; Sequence=VSP_011128, VSP_011132; CC Name=5; Synonyms=Phi; CC IsoId=Q99K82-5; Sequence=VSP_011130; CC Name=6; Synonyms=Beta; CC IsoId=Q99K82-6; Sequence=VSP_011136, VSP_011138; CC Name=7; Synonyms=Gamma; CC IsoId=Q99K82-7; Sequence=VSP_011135, VSP_011138; CC Note=No detectable activity. Cytoplasmic; CC Name=8; Synonyms=Polyamine oxidase-m; CC IsoId=Q99K82-8; Sequence=VSP_011134; CC Name=9; Synonyms=Polyamine oxidase-s; CC IsoId=Q99K82-9; Sequence=VSP_011129, VSP_011133; CC Name=10; Synonyms=Delta; CC IsoId=Q99K82-10; Sequence=VSP_011127; CC Note=No detectable activity. Cytoplasmic; CC -!- TISSUE SPECIFICITY: Widely expressed. Isoform 1 and isoform 2 are CC expressed at higher level in brain and skeletal muscle. Isoform 7 CC is found in brain and spleen, isoform 10 is widely expressed but CC found at lower level in heart, kidney, liver and lung. CC -!- INDUCTION: By antitumor polyamine analogs (Probable). CC -!- SIMILARITY: Belongs to the flavin monoamine oxidase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJ567473; CAD98866.1; -; mRNA. DR EMBL; AJ567474; CAD98867.1; -; mRNA. DR EMBL; AJ567475; CAD98868.1; -; mRNA. DR EMBL; AJ567476; CAD98869.1; -; mRNA. DR EMBL; AJ567477; CAD98870.1; -; mRNA. DR EMBL; AJ567478; CAD98871.1; -; mRNA. DR EMBL; AJ567479; CAD98872.1; -; mRNA. DR EMBL; AJ567480; CAD98873.1; -; mRNA. DR EMBL; AF495851; AAN32908.1; -; mRNA. DR EMBL; AF495852; AAN32909.1; -; mRNA. DR EMBL; AF495853; AAN32910.1; -; mRNA. DR EMBL; AF498364; AAN32915.1; -; Genomic_DNA. DR EMBL; AL831781; CAM20374.1; -; Genomic_DNA. DR EMBL; AL831731; CAM20374.1; JOINED; Genomic_DNA. DR EMBL; AL831781; CAM20375.1; -; Genomic_DNA. DR EMBL; AL831731; CAM20375.1; JOINED; Genomic_DNA. DR EMBL; AL831781; CAM20376.1; -; Genomic_DNA. DR EMBL; AL831731; CAM20376.1; JOINED; Genomic_DNA. DR EMBL; AL831781; CAM20378.1; -; Genomic_DNA. DR EMBL; AL831731; CAM20378.1; JOINED; Genomic_DNA. DR EMBL; AL831781; CAM20379.1; -; Genomic_DNA. DR EMBL; AL831731; CAM20379.1; JOINED; Genomic_DNA. DR EMBL; AL831731; CAM24528.1; -; Genomic_DNA. DR EMBL; AL831781; CAM24528.1; JOINED; Genomic_DNA. DR EMBL; AL831731; CAM24529.1; -; Genomic_DNA. DR EMBL; AL831781; CAM24529.1; JOINED; Genomic_DNA. DR EMBL; AL831731; CAM24530.1; -; Genomic_DNA. DR EMBL; AL831781; CAM24530.1; JOINED; Genomic_DNA. DR EMBL; AL831731; CAM24531.1; -; Genomic_DNA. DR EMBL; AL831781; CAM24531.1; JOINED; Genomic_DNA. DR EMBL; AL831731; CAM24532.1; -; Genomic_DNA. DR EMBL; AL831781; CAM24532.1; JOINED; Genomic_DNA. DR EMBL; BC004831; AAH04831.1; -; mRNA. DR RefSeq; NP_001171304.1; NM_001177833.1. DR RefSeq; NP_001171305.1; NM_001177834.1. DR RefSeq; NP_001171306.1; NM_001177835.1. DR RefSeq; NP_001171307.1; NM_001177836.1. DR RefSeq; NP_001171309.1; NM_001177838.1. DR RefSeq; NP_001171310.1; NM_001177839.1. DR RefSeq; NP_001171311.1; NM_001177840.1. DR RefSeq; NP_663508.1; NM_145533.2. DR RefSeq; XP_006499350.1; XM_006499287.1. DR RefSeq; XP_006499351.1; XM_006499288.1. DR UniGene; Mm.136586; -. DR ProteinModelPortal; Q99K82; -. DR SMR; Q99K82; 25-547. DR PhosphoSite; Q99K82; -. DR PRIDE; Q99K82; -. DR Ensembl; ENSMUST00000028806; ENSMUSP00000028806; ENSMUSG00000027333. [Q99K82-1] DR Ensembl; ENSMUST00000110180; ENSMUSP00000105809; ENSMUSG00000027333. [Q99K82-8] DR Ensembl; ENSMUST00000110182; ENSMUSP00000105811; ENSMUSG00000027333. [Q99K82-10] DR Ensembl; ENSMUST00000110183; ENSMUSP00000105812; ENSMUSG00000027333. [Q99K82-5] DR Ensembl; ENSMUST00000110186; ENSMUSP00000105815; ENSMUSG00000027333. [Q99K82-2] DR Ensembl; ENSMUST00000110188; ENSMUSP00000105817; ENSMUSG00000027333. [Q99K82-6] DR Ensembl; ENSMUST00000110189; ENSMUSP00000105818; ENSMUSG00000027333. [Q99K82-7] DR Ensembl; ENSMUST00000183947; ENSMUSP00000139278; ENSMUSG00000027333. [Q99K82-4] DR GeneID; 228608; -. DR KEGG; mmu:228608; -. DR UCSC; uc008mlm.2; mouse. [Q99K82-1] DR UCSC; uc008mln.2; mouse. [Q99K82-2] DR UCSC; uc008mls.2; mouse. [Q99K82-10] DR UCSC; uc008mlt.2; mouse. [Q99K82-6] DR UCSC; uc012cep.1; mouse. [Q99K82-7] DR UCSC; uc012ceq.1; mouse. [Q99K82-5] DR CTD; 54498; -. DR MGI; MGI:2445356; Smox. DR eggNOG; NOG311398; -. DR GeneTree; ENSGT00530000062888; -. DR HOVERGEN; HBG053499; -. DR InParanoid; A2ANR0; -. DR KO; K12259; -. DR OMA; QEFFRHG; -. DR OrthoDB; EOG751NFD; -. DR TreeFam; TF318348; -. DR UniPathway; UPA00211; -. DR NextBio; 379060; -. DR PRO; PR:Q99K82; -. DR ArrayExpress; Q99K82; -. DR Bgee; Q99K82; -. DR CleanEx; MM_SMO; -. DR CleanEx; MM_SMOX; -. DR Genevestigator; Q99K82; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0052895; F:N1-acetylspermine:oxygen oxidoreductase (N1-acetylspermidine-forming) activity; IEA:UniProtKB-EC. DR GO; GO:0052894; F:norspermine:oxygen oxidoreductase activity; IEA:UniProtKB-EC. DR GO; GO:0046592; F:polyamine oxidase activity; IDA:MGI. DR GO; GO:0052901; F:spermine:oxygen oxidoreductase (spermidine-forming) activity; IEA:UniProtKB-EC. DR GO; GO:0046208; P:spermine catabolic process; IDA:MGI. DR InterPro; IPR002937; Amino_oxidase. DR Pfam; PF01593; Amino_oxidase; 2. PE 1: Evidence at protein level; KW Alternative splicing; Complete proteome; Cytoplasm; FAD; Flavoprotein; KW Nucleus; Oxidoreductase; Reference proteome. FT CHAIN 1 555 Spermine oxidase. FT /FTId=PRO_0000099878. FT VAR_SEQ 146 510 Missing (in isoform 10). FT /FTId=VSP_011127. FT VAR_SEQ 204 510 Missing (in isoform 5). FT /FTId=VSP_011130. FT VAR_SEQ 204 243 VESCESSSHSIDEVSLSAFGEWTEIPGAHHIIPSGFMRVV FT -> GTPIYQNLGESCAQPGAATHTSGVPIPTHRWAQVGRMW FT RS (in isoform 9). FT /FTId=VSP_011129. FT VAR_SEQ 204 209 VESCES -> SAMAMC (in isoform 4). FT /FTId=VSP_011128. FT VAR_SEQ 205 555 ESCESSSHSIDEVSLSAFGEWTEIPGAHHIIPSGFMRVVEL FT LAEGIPPHVIQLGKPVRCIHWDQASAHPRGPEIEPRGEGDH FT NHDTGEGGQSGENPQQGRWDEDEPWPVVVECEDCEVIPADH FT VIVTVSLGVLKRQYTSFFRPCLPTEKVAAIHRLGIGTTDKI FT FLEFEEPFWGPECNSLQFVWEDEAESCTLTYPPELWYRKIC FT GFDVLYPPERYGHVLSGWICGEEALVMERCDDEAVAEICTE FT MLRQFTGNPNIPKPRRILRSAWGSNPYFRGSYSYTQVGSSG FT ADVEKLAKPLPYTESSKTAPMQVLFSGEATHRKYYSTTHGA FT LLSGQREAARLIEMYRDLFQQGP -> SLLWSIDARVKKMN FT SGGVSVQSALLLRALVPCMA (in isoform 3). FT /FTId=VSP_011131. FT VAR_SEQ 210 555 Missing (in isoform 4). FT /FTId=VSP_011132. FT VAR_SEQ 244 255 Missing (in isoform 9). FT /FTId=VSP_011133. FT VAR_SEQ 282 417 Missing (in isoform 8). FT /FTId=VSP_011134. FT VAR_SEQ 457 512 GNPNIPKPRRILRSAWGSNPYFRGSYSYTQVGSSGADVEKL FT AKPLPYTESSKTAPM -> AHAGALLRGGHTP (in FT isoform 7). FT /FTId=VSP_011135. FT VAR_SEQ 458 512 NPNIPKPRRILRSAWGSNPYFRGSYSYTQVGSSGADVEKLA FT KPLPYTESSKTAPM -> GLKWGGCGEASQAPALHRELQDS FT AHAGALLRGGHTP (in isoform 6). FT /FTId=VSP_011136. FT VAR_SEQ 510 510 A -> AHRSSTEQQPGHLLPSKCPEQSLDPSRGSIK (in FT isoform 2). FT /FTId=VSP_011137. FT VAR_SEQ 516 555 FSGEATHRKYYSTTHGALLSGQREAARLIEMYRDLFQQGP FT -> LHHPRCSALWPARGRPAHRDVPRPLPAGALKGVLTAKC FT VP (in isoform 6 and isoform 7). FT /FTId=VSP_011138. FT MUTAGEN 320 320 C->R: No change in enzymatic activity. SQ SEQUENCE 555 AA; 61852 MW; A297E9DBD094EA74 CRC64; MQSCESSGDS ADDPLSRGLR RRGQPRVVVI GAGLAGLAAA RALLEQGFTD VTVLEASSHI GGRVQSVRLG DTTFELGATW IHGSHGNPIY QLAEANGLLE ETTDGERSVG RISLYSKNGV ACYLTNRGCR IPKDVVEEFS DLYNEVYNMT QEFFRHGKPV NAESQNSVGV FTREKVRNRI RDDPDDTEAT KRLKLAMIQQ YLKVESCESS SHSIDEVSLS AFGEWTEIPG AHHIIPSGFM RVVELLAEGI PPHVIQLGKP VRCIHWDQAS AHPRGPEIEP RGEGDHNHDT GEGGQSGENP QQGRWDEDEP WPVVVECEDC EVIPADHVIV TVSLGVLKRQ YTSFFRPCLP TEKVAAIHRL GIGTTDKIFL EFEEPFWGPE CNSLQFVWED EAESCTLTYP PELWYRKICG FDVLYPPERY GHVLSGWICG EEALVMERCD DEAVAEICTE MLRQFTGNPN IPKPRRILRS AWGSNPYFRG SYSYTQVGSS GADVEKLAKP LPYTESSKTA PMQVLFSGEA THRKYYSTTH GALLSGQREA ARLIEMYRDL FQQGP // ID SODE_MOUSE Reviewed; 251 AA. AC O09164; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1997, sequence version 1. DT 19-MAR-2014, entry version 120. DE RecName: Full=Extracellular superoxide dismutase [Cu-Zn]; DE Short=EC-SOD; DE EC=1.15.1.1; DE Flags: Precursor; GN Name=Sod3; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 25-36. RC STRAIN=C57BL/6 X CBA; TISSUE=Lung; RX PubMed=9376114; DOI=10.1165/ajrcmb.17.4.2826; RA Folz R.J., Guan J., Seldin M.F., Oury T.D., Enghild J.J., Crapo J.D.; RT "Mouse extracellular superoxide dismutase: primary structure, tissue- RT specific gene expression, chromosomal localization, and lung in situ RT hybridization."; RL Am. J. Respir. Cell Mol. Biol. 17:393-403(1997). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=C57BL/6J; TISSUE=Kidney; RX PubMed=9163733; RA Suh J.-G., Takai S., Yamanishi T., Kikuchi T., Folz R.J., Tanaka K., RA Oh Y.-S., Wada K.; RT "Sequence analysis, tissue expression and chromosomal localization of RT a mouse secreted superoxide dismutase gene."; RL Mol. Cells 7:204-207(1997). RN [3] RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6; TISSUE=Liver; RA Siegfried M.R., Schultz D., Harrison D.G., Fukai T.; RT "Murine extracellular superoxide dismutase genomic sequence."; RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Protect the extracellular space from toxic effect of CC reactive oxygen intermediates by converting superoxide radicals CC into hydrogen peroxide and oxygen (By similarity). CC -!- CATALYTIC ACTIVITY: 2 superoxide + 2 H(+) = O(2) + H(2)O(2). CC -!- COFACTOR: Binds 1 copper ion per subunit (By similarity). CC -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity). CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space. CC -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U38261; AAB51106.1; -; mRNA. DR EMBL; D50856; BAA23493.1; -; mRNA. DR EMBL; AF223251; AAF27932.1; -; Genomic_DNA. DR RefSeq; NP_035565.1; NM_011435.3. DR UniGene; Mm.2407; -. DR PDB; 2DZ2; Model; -; A=120-228. DR PDB; 2DZ3; Model; -; A=84-228. DR PDBsum; 2DZ2; -. DR PDBsum; 2DZ3; -. DR ProteinModelPortal; O09164; -. DR SMR; O09164; 73-235. DR BioGrid; 203389; 1. DR IntAct; O09164; 1. DR MINT; MINT-4135206; -. DR PhosphoSite; O09164; -. DR PaxDb; O09164; -. DR PRIDE; O09164; -. DR Ensembl; ENSMUST00000101208; ENSMUSP00000098768; ENSMUSG00000072941. DR GeneID; 20657; -. DR KEGG; mmu:20657; -. DR UCSC; uc008xkl.1; mouse. DR CTD; 6649; -. DR MGI; MGI:103181; Sod3. DR eggNOG; COG2032; -. DR HOGENOM; HOG000263447; -. DR HOVERGEN; HBG000062; -. DR InParanoid; O09164; -. DR KO; K16627; -. DR OMA; HPRHPGD; -. DR OrthoDB; EOG77HDHG; -. DR TreeFam; TF105133; -. DR Reactome; REACT_188957; Cellular responses to stress. DR NextBio; 299089; -. DR PRO; PR:O09164; -. DR ArrayExpress; O09164; -. DR Bgee; O09164; -. DR CleanEx; MM_SOD3; -. DR Genevestigator; O09164; -. DR GO; GO:0005829; C:cytosol; IBA:RefGenome. DR GO; GO:0031012; C:extracellular matrix; IEA:Ensembl. DR GO; GO:0005615; C:extracellular space; IDA:MGI. DR GO; GO:0005739; C:mitochondrion; IBA:RefGenome. DR GO; GO:0005634; C:nucleus; IBA:RefGenome. DR GO; GO:0005802; C:trans-Golgi network; IDA:MGI. DR GO; GO:0005507; F:copper ion binding; IBA:RefGenome. DR GO; GO:0004784; F:superoxide dismutase activity; IDA:MGI. DR GO; GO:0008270; F:zinc ion binding; IBA:RefGenome. DR GO; GO:0019430; P:removal of superoxide radicals; IBA:RefGenome. DR GO; GO:0046688; P:response to copper ion; IEA:Ensembl. DR GO; GO:0001666; P:response to hypoxia; IMP:MGI. DR Gene3D; 2.60.40.200; -; 1. DR InterPro; IPR024134; SOD_Cu/Zn_/chaperone. DR InterPro; IPR018152; SOD_Cu/Zn_BS. DR InterPro; IPR024141; SOD_Cu/Zn_extracel. DR InterPro; IPR001424; SOD_Cu_Zn_dom. DR PANTHER; PTHR10003; PTHR10003; 1. DR PANTHER; PTHR10003:SF10; PTHR10003:SF10; 1. DR Pfam; PF00080; Sod_Cu; 1. DR PRINTS; PR00068; CUZNDISMTASE. DR SUPFAM; SSF49329; SSF49329; 1. DR PROSITE; PS00087; SOD_CU_ZN_1; 1. DR PROSITE; PS00332; SOD_CU_ZN_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Antioxidant; Complete proteome; Copper; KW Direct protein sequencing; Disulfide bond; Glycoprotein; KW Metal-binding; Oxidoreductase; Reference proteome; Secreted; Signal; KW Zinc. FT SIGNAL 1 15 By similarity. FT PROPEP 16 24 FT /FTId=PRO_0000032856. FT CHAIN 25 251 Extracellular superoxide dismutase [Cu- FT Zn]. FT /FTId=PRO_0000032857. FT METAL 128 128 Copper; catalytic (By similarity). FT METAL 130 130 Copper; catalytic (By similarity). FT METAL 145 145 Copper; catalytic (By similarity). FT METAL 145 145 Zinc; structural (By similarity). FT METAL 153 153 Zinc; structural (By similarity). FT METAL 156 156 Zinc; structural (By similarity). FT METAL 159 159 Zinc; structural (By similarity). FT METAL 195 195 Copper; catalytic (By similarity). FT CARBOHYD 121 121 N-linked (GlcNAc...) (Potential). FT DISULFID 77 222 By similarity. FT DISULFID 139 221 By similarity. SQ SEQUENCE 251 AA; 27392 MW; 9EAF850E458966C4 CRC64; MLAFLFYGLL LAACGSVTMS NPGESSFDLA DRLDPVEKID RLDLVEKIGD THAKVLEIWM ELGRRREVDA AEMHAICRVQ PSATLPPDQP QITGLVLFRQ LGPGSRLEAY FSLEGFPAEQ NASNRAIHVH EFGDLSQGCD STGPHYNPME VPHPQHPGDF GNFVVRNGQL WRHRVGLTAS LAGPHAILGR SVVVHAGEDD LGKGGNQASL QNGNAGRRLA CCVVGTSSSA AWESQTKERK KRRRESECKT T // ID SODC_MOUSE Reviewed; 154 AA. AC P08228; DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 19-MAR-2014, entry version 159. DE RecName: Full=Superoxide dismutase [Cu-Zn]; DE EC=1.15.1.1; GN Name=Sod1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=SWR/J; TISSUE=Liver; RX PubMed=3362683; DOI=10.1093/nar/16.6.2728; RA Bewley G.C.; RT "cDNA and deduced amino acid sequence of murine Cu-Zn superoxide RT dismutase."; RL Nucleic Acids Res. 16:2728-2728(1988). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=2022332; DOI=10.1016/0378-1119(91)90126-V; RA Benedetto M.T., Anzai Y., Gordon J.W.; RT "Isolation and analysis of the mouse genomic sequence encoding Cu(2+)- RT Zn2+ superoxide dismutase."; RL Gene 99:191-195(1991). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Ovary, Urinary bladder, and Uterus; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Liver, Mammary gland, and Retina; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP PROTEIN SEQUENCE OF 4-23. RX PubMed=2391363; DOI=10.1083/jcb.111.3.1217; RA Pluthero F.G., Shreeve M., Eskinazi D., van der Gaag H., Huang K.S., RA Hulmes J.D., Blum M., Axelrad A.A.; RT "Purification of an inhibitor of erythroid progenitor cell cycling and RT antagonist to interleukin 3 from mouse marrow cell supernatants and RT its identification as cytosolic superoxide dismutase."; RL J. Cell Biol. 111:1217-1223(1990). RN [6] RP PROTEIN SEQUENCE OF 11-24 AND 104-116, AND MASS SPECTROMETRY. RC STRAIN=OF1; TISSUE=Hippocampus; RA Lubec G., Klug S., Sunyer B., Chen W.-Q.; RL Submitted (JAN-2009) to UniProtKB. RN [7] RP DISRUPTION PHENOTYPE. RC TISSUE=Liver; RX PubMed=21420488; DOI=10.1016/j.freeradbiomed.2011.03.018; RA Wang S.K., Weaver J.D., Zhang S., Lei X.G.; RT "Knockout of SOD1 promotes conversion of selenocysteine to RT dehydroalanine in murine hepatic GPX1 protein."; RL Free Radic. Biol. Med. 51:197-204(2011). RN [8] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2 AND LYS-123, SUCCINYLATION RP [LARGE SCALE ANALYSIS] AT LYS-4; LYS-10; LYS-92; LYS-123 AND LYS-137, RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], AND RP CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic fibroblast, and Liver; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., RA Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). RN [9] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-137, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23576753; DOI=10.1073/pnas.1302961110; RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., RA Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.; RT "Label-free quantitative proteomics of the lysine acetylome in RT mitochondria identifies substrates of SIRT3 in metabolic pathways."; RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013). RN [10] RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 2-154 IN COMPLEX WITH ZINC. RX PubMed=20727846; DOI=10.1016/j.abb.2010.08.014; RA Seetharaman S.V., Taylor A.B., Holloway S., Hart P.J.; RT "Structures of mouse SOD1 and human/mouse SOD1 chimeras."; RL Arch. Biochem. Biophys. 503:183-190(2010). CC -!- FUNCTION: Destroys radicals which are normally produced within the CC cells and which are toxic to biological systems. CC -!- CATALYTIC ACTIVITY: 2 superoxide + 2 H(+) = O(2) + H(2)O(2). CC -!- COFACTOR: Binds 1 copper ion per subunit (By similarity). CC -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity). CC -!- SUBUNIT: Homodimer. CC -!- INTERACTION: CC P63001:Rac1; NbExp=4; IntAct=EBI-1635090, EBI-413646; CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus (By similarity). CC -!- PTM: Palmitoylation helps nuclear targeting and decreases CC catalytic activity (By similarity). CC -!- PTM: Succinylation, adjacent to copper catalytic site probably CC inhibit activity. Desuccinylated by SIRT5, enhancing activity (By CC similarity). CC -!- DISRUPTION PHENOTYPE: 40% reduction in hepatic GPX1 activity. CC -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X06683; CAA29880.1; -; mRNA. DR EMBL; M60798; AAA40121.1; -; Genomic_DNA. DR EMBL; M60794; AAA40121.1; JOINED; Genomic_DNA. DR EMBL; M60795; AAA40121.1; JOINED; Genomic_DNA. DR EMBL; M60796; AAA40121.1; JOINED; Genomic_DNA. DR EMBL; M60797; AAA40121.1; JOINED; Genomic_DNA. DR EMBL; M35725; AAA37518.1; -; mRNA. DR EMBL; AK020624; BAB32154.1; -; mRNA. DR EMBL; AK077284; BAC36730.1; -; mRNA. DR EMBL; BC002066; AAH02066.1; -; mRNA. DR EMBL; BC048874; AAH48874.1; -; mRNA. DR EMBL; BC086886; AAH86886.1; -; mRNA. DR PIR; JQ0915; JQ0915. DR RefSeq; NP_035564.1; NM_011434.1. DR UniGene; Mm.276325; -. DR UniGene; Mm.466779; -. DR PDB; 3GTT; X-ray; 2.40 A; A/B/C/D/E/F=2-154. DR PDB; 3GTV; X-ray; 2.20 A; A/B/C/D/E/F/G/H/I/J/K/L=82-154. DR PDB; 3LTV; X-ray; 2.45 A; A/B/C/D/E/F=2-39. DR PDBsum; 3GTT; -. DR PDBsum; 3GTV; -. DR PDBsum; 3LTV; -. DR ProteinModelPortal; P08228; -. DR SMR; P08228; 2-154. DR BioGrid; 203387; 9. DR DIP; DIP-48691N; -. DR IntAct; P08228; 11. DR MINT; MINT-1869618; -. DR STRING; 10090.ENSMUSP00000023707; -. DR PhosphoSite; P08228; -. DR DOSAC-COBS-2DPAGE; P08228; -. DR REPRODUCTION-2DPAGE; IPI00130589; -. DR REPRODUCTION-2DPAGE; P08228; -. DR SWISS-2DPAGE; P08228; -. DR UCD-2DPAGE; P08228; -. DR PaxDb; P08228; -. DR PRIDE; P08228; -. DR Ensembl; ENSMUST00000023707; ENSMUSP00000023707; ENSMUSG00000022982. DR GeneID; 20655; -. DR KEGG; mmu:20655; -. DR UCSC; uc007zvz.1; mouse. DR CTD; 6647; -. DR MGI; MGI:98351; Sod1. DR eggNOG; COG2032; -. DR GeneTree; ENSGT00530000063226; -. DR HOGENOM; HOG000263447; -. DR HOVERGEN; HBG000062; -. DR InParanoid; P08228; -. DR KO; K04565; -. DR OMA; NDPNAKR; -. DR OrthoDB; EOG776SR4; -. DR TreeFam; TF105131; -. DR Reactome; REACT_188957; Cellular responses to stress. DR ChiTaRS; SOD1; mouse. DR EvolutionaryTrace; P08228; -. DR NextBio; 299081; -. DR PRO; PR:P08228; -. DR Bgee; P08228; -. DR CleanEx; MM_SOD1; -. DR Genevestigator; P08228; -. DR GO; GO:0031410; C:cytoplasmic vesicle; ISS:UniProtKB. DR GO; GO:0005829; C:cytosol; ISS:UniProtKB. DR GO; GO:0032839; C:dendrite cytoplasm; ISS:UniProtKB. DR GO; GO:0031012; C:extracellular matrix; ISS:UniProtKB. DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB. DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB. DR GO; GO:0043025; C:neuronal cell body; ISS:UniProtKB. DR GO; GO:0005634; C:nucleus; ISS:UniProtKB. DR GO; GO:0005777; C:peroxisome; IEA:Ensembl. DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl. DR GO; GO:0043234; C:protein complex; ISS:UniProtKB. DR GO; GO:0051087; F:chaperone binding; ISS:UniProtKB. DR GO; GO:0005507; F:copper ion binding; ISS:UniProtKB. DR GO; GO:0030346; F:protein phosphatase 2B binding; ISS:UniProtKB. DR GO; GO:0004784; F:superoxide dismutase activity; IDA:MGI. DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB. DR GO; GO:0000187; P:activation of MAPK activity; IDA:MGI. DR GO; GO:0007568; P:aging; IMP:MGI. DR GO; GO:0008089; P:anterograde axon cargo transport; IMP:BHF-UCL. DR GO; GO:0060088; P:auditory receptor cell stereocilium organization; IMP:MGI. DR GO; GO:0007569; P:cell aging; IEA:Ensembl. DR GO; GO:0006879; P:cellular iron ion homeostasis; IMP:MGI. DR GO; GO:0007566; P:embryo implantation; IMP:MGI. DR GO; GO:0006749; P:glutathione metabolic process; IMP:MGI. DR GO; GO:0060047; P:heart contraction; IMP:MGI. DR GO; GO:0050665; P:hydrogen peroxide biosynthetic process; IMP:MGI. DR GO; GO:0007626; P:locomotory behavior; IMP:MGI. DR GO; GO:0046716; P:muscle cell cellular homeostasis; IMP:MGI. DR GO; GO:0002262; P:myeloid cell homeostasis; IMP:MGI. DR GO; GO:0045541; P:negative regulation of cholesterol biosynthetic process; ISS:UniProtKB. DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IMP:MGI. DR GO; GO:0060052; P:neurofilament cytoskeleton organization; IMP:MGI. DR GO; GO:0001541; P:ovarian follicle development; IMP:MGI. DR GO; GO:0032287; P:peripheral nervous system myelin maintenance; IMP:MGI. DR GO; GO:0001819; P:positive regulation of cytokine production; ISS:UniProtKB. DR GO; GO:1902177; P:positive regulation of intrinsic apoptotic signaling pathway in response to oxidative stress; IEA:Ensembl. DR GO; GO:0032930; P:positive regulation of superoxide anion generation; IEA:Ensembl. DR GO; GO:0008217; P:regulation of blood pressure; IMP:MGI. DR GO; GO:0051881; P:regulation of mitochondrial membrane potential; ISS:UniProtKB. DR GO; GO:0040014; P:regulation of multicellular organism growth; IMP:MGI. DR GO; GO:0032314; P:regulation of Rac GTPase activity; IEA:Ensembl. DR GO; GO:0060087; P:relaxation of vascular smooth muscle; IMP:MGI. DR GO; GO:0019430; P:removal of superoxide radicals; IMP:MGI. DR GO; GO:0001975; P:response to amphetamine; IEA:Ensembl. DR GO; GO:0048678; P:response to axon injury; IMP:MGI. DR GO; GO:0046688; P:response to copper ion; IEA:Ensembl. DR GO; GO:0042493; P:response to drug; IMP:MGI. DR GO; GO:0045471; P:response to ethanol; IMP:MGI. DR GO; GO:0009408; P:response to heat; IMP:MGI. DR GO; GO:0042542; P:response to hydrogen peroxide; IMP:MGI. DR GO; GO:0031667; P:response to nutrient levels; IEA:Ensembl. DR GO; GO:0001895; P:retina homeostasis; IMP:MGI. DR GO; GO:0008090; P:retrograde axon cargo transport; IMP:BHF-UCL. DR GO; GO:0007605; P:sensory perception of sound; IMP:MGI. DR GO; GO:0007283; P:spermatogenesis; IMP:MGI. DR GO; GO:0042554; P:superoxide anion generation; IDA:MGI. DR GO; GO:0019226; P:transmission of nerve impulse; IMP:MGI. DR Gene3D; 2.60.40.200; -; 1. DR InterPro; IPR024134; SOD_Cu/Zn_/chaperone. DR InterPro; IPR018152; SOD_Cu/Zn_BS. DR InterPro; IPR001424; SOD_Cu_Zn_dom. DR PANTHER; PTHR10003; PTHR10003; 1. DR Pfam; PF00080; Sod_Cu; 1. DR PRINTS; PR00068; CUZNDISMTASE. DR SUPFAM; SSF49329; SSF49329; 1. DR PROSITE; PS00087; SOD_CU_ZN_1; 1. DR PROSITE; PS00332; SOD_CU_ZN_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Antioxidant; Complete proteome; Copper; KW Cytoplasm; Direct protein sequencing; Disulfide bond; Lipoprotein; KW Metal-binding; Nucleus; Oxidoreductase; Palmitate; Phosphoprotein; KW Reference proteome; Zinc. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 154 Superoxide dismutase [Cu-Zn]. FT /FTId=PRO_0000164062. FT METAL 47 47 Copper; catalytic (By similarity). FT METAL 49 49 Copper; catalytic (By similarity). FT METAL 64 64 Copper; catalytic (By similarity). FT METAL 64 64 Zinc; via pros nitrogen. FT METAL 72 72 Zinc; via pros nitrogen. FT METAL 81 81 Zinc; via pros nitrogen. FT METAL 84 84 Zinc; structural. FT METAL 121 121 Copper; catalytic (By similarity). FT MOD_RES 2 2 N-acetylalanine. FT MOD_RES 4 4 N6-succinyllysine. FT MOD_RES 10 10 N6-succinyllysine. FT MOD_RES 92 92 N6-succinyllysine. FT MOD_RES 99 99 Phosphoserine (By similarity). FT MOD_RES 123 123 N6-acetyllysine; alternate. FT MOD_RES 123 123 N6-succinyllysine; alternate. FT MOD_RES 137 137 N6-acetyllysine; alternate. FT MOD_RES 137 137 N6-succinyllysine; alternate. FT LIPID 7 7 S-palmitoyl cysteine (By similarity). FT DISULFID 58 147 By similarity. FT CONFLICT 102 102 D -> H (in Ref. 2; AAA40121). FT STRAND 3 10 FT STRAND 12 14 FT STRAND 16 25 FT STRAND 30 38 FT STRAND 41 50 FT TURN 55 58 FT HELIX 59 61 FT STRAND 77 79 FT STRAND 84 90 FT STRAND 96 109 FT STRAND 116 123 FT STRAND 130 132 FT HELIX 133 138 FT STRAND 143 149 SQ SEQUENCE 154 AA; 15943 MW; CAE548C66043BAC4 CRC64; MAMKAVCVLK GDGPVQGTIH FEQKASGEPV VLSGQITGLT EGQHGFHVHQ YGDNTQGCTS AGPHFNPHSK KHGGPADEER HVGDLGNVTA GKDGVANVSI EDRVISLSGE HSIIGRTMVV HEKQDDLGKG GNEESTKTGN AGSRLACGVI GIAQ // ID SODM_MOUSE Reviewed; 222 AA. AC P09671; Q64670; Q8VEM5; DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1998, sequence version 3. DT 19-MAR-2014, entry version 146. DE RecName: Full=Superoxide dismutase [Mn], mitochondrial; DE EC=1.15.1.1; DE Flags: Precursor; GN Name=Sod2; Synonyms=Sod-2; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Placenta; RX PubMed=3797253; DOI=10.1093/nar/14.23.9539; RA Hallewell R.A., Mullenbach G.T., Stempien M.M., Bell G.I.; RT "Sequence of a cDNA coding for mouse manganese superoxide dismutase."; RL Nucleic Acids Res. 14:9539-9539(1986). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=BALB/c, and C3H; RX PubMed=8406027; DOI=10.1016/0378-1119(93)90311-P; RA Sun Y., Hegamyer G., Colburn N.M.; RT "Sequence of manganese superoxide dismutase-encoding cDNAs from RT multiple mouse organs."; RL Gene 131:301-302(1993). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=7875582; DOI=10.1016/0378-1119(94)00666-G; RA Jones P.L., Kucera G., Gordon H.M., Boss J.M.; RT "Cloning and characterization of the murine manganous superoxide RT dismutase-encoding gene."; RL Gene 153:155-161(1995). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=7613035; DOI=10.1007/BF00352417; RA Disilvestre D., Kleeberger S.R., Johns J., Levitt R.C.; RT "Structure and DNA sequence of the mouse MnSOD gene."; RL Mamm. Genome 6:281-284(1995). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Embryo, and Kidney; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Mammary gland; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [7] RP PROTEIN SEQUENCE OF 54-68; 76-108; 115-130 AND 203-216, AND MASS RP SPECTROMETRY. RC STRAIN=C57BL/6; TISSUE=Brain, and Hippocampus; RA Lubec G., Kang S.U., Klug S., Yang J.W., Zigmond M.; RL Submitted (JUL-2007) to UniProtKB. RN [8] RP ACETYLATION AT LYS-122, DEACETYLATION BY SIRT3, AND MUTAGENESIS OF RP LYS-122. RX PubMed=21172655; DOI=10.1016/j.molcel.2010.12.013; RA Tao R., Coleman M.C., Pennington J.D., Ozden O., Park S.H., Jiang H., RA Kim H.S., Flynn C.R., Hill S., Hayes McDonald W., Olivier A.K., RA Spitz D.R., Gius D.; RT "Sirt3-mediated deacetylation of evolutionarily conserved lysine 122 RT regulates MnSOD activity in response to stress."; RL Mol. Cell 40:893-904(2010). RN [9] RP INDUCTION. RX PubMed=20668652; DOI=10.1371/journal.pone.0011786; RA Goitre L., Balzac F., Degani S., Degan P., Marchi S., Pinton P., RA Retta S.F.; RT "KRIT1 regulates the homeostasis of intracellular reactive oxygen RT species."; RL PLoS ONE 5:E11786-E11786(2010). RN [10] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-130, SUCCINYLATION [LARGE RP SCALE ANALYSIS] AT LYS-68; LYS-75; LYS-122 AND LYS-130, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic fibroblast, and Liver; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., RA Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). RN [11] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-68; LYS-75; LYS-114; RP LYS-122; LYS-130 AND LYS-202, AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23576753; DOI=10.1073/pnas.1302961110; RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., RA Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.; RT "Label-free quantitative proteomics of the lysine acetylome in RT mitochondria identifies substrates of SIRT3 in metabolic pathways."; RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013). CC -!- FUNCTION: Destroys superoxide anion radicals which are normally CC produced within the cells and which are toxic to biological CC systems. CC -!- CATALYTIC ACTIVITY: 2 superoxide + 2 H(+) = O(2) + H(2)O(2). CC -!- COFACTOR: Binds 1 manganese ion per subunit (By similarity). CC -!- SUBUNIT: Homotetramer. CC -!- INTERACTION: CC P54099:Polg; NbExp=2; IntAct=EBI-1635071, EBI-863636; CC P02340:Tp53; NbExp=2; IntAct=EBI-1635071, EBI-474016; CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix. CC -!- INDUCTION: Expression is regulated by KRIT1. CC -!- PTM: Nitrated under oxidative stress. Nitration coupled with CC oxidation inhibits the catalytic activity (By similarity). CC -!- PTM: Acetylation at Lys-122 decreases enzymatic activity. CC Deacetylated by SIRT3 upon exposure to ionizing radiations or CC after long fasting. CC -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase CC family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X04972; CAA28645.1; -; mRNA. DR EMBL; Z18857; CAA79308.1; -; mRNA. DR EMBL; L35528; AAB60902.1; -; Genomic_DNA. DR EMBL; L35525; AAB60902.1; JOINED; Genomic_DNA. DR EMBL; L35526; AAB60902.1; JOINED; Genomic_DNA. DR EMBL; L35527; AAB60902.1; JOINED; Genomic_DNA. DR EMBL; S78846; AAB34899.1; -; Genomic_DNA. DR EMBL; S78832; AAB34899.1; JOINED; Genomic_DNA. DR EMBL; S78842; AAB34899.1; JOINED; Genomic_DNA. DR EMBL; S78844; AAB34899.1; JOINED; Genomic_DNA. DR EMBL; AK002428; BAB22095.1; -; mRNA. DR EMBL; AK002534; BAB22170.1; -; mRNA. DR EMBL; AK012354; BAB28183.1; -; mRNA. DR EMBL; BC010548; AAH10548.1; -; mRNA. DR EMBL; BC018173; AAH18173.1; -; mRNA. DR PIR; I57023; I57023. DR RefSeq; NP_038699.2; NM_013671.3. DR UniGene; Mm.290876; -. DR ProteinModelPortal; P09671; -. DR SMR; P09671; 25-222. DR BioGrid; 203388; 1. DR IntAct; P09671; 5. DR MINT; MINT-1861884; -. DR PhosphoSite; P09671; -. DR REPRODUCTION-2DPAGE; IPI00109109; -. DR REPRODUCTION-2DPAGE; P09671; -. DR SWISS-2DPAGE; P09671; -. DR PaxDb; P09671; -. DR PRIDE; P09671; -. DR Ensembl; ENSMUST00000007012; ENSMUSP00000007012; ENSMUSG00000006818. DR GeneID; 20656; -. DR KEGG; mmu:20656; -. DR UCSC; uc008alv.1; mouse. DR CTD; 6648; -. DR MGI; MGI:98352; Sod2. DR eggNOG; COG0605; -. DR HOGENOM; HOG000013583; -. DR HOVERGEN; HBG004451; -. DR InParanoid; P09671; -. DR KO; K04564; -. DR OMA; EQVYDHQ; -. DR OrthoDB; EOG7FV3R5; -. DR TreeFam; TF105132; -. DR ChiTaRS; SOD2; mouse. DR NextBio; 299085; -. DR PRO; PR:P09671; -. DR ArrayExpress; P09671; -. DR Bgee; P09671; -. DR CleanEx; MM_SOD2; -. DR Genevestigator; P09671; -. DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:MGI. DR GO; GO:0042645; C:mitochondrial nucleoid; IEA:Ensembl. DR GO; GO:0003677; F:DNA binding; IEA:Ensembl. DR GO; GO:0030145; F:manganese ion binding; ISS:UniProtKB. DR GO; GO:0019825; F:oxygen binding; IEA:Ensembl. DR GO; GO:0004784; F:superoxide dismutase activity; ISS:UniProtKB. DR GO; GO:0001315; P:age-dependent response to reactive oxygen species; ISS:UniProtKB. DR GO; GO:0071361; P:cellular response to ethanol; IEA:Ensembl. DR GO; GO:0003032; P:detection of oxygen; IMP:MGI. DR GO; GO:0048773; P:erythrophore differentiation; IMP:MGI. DR GO; GO:0006749; P:glutathione metabolic process; IMP:MGI. DR GO; GO:0007507; P:heart development; IMP:MGI. DR GO; GO:0030097; P:hemopoiesis; IMP:MGI. DR GO; GO:0050665; P:hydrogen peroxide biosynthetic process; IEA:Ensembl. DR GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IMP:MGI. DR GO; GO:0008631; P:intrinsic apoptotic signaling pathway in response to oxidative stress; IMP:MGI. DR GO; GO:0055072; P:iron ion homeostasis; IMP:MGI. DR GO; GO:0001889; P:liver development; IMP:MGI. DR GO; GO:0007626; P:locomotory behavior; IMP:MGI. DR GO; GO:0045599; P:negative regulation of fat cell differentiation; IMP:MGI. DR GO; GO:0048147; P:negative regulation of fibroblast proliferation; IDA:MGI. DR GO; GO:1902176; P:negative regulation of intrinsic apoptotic signaling pathway in response to oxidative stress; IEA:Ensembl. DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IEA:Ensembl. DR GO; GO:0048666; P:neuron development; IMP:MGI. DR GO; GO:0032364; P:oxygen homeostasis; IEA:Ensembl. DR GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; IMP:MGI. DR GO; GO:0009791; P:post-embryonic development; IMP:MGI. DR GO; GO:0051289; P:protein homotetramerization; IEA:Ensembl. DR GO; GO:0050790; P:regulation of catalytic activity; IMP:MGI. DR GO; GO:0051881; P:regulation of mitochondrial membrane potential; IMP:MGI. DR GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; ISS:UniProtKB. DR GO; GO:0001836; P:release of cytochrome c from mitochondria; IMP:MGI. DR GO; GO:0019430; P:removal of superoxide radicals; IMP:MGI. DR GO; GO:0022904; P:respiratory electron transport chain; IMP:MGI. DR GO; GO:0014823; P:response to activity; IMP:MGI. DR GO; GO:0048678; P:response to axon injury; IMP:MGI. DR GO; GO:0046686; P:response to cadmium ion; IEA:Ensembl. DR GO; GO:0042493; P:response to drug; IEA:Ensembl. DR GO; GO:0051602; P:response to electrical stimulus; IEA:Ensembl. DR GO; GO:0010332; P:response to gamma radiation; IGI:MGI. DR GO; GO:0042542; P:response to hydrogen peroxide; IMP:MGI. DR GO; GO:0055093; P:response to hyperoxia; IMP:MGI. DR GO; GO:0001666; P:response to hypoxia; IEA:Ensembl. DR GO; GO:0033591; P:response to L-ascorbic acid; IEA:Ensembl. DR GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl. DR GO; GO:0010042; P:response to manganese ion; IEA:Ensembl. DR GO; GO:0010269; P:response to selenium ion; IEA:Ensembl. DR GO; GO:0034021; P:response to silicon dioxide; IEA:Ensembl. DR GO; GO:0010043; P:response to zinc ion; IEA:Ensembl. DR GO; GO:0042554; P:superoxide anion generation; IMP:MGI. DR GO; GO:0003069; P:vasodilation by acetylcholine involved in regulation of systemic arterial blood pressure; IMP:MGI. DR InterPro; IPR001189; Mn/Fe_SOD. DR InterPro; IPR019833; Mn/Fe_SOD_BS. DR InterPro; IPR019832; Mn/Fe_SOD_C. DR InterPro; IPR019831; Mn/Fe_SOD_N. DR PANTHER; PTHR11404; PTHR11404; 1. DR Pfam; PF02777; Sod_Fe_C; 1. DR Pfam; PF00081; Sod_Fe_N; 1. DR PIRSF; PIRSF000349; SODismutase; 1. DR PRINTS; PR01703; MNSODISMTASE. DR SUPFAM; SSF46609; SSF46609; 1. DR SUPFAM; SSF54719; SSF54719; 1. DR PROSITE; PS00088; SOD_MN; 1. PE 1: Evidence at protein level; KW Acetylation; Complete proteome; Direct protein sequencing; Manganese; KW Metal-binding; Mitochondrion; Nitration; Oxidoreductase; KW Reference proteome; Transit peptide. FT TRANSIT 1 24 Mitochondrion. FT CHAIN 25 222 Superoxide dismutase [Mn], mitochondrial. FT /FTId=PRO_0000032871. FT METAL 50 50 Manganese (By similarity). FT METAL 98 98 Manganese (By similarity). FT METAL 183 183 Manganese (By similarity). FT METAL 187 187 Manganese (By similarity). FT MOD_RES 58 58 Nitrated tyrosine (By similarity). FT MOD_RES 68 68 N6-acetyllysine; alternate. FT MOD_RES 68 68 N6-succinyllysine; alternate. FT MOD_RES 75 75 N6-acetyllysine; alternate. FT MOD_RES 75 75 N6-succinyllysine; alternate. FT MOD_RES 114 114 N6-acetyllysine. FT MOD_RES 122 122 N6-acetyllysine; alternate. FT MOD_RES 122 122 N6-succinyllysine; alternate. FT MOD_RES 130 130 N6-acetyllysine; alternate. FT MOD_RES 130 130 N6-succinyllysine; alternate. FT MOD_RES 202 202 N6-acetyllysine. FT MUTAGEN 122 122 K->R: Reverses IR-Induced increases in FT superoxide and genomic Instability in FT SIRT3-deficient mice. FT CONFLICT 5 5 A -> G (in Ref. 5; AAH18173). FT CONFLICT 18 18 G -> V (in Ref. 1; CAA28645). FT CONFLICT 138 138 V -> M (in Ref. 1 and 3). SQ SEQUENCE 222 AA; 24603 MW; 9AE804C55A8357D9 CRC64; MLCRAACSTG RRLGPVAGAA GSRHKHSLPD LPYDYGALEP HINAQIMQLH HSKHHAAYVN NLNATEEKYH EALAKGDVTT QVALQPALKF NGGGHINHTI FWTNLSPKGG GEPKGELLEA IKRDFGSFEK FKEKLTAVSV GVQGSGWGWL GFNKEQGRLQ IAACSNQDPL QGTTGLIPLL GIDVWEHAYY LQYKNVRPDY LKAIWNVINW ENVTERYTAC KK // ID SOX_MOUSE Reviewed; 390 AA. AC Q9D826; O55223; DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 19-MAR-2014, entry version 99. DE RecName: Full=Peroxisomal sarcosine oxidase; DE Short=PSO; DE EC=1.5.3.1; DE EC=1.5.3.7; DE AltName: Full=L-pipecolate oxidase; DE AltName: Full=L-pipecolic acid oxidase; GN Name=Pipox; Synonyms=Pso; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Embryo; RX PubMed=9441754; DOI=10.1006/geno.1997.5050; RA Herbst R., Barton J.L., Nicklin M.J.H.; RT "A mammalian homolog of the bacterial monomeric sarcosine oxidases RT maps to mouse chromosome 11, close to Cryba1."; RL Genomics 46:480-482(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Small intestine; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Kidney; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-126 AND LYS-287, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23576753; DOI=10.1073/pnas.1302961110; RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., RA Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.; RT "Label-free quantitative proteomics of the lysine acetylome in RT mitochondria identifies substrates of SIRT3 in metabolic pathways."; RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013). CC -!- FUNCTION: Metabolizes sarcosine, L-pipecolic acid and L-proline CC (By similarity). CC -!- CATALYTIC ACTIVITY: Sarcosine + H(2)O + O(2) = glycine + CC formaldehyde + H(2)O(2). CC -!- CATALYTIC ACTIVITY: L-pipecolate + O(2) = (S)-2,3,4,5- CC tetrahydropyridine-2-carboxylate + H(2)O(2). CC -!- COFACTOR: Binds 1 FAD per subunit. CC -!- SUBUNIT: Monomer (By similarity). CC -!- SUBCELLULAR LOCATION: Peroxisome (By similarity). CC -!- TISSUE SPECIFICITY: Kidney and liver. CC -!- SIMILARITY: Belongs to the MSOX/MTOX family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U94700; AAC39948.1; -; mRNA. DR EMBL; AK008555; BAB25741.1; -; mRNA. DR EMBL; BC013525; AAH13525.1; -; mRNA. DR RefSeq; NP_032978.2; NM_008952.2. DR UniGene; Mm.8543; -. DR ProteinModelPortal; Q9D826; -. DR SMR; Q9D826; 7-381. DR IntAct; Q9D826; 4. DR MINT; MINT-1850149; -. DR PhosphoSite; Q9D826; -. DR PaxDb; Q9D826; -. DR PRIDE; Q9D826; -. DR Ensembl; ENSMUST00000017597; ENSMUSP00000017597; ENSMUSG00000017453. DR GeneID; 19193; -. DR KEGG; mmu:19193; -. DR UCSC; uc007khm.2; mouse. DR CTD; 51268; -. DR MGI; MGI:1197006; Pipox. DR eggNOG; COG0665; -. DR GeneTree; ENSGT00390000011000; -. DR HOGENOM; HOG000236097; -. DR HOVERGEN; HBG023161; -. DR InParanoid; Q9D826; -. DR KO; K00306; -. DR OMA; ILCRFVR; -. DR OrthoDB; EOG71RXJP; -. DR TreeFam; TF313837; -. DR NextBio; 295904; -. DR PRO; PR:Q9D826; -. DR ArrayExpress; Q9D826; -. DR Bgee; Q9D826; -. DR CleanEx; MM_PIPOX; -. DR Genevestigator; Q9D826; -. DR GO; GO:0005777; C:peroxisome; IDA:HGNC. DR GO; GO:0050031; F:L-pipecolate oxidase activity; ISS:UniProtKB. DR GO; GO:0008115; F:sarcosine oxidase activity; ISS:UniProtKB. DR GO; GO:0033514; P:L-lysine catabolic process to acetyl-CoA via L-pipecolate; ISS:UniProtKB. DR GO; GO:0046653; P:tetrahydrofolate metabolic process; IEA:InterPro. DR InterPro; IPR006076; FAD-dep_OxRdtase. DR InterPro; IPR006281; SoxA_mon. DR Pfam; PF01266; DAO; 1. DR TIGRFAMs; TIGR01377; soxA_mon; 1. PE 1: Evidence at protein level; KW Acetylation; Complete proteome; FAD; Flavoprotein; Oxidoreductase; KW Peroxisome; Reference proteome. FT CHAIN 1 390 Peroxisomal sarcosine oxidase. FT /FTId=PRO_0000213774. FT NP_BIND 9 39 FAD (Potential). FT MOTIF 388 390 Microbody targeting signal (Potential). FT MOD_RES 126 126 N6-acetyllysine. FT MOD_RES 287 287 N6-acetyllysine. FT MOD_RES 319 319 S-8alpha-FAD cysteine (Probable). FT CONFLICT 164 164 Q -> H (in Ref. 1; AAC39948). FT CONFLICT 333 333 C -> W (in Ref. 1; AAC39948). FT CONFLICT 352 352 K -> T (in Ref. 1; AAC39948). SQ SEQUENCE 390 AA; 43847 MW; 0C33A96A24731EE0 CRC64; MAAQTDFWDA IVIGAGIQGC FTAYHLAKHS KSVLLLEQFF LPHSRGSSHG QSRIIRKAYP EDFYTMMMKE CYQTWAQLER EAGTQLHRQT ELLLLGTKEN PGLKTIQATL SRQGIDHEYL SSVDLKQRFP NIRFTRGEVG LLDKTGGVLY ADKALRALQH IICQLGGTVC DGEKVVEIRP GLPVTVKTTL KSYQANSLVI TAGPWTNRLL HPLGIELPLQ TLRINVCYWR EKVPGSYGVS QAFPCILGLD LAPHHIYGLP ASEYPGLMKI CYHHGDNVDP EERDCPKTFS DIQDVQILCH FVRDHLPGLR AEPDIMERCM YTNTPDEHFI LDCHPKYDNI VIGAGFSGHG FKLAPVVGKI LYELSMKLPP SYDLAPFRMS RFSTLSKAHL // ID SPRE_MOUSE Reviewed; 261 AA. AC Q64105; Q63996; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 22-JAN-2014, entry version 109. DE RecName: Full=Sepiapterin reductase; DE Short=SPR; DE EC=1.1.1.153; GN Name=Spr; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=7873607; DOI=10.1016/0167-4781(94)00225-R; RA Ota A., Ichinose H., Nagatsu T.; RT "Mouse sepiapterin reductase: an enzyme involved in the final step of RT tetrahydrobiopterin biosynthesis. Primary structure deduced from the RT cDNA sequence."; RL Biochim. Biophys. Acta 1260:320-322(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=129; RX PubMed=10209270; DOI=10.1016/S0167-4781(99)00030-5; RA Lee S.W., Park I.Y., Hahn Y., Lee J.E., Seong C.S., Chung J.H., RA Park Y.S.; RT "Cloning of mouse sepiapterin reductase gene and characterization of RT its promoter region."; RL Biochim. Biophys. Acta 1445:165-171(1999). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] OF 209-261. RX PubMed=8304109; RA Maier J., Schott K., Werner T., Bacher A., Ziegler I.; RT "Northern blot analysis of sepiapterin reductase mRNA in mammalian RT cell lines and tissues."; RL Adv. Exp. Med. Biol. 338:195-198(1993). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] OF 209-255. RX PubMed=8440319; DOI=10.1006/excr.1993.1027; RA Maier J., Schott K., Werner T., Bacher A., Ziegler I.; RT "Detection of a novel sepiapterin reductase mRNA: assay of mRNA in RT various cells and tissues of various species."; RL Exp. Cell Res. 204:217-222(1993). RN [5] RP X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS) IN COMPLEXES WITH PTERIN; RP N-ACETYL SEROTONIN AND NADP, ENZYME MECHANISM, AND SUBUNIT. RX PubMed=9405351; DOI=10.1093/emboj/16.24.7219; RA Auerbach G., Herrmann A., Gutlich M., Fischer M., Jacob U., Bacher A., RA Huber R.; RT "The 1.25-A crystal structure of sepiapterin reductase reveals its RT binding mode to pterins and brain neurotransmitters."; RL EMBO J. 16:7219-7230(1997). CC -!- FUNCTION: Catalyzes the final one or two reductions in tetra- CC hydrobiopterin biosynthesis to form 5,6,7,8-tetrahydrobiopterin. CC -!- CATALYTIC ACTIVITY: L-erythro-7,8-dihydrobiopterin + NADP(+) = CC sepiapterin + NADPH. CC -!- CATALYTIC ACTIVITY: L-erythro-tetrahydrobiopterin + 2 NADP(+) = 6- CC pyruvoyl-5,6,7,8-tetrahydropterin + 2 NADPH. CC -!- SUBUNIT: Homodimer. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the sepiapterin reductase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; S77493; AAB33611.1; -; mRNA. DR EMBL; U78077; AAC69364.1; -; Genomic_DNA. DR EMBL; U78076; AAC69364.1; JOINED; Genomic_DNA. DR EMBL; S71375; -; NOT_ANNOTATED_CDS; mRNA. DR PIR; S52110; S52110. DR UniGene; Mm.28393; -. DR PDB; 1NAS; X-ray; 2.10 A; A=3-261. DR PDB; 1OAA; X-ray; 1.25 A; A=3-261. DR PDB; 1SEP; X-ray; 1.95 A; A=1-261. DR PDBsum; 1NAS; -. DR PDBsum; 1OAA; -. DR PDBsum; 1SEP; -. DR ProteinModelPortal; Q64105; -. DR SMR; Q64105; 3-261. DR MINT; MINT-1869513; -. DR STRING; 10090.ENSMUSP00000048111; -. DR PhosphoSite; Q64105; -. DR REPRODUCTION-2DPAGE; Q64105; -. DR PaxDb; Q64105; -. DR PRIDE; Q64105; -. DR MGI; MGI:103078; Spr. DR eggNOG; COG1028; -. DR HOVERGEN; HBG006973; -. DR InParanoid; Q64105; -. DR ChiTaRS; SPR; mouse. DR EvolutionaryTrace; Q64105; -. DR PRO; PR:Q64105; -. DR CleanEx; MM_SPR; -. DR Genevestigator; Q64105; -. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR GO; GO:0004757; F:sepiapterin reductase activity; ISS:UniProtKB. DR GO; GO:0048667; P:cell morphogenesis involved in neuron differentiation; IMP:MGI. DR GO; GO:0016265; P:death; IMP:MGI. DR GO; GO:0042417; P:dopamine metabolic process; IMP:MGI. DR GO; GO:0006558; P:L-phenylalanine metabolic process; IMP:MGI. DR GO; GO:0042415; P:norepinephrine metabolic process; IMP:MGI. DR GO; GO:0019889; P:pteridine metabolic process; IMP:MGI. DR GO; GO:0040014; P:regulation of multicellular organism growth; IMP:MGI. DR GO; GO:0042428; P:serotonin metabolic process; IMP:MGI. DR GO; GO:0006729; P:tetrahydrobiopterin biosynthetic process; IEA:InterPro. DR GO; GO:0046146; P:tetrahydrobiopterin metabolic process; IMP:MGI. DR GO; GO:0050882; P:voluntary musculoskeletal movement; IMP:MGI. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR002198; DH_sc/Rdtase_SDR. DR InterPro; IPR002347; Glc/ribitol_DH. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR006393; Sepiapterin_red. DR Pfam; PF00106; adh_short; 1. DR PRINTS; PR00081; GDHRDH. DR TIGRFAMs; TIGR01500; sepiapter_red; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Complete proteome; Cytoplasm; NADP; KW Oxidoreductase; Phosphoprotein; Reference proteome. FT CHAIN 1 261 Sepiapterin reductase. FT /FTId=PRO_0000072150. FT NP_BIND 15 21 NADP. FT NP_BIND 43 44 NADP. FT NP_BIND 70 71 NADP. FT NP_BIND 202 207 NADP. FT REGION 158 159 Substrate binding. FT BINDING 171 171 Substrate. FT BINDING 175 175 NADP. FT BINDING 200 200 Substrate; via amide nitrogen. FT BINDING 222 222 Substrate. FT BINDING 258 258 Substrate. FT MOD_RES 1 1 N-acetylmethionine (By similarity). FT MOD_RES 46 46 Phosphoserine (By similarity). FT MOD_RES 196 196 Phosphoserine (By similarity). FT MOD_RES 214 214 Phosphoserine (By similarity). FT CONFLICT 4 4 D -> G (in Ref. 2; AAC69364). FT STRAND 7 15 FT HELIX 19 29 FT STRAND 37 43 FT HELIX 45 58 FT STRAND 62 68 FT HELIX 74 86 FT STRAND 95 100 FT HELIX 112 114 FT HELIX 118 128 FT HELIX 130 141 FT STRAND 150 156 FT HELIX 159 161 FT HELIX 169 188 FT STRAND 192 198 FT STRAND 201 204 FT HELIX 205 213 FT HELIX 217 228 FT HELIX 235 248 FT STRAND 255 258 SQ SEQUENCE 261 AA; 27883 MW; 102294E439CB8AEC CRC64; MEADGLGCAV CVLTGASRGF GRALAPQLAR LLSPGSVMLV SARSESMLRQ LKEELGAQQP DLKVVLAAAD LGTEAGVQRL LSAVRELPRP EGLQRLLLIN NAATLGDVSK GFLNVNDLAE VNNYWALNLT SMLCLTSGTL NAFQDSPGLS KTVVNISSLC ALQPYKGWGL YCAGKAARDM LYQVLAAEEP SVRVLSYAPG PLDNDMQQLA RETSKDPELR SKLQKLKSDG ALVDCGTSAQ KLLGLLQKDT FQSGAHVDFY D // ID SQRD_MOUSE Reviewed; 450 AA. AC Q9R112; Q8BW20; Q91XA1; Q9D891; DT 13-DEC-2002, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 3. DT 19-MAR-2014, entry version 100. DE RecName: Full=Sulfide:quinone oxidoreductase, mitochondrial; DE EC=1.-.-.-; DE Flags: Precursor; GN Name=Sqrdl; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=C57BL/6 X CBA; TISSUE=Liver; RA Huang L., Gitschier J.; RT "Positional cloning of the pallid gene in the pallid mutant."; RL Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Kidney, and Small intestine; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Liver; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-134 AND LYS-173, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23576753; DOI=10.1073/pnas.1302961110; RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., RA Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.; RT "Label-free quantitative proteomics of the lysine acetylome in RT mitochondria identifies substrates of SIRT3 in metabolic pathways."; RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013). CC -!- FUNCTION: Catalyzes the oxidation of hydrogen sulfide, with the CC help of a quinone (By similarity). CC -!- COFACTOR: Binds 1 FAD per subunit (By similarity). CC -!- SUBCELLULAR LOCATION: Mitochondrion (Probable). CC -!- SIMILARITY: Belongs to the SQRD family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF174535; AAD50300.1; -; mRNA. DR EMBL; AK008290; BAB25580.1; -; mRNA. DR EMBL; AK075598; BAC35847.1; -; mRNA. DR EMBL; AL928950; CAM26699.1; -; Genomic_DNA. DR EMBL; BC011153; AAH11153.1; -; mRNA. DR RefSeq; NP_001155975.1; NM_001162503.1. DR RefSeq; NP_067482.4; NM_021507.5. DR RefSeq; XP_006500029.1; XM_006499966.1. DR UniGene; Mm.28986; -. DR ProteinModelPortal; Q9R112; -. DR SMR; Q9R112; 42-404. DR BioGrid; 208481; 1. DR IntAct; Q9R112; 3. DR MINT; MINT-4112946; -. DR STRING; 10090.ENSMUSP00000106133; -. DR PhosphoSite; Q9R112; -. DR PaxDb; Q9R112; -. DR PRIDE; Q9R112; -. DR DNASU; 59010; -. DR Ensembl; ENSMUST00000005953; ENSMUSP00000005953; ENSMUSG00000005803. DR Ensembl; ENSMUST00000110506; ENSMUSP00000106133; ENSMUSG00000005803. DR GeneID; 59010; -. DR KEGG; mmu:59010; -. DR UCSC; uc008mbh.2; mouse. DR CTD; 58472; -. DR MGI; MGI:1929899; Sqrdl. DR eggNOG; COG0446; -. DR GeneTree; ENSGT00390000019406; -. DR HOGENOM; HOG000249874; -. DR HOVERGEN; HBG029110; -. DR InParanoid; Q8BW20; -. DR KO; K17218; -. DR OMA; DKHYYQP; -. DR OrthoDB; EOG79SDXB; -. DR TreeFam; TF314384; -. DR NextBio; 314552; -. DR PRO; PR:Q9R112; -. DR ArrayExpress; Q9R112; -. DR Bgee; Q9R112; -. DR CleanEx; MM_SQRDL; -. DR Genevestigator; Q9R112; -. DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:MGI. DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW. DR InterPro; IPR023753; Pyr_nucl-diS_OxRdtase_FAD/NAD. DR InterPro; IPR015904; Sulphide_quinone_reductase. DR PANTHER; PTHR10632; PTHR10632; 1. DR Pfam; PF07992; Pyr_redox_2; 1. PE 1: Evidence at protein level; KW Acetylation; Complete proteome; FAD; Flavoprotein; Mitochondrion; KW NADP; Oxidoreductase; Reference proteome; Transit peptide. FT TRANSIT 1 ? Mitochondrion (Potential). FT CHAIN ? 450 Sulfide:quinone oxidoreductase, FT mitochondrial. FT /FTId=PRO_0000022409. FT MOD_RES 134 134 N6-acetyllysine. FT MOD_RES 173 173 N6-acetyllysine. FT CONFLICT 6 6 T -> A (in Ref. 3; AAH11153). FT CONFLICT 99 99 S -> T (in Ref. 2; BAB25580). FT CONFLICT 184 184 G -> D (in Ref. 1; AAD50300 and 3; FT AAH11153). FT CONFLICT 185 185 F -> L (in Ref. 1; AAD50300). SQ SEQUENCE 450 AA; 50282 MW; CBA500CE60803C8F CRC64; MAPLVTVVSS PRARLFACFL RLGTQQAGPL QLHTGACCTA KNHYEVLVLG GGAGGITMAT RMKRRVGAEN VAIVEPSERH FYQPIWTLVG AGAKELSLSV RSTLSVIPSG VQWIQDRVAE LNPDENCIRT DSGKEISYRY LIIALGIQLD YEKIKGLPEG FAYPKIGSNY SVKTVEKTWK ALQGFKEGNA LFTFPNTPVK CAGAPQKIMY LSEAYFRKTG KRPKANIIFN TALGTIFGVK KYADALQEII RERDVSVNYK HNLIEVRPDK QEAVFEILDK PGETHVIPYE MLHVTPPMSA PDVLKRSPVA DSAGWVDVDK ETLQHKKYPN VFGIGDCTNL PTSKTAAAVA AQSGILDRTM CLIMKNQRPI KKYDGYTSCP LVTGYNRVIL AEFDYTAQPL ETFPFDQSKE RITMYLMKAD MMPFLYWNMM LRGYWGGPAF LRKLFHLGMN // ID SRXN1_MOUSE Reviewed; 136 AA. AC Q9D975; Q3TWN6; Q91VN5; DT 30-APR-2003, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 22-JAN-2014, entry version 86. DE RecName: Full=Sulfiredoxin-1; DE EC=1.8.98.2; DE AltName: Full=Neoplastic progression protein 3; GN Name=Srxn1; Synonyms=Npn3, Srx; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Mammary carcinoma, and Testis; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Mammary gland, and Retina; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP FUNCTION. RX PubMed=15448164; DOI=10.1074/jbc.M409482200; RA Chang T.-S., Jeong W., Woo H.A., Lee S.M., Park S., Rhee S.G.; RT "Characterization of mammalian sulfiredoxin and its reactivation of RT hyperoxidized peroxiredoxin through reduction of cysteine sulfinic RT acid in the active site to cysteine."; RL J. Biol. Chem. 279:50994-51001(2004). CC -!- FUNCTION: Contributes to oxidative stress resistance by reducing CC cysteine-sulfinic acid formed under exposure to oxidants in the CC peroxiredoxins PRDX1, PRDX2, PRDX3 and PRDX4. Does not act on CC PRDX5 or PRDX6. May catalyze the reduction in a multi-step process CC by acting both as a specific phosphotransferase and a CC thioltransferase. CC -!- CATALYTIC ACTIVITY: Peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP CC + 2 R-SH = peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + CC R-S-S-R. CC -!- COFACTOR: Magnesium (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the sulfiredoxin family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK007296; BAB24939.1; -; mRNA. DR EMBL; AK089976; BAC41025.1; -; mRNA. DR EMBL; AK159613; BAE35230.1; -; mRNA. DR EMBL; BC011325; AAH11325.1; -; mRNA. DR EMBL; BC049957; AAH49957.1; -; mRNA. DR RefSeq; NP_083964.2; NM_029688.5. DR UniGene; Mm.218639; -. DR ProteinModelPortal; Q9D975; -. DR SMR; Q9D975; 31-136. DR PhosphoSite; Q9D975; -. DR PRIDE; Q9D975; -. DR Ensembl; ENSMUST00000099225; ENSMUSP00000096830; ENSMUSG00000032802. DR GeneID; 76650; -. DR KEGG; mmu:76650; -. DR UCSC; uc008new.1; mouse. DR CTD; 140809; -. DR MGI; MGI:104971; Srxn1. DR eggNOG; COG5119; -. DR GeneTree; ENSGT00390000007832; -. DR HOGENOM; HOG000231799; -. DR HOVERGEN; HBG080441; -. DR InParanoid; Q9D975; -. DR KO; K12260; -. DR NextBio; 345548; -. DR PRO; PR:Q9D975; -. DR ArrayExpress; Q9D975; -. DR Bgee; Q9D975; -. DR CleanEx; MM_SRXN1; -. DR Genevestigator; Q9D975; -. DR GO; GO:0005829; C:cytosol; ISS:UniProtKB. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016667; F:oxidoreductase activity, acting on a sulfur group of donors; IDA:UniProtKB. DR GO; GO:0032542; F:sulfiredoxin activity; IEA:UniProtKB-EC. DR GO; GO:0006979; P:response to oxidative stress; IDA:UniProtKB. DR InterPro; IPR003115; ParB/Sulfiredoxin_dom. DR InterPro; IPR016692; Sulfiredoxin. DR PANTHER; PTHR21348; PTHR21348; 1. DR Pfam; PF02195; ParBc; 1. DR PIRSF; PIRSF017267; Sulfiredoxin; 1. DR SUPFAM; SSF110849; SSF110849; 1. PE 2: Evidence at transcript level; KW Antioxidant; ATP-binding; Complete proteome; Cytoplasm; KW Disulfide bond; Magnesium; Nucleotide-binding; Oxidoreductase; KW Reference proteome. FT CHAIN 1 136 Sulfiredoxin-1. FT /FTId=PRO_0000211432. FT NP_BIND 97 100 ATP (By similarity). FT DISULFID 98 98 Interchain (By similarity). FT CONFLICT 20 22 EGQ -> VVH (in Ref. 2; AAH11325). SQ SEQUENCE 136 AA; 14149 MW; D8BCDAC6277E27DE CRC64; MGLRAGGALR RAGAGPGAPE GQGPGGAQGG SIHSGCIATV HNVPIAVLIR PLPSVLDPAK VQSLVDTILA DPDSVPPIDV LWIKGAQGGD YYYSFGGCHR YAAYQQLQRE TIPAKLVRST LSDLRMYLGA STPDLQ // ID SSDH_MOUSE Reviewed; 523 AA. AC Q8BWF0; Q5SZW1; DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 19-MAR-2014, entry version 108. DE RecName: Full=Succinate-semialdehyde dehydrogenase, mitochondrial; DE EC=1.2.1.24; DE AltName: Full=Aldehyde dehydrogenase family 5 member A1; DE AltName: Full=NAD(+)-dependent succinic semialdehyde dehydrogenase; DE Flags: Precursor; GN Name=Aldh5a1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Kidney; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [3] RP PROTEIN SEQUENCE OF 57-87; 115-123; 129-160; 162-172; 181-201; RP 254-289; 291-320; 323-333; 339-347; 358-375; 401-436; 469-496 AND RP 507-516, AND MASS SPECTROMETRY. RC STRAIN=C57BL/6, and OF1; TISSUE=Brain, and Hippocampus; RA Lubec G., Klug S., Kang S.U., Sunyer B., Chen W.-Q.; RL Submitted (JAN-2009) to UniProtKB. RN [4] RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-114; LYS-123; LYS-172; RP LYS-253; LYS-347 AND LYS-390, AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., RA Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). RN [5] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-74; LYS-114; LYS-128; RP LYS-253; LYS-347; LYS-353 AND LYS-399, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23576753; DOI=10.1073/pnas.1302961110; RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., RA Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.; RT "Label-free quantitative proteomics of the lysine acetylome in RT mitochondria identifies substrates of SIRT3 in metabolic pathways."; RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013). CC -!- FUNCTION: Catalyzes one step in the degradation of the inhibitory CC neurotransmitter gamma-aminobutyric acid (GABA) (By similarity). CC -!- CATALYTIC ACTIVITY: Succinate semialdehyde + NAD(+) + H(2)O = CC succinate + NADH. CC -!- ENZYME REGULATION: Redox-regulated. Inhibited under oxydizing CC conditions (By similarity). CC -!- PATHWAY: Amino-acid degradation; 4-aminobutanoate degradation. CC -!- SUBUNIT: Homotetramer (By similarity). CC -!- SUBCELLULAR LOCATION: Mitochondrion (By similarity). CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK052703; BAC35105.1; -; mRNA. DR EMBL; AK144030; BAE25663.1; -; mRNA. DR EMBL; AL589699; CAI26086.1; -; Genomic_DNA. DR RefSeq; NP_766120.1; NM_172532.3. DR UniGene; Mm.393311; -. DR ProteinModelPortal; Q8BWF0; -. DR SMR; Q8BWF0; 44-523. DR IntAct; Q8BWF0; 3. DR MINT; MINT-1861868; -. DR STRING; 10090.ENSMUSP00000040591; -. DR PhosphoSite; Q8BWF0; -. DR PaxDb; Q8BWF0; -. DR PRIDE; Q8BWF0; -. DR Ensembl; ENSMUST00000037615; ENSMUSP00000040591; ENSMUSG00000035936. DR GeneID; 214579; -. DR KEGG; mmu:214579; -. DR UCSC; uc007pwp.2; mouse. DR CTD; 7915; -. DR MGI; MGI:2441982; Aldh5a1. DR eggNOG; COG1012; -. DR GeneTree; ENSGT00740000115598; -. DR HOGENOM; HOG000271509; -. DR HOVERGEN; HBG108515; -. DR InParanoid; Q8BWF0; -. DR KO; K00139; -. DR OMA; EIKYICM; -. DR OrthoDB; EOG72G173; -. DR TreeFam; TF352906; -. DR UniPathway; UPA00733; -. DR ChiTaRS; ALDH5A1; mouse. DR NextBio; 374368; -. DR PRO; PR:Q8BWF0; -. DR ArrayExpress; Q8BWF0; -. DR Bgee; Q8BWF0; -. DR CleanEx; MM_ALDH5A1; -. DR Genevestigator; Q8BWF0; -. DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB. DR GO; GO:0004777; F:succinate-semialdehyde dehydrogenase (NAD+) activity; ISS:UniProtKB. DR GO; GO:0009013; F:succinate-semialdehyde dehydrogenase [NAD(P)+] activity; IEA:InterPro. DR GO; GO:0006083; P:acetate metabolic process; IMP:MGI. DR GO; GO:0007417; P:central nervous system development; ISS:UniProtKB. DR GO; GO:0006681; P:galactosylceramide metabolic process; IMP:MGI. DR GO; GO:0009450; P:gamma-aminobutyric acid catabolic process; ISS:UniProtKB. DR GO; GO:0006006; P:glucose metabolic process; IMP:MGI. DR GO; GO:0006678; P:glucosylceramide metabolic process; IMP:MGI. DR GO; GO:0006536; P:glutamate metabolic process; IMP:MGI. DR GO; GO:0006541; P:glutamine metabolic process; IMP:MGI. DR GO; GO:0006749; P:glutathione metabolic process; IMP:MGI. DR GO; GO:0006650; P:glycerophospholipid metabolic process; IMP:MGI. DR GO; GO:0042135; P:neurotransmitter catabolic process; IMP:MGI. DR GO; GO:0009791; P:post-embryonic development; IMP:MGI. DR GO; GO:0051289; P:protein homotetramerization; IEA:Ensembl. DR GO; GO:0022904; P:respiratory electron transport chain; IMP:MGI. DR GO; GO:0046459; P:short-chain fatty acid metabolic process; IMP:MGI. DR GO; GO:0006105; P:succinate metabolic process; IMP:MGI. DR Gene3D; 3.40.309.10; -; 1. DR Gene3D; 3.40.605.10; -; 1. DR InterPro; IPR016161; Ald_DH/histidinol_DH. DR InterPro; IPR016163; Ald_DH_C. DR InterPro; IPR016160; Ald_DH_CS. DR InterPro; IPR016162; Ald_DH_N. DR InterPro; IPR015590; Aldehyde_DH_dom. DR InterPro; IPR010102; Succ_semiAld_DH. DR Pfam; PF00171; Aldedh; 1. DR SUPFAM; SSF53720; SSF53720; 1. DR TIGRFAMs; TIGR01780; SSADH; 1. DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1. DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1. PE 1: Evidence at protein level; KW Acetylation; Complete proteome; Direct protein sequencing; KW Disulfide bond; Mitochondrion; NAD; Oxidoreductase; KW Reference proteome; Transit peptide. FT TRANSIT 1 35 Mitochondrion (By similarity). FT CHAIN 36 523 Succinate-semialdehyde dehydrogenase, FT mitochondrial. FT /FTId=PRO_0000007185. FT NP_BIND 216 219 NAD (By similarity). FT NP_BIND 272 277 NAD (By similarity). FT ACT_SITE 294 294 Proton acceptor (By similarity). FT ACT_SITE 328 328 Nucleophile (By similarity). FT BINDING 201 201 NAD (By similarity). FT BINDING 201 201 Substrate (By similarity). FT BINDING 322 322 Substrate (By similarity). FT BINDING 486 486 Substrate (By similarity). FT SITE 193 193 Transition state stabilizer (By FT similarity). FT MOD_RES 74 74 N6-acetyllysine. FT MOD_RES 114 114 N6-acetyllysine; alternate. FT MOD_RES 114 114 N6-succinyllysine; alternate. FT MOD_RES 123 123 N6-succinyllysine. FT MOD_RES 128 128 N6-acetyllysine. FT MOD_RES 172 172 N6-succinyllysine. FT MOD_RES 253 253 N6-acetyllysine; alternate. FT MOD_RES 253 253 N6-succinyllysine; alternate. FT MOD_RES 347 347 N6-acetyllysine; alternate. FT MOD_RES 347 347 N6-succinyllysine; alternate. FT MOD_RES 353 353 N6-acetyllysine. FT MOD_RES 390 390 N6-succinyllysine. FT MOD_RES 399 399 N6-acetyllysine. FT DISULFID 328 330 In inhibited form (By similarity). SQ SEQUENCE 523 AA; 55968 MW; E0CF82E4F4FAE9D0 CRC64; MATCFLLRSF WAARPALPPP GRFRPEPAGT PRRSYASGPG GLHADLLRGD SFVGGRWLPA PATFPVYDPA SGAKLGTVAD CGVPEARAAV RAAYDAFNSW KGVSVKERSL LLRKWYDLMI QNKDDLAKII TAESGKPLKE AQGEILYSAL FLEWFSEEAR RIYGDIIYTS AKDKRGLVLK QPVGVAAIIT PWNFPSAMIT RKVGAALAAG CTVVVKPAED TPYSALALAQ LANQAGIPAG VYNVIPCSRN KAKEVGEVLC TDPLVSKISF TGSTATGKIL LHHAANSVKR VSMELGGLAP FIVFDSANVD QAVAGAMASK FRNAGQTCVC SNRFLVQRGI HDSFVTKFAE AMKKSLRVGN GFEEGTTQGP LINEKAVEKV EKQVNDAVAK GATVVTGGKR HQSGGNFFEP TLLSNVTRDM LCITEETFGP LAPVIKFDKE EEAVAIANAA EVGLAGYFYS QDPAQIWRVA EQLEVGMVGV NEGLISSVEC PFGGVKQSGL GREGSKYGID EYLEVKYVCY GGL // ID STEA1_MOUSE Reviewed; 339 AA. AC Q9CWR7; Q6P8X4; DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot. DT 10-MAY-2005, sequence version 2. DT 19-MAR-2014, entry version 87. DE RecName: Full=Metalloreductase STEAP1; DE EC=1.16.1.-; DE AltName: Full=Six-transmembrane epithelial antigen of prostate 1; GN Name=Steap1; Synonyms=Steap; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Kidney; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP FUNCTION, ENZYME ACTIVITY, AND SUBCELLULAR LOCATION. RX PubMed=16609065; DOI=10.1182/blood-2006-02-003681; RA Ohgami R.S., Campagna D.R., McDonald A., Fleming M.D.; RT "The Steap proteins are metalloreductases."; RL Blood 108:1388-1394(2006). RN [4] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic fibroblast; RX PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200; RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.; RT "Large scale localization of protein phosphorylation by use of RT electron capture dissociation mass spectrometry."; RL Mol. Cell. Proteomics 8:904-912(2009). CC -!- FUNCTION: Metalloreductase that has the ability to reduce both CC Fe(3+) to Fe(2+) and Cu(2+) to Cu(1+). Uses NAD(+) as acceptor. CC -!- COFACTOR: FAD (By similarity). CC -!- SUBCELLULAR LOCATION: Endosome membrane; Multi-pass membrane CC protein. CC -!- SIMILARITY: Belongs to the STEAP family. CC -!- SIMILARITY: Contains 1 ferric oxidoreductase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK010437; BAB26938.1; -; mRNA. DR EMBL; BC061023; AAH61023.1; -; mRNA. DR RefSeq; NP_081675.2; NM_027399.3. DR UniGene; Mm.85429; -. DR ProteinModelPortal; Q9CWR7; -. DR PhosphoSite; Q9CWR7; -. DR PRIDE; Q9CWR7; -. DR Ensembl; ENSMUST00000015796; ENSMUSP00000015796; ENSMUSG00000015652. DR GeneID; 70358; -. DR KEGG; mmu:70358; -. DR UCSC; uc008wjb.2; mouse. DR CTD; 26872; -. DR MGI; MGI:1917608; Steap1. DR eggNOG; NOG41654; -. DR GeneTree; ENSGT00390000008042; -. DR HOGENOM; HOG000252937; -. DR HOVERGEN; HBG062286; -. DR InParanoid; Q9CWR7; -. DR KO; K14737; -. DR OMA; IYSLSYP; -. DR OrthoDB; EOG7Z0JWH; -. DR TreeFam; TF332031; -. DR NextBio; 331442; -. DR PRO; PR:Q9CWR7; -. DR Bgee; Q9CWR7; -. DR Genevestigator; Q9CWR7; -. DR GO; GO:0005768; C:endosome; IDA:MGI. DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IDA:MGI. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW. DR GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW. DR GO; GO:0055072; P:iron ion homeostasis; IEA:UniProtKB-KW. DR InterPro; IPR013130; Fe3_Rdtase_TM_dom. DR Pfam; PF01794; Ferric_reduct; 1. PE 1: Evidence at protein level; KW Complete proteome; Copper; Electron transport; Endosome; FAD; KW Flavoprotein; Ion transport; Iron; Iron transport; Membrane; KW Metal-binding; NAD; Oxidoreductase; Phosphoprotein; KW Reference proteome; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 339 Metalloreductase STEAP1. FT /FTId=PRO_0000191695. FT TRANSMEM 79 99 Helical; (Potential). FT TRANSMEM 109 129 Helical; (Potential). FT TRANSMEM 164 184 Helical; (Potential). FT TRANSMEM 218 238 Helical; (Potential). FT TRANSMEM 258 278 Helical; (Potential). FT TRANSMEM 283 303 Helical; (Potential). FT DOMAIN 118 265 Ferric oxidoreductase. FT METAL 175 175 Iron (heme axial ligand) (By similarity). FT METAL 268 268 Iron (heme axial ligand) (By similarity). FT MOD_RES 28 28 Phosphoserine. FT CONFLICT 161 161 R -> K (in Ref. 1; BAB26938). SQ SEQUENCE 339 AA; 39292 MW; BF63B35AEE4356A0 CRC64; MEISDDVTNP EQLWKMKPKG NLEDDSYSTK DSGETSMLKR PGLSHLQHAV HVDAFDCPSE LQHTQEFFPN WRLPVKVAAI ISSLTFLYTL LREIIYPLVT SREQYFYKIP ILVINKVLPM VAITLLALVY LPGELAAVVQ LRNGTKYKKF PPWLDRWMLA RKQFGLLSFF FAVLHAVYSL SYPMRRSYRY KLLNWAYKQV QQNKEDAWVE HDVWRMEIYV SLGIVGLAIL ALLAVTSIPS VSDSLTWREF HYIQSKLGIV SLLLGTVHAL VFAWNKWVDV SQFVWYMPPT FMIAVFLPTL VLICKIALCL PCLRKKILKI RCGWEDVSKI NRTEMASRL // ID STEA3_MOUSE Reviewed; 488 AA. AC Q8CI59; Q3TKE4; Q80ZF3; Q8C5F0; Q924Z1; DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 19-MAR-2014, entry version 89. DE RecName: Full=Metalloreductase STEAP3; DE EC=1.16.1.-; DE AltName: Full=Dudulin-2; DE AltName: Full=Protein nm1054; DE AltName: Full=Six-transmembrane epithelial antigen of prostate 3; DE AltName: Full=Tumor suppressor-activated pathway protein 6; GN Name=Steap3; Synonyms=Tsap6; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY. RX PubMed=12606722; DOI=10.1073/pnas.0530298100; RA Passer B.J., Nancy-Portebois V., Amzallag N., Prieur S., Cans C., RA Roborel de Climens A., Fiucci G., Bouvard V., Tuynder M., Susini L., RA Morchoisne S., Crible V., Lespagnol A., Dausset J., Oren M., Amson R., RA Telerman A.; RT "The p53-inducible TSAP6 gene product regulates apoptosis and the cell RT cycle and interacts with Nix and the Myt1 kinase."; RL Proc. Natl. Acad. Sci. U.S.A. 100:2284-2289(2003). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RA Serru V., Lamblin D., Lenoir C., Manivet P., Vaubourdolle M., RA Kellermann O., Loric S.; RL Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC STRAIN=C57BL/6J, and NOD; TISSUE=Testis; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC STRAIN=Czech II; TISSUE=Mammary tumor; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP FUNCTION, ENZYME ACTIVITY, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, RP HEME-BINDING, COFACTOR, TISSUE SPECIFICITY, AND MUTAGENESIS OF HIS-316 RP AND HIS-409. RX PubMed=16227996; DOI=10.1038/ng1658; RA Ohgami R.S., Campagna D.R., Greer E.L., Antiochos B., McDonald A., RA Chen J., Sharp J.J., Fujiwara Y., Barker J.E., Fleming M.D.; RT "Identification of a ferrireductase required for efficient RT transferrin-dependent iron uptake in erythroid cells."; RL Nat. Genet. 37:1264-1269(2005). RN [6] RP FUNCTION. RX PubMed=16609065; DOI=10.1182/blood-2006-02-003681; RA Ohgami R.S., Campagna D.R., McDonald A., Fleming M.D.; RT "The Steap proteins are metalloreductases."; RL Blood 108:1388-1394(2006). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=17242355; DOI=10.1073/pnas.0609836104; RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; RT "Large-scale phosphorylation analysis of mouse liver."; RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17 AND SER-20, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006; RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M., RA Thibault P.; RT "The phagosomal proteome in interferon-gamma-activated macrophages."; RL Immunity 30:143-154(2009). CC -!- FUNCTION: Endosomal ferrireductase required for efficient CC transferrin-dependent iron uptake in erythroid cells. Participates CC in erythroid iron homeostasis by reducing Fe(3+) to Fe(2+). Also CC mediates reduction of Cu(2+) to Cu(1+), suggesting that it CC participates in copper homeostasis. Uses NADP(+) as acceptor. May CC play a role downstream of p53/TP53 to interface apoptosis and cell CC cycle progression. Indirectly involved in exosome secretion by CC facilitating the secretion of proteins such as TCTP. CC -!- COFACTOR: FAD (Probable). CC -!- COFACTOR: NADP (By similarity). CC -!- SUBUNIT: Homodimer. Interacts with BNIP3L, MYT1, RHBDL4/RHBDD1 and CC TCTP (By similarity). CC -!- SUBCELLULAR LOCATION: Endosome membrane; Multi-pass membrane CC protein. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q8CI59-1; Sequence=Displayed; CC Name=2; CC IsoId=Q8CI59-2; Sequence=VSP_024832; CC -!- TISSUE SPECIFICITY: Highly expressed in fetal liver (the site of CC midgestational hematopoiesis). CC -!- PTM: Proteolytically cleaved by RHBDL4/RHBDD1. RHBDL4/RHBDD1- CC induced cleavage occurs at multiple sites in a glycosylation- CC independent manner (By similarity). CC -!- PTM: Glycosylated (By similarity). CC -!- DISRUPTION PHENOTYPE: Mice display iron deficiency anemia, due to CC a defect in iron release through the transferrin cycle. CC -!- SIMILARITY: Belongs to the STEAP family. CC -!- SIMILARITY: Contains 1 ferric oxidoreductase domain. CC -!- SEQUENCE CAUTION: CC Sequence=AAK50539.1; Type=Frameshift; Positions=171, 173, 479; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AY214462; AAO38239.1; -; mRNA. DR EMBL; AY029586; AAK50539.1; ALT_FRAME; mRNA. DR EMBL; AK078769; BAC37383.1; -; mRNA. DR EMBL; AK167028; BAE39201.1; -; mRNA. DR EMBL; AK171237; BAE42333.1; -; mRNA. DR EMBL; BC037435; AAH37435.1; -; mRNA. DR RefSeq; NP_001078878.1; NM_001085409.1. DR RefSeq; NP_573449.2; NM_133186.3. DR UniGene; Mm.181033; -. DR ProteinModelPortal; Q8CI59; -. DR SMR; Q8CI59; 29-209. DR PhosphoSite; Q8CI59; -. DR PaxDb; Q8CI59; -. DR PRIDE; Q8CI59; -. DR Ensembl; ENSMUST00000112639; ENSMUSP00000108258; ENSMUSG00000026389. DR Ensembl; ENSMUST00000112640; ENSMUSP00000108259; ENSMUSG00000026389. DR Ensembl; ENSMUST00000112641; ENSMUSP00000108260; ENSMUSG00000026389. DR GeneID; 68428; -. DR KEGG; mmu:68428; -. DR CTD; 55240; -. DR MGI; MGI:1915678; Steap3. DR eggNOG; COG2085; -. DR GeneTree; ENSGT00390000008042; -. DR HOGENOM; HOG000234491; -. DR HOVERGEN; HBG054379; -. DR InParanoid; Q8CI59; -. DR KO; K10142; -. DR TreeFam; TF332031; -. DR NextBio; 327158; -. DR PRO; PR:Q8CI59; -. DR ArrayExpress; Q8CI59; -. DR Bgee; Q8CI59; -. DR CleanEx; MM_STEAP3; -. DR Genevestigator; Q8CI59; -. DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005771; C:multivesicular body; ISA:MGI. DR GO; GO:0005886; C:plasma membrane; IDA:MGI. DR GO; GO:0008823; F:cupric reductase activity; IDA:MGI. DR GO; GO:0052851; F:ferric-chelate reductase (NADPH) activity; IDA:MGI. DR GO; GO:0000293; F:ferric-chelate reductase activity; IDA:MGI. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0015677; P:copper ion import; IDA:MGI. DR GO; GO:1990182; P:exosomal secretion; IMP:MGI. DR GO; GO:0097461; P:ferric iron import into cell; IDA:MGI. DR GO; GO:0055072; P:iron ion homeostasis; IEA:UniProtKB-KW. DR GO; GO:0043065; P:positive regulation of apoptotic process; IEA:Ensembl. DR GO; GO:1902167; P:positive regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; IMP:MGI. DR GO; GO:0009306; P:protein secretion; ISS:UniProtKB. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR013130; Fe3_Rdtase_TM_dom. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Pfam; PF01794; Ferric_reduct; 1. PE 1: Evidence at protein level; KW Alternative splicing; Apoptosis; Cell cycle; Complete proteome; KW Copper; Endosome; FAD; Flavoprotein; Glycoprotein; Ion transport; KW Iron; Iron transport; Membrane; Metal-binding; NADP; Oxidoreductase; KW Phosphoprotein; Reference proteome; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1 488 Metalloreductase STEAP3. FT /FTId=PRO_0000285172. FT TOPO_DOM 1 207 Cytoplasmic (Potential). FT TRANSMEM 208 228 Helical; (Potential). FT TOPO_DOM 229 258 Vesicular (Potential). FT TRANSMEM 259 279 Helical; (Potential). FT TOPO_DOM 280 304 Cytoplasmic (Potential). FT TRANSMEM 305 325 Helical; (Potential). FT TOPO_DOM 326 358 Vesicular (Potential). FT TRANSMEM 359 379 Helical; (Potential). FT TOPO_DOM 380 390 Cytoplasmic (Potential). FT TRANSMEM 391 411 Helical; (Potential). FT TOPO_DOM 412 433 Vesicular (Potential). FT TRANSMEM 434 454 Helical; (Potential). FT TOPO_DOM 455 488 Cytoplasmic (Potential). FT DOMAIN 259 407 Ferric oxidoreductase. FT METAL 316 316 Iron (heme axial ligand) (Probable). FT METAL 409 409 Iron (heme axial ligand) (Probable). FT BINDING 36 36 NADP (By similarity). FT BINDING 38 38 NADP; via amide nitrogen (By similarity). FT BINDING 39 39 NADP; via amide nitrogen (By similarity). FT BINDING 58 58 NADP (By similarity). FT BINDING 59 59 NADP (By similarity). FT BINDING 91 91 NADP; via carbonyl oxygen (By FT similarity). FT BINDING 116 116 NADP; via amide nitrogen (By similarity). FT BINDING 151 151 NADP; via amide nitrogen (By similarity). FT SITE 325 326 Cleavage; by RHBDL4/RHBDD1 (By FT similarity). FT MOD_RES 17 17 Phosphoserine. FT MOD_RES 20 20 Phosphoserine. FT CARBOHYD 256 256 N-linked (GlcNAc...) (Potential). FT VAR_SEQ 1 1 M -> MAAEAHRQQGSCPTIPSEGCGKSPEKKGSAADSRPG FT TAM (in isoform 2). FT /FTId=VSP_024832. FT MUTAGEN 316 316 H->L: Loss of function. FT MUTAGEN 409 409 H->L: Loss of function. FT CONFLICT 81 81 V -> M (in Ref. 3; BAC37383). FT CONFLICT 157 157 G -> V (in Ref. 2; AAK50539). FT CONFLICT 169 172 SDQP -> GNQQ (in Ref. 2; AAK50539). FT CONFLICT 176 179 RTIS -> QRVM (in Ref. 2; AAK50539). FT CONFLICT 212 212 W -> G (in Ref. 2; AAK50539). FT CONFLICT 350 350 V -> A (in Ref. 3; BAC37383/BAE39201). FT CONFLICT 455 455 S -> N (in Ref. 3; BAC37383/BAE39201). SQ SEQUENCE 488 AA; 54749 MW; 9A08D99C90CF83F4 CRC64; MSGEMDKPLI SRRLVDSDGS LAEVPKEAPK VGILGSGDFA RSLATRLVGS GFSVVVGSRN PKRTAGLFPS LAQVTFQEEA VSSPEVIFVA VFREHYSSLC SLADQLAGKI LVDVSNPTEK EHLQHRQSNA EYLASLFPAC TVVKAFNVIS AWALQAGPRD GNRQVLICSD QPEAKRTISE MARAMGFTPL DMGSLASARE VEAIPLRLLP SWKVPTLLAL GLFVCFYTYN FIRDVLQPYI RKDENKFYKM PLSVVNTTLP CVAYVLLSLV YLPGVLAAAL QLRRGTKYQR FPDWLDHWLQ HRKQIGLLSF FFAMLHALYS FCLPLRRSHR YDLVNLAVKQ VLANKSRLWV EEEVWRMEIY LSLGVLALGM LSLLAVTSLP SIANSLNWKE FSFVQSTLGF VALILSTMHT LTYGWTRAFE ENHYKFYLPP TFTLTLLLPC VIILAKGLFL LPCLSRRLTK IRRGWEKDGA VKFMLPGDHT QGEKTSHV // ID STEA4_MOUSE Reviewed; 470 AA. AC Q923B6; Q91W31; Q91ZE8; DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 19-FEB-2014, entry version 86. DE RecName: Full=Metalloreductase STEAP4; DE EC=1.16.1.-; DE AltName: Full=Dudulin-4; DE AltName: Full=Six-transmembrane epithelial antigen of prostate 4; DE AltName: Full=Tumor necrosis factor-alpha-induced adipose-related protein; GN Name=Steap4; Synonyms=Tiarp; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION BY TNFA. RC STRAIN=Swiss; TISSUE=Adipose tissue; RX PubMed=11443137; DOI=10.1074/jbc.M105726200; RA Moldes M., Lasnier F., Gauthereau X., Klein C., Pairault J., Feve B., RA Chambaut-Guerin A.-M.; RT "Tumor necrosis factor-alpha-induced adipose-related protein (TIARP), RT a cell-surface protein that is highly induced by tumor necrosis RT factor-alpha and adipose conversion."; RL J. Biol. Chem. 276:33938-33946(2001). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Serru V., Lamblin D., Manivet P., Pernet P., Vaubourdolle M., RA Kellermann O., Loric S.; RT "Molecular cloning and expression of two new members of the dudulin RT family."; RL Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Aorta, and Vein; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Mammary tumor; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP INDUCTION BY IL6, AND TISSUE SPECIFICITY. RX PubMed=14988015; DOI=10.1016/S0014-5793(04)00096-1; RA Fasshauer M., Kralisch S., Klier M., Lossner U., Bluher M., RA Chambaut-Guerin A.-M., Klein J., Paschke R.; RT "Interleukin-6 is a positive regulator of tumor necrosis factor alpha- RT induced adipose-related protein in 3T3-L1 adipocytes."; RL FEBS Lett. 560:153-157(2004). RN [6] RP FUNCTION, AND ENZYME ACTIVITY. RX PubMed=16609065; DOI=10.1182/blood-2006-02-003681; RA Ohgami R.S., Campagna D.R., McDonald A., Fleming M.D.; RT "The Steap proteins are metalloreductases."; RL Blood 108:1388-1394(2006). RN [7] RP FUNCTION, INDUCTION BY TNFA, AND DISRUPTION PHENOTYPE. RX PubMed=17482547; DOI=10.1016/j.cell.2007.02.049; RA Wellen K.E., Fucho R., Gregor M.F., Furuhashi M., Morgan C., RA Lindstad T., Vaillancourt E., Gorgun C.Z., Saatcioglu F., RA Hotamisligil G.S.; RT "Coordinated regulation of nutrient and inflammatory responses by RT STAMP2 is essential for metabolic homeostasis."; RL Cell 129:537-548(2007). RN [8] RP FUNCTION, INDUCTION BY TNFA, AND TISSUE SPECIFICITY. RX PubMed=19660107; DOI=10.1186/ar2779; RA Inoue A., Matsumoto I., Tanaka Y., Iwanami K., Kanamori A., Ochiai N., RA Goto D., Ito S., Sumida T.; RT "Tumor necrosis factor alpha-induced adipose-related protein RT expression in experimental arthritis and in rheumatoid arthritis."; RL Arthritis Res. Ther. 11:R118-R118(2009). RN [9] RP INDUCTION BY IL1B. RX PubMed=19289123; DOI=10.1016/j.febslet.2009.03.015; RA Kralisch S., Sommer G., Weise S., Lipfert J., Lossner U., Kamprad M., RA Schrock K., Bluher M., Stumvoll M., Fasshauer M.; RT "Interleukin-1beta is a positive regulator of TIARP/STAMP2 gene and RT protein expression in adipocytes in vitro."; RL FEBS Lett. 583:1196-1200(2009). CC -!- FUNCTION: Metalloreductase that has the ability to reduce both CC Fe(3+) to Fe(2+) and Cu(2+) to Cu(1+). Uses NAD(+) as acceptor. CC Inhibits anchorage-independent cell proliferation (By similarity). CC Associated with obesity and insulin-resistance. Involved in CC inflammatory arthritis, through the regulation of inflammatory CC cytokines. Plays a role in systemic metabolic homeostasis, CC integrating inflammatory and metabolic responses. CC -!- COFACTOR: FAD (By similarity). CC -!- SUBUNIT: Interacts with and phosphorylates PTK2/FAK1 (By CC similarity). CC -!- SUBCELLULAR LOCATION: Cell membrane. Golgi apparatus membrane; CC Multi-pass membrane protein (By similarity). CC -!- TISSUE SPECIFICITY: Expressed in white and brown adipose tissues CC cells, as well as in muscle and liver cells. Detected in joints CC and spleens of arthritic mice. CC -!- INDUCTION: By Tnfa (TNF-alpha), by Il6 in white and brown adipose CC tissue, and IL1B in white adipose tissue. Tnfa, Il6 and Il1b shows CC sinergistic stimulatory effects. CC -!- DISRUPTION PHENOTYPE: Mice are viable and fertile, but exhibit CC overt inflammation with increased expression of Il6, Tnfa, Ccl2, CC haptoglobin and Socs3 in visceral adipose tissue as well as CC macrophage infiltration. They develop metabolic disease on regular CC diet with insulin resistance, glucose intolerance, mild CC hyperglycemia, dyslipidemia, and fatty liver disease. Adipocytes CC isolated from visceral fat exhibit severily defective glucose CC transport, with decreased expression of Slc2a4, Adipoq, Fas and CC Pparg. Glucose disposal is lower in response to insulin CC stimulation and hepatic glucose production is higher, confirming CC systemic and hepatic insulin-resistance. CC -!- SIMILARITY: Belongs to the STEAP family. CC -!- SIMILARITY: Contains 1 ferric oxidoreductase domain. CC -!- SEQUENCE CAUTION: CC Sequence=AAK40270.1; Type=Frameshift; Positions=334, 336, 453; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJ319746; CAC41351.1; -; mRNA. DR EMBL; AY029778; AAK40270.1; ALT_FRAME; mRNA. DR EMBL; AK040760; BAC30696.1; -; mRNA. DR EMBL; BC006651; AAH06651.1; -; mRNA. DR RefSeq; NP_473439.2; NM_054098.3. DR UniGene; Mm.31403; -. DR ProteinModelPortal; Q923B6; -. DR SMR; Q923B6; 19-195. DR PhosphoSite; Q923B6; -. DR PaxDb; Q923B6; -. DR PRIDE; Q923B6; -. DR Ensembl; ENSMUST00000115421; ENSMUSP00000111081; ENSMUSG00000012428. DR GeneID; 117167; -. DR KEGG; mmu:117167; -. DR UCSC; uc008wjg.1; mouse. DR CTD; 79689; -. DR MGI; MGI:1923560; Steap4. DR eggNOG; COG2085; -. DR GeneTree; ENSGT00390000008042; -. DR HOGENOM; HOG000234491; -. DR HOVERGEN; HBG054379; -. DR InParanoid; Q923B6; -. DR OMA; AKQRVMD; -. DR OrthoDB; EOG7Z0JWH; -. DR TreeFam; TF332031; -. DR NextBio; 369548; -. DR PRO; PR:Q923B6; -. DR Bgee; Q923B6; -. DR CleanEx; MM_STEAP4; -. DR Genevestigator; Q923B6; -. DR GO; GO:0005768; C:endosome; IDA:MGI. DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005887; C:integral component of plasma membrane; TAS:UniProtKB. DR GO; GO:0008823; F:cupric reductase activity; IDA:MGI. DR GO; GO:0052851; F:ferric-chelate reductase (NADPH) activity; IDA:MGI. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0015677; P:copper ion import; IDA:MGI. DR GO; GO:0045444; P:fat cell differentiation; IEP:UniProtKB. DR GO; GO:0097461; P:ferric iron import into cell; IDA:MGI. DR GO; GO:0055072; P:iron ion homeostasis; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR013130; Fe3_Rdtase_TM_dom. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Pfam; PF01794; Ferric_reduct; 1. PE 2: Evidence at transcript level; KW Cell membrane; Complete proteome; Copper; FAD; Flavoprotein; KW Golgi apparatus; Ion transport; Iron; Iron transport; Membrane; KW Metal-binding; NAD; Oxidoreductase; Reference proteome; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1 470 Metalloreductase STEAP4. FT /FTId=PRO_0000285175. FT TRANSMEM 196 216 Helical; (Potential). FT TRANSMEM 247 267 Helical; (Potential). FT TRANSMEM 293 313 Helical; (Potential). FT TRANSMEM 348 368 Helical; (Potential). FT TRANSMEM 386 402 Helical; (Potential). FT TRANSMEM 419 439 Helical; (Potential). FT DOMAIN 247 395 Ferric oxidoreductase. FT METAL 304 304 Iron (heme axial ligand) (By similarity). FT METAL 397 397 Iron (heme axial ligand) (By similarity). FT CONFLICT 36 36 L -> M (in Ref. 2; AAK40270). FT CONFLICT 95 95 Y -> C (in Ref. 1; CAC41351). FT CONFLICT 108 108 R -> H (in Ref. 2; AAK40270). FT CONFLICT 127 127 G -> E (in Ref. 2; AAK40270). FT CONFLICT 154 154 F -> L (in Ref. 2; AAK40270). FT CONFLICT 164 164 Q -> H (in Ref. 1; CAC41351). FT CONFLICT 212 212 V -> I (in Ref. 1; CAC41351 and 2; FT AAK40270). FT CONFLICT 216 216 V -> L (in Ref. 2; AAK40270). FT CONFLICT 228 228 V -> M (in Ref. 2; AAK40270). FT CONFLICT 305 305 V -> A (in Ref. 2; AAK40270). FT CONFLICT 323 323 N -> K (in Ref. 2; AAK40270). FT CONFLICT 332 332 N -> S (in Ref. 2; AAK40270). FT CONFLICT 362 362 L -> V (in Ref. 2; AAK40270). FT CONFLICT 425 425 V -> I (in Ref. 1; CAC41351). SQ SEQUENCE 470 AA; 52994 MW; 6823E7682AC78B19 CRC64; MEKAHADEFP LTTDSSEKQG VVCIFGTGDF GKSLGLKMLQ CGYSIVFGSR NPQVSSLLPR GAEVLSYSEA ASKSDIIILA MHREHYDSLT ELVDYLKGKV LVDVSNNRKI NQYPESNAEY LAQLEPGAHV VKAFNTISAW ALQSGTLDAS RQVFVCGNDS KAKQRVMDIA RTLGLTPLDQ GSLMAASEIE NYPLQLFPMW RFPFYLSSVL CVFFFVYCAI REVIYPYVNG KTDATYRLAI SIPNRVFPIT ALILLALVYL PGILAAILQL YRGTKYRRFP NWLDHWMLCR KQLGLVALGF AFLHVIYTLV IPIRYYVRWR LRNATITQAL TNKDSPFITS YAWINDSYLA LGILGFFLFL LLGITSLPSV SNMVNWREFR FVQSKLGYLT LVLCTAHTLV YGGKRFLSPS ILRWSLPSAY ILALVIPCAV LVLKCILIMP CIDKTLTRIR QGWERNSKYT QSALNGKSDI // ID STEA2_MOUSE Reviewed; 489 AA. AC Q8BWB6; Q3TS12; DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 19-FEB-2014, entry version 85. DE RecName: Full=Metalloreductase STEAP2; DE EC=1.16.1.-; DE AltName: Full=Six-transmembrane epithelial antigen of prostate 2; GN Name=Steap2; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Epididymis, and Head; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP FUNCTION, ENZYME ACTIVITY, AND SUBCELLULAR LOCATION. RX PubMed=16609065; DOI=10.1182/blood-2006-02-003681; RA Ohgami R.S., Campagna D.R., McDonald A., Fleming M.D.; RT "The Steap proteins are metalloreductases."; RL Blood 108:1388-1394(2006). CC -!- FUNCTION: Metalloreductase that has the ability to reduce both CC Fe(3+) to Fe(2+) and Cu(2+) to Cu(1+). Uses NAD(+) as acceptor. CC -!- COFACTOR: FAD (By similarity). CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein CC (By similarity). Endosome membrane; Multi-pass membrane protein. CC -!- SIMILARITY: Belongs to the STEAP family. CC -!- SIMILARITY: Contains 1 ferric oxidoreductase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK052981; BAC35230.1; -; mRNA. DR EMBL; AK162343; BAE36864.1; -; mRNA. DR RefSeq; NP_001096626.1; NM_001103156.2. DR RefSeq; NP_001096627.1; NM_001103157.2. DR RefSeq; NP_001272398.1; NM_001285469.1. DR RefSeq; NP_001272399.1; NM_001285470.1. DR RefSeq; NP_083010.2; NM_028734.5. DR UniGene; Mm.274956; -. DR ProteinModelPortal; Q8BWB6; -. DR SMR; Q8BWB6; 32-207. DR PhosphoSite; Q8BWB6; -. DR PRIDE; Q8BWB6; -. DR Ensembl; ENSMUST00000015797; ENSMUSP00000015797; ENSMUSG00000015653. DR Ensembl; ENSMUST00000115424; ENSMUSP00000111084; ENSMUSG00000015653. DR Ensembl; ENSMUST00000115425; ENSMUSP00000111085; ENSMUSG00000015653. DR Ensembl; ENSMUST00000115426; ENSMUSP00000111086; ENSMUSG00000015653. DR Ensembl; ENSMUST00000164219; ENSMUSP00000132501; ENSMUSG00000015653. DR GeneID; 74051; -. DR KEGG; mmu:74051; -. DR UCSC; uc008wiw.2; mouse. DR CTD; 261729; -. DR MGI; MGI:1921301; Steap2. DR eggNOG; COG2085; -. DR GeneTree; ENSGT00390000008042; -. DR HOGENOM; HOG000234491; -. DR HOVERGEN; HBG054379; -. DR InParanoid; Q8BWB6; -. DR KO; K14738; -. DR OMA; FFFASVH; -. DR TreeFam; TF332031; -. DR ChiTaRS; STEAP2; mouse. DR NextBio; 339632; -. DR PRO; PR:Q8BWB6; -. DR ArrayExpress; Q8BWB6; -. DR Bgee; Q8BWB6; -. DR Genevestigator; Q8BWB6; -. DR GO; GO:0005829; C:cytosol; ISS:UniProtKB. DR GO; GO:0005769; C:early endosome; ISS:UniProtKB. DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell. DR GO; GO:0030173; C:integral component of Golgi membrane; ISS:UniProtKB. DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB. DR GO; GO:0030140; C:trans-Golgi network transport vesicle; ISS:UniProtKB. DR GO; GO:0008823; F:cupric reductase activity; IDA:MGI. DR GO; GO:0052851; F:ferric-chelate reductase (NADPH) activity; IDA:MGI. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0005215; F:transporter activity; ISS:UniProtKB. DR GO; GO:0015677; P:copper ion import; IDA:MGI. DR GO; GO:0006897; P:endocytosis; ISS:UniProtKB. DR GO; GO:0097461; P:ferric iron import into cell; IDA:MGI. DR GO; GO:0006893; P:Golgi to plasma membrane transport; ISS:UniProtKB. DR GO; GO:0055072; P:iron ion homeostasis; IEA:UniProtKB-KW. DR GO; GO:0045055; P:regulated secretory pathway; ISS:UniProtKB. DR GO; GO:0009725; P:response to hormone; ISS:UniProtKB. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR013130; Fe3_Rdtase_TM_dom. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Pfam; PF01794; Ferric_reduct; 1. PE 2: Evidence at transcript level; KW Cell membrane; Complete proteome; Copper; Electron transport; KW Endosome; FAD; Flavoprotein; Ion transport; Iron; Iron transport; KW Membrane; Metal-binding; NAD; Oxidoreductase; Reference proteome; KW Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 489 Metalloreductase STEAP2. FT /FTId=PRO_0000191698. FT TRANSMEM 207 227 Helical; (Potential). FT TRANSMEM 258 278 Helical; (Potential). FT TRANSMEM 304 324 Helical; (Potential). FT TRANSMEM 358 378 Helical; (Potential). FT TRANSMEM 392 412 Helical; (Potential). FT TRANSMEM 431 451 Helical; (Potential). FT DOMAIN 258 406 Ferric oxidoreductase. FT METAL 315 315 Iron (heme axial ligand) (By similarity). FT METAL 408 408 Iron (heme axial ligand) (By similarity). SQ SEQUENCE 489 AA; 55760 MW; 98CD63D59DDDF24C CRC64; MESISMMGSP KSLETFLPNG INGIKDARQV TVGVIGSGDF AKSLTIRLIR CGYHVVIGSR NPKFASEFFP HVVDVTHHED ALTKTNIIFV AIHREHYTSL WDLRHLLVGK ILIDVSNNMR VNQYPESNAE YLASLFPDSL IVKGFNVISA WALQLGPKDA SRQVYICSNN IQARQQVIEL ARQLNFIPVD LGSLSSAKEI ENLPLRLFTL WRGPVVVAIS LATFFFLYSF VRDVIHPYAR NQQSDFYKIP IEIVNKTLPI VAITLLSLVY LAGLLAAAYQ LYYGTKYRRF PPWLDTWLQC RKQLGLLSFF FAVVHVAYSL CLPMRRSERY LFLNMAYQQV HANIENAWNE EEVWRIEMYI SFGIMSLGLL SLLAVTSIPS VSNALNWREF SFIQSTLGYV ALLITTFHVL IYGWKRAFAE EYYRFYTPPN FVLALVLPSI VILGKMILLL PCISRKLKRI KKGWEKSQFL DEGMGGAVPH LSPERVTVM // ID SUMF1_MOUSE Reviewed; 372 AA. AC Q8R0F3; Q3TTT6; Q3TXM8; Q3U9A5; DT 25-JUL-2003, integrated into UniProtKB/Swiss-Prot. DT 25-JUL-2003, sequence version 2. DT 19-FEB-2014, entry version 90. DE RecName: Full=Sulfatase-modifying factor 1; DE EC=1.8.99.-; DE AltName: Full=C-alpha-formylglycine-generating enzyme 1; DE Flags: Precursor; GN Name=Sumf1; Synonyms=Fge; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Bone marrow macrophage, and Head; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6; TISSUE=Retina; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: Using molecular oxygen and an unidentified reducing CC agent, oxidizes a cysteine residue in the substrate sulfatase to CC an active site 3-oxoalanine residue, which is also called CC C(alpha)-formylglycine. Known substrates include GALNS, ARSA, STS CC and ARSE (By similarity). CC -!- CATALYTIC ACTIVITY: [sulfatase]-cysteine + acceptor = [sulfatase]- CC 3-oxoalanine + reduced acceptor. CC -!- PATHWAY: Protein modification; sulfatase oxidation. CC -!- SUBUNIT: Monomer, homodimer and heterodimer with SUMF2 (By CC similarity). CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen (By similarity). CC -!- MISCELLANEOUS: The resulting 3-oxoalanine in the substrate protein CC is called C(alpha)-formylglycine by many authors. It should not be CC confused with N-formylglycine. CC -!- SIMILARITY: Belongs to the sulfatase-modifying factor family. CC -!- SEQUENCE CAUTION: CC Sequence=AAH26981.1; Type=Erroneous initiation; CC Sequence=BAE30762.1; Type=Erroneous initiation; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK151874; BAE30762.1; ALT_INIT; mRNA. DR EMBL; AK159192; BAE34887.1; -; mRNA. DR EMBL; AK160917; BAE36091.1; -; mRNA. DR EMBL; AK161203; BAE36238.1; -; mRNA. DR EMBL; BC026981; AAH26981.1; ALT_INIT; mRNA. DR RefSeq; NP_666049.2; NM_145937.3. DR UniGene; Mm.439876; -. DR ProteinModelPortal; Q8R0F3; -. DR SMR; Q8R0F3; 84-369. DR BioGrid; 208463; 2. DR IntAct; Q8R0F3; 2. DR MINT; MINT-4136123; -. DR PhosphoSite; Q8R0F3; -. DR PaxDb; Q8R0F3; -. DR PRIDE; Q8R0F3; -. DR Ensembl; ENSMUST00000032191; ENSMUSP00000032191; ENSMUSG00000030101. DR GeneID; 58911; -. DR KEGG; mmu:58911; -. DR UCSC; uc009ddf.2; mouse. DR CTD; 285362; -. DR MGI; MGI:1889844; Sumf1. DR eggNOG; COG1262; -. DR GeneTree; ENSGT00390000008983; -. DR HOGENOM; HOG000135466; -. DR HOVERGEN; HBG054193; -. DR InParanoid; Q8R0F3; -. DR KO; K13444; -. DR OMA; FRCAADH; -. DR OrthoDB; EOG7VX8WN; -. DR TreeFam; TF324027; -. DR UniPathway; UPA00910; -. DR NextBio; 314476; -. DR PRO; PR:Q8R0F3; -. DR ArrayExpress; Q8R0F3; -. DR Bgee; Q8R0F3; -. DR CleanEx; MM_SUMF1; -. DR Genevestigator; Q8R0F3; -. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI. DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW. DR Gene3D; 3.90.1580.10; -; 1. DR InterPro; IPR016187; C-type_lectin_fold. DR InterPro; IPR005532; FGE_dom. DR Pfam; PF03781; FGE-sulfatase; 1. DR SUPFAM; SSF56436; SSF56436; 1. PE 1: Evidence at protein level; KW Calcium; Complete proteome; Disulfide bond; Endoplasmic reticulum; KW Glycoprotein; Metal-binding; Oxidoreductase; Reference proteome; KW Signal. FT SIGNAL 1 31 By similarity. FT CHAIN 32 372 Sulfatase-modifying factor 1. FT /FTId=PRO_0000033457. FT ACT_SITE 331 331 Proton acceptor (By similarity). FT METAL 128 128 Calcium 2 (By similarity). FT METAL 257 257 Calcium 1 (By similarity). FT METAL 258 258 Calcium 1; via carbonyl oxygen (By FT similarity). FT METAL 271 271 Calcium 1 (By similarity). FT METAL 273 273 Calcium 1; via carbonyl oxygen (By FT similarity). FT METAL 291 291 Calcium 2; via carbonyl oxygen (By FT similarity). FT METAL 294 294 Calcium 2; via carbonyl oxygen (By FT similarity). FT METAL 298 298 Calcium 2 (By similarity). FT CARBOHYD 139 139 N-linked (GlcNAc...) (By similarity). FT DISULFID 48 50 FT DISULFID 216 363 By similarity. FT DISULFID 233 344 By similarity. FT DISULFID 334 339 Redox-active (By similarity). FT CONFLICT 39 39 E -> V (in Ref. 1; BAE34887). SQ SEQUENCE 372 AA; 40659 MW; 3C96D488B4291068 CRC64; MAAPAREPAL RCCIRLARVF LLLVLACEVA GSDEAEAREG AASLAGSCGC GTPQRAGAHG SSAAAQRYSR EANAPGLTSG PRPLALTKMV PIPAGVFTMG TDDPQIRQDG EAPARRVTVD GFYMDAYEVS NADFEKFVNS TGYLTEAEKF GDSFVFEGML SEQVKTHIHQ AVAAAPWWLP VKGANWRHPE GPDSSILHRS NHPVLHVSWN DAVAYCTWAG KRLPTEAEWE YSCRGGLQNR LFPWGNKLQP KGQHYANIWQ GKFPVSNTGE DGFQGTAPVD AFPPNGYGLY NIVGNVWEWT SDWWTVHHSV EETFNPKGPT SGKDRVKKGG SYMCHKSYCY RYRCAARSQN TPDSSASNLG FRCAADHLPT AD // ID SUOX_MOUSE Reviewed; 546 AA. AC Q8R086; Q3U3S5; Q3UEP6; DT 20-JUN-2003, integrated into UniProtKB/Swiss-Prot. DT 10-JUL-2007, sequence version 2. DT 19-FEB-2014, entry version 99. DE RecName: Full=Sulfite oxidase, mitochondrial; DE EC=1.8.3.1; DE Flags: Precursor; GN Name=Suox; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J, and NOD; TISSUE=Liver; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Liver; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- CATALYTIC ACTIVITY: Sulfite + O(2) + H(2)O = sulfate + H(2)O(2). CC -!- COFACTOR: Binds 1 heme B (iron-protoporphyrin IX) group non- CC covalently per subunit (By similarity). CC -!- COFACTOR: Binds 1 molybdenum-molybdopterin (Mo-MPT) cofactor per CC subunit (By similarity). CC -!- PATHWAY: Energy metabolism; sulfur metabolism. CC -!- SUBUNIT: Homodimer. CC -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space. CC -!- SIMILARITY: Contains 1 cytochrome b5 heme-binding domain. CC -!- SEQUENCE CAUTION: CC Sequence=BAE32710.1; Type=Erroneous initiation; Note=Translation N-terminally extended; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK149422; BAE28865.1; -; mRNA. DR EMBL; AK154608; BAE32710.1; ALT_INIT; mRNA. DR EMBL; BC027197; AAH27197.2; -; mRNA. DR RefSeq; NP_776094.2; NM_173733.3. DR UniGene; Mm.23352; -. DR ProteinModelPortal; Q8R086; -. DR SMR; Q8R086; 82-544. DR IntAct; Q8R086; 5. DR MINT; MINT-1860734; -. DR PhosphoSite; Q8R086; -. DR REPRODUCTION-2DPAGE; Q8R086; -. DR PaxDb; Q8R086; -. DR PRIDE; Q8R086; -. DR Ensembl; ENSMUST00000054764; ENSMUSP00000056195; ENSMUSG00000049858. DR GeneID; 211389; -. DR KEGG; mmu:211389; -. DR UCSC; uc007hnt.2; mouse. DR CTD; 6821; -. DR MGI; MGI:2446117; Suox. DR eggNOG; COG2041; -. DR GeneTree; ENSGT00390000003749; -. DR HOGENOM; HOG000252609; -. DR HOVERGEN; HBG017865; -. DR InParanoid; Q8R086; -. DR KO; K00387; -. DR OMA; AVHNQSH; -. DR OrthoDB; EOG7P8P7Z; -. DR TreeFam; TF300905; -. DR UniPathway; UPA00096; -. DR NextBio; 373222; -. DR PRO; PR:Q8R086; -. DR Bgee; Q8R086; -. DR CleanEx; MM_SUOX; -. DR Genevestigator; Q8R086; -. DR GO; GO:0005758; C:mitochondrial intermembrane space; IEA:UniProtKB-SubCell. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0030151; F:molybdenum ion binding; IEA:InterPro. DR GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro. DR GO; GO:0008482; F:sulfite oxidase activity; IEA:UniProtKB-EC. DR GO; GO:0006790; P:sulfur compound metabolic process; IEA:UniProtKB-UniPathway. DR Gene3D; 2.60.40.650; -; 1. DR Gene3D; 3.10.120.10; -; 1. DR Gene3D; 3.90.420.10; -; 1. DR InterPro; IPR001199; Cyt_B5-like_heme/steroid-bd. DR InterPro; IPR018506; Cyt_B5_heme-BS. DR InterPro; IPR014756; Ig_E-set. DR InterPro; IPR005066; MoCF_OxRdtse_dimer. DR InterPro; IPR008335; Mopterin_OxRdtase_euk. DR InterPro; IPR000572; OxRdtase_Mopterin-bd_dom. DR InterPro; IPR022407; OxRdtase_Mopterin_BS. DR Pfam; PF00173; Cyt-b5; 1. DR Pfam; PF03404; Mo-co_dimer; 1. DR Pfam; PF00174; Oxidored_molyb; 1. DR PRINTS; PR00363; CYTOCHROMEB5. DR PRINTS; PR00407; EUMOPTERIN. DR SUPFAM; SSF55856; SSF55856; 1. DR SUPFAM; SSF56524; SSF56524; 1. DR SUPFAM; SSF81296; SSF81296; 1. DR PROSITE; PS00191; CYTOCHROME_B5_1; 1. DR PROSITE; PS50255; CYTOCHROME_B5_2; 1. DR PROSITE; PS00559; MOLYBDOPTERIN_EUK; 1. PE 2: Evidence at transcript level; KW Complete proteome; Heme; Iron; Metal-binding; Mitochondrion; KW Molybdenum; Oxidoreductase; Reference proteome; Transit peptide. FT TRANSIT 1 80 Mitochondrion (By similarity). FT CHAIN 81 546 Sulfite oxidase, mitochondrial. FT /FTId=PRO_0000006483. FT DOMAIN 83 162 Cytochrome b5 heme-binding. FT REGION 166 175 Hinge (By similarity). FT REGION 176 402 Moco domain (By similarity). FT REGION 216 220 Molybdopterin-binding (By similarity). FT REGION 378 380 Molybdopterin-binding (By similarity). FT REGION 403 539 Homodimerization (By similarity). FT METAL 119 119 Iron (heme axial ligand) (By similarity). FT METAL 144 144 Iron (heme axial ligand) (By similarity). FT METAL 265 265 Molybdenum (By similarity). FT BINDING 146 146 Heme b (By similarity). FT BINDING 148 148 Heme b (By similarity). FT BINDING 323 323 Molybdopterin (By similarity). FT BINDING 362 362 Molybdopterin (By similarity). FT BINDING 367 367 Molybdopterin (By similarity). FT CONFLICT 455 455 G -> S (in Ref. 1; BAE28865). SQ SEQUENCE 546 AA; 60756 MW; A10ADF73FFA8DE51 CRC64; MLLQLYRSVV VRLPQAIRVK STPLRLCIQA CSTNDSLEPQ HPSLTFSDDN SRTRRWKVMG TLLGLGVVLV YHEHRCRASQ ESPRMYSKED VRSHNNPKTG VWVTLGSEVF DVTKFVDLHP GGPSKLMLAA GGPLEPFWAL YAVHNQPHVR ELLAEYKIGE LNPEDSMSPS VEASDPYADD PIRHPALRIN SQRPFNAEPP PELLTEGYIT PNPIFFTRNH LPVPNLDPHT YRLHVVGAPG GQSLSLSLDD LHKFPKHEVT VTLQCAGNRR SEMSKVKEVK GLEWRTGAIS TARWAGARLC DVLAQAGHRL CDSEAHVCFE GLDSDPTGTA YGASIPLARA MDPEAEVLLA YEMNGQPLPR DHGFPVRVVV PGVVGARHVK WLGRVSVESE ESYSHWQRRD YKGFSPSVDW DTVNFDLAPS IQELPIQSAI TQPQDGAIVE SGEVTIKGYA WSGGGRAVIR VDVSVDGGLT WQEAELEGEE QCPRKAWAWR IWQLKAQVPA EQKELNIICK AVDDSYNVQP DTVAPIWNLR GVLSNAWHRV HVQVVP // ID T23O_MOUSE Reviewed; 406 AA. AC P48776; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 20-JAN-2009, sequence version 2. DT 19-MAR-2014, entry version 102. DE RecName: Full=Tryptophan 2,3-dioxygenase; DE Short=TDO; DE EC=1.13.11.11; DE AltName: Full=Tryptamin 2,3-dioxygenase; DE AltName: Full=Tryptophan oxygenase; DE Short=TO; DE Short=TRPO; DE AltName: Full=Tryptophan pyrrolase; DE AltName: Full=Tryptophanase; GN Name=Tdo2; Synonyms=Tdo; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=DBA/2J; RA Novoradovsky A., Goldman D.; RL Submitted (APR-1995) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). CC -!- FUNCTION: Incorporates oxygen into the indole moiety of CC tryptophan. Has a broad specificity towards tryptamine and CC derivatives including D- and L-tryptophan, 5-hydroxytryptophan and CC serotonin (By similarity). CC -!- CATALYTIC ACTIVITY: L-tryptophan + O(2) = N-formyl-L-kynurenine. CC -!- COFACTOR: Binds 2 heme groups per tetramer (By similarity). CC -!- PATHWAY: Amino-acid degradation; L-tryptophan degradation via CC kynurenine pathway; L-kynurenine from L-tryptophan: step 1/2. CC -!- SUBUNIT: Homotetramer (By similarity). CC -!- SIMILARITY: Belongs to the tryptophan 2,3-dioxygenase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U24493; AAB60491.1; -; mRNA. DR EMBL; AC159260; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; NP_064295.2; NM_019911.2. DR UniGene; Mm.258622; -. DR ProteinModelPortal; P48776; -. DR SMR; P48776; 39-383. DR STRING; 10090.ENSMUSP00000029645; -. DR BindingDB; P48776; -. DR ChEMBL; CHEMBL1075307; -. DR PhosphoSite; P48776; -. DR PaxDb; P48776; -. DR PRIDE; P48776; -. DR Ensembl; ENSMUST00000029645; ENSMUSP00000029645; ENSMUSG00000028011. DR GeneID; 56720; -. DR KEGG; mmu:56720; -. DR UCSC; uc008poo.1; mouse. DR CTD; 6999; -. DR MGI; MGI:1928486; Tdo2. DR eggNOG; COG3483; -. DR HOGENOM; HOG000221584; -. DR HOVERGEN; HBG003043; -. DR InParanoid; P48776; -. DR KO; K00453; -. DR OMA; YGEYLML; -. DR OrthoDB; EOG7MD4Q2; -. DR TreeFam; TF105827; -. DR BRENDA; 1.13.11.11; 3474. DR UniPathway; UPA00333; UER00453. DR ChiTaRS; TDO2; mouse. DR NextBio; 313194; -. DR PRO; PR:P48776; -. DR ArrayExpress; P48776; -. DR Bgee; P48776; -. DR CleanEx; MM_TDO2; -. DR Genevestigator; P48776; -. DR GO; GO:0016597; F:amino acid binding; IEA:Ensembl. DR GO; GO:0020037; F:heme binding; IBA:RefGenome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0019825; F:oxygen binding; IEA:Ensembl. DR GO; GO:0004833; F:tryptophan 2,3-dioxygenase activity; IBA:RefGenome. DR GO; GO:0019442; P:tryptophan catabolic process to acetyl-CoA; IBA:RefGenome. DR GO; GO:0019441; P:tryptophan catabolic process to kynurenine; IEA:UniProtKB-UniPathway. DR HAMAP; MF_01972; T23O; 1. DR InterPro; IPR004981; Trp_2_3_dOase. DR PANTHER; PTHR10138; PTHR10138; 1. DR Pfam; PF03301; Trp_dioxygenase; 1. PE 2: Evidence at transcript level; KW Coiled coil; Complete proteome; Dioxygenase; Heme; Iron; KW Metal-binding; Oxidoreductase; Reference proteome; KW Tryptophan catabolism. FT CHAIN 1 406 Tryptophan 2,3-dioxygenase. FT /FTId=PRO_0000072400. FT REGION 42 46 Substrate binding (By similarity). FT REGION 72 76 Substrate binding (By similarity). FT COILED 231 268 Potential. FT METAL 328 328 Iron (heme axial ligand) (By similarity). FT BINDING 144 144 Substrate (By similarity). FT BINDING 151 151 Heme (By similarity). FT BINDING 342 342 Substrate (By similarity). FT CONFLICT 18 18 V -> L (in Ref. 1; AAB60491). FT CONFLICT 229 229 N -> K (in Ref. 1; AAB60491). FT CONFLICT 240 240 R -> K (in Ref. 1; AAB60491). FT CONFLICT 245 245 T -> K (in Ref. 1; AAB60491). SQ SEQUENCE 406 AA; 47756 MW; 201835A021BE7A24 CRC64; MSGCPFAGNS VGYTLKNVSM EDNEEDRAQT GVNRASKGGL IYGNYLQLEK ILNAQELQSE VKGNKIHDEH LFIITHQAYE LWFKQILWEL DSVREIFQNG HVRDERNMLK VIARMHRVVV IFKLLVQQFS VLETMTALDF NDFREYLSPA SGFQSLQFRL LENKIGVLQS LRVPYNRKHY RDNFGGDYNE LLLKSEQEQT LLQLVEAWLE RTPGLEPNGF NFWGKFEKNI LKGLEEEFLR IQAKTDSEEK EEQMAEFRKQ KEVLLCLFDE KRHDYLLSKG ERRLSYRALQ GALMIYFYRE EPRFQVPFQL LTSLMDIDTL MTKWRYNHVC MVHRMLGTKA GTGGSSGYHY LRSTVSDRYK VFVDLFNLST YLVPRHWVPK MNPIIHKFLY TAEYSDSSYF SSDESD // ID TDH_MOUSE Reviewed; 373 AA. AC Q8K3F7; Q6PD91; Q9JLU3; DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2002, sequence version 1. DT 19-FEB-2014, entry version 83. DE RecName: Full=L-threonine 3-dehydrogenase, mitochondrial; DE EC=1.1.1.103; DE Flags: Precursor; GN Name=Tdh; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=BALB/c; TISSUE=Liver; RX PubMed=12097150; DOI=10.1186/1472-2091-3-19; RA Edgar A.J.; RT "Molecular cloning and tissue distribution of mammalian L-threonine 3- RT dehydrogenases."; RL BMC Biochem. 3:19-19(2002). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Embryo; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Embryo; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- CATALYTIC ACTIVITY: L-threonine + NAD(+) = L-2-amino-3- CC oxobutanoate + NADH. CC -!- PATHWAY: Amino-acid degradation; L-threonine degradation via CC oxydo-reductase pathway; glycine from L-threonine: step 1/2. CC -!- SUBCELLULAR LOCATION: Mitochondrion (By similarity). CC -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase CC family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF134346; AAF61395.2; -; mRNA. DR EMBL; AY116662; AAM51557.1; -; mRNA. DR EMBL; AK077571; BAC36870.1; -; mRNA. DR EMBL; BC058860; AAH58860.1; -; mRNA. DR RefSeq; NP_067455.5; NM_021480.5. DR UniGene; Mm.354229; -. DR ProteinModelPortal; Q8K3F7; -. DR SMR; Q8K3F7; 56-360. DR BioGrid; 208451; 2. DR STRING; 10090.ENSMUSP00000022522; -. DR PaxDb; Q8K3F7; -. DR PRIDE; Q8K3F7; -. DR Ensembl; ENSMUST00000022522; ENSMUSP00000022522; ENSMUSG00000021953. DR GeneID; 58865; -. DR KEGG; mmu:58865; -. DR UCSC; uc007uhs.1; mouse. DR CTD; 157739; -. DR MGI; MGI:1926231; Tdh. DR eggNOG; COG0451; -. DR GeneTree; ENSGT00390000014037; -. DR HOGENOM; HOG000034276; -. DR HOVERGEN; HBG062086; -. DR InParanoid; Q8K3F7; -. DR KO; K15789; -. DR OMA; VFWPSSI; -. DR OrthoDB; EOG74J98K; -. DR TreeFam; TF314544; -. DR BRENDA; 1.1.1.103; 3474. DR UniPathway; UPA00046; UER00505. DR NextBio; 314424; -. DR PRO; PR:Q8K3F7; -. DR ArrayExpress; Q8K3F7; -. DR Bgee; Q8K3F7; -. DR CleanEx; MM_TDH; -. DR Genevestigator; Q8K3F7; -. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR GO; GO:0050662; F:coenzyme binding; IEA:InterPro. DR GO; GO:0008743; F:L-threonine 3-dehydrogenase activity; IDA:MGI. DR GO; GO:0019518; P:L-threonine catabolic process to glycine; IEA:UniProtKB-UniPathway. DR GO; GO:0006567; P:threonine catabolic process; IDA:MGI. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR001509; Epimerase_deHydtase. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Pfam; PF01370; Epimerase; 1. PE 2: Evidence at transcript level; KW Complete proteome; Mitochondrion; NAD; Oxidoreductase; KW Reference proteome; Transit peptide. FT TRANSIT 1 ? Mitochondrion (Potential). FT CHAIN ? 373 L-threonine 3-dehydrogenase, FT mitochondrial. FT /FTId=PRO_0000298784. FT NP_BIND 9 46 NAD (By similarity). FT ACT_SITE 195 195 Proton acceptor (By similarity). FT CONFLICT 82 82 D -> N (in Ref. 3; AAH58860). FT CONFLICT 214 214 G -> V (in Ref. 1; AAF61395). FT CONFLICT 232 232 P -> R (in Ref. 1; AAF61395). FT CONFLICT 318 318 Y -> H (in Ref. 3; AAH58860). FT CONFLICT 361 361 N -> S (in Ref. 1; AAF61395). SQ SEQUENCE 373 AA; 41462 MW; 6A416A079A7EC381 CRC64; MLFLGMLKQV VNGTAQSKAS SCRKLVLPLK FLGTSQHRIP ADANFHSTSI SEAEPPRVLI TGGLGQLGVG LANLLRKRFG KDNVILSDIR KPPAHVFHSG PFVYANILDY KSLREIVVNH RISWLFHYSA LLSAVGEANV SLARDVNITG LHNVLDVAAE YNVRLFVPST IGAFGPTSPR NPAPDLCIQR PRTIYGVSKV HTELMGEYYY YRYGLDFRCL RYPGIISADS QPGGGTTDYA VQIFHAAAKN GTFECNLEAG TRLPMMYISD CLRATLEVME APAERLSMRT YNISAMSFTP EELAQALRKH APDFQITYCV DPLRQAIAES WPMILDDSNA RKDWGWKHDF DLPELVATML NFHGVSTRVA QVN // ID TECRL_MOUSE Reviewed; 361 AA. AC Q8BFZ1; Q8CIX3; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 19-FEB-2014, entry version 70. DE RecName: Full=Trans-2,3-enoyl-CoA reductase-like; DE EC=1.3.1.-; DE AltName: Full=Steroid 5-alpha-reductase 2-like 2 protein; GN Name=Tecrl; Synonyms=Srd5a2l2; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=BALB/c; TISSUE=Heart; RA Chen X.-G., Yong L., Zhang D.-L., Cheng J., Zhu W.-L., Dao J.-J.; RT "Molecular cloning and expression analysis of Srd5a2l2, a novel mouse RT member of steroid 5 alpha-reductase family."; RL Sheng Wu Hua Xue Yu Sheng Wu Wu Li Jin Zhan 30:894-899(2003). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Heart; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein CC (Potential). CC -!- SIMILARITY: Belongs to the steroid 5-alpha reductase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF548365; AAN40798.1; -; mRNA. DR EMBL; AK052276; BAC34913.1; -; mRNA. DR EMBL; AK052284; BAC34916.1; -; mRNA. DR EMBL; BC107366; AAI07367.1; -; mRNA. DR EMBL; BC107367; AAI07368.1; -; mRNA. DR RefSeq; NP_722496.2; NM_153801.3. DR UniGene; Mm.126783; -. DR ProteinModelPortal; Q8BFZ1; -. DR SMR; Q8BFZ1; 53-135. DR PhosphoSite; Q8BFZ1; -. DR PaxDb; Q8BFZ1; -. DR PRIDE; Q8BFZ1; -. DR Ensembl; ENSMUST00000053543; ENSMUSP00000062122; ENSMUSG00000049537. DR GeneID; 243078; -. DR KEGG; mmu:243078; -. DR UCSC; uc008xwu.2; mouse. DR CTD; 253017; -. DR MGI; MGI:2444966; Tecrl. DR eggNOG; NOG306265; -. DR GeneTree; ENSGT00510000046645; -. DR HOGENOM; HOG000190918; -. DR InParanoid; Q8BFZ1; -. DR OMA; ICIVDKV; -. DR OrthoDB; EOG7D2FF3; -. DR TreeFam; TF300908; -. DR NextBio; 385641; -. DR PRO; PR:Q8BFZ1; -. DR ArrayExpress; Q8BFZ1; -. DR Bgee; Q8BFZ1; -. DR CleanEx; MM_SRD5A2L2; -. DR Genevestigator; Q8BFZ1; -. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro. DR GO; GO:0006629; P:lipid metabolic process; IEA:InterPro. DR InterPro; IPR001104; 3-oxo-5_a-steroid_4-DH_C. DR Pfam; PF02544; Steroid_dh; 1. DR PROSITE; PS50244; S5A_REDUCTASE; 1. PE 2: Evidence at transcript level; KW Complete proteome; Membrane; Oxidoreductase; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 361 Trans-2,3-enoyl-CoA reductase-like. FT /FTId=PRO_0000317714. FT TRANSMEM 139 159 Helical; (Potential). FT TRANSMEM 181 201 Helical; (Potential). FT TRANSMEM 215 235 Helical; (Potential). FT TRANSMEM 309 329 Helical; (Potential). FT CONFLICT 232 232 Y -> H (in Ref. 1; AAN40798). SQ SEQUENCE 361 AA; 41893 MW; DBE3D7C080A82113 CRC64; MFKRHKSLER KRELLFQGLP QSTMKNNARN FHSLSQLVLS AGPLKTTTAV KHSKTTHFEI EILDAHTRKQ ICIVDKVTQT STIHDVKQKF HKACPKWYPS RIGLQLEYGG PYLRDYITVQ SVAASSIITL YFTDLGQQVG WTTVFLAEYS GPLLIYLLFY LRSSYIYDVK ESTRWPRHPV VHLAFFCHCI HYIRLLLETL FVHKVSTGHS PMKNLIKGCA FYWGFTSWMA YYINHPRYTP PSFGNRQVIV SAINFLFCEA GNHFINTVLA HPNHTGSNAC FPSPNYNPFT WLFFLVSCPN YTYEIGSWIS FTVMTQTLPV GIFTILMTIQ MSLWARKKHK IYRKKFNSYV HRKSAIIPLI L // ID TECR_MOUSE Reviewed; 308 AA. AC Q9CY27; DT 16-APR-2002, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 19-MAR-2014, entry version 98. DE RecName: Full=Very-long-chain enoyl-CoA reductase; DE EC=1.3.1.93; DE AltName: Full=Synaptic glycoprotein SC2; DE AltName: Full=Trans-2,3-enoyl-CoA reductase; DE Short=TER; GN Name=Tecr; Synonyms=Gpsn2; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Embryonic liver; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Kidney; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-60, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic fibroblast; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., RA Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). CC -!- FUNCTION: Reduces trans-2,3-stearoyl-CoA to stearoyl-CoA of long CC and very long chain fatty acids (By similarity). CC -!- CATALYTIC ACTIVITY: A very-long-chain acyl-CoA + NADP(+) = a very- CC long-chain trans-2,3-dehydroacyl-CoA + NADPH. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass CC membrane protein (By similarity). CC -!- SIMILARITY: Belongs to the steroid 5-alpha reductase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK010984; BAB27305.1; -; mRNA. DR EMBL; BC019984; AAH19984.1; -; mRNA. DR RefSeq; NP_081455.1; NM_027179.1. DR RefSeq; NP_598879.1; NM_134118.5. DR UniGene; Mm.352239; -. DR ProteinModelPortal; Q9CY27; -. DR SMR; Q9CY27; 1-81. DR IntAct; Q9CY27; 3. DR MINT; MINT-1858664; -. DR STRING; 10090.ENSMUSP00000019382; -. DR PhosphoSite; Q9CY27; -. DR PaxDb; Q9CY27; -. DR PRIDE; Q9CY27; -. DR Ensembl; ENSMUST00000019382; ENSMUSP00000019382; ENSMUSG00000031708. DR GeneID; 106529; -. DR KEGG; mmu:106529; -. DR UCSC; uc009mkl.2; mouse. DR CTD; 9524; -. DR MGI; MGI:1915408; Tecr. DR eggNOG; NOG306265; -. DR GeneTree; ENSGT00510000046645; -. DR HOGENOM; HOG000190918; -. DR InParanoid; Q9CY27; -. DR KO; K10258; -. DR OrthoDB; EOG7D2FF3; -. DR BRENDA; 1.3.1.38; 3474. DR ChiTaRS; TECR; mouse. DR NextBio; 358246; -. DR PRO; PR:Q9CY27; -. DR ArrayExpress; Q9CY27; -. DR Bgee; Q9CY27; -. DR CleanEx; MM_GPSN2; -. DR Genevestigator; Q9CY27; -. DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; ISS:UniProtKB. DR GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro. DR GO; GO:0030497; P:fatty acid elongation; ISS:UniProtKB. DR GO; GO:0006694; P:steroid biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0042761; P:very long-chain fatty acid biosynthetic process; ISS:UniProtKB. DR InterPro; IPR001104; 3-oxo-5_a-steroid_4-DH_C. DR Pfam; PF02544; Steroid_dh; 1. DR PROSITE; PS50244; S5A_REDUCTASE; 1. PE 1: Evidence at protein level; KW Acetylation; Complete proteome; Endoplasmic reticulum; Glycoprotein; KW Lipid biosynthesis; Lipid metabolism; Membrane; NADP; Oxidoreductase; KW Reference proteome; Steroid biosynthesis; Transmembrane; KW Transmembrane helix. FT CHAIN 1 308 Very-long-chain enoyl-CoA reductase. FT /FTId=PRO_0000213684. FT TRANSMEM 87 107 Helical; (Potential). FT TRANSMEM 194 214 Helical; (Potential). FT TRANSMEM 255 275 Helical; (Potential). FT MOD_RES 22 22 N6-acetyllysine (By similarity). FT MOD_RES 60 60 N6-acetyllysine. FT CARBOHYD 164 164 N-linked (GlcNAc...) (Potential). FT CARBOHYD 247 247 N-linked (GlcNAc...) (Potential). SQ SEQUENCE 308 AA; 36090 MW; 0576C2813F2C5E4A CRC64; MKHYEVEIRD AKTREKLCFL DKVEPQATIS EIKTLFTKTH PQWYPARQSL RLDPKGKSLK DEDVLQKLPV GTTATLYFRD LGAQISWVTV FLTEYAGPLF IYLLFYFRVP FIYGRKYDFT SSRHTVVHLA CMCHSFHYIK RLLETLFVHR FSHGTMPLRN IFKNCTYYWG FAAWMAYYIN HPLYTPPTYG VQQVKLALAV FVICQLGNFS IHMALRDLRP AGSKTRKIPY PTKNPFTWLF LLVSCPNYTY EVGSWIGFAI LTQCVPVALF SLVGFTQMTI WAKGKHRSYL KEFRDYPPLR MPIIPFLL // ID TET1_MOUSE Reviewed; 2007 AA. AC Q3URK3; Q6ZPK2; Q9CY36; DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot. DT 16-JUN-2009, sequence version 2. DT 19-MAR-2014, entry version 58. DE RecName: Full=Methylcytosine dioxygenase TET1; DE EC=1.14.11.n2; DE AltName: Full=CXXC-type zinc finger protein 6; DE AltName: Full=Ten-eleven translocation 1 gene protein homolog; GN Name=Tet1; Synonyms=Cxxc6, Kiaa1676; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 655-1066 AND 1773-2007. RC STRAIN=C57BL/6J; TISSUE=Liver, and Spinal cord; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1351-1946. RC TISSUE=Embryonic tail; RX PubMed=14621295; DOI=10.1093/dnares/10.4.167; RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., RA Saga Y., Nagase T., Ohara O., Koga H.; RT "Prediction of the coding sequences of mouse homologues of KIAA gene: RT III. The complete nucleotide sequences of 500 mouse KIAA-homologous RT cDNAs identified by screening of terminal sequences of cDNA clones RT randomly sampled from size-fractionated libraries."; RL DNA Res. 10:167-180(2003). RN [4] RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE RP SPECIFICITY, AND MUTAGENESIS OF HIS-1620 AND ASP-1622. RX PubMed=20639862; DOI=10.1038/nature09303; RA Ito S., D'Alessio A.C., Taranova O.V., Hong K., Sowers L.C., Zhang Y.; RT "Role of Tet proteins in 5mC to 5hmC conversion, ES-cell self-renewal RT and inner cell mass specification."; RL Nature 466:1129-1133(2010). RN [5] RP FUNCTION IN DNA DEMETHYLATION. RX PubMed=21496894; DOI=10.1016/j.cell.2011.03.022; RA Guo J.U., Su Y., Zhong C., Ming G.L., Song H.; RT "Hydroxylation of 5-methylcytosine by TET1 promotes active DNA RT demethylation in the adult brain."; RL Cell 145:423-434(2011). RN [6] RP DISRUPTION PHENOTYPE. RX PubMed=21816367; DOI=10.1016/j.stem.2011.07.010; RA Dawlaty M.M., Ganz K., Powell B.E., Hu Y.C., Markoulaki S., RA Cheng A.W., Gao Q., Kim J., Choi S.W., Page D.C., Jaenisch R.; RT "Tet1 is dispensable for maintaining pluripotency and its loss is RT compatible with embryonic and postnatal development."; RL Cell Stem Cell 9:166-175(2011). RN [7] RP DISRUPTION PHENOTYPE. RX PubMed=23352810; DOI=10.1016/j.devcel.2012.12.015; RA Dawlaty M.M., Breiling A., Le T., Raddatz G., Barrasa M.I., RA Cheng A.W., Gao Q., Powell B.E., Li Z., Xu M., Faull K.F., Lyko F., RA Jaenisch R.; RT "Combined deficiency of tet1 and tet2 causes epigenetic abnormalities RT but is compatible with postnatal development."; RL Dev. Cell 24:310-323(2013). RN [8] RP FUNCTION. RX PubMed=21514197; DOI=10.1016/j.molcel.2011.04.005; RA Xu Y., Wu F., Tan L., Kong L., Xiong L., Deng J., Barbera A.J., RA Zheng L., Zhang H., Huang S., Min J., Nicholson T., Chen T., Xu G., RA Shi Y., Zhang K., Shi Y.G.; RT "Genome-wide regulation of 5hmC, 5mC, and gene expression by Tet1 RT hydroxylase in mouse embryonic stem cells."; RL Mol. Cell 42:451-464(2011). RN [9] RP FUNCTION IN TRANSCRIPTIONAL REPRESSION, AND INTERACTION WITH SIN3A. RX PubMed=21490601; DOI=10.1038/nature10066; RA Williams K., Christensen J., Pedersen M.T., Johansen J.V., Cloos P.A., RA Rappsilber J., Helin K.; RT "TET1 and hydroxymethylcytosine in transcription and DNA methylation RT fidelity."; RL Nature 473:343-348(2011). RN [10] RP FUNCTION IN TRANSCRIPTIONAL REPRESSION. RX PubMed=21451524; DOI=10.1038/nature09934; RA Wu H., D'Alessio A.C., Ito S., Xia K., Wang Z., Cui K., Zhao K., RA Eve Sun Y., Zhang Y.; RT "Dual functions of Tet1 in transcriptional regulation in mouse RT embryonic stem cells."; RL Nature 473:389-393(2011). RN [11] RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF HIS-1620 AND RP ASP-1622. RX PubMed=21778364; DOI=10.1126/science.1210597; RA Ito S., Shen L., Dai Q., Wu S.C., Collins L.B., Swenberg J.A., He C., RA Zhang Y.; RT "Tet proteins can convert 5-methylcytosine to 5-formylcytosine and 5- RT carboxylcytosine."; RL Science 333:1300-1303(2011). RN [12] RP FUNCTION, INTERACTION WITH OGT AND HCFC1, AND GLYCOSYLATION. RX PubMed=23352454; DOI=10.1016/j.molcel.2012.12.019; RA Vella P., Scelfo A., Jammula S., Chiacchiera F., Williams K., RA Cuomo A., Roberto A., Christensen J., Bonaldi T., Helin K., Pasini D.; RT "Tet proteins connect the O-linked N-acetylglucosamine transferase Ogt RT to chromatin in embryonic stem cells."; RL Mol. Cell 49:645-656(2013). CC -!- FUNCTION: Dioxygenase that catalyzes the conversion of the CC modified genomic base 5-methylcytosine (5mC) into 5- CC hydroxymethylcytosine (5hmC) and plays a key role in active DNA CC demethylation. Also mediates subsequent conversion of 5hmC into 5- CC formylcytosine (5fC), and conversion of 5fC to 5-carboxylcytosine CC (5caC). Conversion of 5mC into 5hmC, 5fC and 5caC probably CC constitutes the first step in cytosine demethylation. Methylation CC at the C5 position of cytosine bases is an epigenetic modification CC of the mammalian genome which plays an important role in CC transcriptional regulation. In addition to its role in DNA CC demethylation, plays a more general role in chromatin regulation. CC Preferentially binds to CpG-rich sequences at promoters of both CC transcriptionally active and Polycomb-repressed genes. Involved in CC the recruitment of the O-GlcNAc transferase OGT to CpG-rich CC transcription start sites of active genes, thereby promoting CC histone H2B GlcNAcylation by OGT. Also involved in transcription CC repression of a subset of genes through recruitment of CC transcriptional repressors to promoters. Involved in the balance CC between pluripotency and lineage commitment of cells it plays a CC role in embryonic stem cells maintenance and inner cell mass cell CC specification. CC -!- CATALYTIC ACTIVITY: DNA 5-methylcytosine + 2-oxoglutarate + O(2) = CC DNA 5-hydroxymethylcytosine + succinate + CO(2). CC -!- COFACTOR: Binds 1 Fe(2+) ion per subunit (By similarity). CC -!- COFACTOR: Binds 3 zinc ions per subunit. The zinc ions have a CC structural role (By similarity). CC -!- SUBUNIT: Interacts with SIN3A; recruits the transcriptional co- CC repressor SIN3A to gene promoters. Interacts with HCFC1 and OGT. CC -!- INTERACTION: CC Q60520:Sin3a; NbExp=2; IntAct=EBI-4291699, EBI-349034; CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- TISSUE SPECIFICITY: Present in embryonic stem cells (ES cells). CC -!- PTM: Glycosylated. Interaction with OGT leads to GlcNAcylation. CC -!- DISRUPTION PHENOTYPE: No visible phenotype; mice are viable, CC fertile and grossly normal, although some mice have a slightly CC smaller body size at birth. Embryonic stem cells (ESCs) have CC reduced levels of 5-hydroxymethylcytosine (5hmC) and slight CC changes in global gene expression, but are pluripotent and support CC development. Mice lacking both Tet1 and Tet2 are fertile, with CC females having smaller ovaries and reduced fertility. They display CC decreased 5hmC and abnormal methylation at various imprinted loci. CC ESCs lacking both Tet1 and Tet2 remain pluripotent but lack 5hmC, CC leading to developmental defects in chimeric embryos. CC -!- SIMILARITY: Belongs to the TET family. CC -!- SIMILARITY: Contains 1 CXXC-type zinc finger. CC -!- CAUTION: Subsequent steps in cytosine demethylation are subject to CC discussion. According to a first model cytosine demethylation CC occurs through deamination of 5hmC into 5-hydroxymethyluracil CC (5hmU) and subsequent replacement by unmethylated cytosine by the CC base excision repair system (PubMed:21496894). According to CC another model, cytosine demethylation is rather mediated via CC conversion of 5hmC into 5fC and 5caC, followed by excision by TDG. CC -!- SEQUENCE CAUTION: CC Sequence=BAB27288.1; Type=Erroneous initiation; Note=Translation N-terminally extended; CC Sequence=BAC98231.1; Type=Miscellaneous discrepancy; Note=Partially unspliced pre-RNA; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AC166359; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AK010953; BAB27288.1; ALT_INIT; mRNA. DR EMBL; AK141438; BAE24685.1; -; mRNA. DR EMBL; AK129421; BAC98231.1; ALT_SEQ; Transcribed_RNA. DR RefSeq; NP_081660.1; NM_027384.1. DR UniGene; Mm.17774; -. DR ProteinModelPortal; Q3URK3; -. DR SMR; Q3URK3; 569-613. DR BioGrid; 206599; 10. DR IntAct; Q3URK3; 9. DR STRING; 10090.ENSMUSP00000097266; -. DR PhosphoSite; Q3URK3; -. DR PaxDb; Q3URK3; -. DR PRIDE; Q3URK3; -. DR Ensembl; ENSMUST00000050826; ENSMUSP00000059527; ENSMUSG00000047146. DR GeneID; 52463; -. DR KEGG; mmu:52463; -. DR UCSC; uc007fje.2; mouse. DR CTD; 80312; -. DR MGI; MGI:1098693; Tet1. DR eggNOG; NOG236009; -. DR GeneTree; ENSGT00510000046514; -. DR InParanoid; Q6ZPK2; -. DR KO; K13097; -. DR NextBio; 308987; -. DR PRO; PR:Q3URK3; -. DR ArrayExpress; Q3URK3; -. DR Bgee; Q3URK3; -. DR Genevestigator; Q3URK3; -. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0005506; F:iron ion binding; ISS:UniProtKB. DR GO; GO:0070579; F:methylcytosine dioxygenase activity; IDA:UniProtKB. DR GO; GO:0043566; F:structure-specific DNA binding; ISS:UniProtKB. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0016568; P:chromatin modification; IEA:UniProtKB-KW. DR GO; GO:0080111; P:DNA demethylation; IMP:UniProtKB. DR GO; GO:0001826; P:inner cell mass cell differentiation; IMP:UniProtKB. DR GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IMP:UniProtKB. DR GO; GO:0006493; P:protein O-linked glycosylation; IMP:UniProtKB. DR GO; GO:0044030; P:regulation of DNA methylation; IMP:MGI. DR GO; GO:0019827; P:stem cell maintenance; IMP:UniProtKB. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR InterPro; IPR024779; 2OGFeDO_nucleic_acid_mod. DR InterPro; IPR002857; Znf_CXXC. DR Pfam; PF12851; Tet_JBP; 1. DR Pfam; PF02008; zf-CXXC; 1. DR PROSITE; PS51058; ZF_CXXC; 1. PE 1: Evidence at protein level; KW Activator; Chromatin regulator; Complete proteome; Dioxygenase; KW DNA-binding; Glycoprotein; Iron; Metal-binding; Nucleus; KW Oxidoreductase; Reference proteome; Repressor; Transcription; KW Transcription regulation; Zinc; Zinc-finger. FT CHAIN 1 2007 Methylcytosine dioxygenase TET1. FT /FTId=PRO_0000377549. FT ZN_FING 567 608 CXXC-type. FT REGION 512 657 Sufficient for binding to genomic CpG FT islands (By similarity). FT REGION 1528 1541 Interaction with DNA (By similarity). FT REGION 1922 1924 2-oxoglutarate binding (By similarity). FT REGION 1928 1930 Substrate binding (By similarity). FT METAL 1371 1371 Zinc 1 (By similarity). FT METAL 1373 1373 Zinc 1 (By similarity). FT METAL 1430 1430 Zinc 2 (By similarity). FT METAL 1456 1456 Zinc 1; via pros nitrogen (By FT similarity). FT METAL 1458 1458 Zinc 1 (By similarity). FT METAL 1509 1509 Zinc 2 (By similarity). FT METAL 1511 1511 Zinc 2 (By similarity). FT METAL 1527 1527 Zinc 3 (By similarity). FT METAL 1536 1536 Zinc 3 (By similarity). FT METAL 1596 1596 Zinc 3 (By similarity). FT METAL 1618 1618 Zinc 2; via tele nitrogen (By FT similarity). FT METAL 1620 1620 Iron; catalytic (By similarity). FT METAL 1622 1622 Iron; catalytic (By similarity). FT METAL 1907 1907 Iron; catalytic (By similarity). FT METAL 1938 1938 Zinc 3; via pros nitrogen (By FT similarity). FT BINDING 1499 1499 2-oxoglutarate (By similarity). FT BINDING 1612 1612 2-oxoglutarate (By similarity). FT BINDING 1625 1625 Substrate (By similarity). FT BINDING 1653 1653 2-oxoglutarate (By similarity). FT MUTAGEN 1620 1620 H->Y: Loss of enzyme activity; when FT associated with A-1622. FT MUTAGEN 1622 1622 D->A: Loss of enzyme activity; when FT associated with Y-1620. SQ SEQUENCE 2007 AA; 219261 MW; C563672511ACFFC6 CRC64; MSRSRPAKPS KSVKTKLQKK KDIQMKTKTS KQAVRHGASA KAVNPGKPKQ LIKRRDGKKE TEDKTPTPAP SFLTRAGAAR MNRDRNQVLF QNPDSLTCNG FTMALRRTSL SWRLSQRPVV TPKPKKVPPS KKQCTHNIQD EPGVKHSEND SVPSQHATVS PGTENGEQNR CLVEGESQEI TQSCPVFEER IEDTQSCISA SGNLEAEISW PLEGTHCEEL LSHQTSDNEC TSPQECAPLP QRSTSEVTSQ KNTSNQLADL SSQVESIKLS DPSPNPTGSD HNGFPDSSFR IVPELDLKTC MPLDESVYPT ALIRFILAGS QPDVFDTKPQ EKTLITTPEQ VGSHPNQVLD ATSVLGQAFS TLPLQWGFSG ANLVQVEALG KGSDSPEDLG AITMLNQQET VAMDMDRNAT PDLPIFLPKP PNTVATYSSP LLGPEPHSST SCGLEVQGAT PILTLDSGHT PQLPPNPESS SVPLVIAANG TRAEKQFGTS LFPAVPQGFT VAAENEVQHA PLDLTQGSQA APSKLEGEIS RVSITGSADV KATAMSMPVT QASTSSPPCN STPPMVERRK RKACGVCEPC QQKANCGECT YCKNRKNSHQ ICKKRKCEVL KKKPEATSQA QVTKENKRPQ REKKPKVLKT DFNNKPVNGP KSESMDCSRR GHGEEEQRLD LITHPLENVR KNAGGMTGIE VEKWAPNKKS HLAEGQVKGS CDANLTGVEN PQPSEDDKQQ TNPSPTFAQT IRNGMKNVHC LPTDTHLPLN KLNHEEFSKA LGNNSSKLLT DPSNCKDAMS VTTSGGECDH LKGPRNTLLF QKPGLNCRSG AEPTIFNNHP NTHSAGSRPH PPEKVPNKEP KDGSPVQPSL LSLMKDRRLT LEQVVAIEAL TQLSEAPSES SSPSKPEKDE EAHQKTASLL NSCKAILHSV RKDLQDPNVQ GKGLHHDTVV FNGQNRTFKS PDSFATNQAL IKSQGYPSSP TAEKKGAAGG RAPFDGFENS HPLPIESHNL ENCSQVLSCD QNLSSHDPSC QDAPYSQIEE DVAAQLTQLA STINHINAEV RNAESTPESL VAKNTKQKHS QEKRMVHQKP PSSTQTKPSV PSAKPKKAQK KARATPHANK RKKKPPARSS QENDQKKQEQ LAIEYSKMHD IWMSSKFQRF GQSSPRSFPV LLRNIPVFNQ ILKPVTQSKT PSQHNELFPP INQIKFTRNP ELAKEKVKVE PSDSLPTCQF KTESGGQTFA EPADNSQGQP MVSVNQEAHP LPQSPPSNQC ANIMAGAAQT QFHLGAQENL VHQIPPPTLP GTSPDTLLPD PASILRKGKV LHFDGITVVT EKREAQTSSN GPLGPTTDSA QSEFKESIMD LLSKPAKNLI AGLKEQEAAP CDCDGGTQKE KGPYYTHLGA GPSVAAVREL METRFGQKGK AIRIEKIVFT GKEGKSSQGC PVAKWVIRRS GPEEKLICLV RERVDHHCST AVIVVLILLW EGIPRLMADR LYKELTENLR SYSGHPTDRR CTLNKKRTCT CQGIDPKTCG ASFSFGCSWS MYFNGCKFGR SENPRKFRLA PNYPLHEKQL EKNLQELATV LAPLYKQMAP VAYQNQVEYE EVAGDCRLGN EEGRPFSGVT CCMDFCAHSH KDIHNMHNGS TVVCTLIRAD GRDTNCPEDE QLHVLPLYRL ADTDEFGSVE GMKAKIKSGA IQVNGPTRKR RLRFTEPVPR CGKRAKMKQN HNKSGSHNTK SFSSASSTSH LVKDESTDFC PLQASSAETS TCTYSKTASG GFAETSSILH CTMPSGAHSG ANAAAGECTG TVQPAEVAAH PHQSLPTADS PVHAEPLTSP SEQLTSNQSN QQLPLLSNSQ KLASCQVEDE RHPEADEPQH PEDDNLPQLD EFWSDSEEIY ADPSFGGVAI APIHGSVLIE CARKELHATT SLRSPKRGVP FRVSLVFYQH KSLNKPNHGF DINKIKCKCK KVTKKKPADR ECPDVSPEAN LSHQIPSRVA STLTRDNVVT VSPYSLTHVA GPYNRWV // ID TET2_MOUSE Reviewed; 1912 AA. AC Q4JK59; Q3U5R5; Q3U633; Q3UAI0; Q6ZPN2; Q8K2K3; DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot. DT 16-JUN-2009, sequence version 3. DT 19-MAR-2014, entry version 63. DE RecName: Full=Methylcytosine dioxygenase TET2; DE EC=1.14.11.n2; DE AltName: Full=Protein Ayu17-449; GN Name=Tet2; Synonyms=Kiaa1546; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY. RC STRAIN=C57BL/6J; RX PubMed=16722336; DOI=10.1016/S0379-4172(06)60068-1; RA Tang H., Araki K., Yamamura K.; RT "Cloning and expression analysis of a murine novel gene, Ayu17-449."; RL Yi Chuan Xue Bao 33:413-419(2006). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). RC TISSUE=Brain; RX PubMed=14621295; DOI=10.1093/dnares/10.4.167; RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., RA Saga Y., Nagase T., Ohara O., Koga H.; RT "Prediction of the coding sequences of mouse homologues of KIAA gene: RT III. The complete nucleotide sequences of 500 mouse KIAA-homologous RT cDNAs identified by screening of terminal sequences of cDNA clones RT randomly sampled from size-fractionated libraries."; RL DNA Res. 10:167-180(2003). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC STRAIN=FVB/N; TISSUE=Mammary tumor; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 877-1912 (ISOFORM 2). RC STRAIN=C57BL/6J; TISSUE=Bone marrow; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [5] RP FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, AND MUTAGENESIS OF RP HIS-1295 AND ASP-1297. RX PubMed=20639862; DOI=10.1038/nature09303; RA Ito S., D'Alessio A.C., Taranova O.V., Hong K., Sowers L.C., Zhang Y.; RT "Role of Tet proteins in 5mC to 5hmC conversion, ES-cell self-renewal RT and inner cell mass specification."; RL Nature 466:1129-1133(2010). RN [6] RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF TRP-1204; PRO-1280; RP HIS-1795; ARG-1810 AND CYS-1827. RX PubMed=21057493; DOI=10.1038/nature09586; RA Ko M., Huang Y., Jankowska A.M., Pape U.J., Tahiliani M., RA Bandukwala H.S., An J., Lamperti E.D., Koh K.P., Ganetzky R., RA Liu X.S., Aravind L., Agarwal S., Maciejewski J.P., Rao A.; RT "Impaired hydroxylation of 5-methylcytosine in myeloid cancers with RT mutant TET2."; RL Nature 468:839-843(2010). RN [7] RP DISRUPTION PHENOTYPE. RX PubMed=21803851; DOI=10.1182/blood-2010-12-325241; RA Li Z., Cai X., Cai C.L., Wang J., Zhang W., Petersen B.E., Yang F.C., RA Xu M.; RT "Deletion of Tet2 in mice leads to dysregulated hematopoietic stem RT cells and subsequent development of myeloid malignancies."; RL Blood 118:4509-4518(2011). RN [8] RP DISRUPTION PHENOTYPE. RX PubMed=21723200; DOI=10.1016/j.ccr.2011.06.001; RA Moran-Crusio K., Reavie L., Shih A., Abdel-Wahab O., Ndiaye-Lobry D., RA Lobry C., Figueroa M.E., Vasanthakumar A., Patel J., Zhao X., RA Perna F., Pandey S., Madzo J., Song C., Dai Q., He C., Ibrahim S., RA Beran M., Zavadil J., Nimer S.D., Melnick A., Godley L.A., RA Aifantis I., Levine R.L.; RT "Tet2 loss leads to increased hematopoietic stem cell self-renewal and RT myeloid transformation."; RL Cancer Cell 20:11-24(2011). RN [9] RP DISRUPTION PHENOTYPE. RX PubMed=23352810; DOI=10.1016/j.devcel.2012.12.015; RA Dawlaty M.M., Breiling A., Le T., Raddatz G., Barrasa M.I., RA Cheng A.W., Gao Q., Powell B.E., Li Z., Xu M., Faull K.F., Lyko F., RA Jaenisch R.; RT "Combined deficiency of tet1 and tet2 causes epigenetic abnormalities RT but is compatible with postnatal development."; RL Dev. Cell 24:310-323(2013). RN [10] RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF HIS-1295 AND RP ASP-1297. RX PubMed=21778364; DOI=10.1126/science.1210597; RA Ito S., Shen L., Dai Q., Wu S.C., Collins L.B., Swenberg J.A., He C., RA Zhang Y.; RT "Tet proteins can convert 5-methylcytosine to 5-formylcytosine and 5- RT carboxylcytosine."; RL Science 333:1300-1303(2011). RN [11] RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF HIS-1295 AND RP ASP-1297. RX PubMed=21817016; DOI=10.1126/science.1210944; RA He Y.F., Li B.Z., Li Z., Liu P., Wang Y., Tang Q., Ding J., Jia Y., RA Chen Z., Li L., Sun Y., Li X., Dai Q., Song C.X., Zhang K., He C., RA Xu G.L.; RT "Tet-mediated formation of 5-carboxylcytosine and its excision by TDG RT in mammalian DNA."; RL Science 333:1303-1307(2011). RN [12] RP FUNCTION. RX PubMed=23353889; DOI=10.1038/emboj.2012.357; RA Deplus R., Delatte B., Schwinn M.K., Defrance M., Mendez J., RA Murphy N., Dawson M.A., Volkmar M., Putmans P., Calonne E., Shih A.H., RA Levine R.L., Bernard O., Mercher T., Solary E., Urh M., Daniels D.L., RA Fuks F.; RT "TET2 and TET3 regulate GlcNAcylation and H3K4 methylation through OGT RT and SET1/COMPASS."; RL EMBO J. 32:645-655(2013). RN [13] RP FUNCTION, INTERACTION WITH OGT, AND GLYCOSYLATION. RX PubMed=23352454; DOI=10.1016/j.molcel.2012.12.019; RA Vella P., Scelfo A., Jammula S., Chiacchiera F., Williams K., RA Cuomo A., Roberto A., Christensen J., Bonaldi T., Helin K., Pasini D.; RT "Tet proteins connect the O-linked N-acetylglucosamine transferase Ogt RT to chromatin in embryonic stem cells."; RL Mol. Cell 49:645-656(2013). CC -!- FUNCTION: Dioxygenase that catalyzes the conversion of the CC modified genomic base 5-methylcytosine (5mC) into 5- CC hydroxymethylcytosine (5hmC) and plays a key role in active DNA CC demethylation. Has a preference for 5-hydroxymethylcytosine in CpG CC motifs. Also mediates subsequent conversion of 5hmC into 5- CC formylcytosine (5fC), and conversion of 5fC to 5-carboxylcytosine CC (5caC). Conversion of 5mC into 5hmC, 5fC and 5caC probably CC constitutes the first step in cytosine demethylation. Methylation CC at the C5 position of cytosine bases is an epigenetic modification CC of the mammalian genome which plays an important role in CC transcriptional regulation. In addition to its role in DNA CC demethylation, also involved in the recruitment of the O-GlcNAc CC transferase OGT to CpG-rich transcription start sites of active CC genes, thereby promoting histone H2B GlcNAcylation by OGT. CC -!- CATALYTIC ACTIVITY: DNA 5-methylcytosine + 2-oxoglutarate + O(2) = CC DNA 5-hydroxymethylcytosine + succinate + CO(2). CC -!- COFACTOR: Binds 1 Fe(2+) ion per subunit (By similarity). CC -!- COFACTOR: Binds 3 zinc ions per subunit. The zinc ions have a CC structural role (By similarity). CC -!- SUBUNIT: Interacts with HCFC1 (By similarity). Interacts with OGT. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q4JK59-1; Sequence=Displayed; CC Name=2; CC IsoId=Q4JK59-2; Sequence=VSP_032287; CC Note=No experimental confirmation available; CC Name=3; CC IsoId=Q4JK59-3; Sequence=VSP_032286; CC Note=No experimental confirmation available; CC -!- TISSUE SPECIFICITY: Highly expressed in the brain, kidney, heart, CC lung, muscle and stomach. Present in embryonic stem cells (ES CC cells). CC -!- PTM: May be glycosylated. It is unclear whether interaction with CC OGT leads to GlcNAcylation. According to a report, it is CC GlcNAcylated by OGT (PubMed:23352454). In contrast, another group CC reports no GlcNAcylation by OGT in human ortholog. CC -!- DISRUPTION PHENOTYPE: Mice are viable and fertile but develop CC chronic myelomonocytic leukemia probably caused by dysregulation CC of hematopoietic stem cells. Mice lacking both Tet1 and Tet2 are CC fertile, with females having smaller ovaries and reduced CC fertility. They display decreased 5-hydroxymethylcytosine (5hmC) CC and abnormal methylation at various imprinted loci. Embryonic stem CC cells lacking both Tet1 and Tet2 remain pluripotent but lack 5hmC, CC leading to developmental defects in chimeric embryos. CC -!- SIMILARITY: Belongs to the TET family. CC -!- CAUTION: Subsequent steps in cytosine demethylation are subject to CC discussion. According to a first model cytosine demethylation CC occurs through deamination of 5hmC into 5-hydroxymethyluracil CC (5hmU) and subsequent replacement by unmethylated cytosine by the CC base excision repair system. According to another model, cytosine CC demethylation is rather mediated via conversion of 5hmC into 5fC CC and 5caC, followed by excision by TDG (PubMed:21817016). CC -!- SEQUENCE CAUTION: CC Sequence=AAY90126.1; Type=Frameshift; Positions=1143, 1182; CC Sequence=BAC98199.1; Type=Erroneous initiation; Note=Translation N-terminally shortened; CC Sequence=BAE30334.1; Type=Erroneous initiation; Note=Translation N-terminally extended; CC Sequence=BAE30334.1; Type=Frameshift; Positions=1749, 1760; CC Sequence=BAE31106.1; Type=Erroneous initiation; Note=Translation N-terminally extended; CC Sequence=BAE31842.1; Type=Erroneous initiation; Note=Translation N-terminally extended; CC Sequence=BAE31892.1; Type=Erroneous initiation; Note=Translation N-terminally extended; CC Sequence=BAE32012.1; Type=Erroneous initiation; Note=Translation N-terminally extended; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DQ079067; AAY90126.1; ALT_FRAME; mRNA. DR EMBL; AK129389; BAC98199.1; ALT_INIT; mRNA. DR EMBL; BC031159; AAH31159.1; -; mRNA. DR EMBL; BC040785; AAH40785.1; -; mRNA. DR EMBL; AK151359; BAE30334.1; ALT_SEQ; mRNA. DR EMBL; AK152297; BAE31106.1; ALT_INIT; mRNA. DR EMBL; AK153251; BAE31842.1; ALT_INIT; mRNA. DR EMBL; AK153311; BAE31892.1; ALT_INIT; mRNA. DR EMBL; AK153460; BAE32012.1; ALT_INIT; mRNA. DR RefSeq; NP_001035490.2; NM_001040400.2. DR UniGene; Mm.347816; -. DR BioGrid; 229496; 8. DR IntAct; Q4JK59; 1. DR PhosphoSite; Q4JK59; -. DR PRIDE; Q4JK59; -. DR Ensembl; ENSMUST00000098603; ENSMUSP00000096203; ENSMUSG00000040943. [Q4JK59-1] DR GeneID; 214133; -. DR KEGG; mmu:214133; -. DR UCSC; uc008rko.2; mouse. [Q4JK59-2] DR UCSC; uc008rkp.2; mouse. [Q4JK59-3] DR UCSC; uc008rkq.2; mouse. [Q4JK59-1] DR CTD; 54790; -. DR MGI; MGI:2443298; Tet2. DR eggNOG; NOG76473; -. DR GeneTree; ENSGT00510000046514; -. DR HOGENOM; HOG000168510; -. DR HOVERGEN; HBG108562; -. DR OMA; CRCVEQI; -. DR OrthoDB; EOG7MD4P9; -. DR TreeFam; TF337563; -. DR NextBio; 374198; -. DR PRO; PR:Q4JK59; -. DR Bgee; Q4JK59; -. DR CleanEx; MM_TET2; -. DR Genevestigator; Q4JK59; -. DR GO; GO:0005634; C:nucleus; IC:MGI. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0070579; F:methylcytosine dioxygenase activity; IDA:UniProtKB. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0080111; P:DNA demethylation; TAS:UniProtKB. DR GO; GO:0080182; P:histone H3-K4 trimethylation; IMP:UniProtKB. DR GO; GO:0001822; P:kidney development; IMP:MGI. DR GO; GO:0030099; P:myeloid cell differentiation; IMP:UniProtKB. DR GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IMP:UniProtKB. DR GO; GO:0009791; P:post-embryonic development; IMP:MGI. DR GO; GO:0006493; P:protein O-linked glycosylation; IMP:UniProtKB. DR InterPro; IPR024779; 2OGFeDO_nucleic_acid_mod. DR Pfam; PF12851; Tet_JBP; 1. PE 1: Evidence at protein level; KW Alternative splicing; Cell cycle; Chromatin regulator; KW Complete proteome; Dioxygenase; DNA-binding; Glycoprotein; Iron; KW Metal-binding; Oxidoreductase; Phosphoprotein; Reference proteome; KW Zinc. FT CHAIN 1 1912 Methylcytosine dioxygenase TET2. FT /FTId=PRO_0000324589. FT REGION 1203 1216 Interaction with DNA (By similarity). FT REGION 1810 1812 2-oxoglutarate binding (By similarity). FT REGION 1816 1818 Substrate binding (By similarity). FT COMPBIAS 576 921 Gln-rich. FT COMPBIAS 1364 1367 Poly-Arg. FT COMPBIAS 1426 1475 Gln-rich. FT COMPBIAS 1694 1699 Poly-Ser. FT METAL 1048 1048 Zinc 1 (By similarity). FT METAL 1106 1106 Zinc 2 (By similarity). FT METAL 1132 1132 Zinc 1; via pros nitrogen (By FT similarity). FT METAL 1134 1134 Zinc 1 (By similarity). FT METAL 1184 1184 Zinc 2 (By similarity). FT METAL 1186 1186 Zinc 2 (By similarity). FT METAL 1202 1202 Zinc 3 (By similarity). FT METAL 1211 1211 Zinc 3 (By similarity). FT METAL 1271 1271 Zinc 3 (By similarity). FT METAL 1293 1293 Zinc 2; via tele nitrogen (By FT similarity). FT METAL 1295 1295 Iron; catalytic (By similarity). FT METAL 1297 1297 Iron; catalytic (By similarity). FT METAL 1795 1795 Iron; catalytic (By similarity). FT METAL 1826 1826 Zinc 3; via pros nitrogen (By FT similarity). FT BINDING 1174 1174 2-oxoglutarate (By similarity). FT BINDING 1287 1287 2-oxoglutarate (By similarity). FT BINDING 1300 1300 Substrate (By similarity). FT BINDING 1329 1329 2-oxoglutarate (By similarity). FT MOD_RES 97 97 Phosphoserine (By similarity). FT MOD_RES 1036 1036 Phosphoserine (By similarity). FT VAR_SEQ 1 1332 Missing (in isoform 3). FT /FTId=VSP_032286. FT VAR_SEQ 1 1300 Missing (in isoform 2). FT /FTId=VSP_032287. FT MUTAGEN 1204 1204 W->R: Impairs enzyme activity. FT MUTAGEN 1280 1280 P->S: Impairs enzyme activity. FT MUTAGEN 1295 1295 H->Y: Loss of enzyme activity; when FT associated with A-1297. FT MUTAGEN 1297 1297 D->A: Loss of enzyme activity; when FT associated with Y-1295. FT MUTAGEN 1795 1795 H->R,Q: Loss of enzyme activity. FT MUTAGEN 1810 1810 R->S,M: Impairs enzyme activity. FT MUTAGEN 1827 1827 C->D: Impairs enzyme activity. FT CONFLICT 1225 1225 H -> R (in Ref. 1; AAY90126). FT CONFLICT 1626 1626 Q -> R (in Ref. 4; BAE32012/BAE31842). FT CONFLICT 1736 1736 L -> V (in Ref. 4; BAE30334). FT CONFLICT 1737 1737 T -> A (in Ref. 4; BAE30334). FT CONFLICT 1743 1743 K -> E (in Ref. 4; BAE30334). FT CONFLICT 1767 1767 N -> T (in Ref. 4; BAE30334). FT CONFLICT 1772 1772 C -> A (in Ref. 4; BAE30334). FT CONFLICT 1773 1773 I -> F (in Ref. 4; BAE30334). FT CONFLICT 1795 1795 H -> N (in Ref. 4; BAE30334/BAE31106/ FT BAE31892/BAE31842/BAE32012). SQ SEQUENCE 1912 AA; 212130 MW; F49DEE206CD05670 CRC64; MEQDRTTHAE GTRLSPFLIA PPSPISHTEP LAVKLQNGSP LAERPHPEVN GDTKWQSSQS CYGISHMKGS QSSHESPHED RGYSRCLQNG GIKRTVSEPS LSGLHPNKIL KLDQKAKGES NIFEESQERN HGKSSRQPNV SGLSDNGEPV TSTTQESSGA DAFPTRNYNG VEIQVLNEQE GEKGRSVTLL KNKIVLMPNG ATVSAHSEEN TRGELLEKTQ CYPDCVSIAV QSTASHVNTP SSQAAIELSH EIPQPSLTSA QINFSQTSSL QLPPEPAAMV TKACDADNAS KPAIVPGTCP FQKAEHQQKS ALDIGPSRAE NKTIQGSMEL FAEEYYPSSD RNLQASHGSS EQYSKQKETN GAYFRQSSKF PKDSISPTTV TPPSQSLLAP RLVLQPPLEG KGALNDVALE EHHDYPNRSN RTLLREGKID HQPKTSSSQS LNPSVHTPNP PLMLPEQHQN DCGSPSPEKS RKMSEYLMYY LPNHGHSGGL QEHSQYLMGH REQEIPKDAN GKQTQGSVQA APGWIELKAP NLHEALHQTK RKDISLHSVL HSQTGPVNQM SSKQSTGNVN MPGGFQRLPY LQKTAQPEQK AQMYQVQVNQ GPSPGMGDQH LQFQKALYQE CIPRTDPSSE AHPQAPSVPQ YHFQQRVNPS SDKHLSQQAT ETQRLSGFLQ HTPQTQASQT PASQNSNFPQ ICQQQQQQQL QRKNKEQMPQ TFSHLQGSND KQREGSCFGQ IKVEESFCVG NQYSKSSNFQ THNNTQGGLE QVQNINKNFP YSKILTPNSS NLQILPSNDT HPACEREQAL HPVGSKTSNL QNMQYFPNNV TPNQDVHRCF QEQAQKPQQA SSLQGLKDRS QGESPAPPAE AAQQRYLVHN EAKALPVPEQ GGSQTQTPPQ KDTQKHAALR WLLLQKQEQQ QTQQSQPGHN QMLRPIKTEP VSKPSSYRYP LSPPQENMSS RIKQEISSPS RDNGQPKSII ETMEQHLKQF QLKSLCDYKA LTLKSQKHVK VPTDIQAAES ENHARAAEPQ ATKSTDCSVL DDVSESDTPG EQSQNGKCEG CNPDKDEAPY YTHLGAGPDV AAIRTLMEER YGEKGKAIRI EKVIYTGKEG KSSQGCPIAK WVYRRSSEEE KLLCLVRVRP NHTCETAVMV IAIMLWDGIP KLLASELYSE LTDILGKCGI CTNRRCSQNE TRNCCCQGEN PETCGASFSF GCSWSMYYNG CKFARSKKPR KFRLHGAEPK EEERLGSHLQ NLATVIAPIY KKLAPDAYNN QVEFEHQAPD CCLGLKEGRP FSGVTACLDF SAHSHRDQQN MPNGSTVVVT LNREDNREVG AKPEDEQFHV LPMYIIAPED EFGSTEGQEK KIRMGSIEVL QSFRRRRVIR IGELPKSCKK KAEPKKAKTK KAARKRSSLE NCSSRTEKGK SSSHTKLMEN ASHMKQMTAQ PQLSGPVIRQ PPTLQRHLQQ GQRPQQPQPP QPQPQTTPQP QPQPQHIMPG NSQSVGSHCS GSTSVYTRQP TPHSPYPSSA HTSDIYGDTN HVNFYPTSSH ASGSYLNPSN YMNPYLGLLN QNNQYAPFPY NGSVPVDNGS PFLGSYSPQA QSRDLHRYPN QDHLTNQNLP PIHTLHQQTF GDSPSKYLSY GNQNMQRDAF TTNSTLKPNV HHLATFSPYP TPKMDSHFMG AASRSPYSHP HTDYKTSEHH LPSHTIYSYT AAASGSSSSH AFHNKENDNI ANGLSRVLPG FNHDRTASAQ ELLYSLTGSS QEKQPEVSGQ DAAAVQEIEY WSDSEHNFQD PCIGGVAIAP THGSILIECA KCEVHATTKV NDPDRNHPTR ISLVLYRHKN LFLPKHCLAL WEAKMAEKAR KEEECGKNGS DHVSQKNHGK QEKREPTGPQ EPSYLRFIQS LAENTGSVTT DSTVTTSPYA FTQVTGPYNT FV // ID TET3_MOUSE Reviewed; 1668 AA. AC Q8BG87; Q4VAD3; Q8C8N8; Q8CI60; DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot. DT 16-JUN-2009, sequence version 3. DT 19-MAR-2014, entry version 81. DE RecName: Full=Methylcytosine dioxygenase TET3; DE EC=1.14.11.n2; GN Name=Tet3; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC STRAIN=C57BL/6J; TISSUE=Adipose tissue, and Retina; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 757-1553 (ISOFORM 1). RC STRAIN=C57BL/6J; TISSUE=Egg; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, AND MUTAGENESIS OF RP HIS-950 AND ASP-952. RX PubMed=20639862; DOI=10.1038/nature09303; RA Ito S., D'Alessio A.C., Taranova O.V., Hong K., Sowers L.C., Zhang Y.; RT "Role of Tet proteins in 5mC to 5hmC conversion, ES-cell self-renewal RT and inner cell mass specification."; RL Nature 466:1129-1133(2010). RN [5] RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION RP PHENOTYPE. RX PubMed=21892189; DOI=10.1038/nature10443; RA Gu T.P., Guo F., Yang H., Wu H.P., Xu G.F., Liu W., Xie Z.G., Shi L., RA He X., Jin S.G., Iqbal K., Shi Y.G., Deng Z., Szabo P.E., RA Pfeifer G.P., Li J., Xu G.L.; RT "The role of Tet3 DNA dioxygenase in epigenetic reprogramming by RT oocytes."; RL Nature 477:606-610(2011). RN [6] RP FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE. RX PubMed=21407207; DOI=10.1038/ncomms1240; RA Wossidlo M., Nakamura T., Lepikhov K., Marques C.J., Zakhartchenko V., RA Boiani M., Arand J., Nakano T., Reik W., Walter J.; RT "5-Hydroxymethylcytosine in the mammalian zygote is linked with RT epigenetic reprogramming."; RL Nat. Commun. 2:241-241(2011). RN [7] RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE. RX PubMed=21321204; DOI=10.1073/pnas.1014033108; RA Iqbal K., Jin S.G., Pfeifer G.P., Szabo P.E.; RT "Reprogramming of the paternal genome upon fertilization involves RT genome-wide oxidation of 5-methylcytosine."; RL Proc. Natl. Acad. Sci. U.S.A. 108:3642-3647(2011). RN [8] RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF HIS-950 AND ASP-952. RX PubMed=21778364; DOI=10.1126/science.1210597; RA Ito S., Shen L., Dai Q., Wu S.C., Collins L.B., Swenberg J.A., He C., RA Zhang Y.; RT "Tet proteins can convert 5-methylcytosine to 5-formylcytosine and 5- RT carboxylcytosine."; RL Science 333:1300-1303(2011). RN [9] RP FUNCTION. RX PubMed=22722204; DOI=10.1038/nature11093; RA Nakamura T., Liu Y.J., Nakashima H., Umehara H., Inoue K., Matoba S., RA Tachibana M., Ogura A., Shinkai Y., Nakano T.; RT "PGC7 binds histone H3K9me2 to protect against conversion of 5mC to RT 5hmC in early embryos."; RL Nature 486:415-419(2012). CC -!- FUNCTION: Dioxygenase that catalyzes the conversion of the CC modified genomic base 5-methylcytosine (5mC) into 5- CC hydroxymethylcytosine (5hmC) and plays a key role in epigenetic CC chromatin reprogramming in the zygote following fertilization. CC Also mediates subsequent conversion of 5hmC into 5-formylcytosine CC (5fC), and conversion of 5fC to 5-carboxylcytosine (5caC). CC Conversion of 5mC into 5hmC, 5fC and 5caC probably constitutes the CC first step in cytosine demethylation. In zygotes, DNA CC demethylation occurs selectively in the paternal pronucleus before CC the first cell division, while the adjacent maternal pronucleus CC and certain paternally-imprinted loci are protected from this CC process. Participates in DNA demethylation in the paternal CC pronucleus by mediating conversion of 5mC into 5hmC, 5fC and 5caC. CC Does not mediate DNA demethylation of maternal pronucleus because CC of the presence of DPPA3/PGC7 on maternal chromatin that prevents CC TET3-binding to chromatin. In addition to its role in DNA CC demethylation, also involved in the recruitment of the O-GlcNAc CC transferase OGT to CpG-rich transcription start sites of active CC genes, thereby promoting histone H2B GlcNAcylation by OGT. CC -!- CATALYTIC ACTIVITY: DNA 5-methylcytosine + 2-oxoglutarate + O(2) = CC DNA 5-hydroxymethylcytosine + succinate + CO(2). CC -!- COFACTOR: Binds 1 Fe(2+) ion per subunit (By similarity). CC -!- COFACTOR: Binds 3 zinc ions per subunit. The zinc ions have a CC structural role (By similarity). CC -!- SUBUNIT: Interacts with HCFC1 and OGT (By similarity). CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=At the zygotic CC stage, localizes in the male pronucleus, while it localizes to the CC cytoplasm at other preimplantation stages. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q8BG87-1; Sequence=Displayed; CC Name=2; CC IsoId=Q8BG87-2; Sequence=VSP_034193, VSP_034194; CC -!- TISSUE SPECIFICITY: Highly expressed in oocytes and zygotes. Not CC expressed in embryonic stem cells (ES cells). CC -!- DEVELOPMENTAL STAGE: Expressed maternally. Expressed at high CC levels in oocytes and zygotes, with rapidly declining levels at CC the two-cell stage. CC -!- DISRUPTION PHENOTYPE: Neonatal lethality. A germline-specific CC conditional knockout produces females that are normal in growth CC and morphology but display much reduced fecundity in terms of the CC frequency of successful pregnancy per mating and the litter size. CC No 5hmC signal is detected in the late male pronuclei of zygotes CC collected from the conditional knockout females mated with wild- CC type males. In contrast, deletion of Tet3 from the male germ cells CC does not seem to affect the change in 5hmC and 5mC. CC -!- SIMILARITY: Belongs to the TET family. CC -!- CAUTION: Subsequent steps in cytosine demethylation are subject to CC discussion. According to a first model cytosine demethylation CC occurs through deamination of 5hmC into 5-hydroxymethyluracil CC (5hmU) and subsequent replacement by unmethylated cytosine by the CC base excision repair system. According to another model, cytosine CC demethylation is rather mediated via conversion of 5hmC into 5fC CC and 5caC, followed by excision by TDG. CC -!- SEQUENCE CAUTION: CC Sequence=AAH96437.1; Type=Erroneous initiation; Note=Translation N-terminally extended; CC Sequence=AAH96437.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK044758; BAC32068.1; -; mRNA. DR EMBL; AK046543; BAC32779.1; -; mRNA. DR EMBL; AK046552; BAC32784.1; -; mRNA. DR EMBL; AK046553; BAC32785.1; -; mRNA. DR EMBL; AC090648; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC159713; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC096437; AAH96437.1; ALT_SEQ; mRNA. DR RefSeq; NP_898961.2; NM_183138.2. DR UniGene; Mm.211030; -. DR UniGene; Mm.479194; -. DR ProteinModelPortal; Q8BG87; -. DR PhosphoSite; Q8BG87; -. DR PRIDE; Q8BG87; -. DR Ensembl; ENSMUST00000089622; ENSMUSP00000087049; ENSMUSG00000034832. [Q8BG87-1] DR GeneID; 194388; -. DR KEGG; mmu:194388; -. DR UCSC; uc009cni.2; mouse. [Q8BG87-1] DR UCSC; uc009cnl.1; mouse. [Q8BG87-2] DR CTD; 200424; -. DR MGI; MGI:2446229; Tet3. DR eggNOG; NOG140185; -. DR GeneTree; ENSGT00510000046514; -. DR HOGENOM; HOG000203929; -. DR HOVERGEN; HBG079550; -. DR InParanoid; Q4VAD3; -. DR OMA; QKPDWEA; -. DR OrthoDB; EOG789C9H; -. DR TreeFam; TF342373; -. DR ChiTaRS; TET3; mouse. DR NextBio; 371587; -. DR PRO; PR:Q8BG87; -. DR ArrayExpress; Q8BG87; -. DR Bgee; Q8BG87; -. DR Genevestigator; Q8BG87; -. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0001939; C:female pronucleus; IDA:MGI. DR GO; GO:0001940; C:male pronucleus; IDA:UniProtKB. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0070579; F:methylcytosine dioxygenase activity; IDA:UniProtKB. DR GO; GO:0080111; P:DNA demethylation; IMP:UniProtKB. DR GO; GO:0044727; P:DNA demethylation of male pronucleus; IMP:UniProtKB. DR GO; GO:0080182; P:histone H3-K4 trimethylation; ISS:UniProtKB. DR GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; ISS:UniProtKB. DR GO; GO:0006493; P:protein O-linked glycosylation; ISS:UniProtKB. DR InterPro; IPR024779; 2OGFeDO_nucleic_acid_mod. DR Pfam; PF12851; Tet_JBP; 1. PE 1: Evidence at protein level; KW Alternative splicing; Chromatin regulator; Complete proteome; KW Cytoplasm; Developmental protein; Dioxygenase; DNA-binding; Iron; KW Metal-binding; Nucleus; Oxidoreductase; Reference proteome; Zinc. FT CHAIN 1 1668 Methylcytosine dioxygenase TET3. FT /FTId=PRO_0000340228. FT REGION 858 871 Interaction with DNA (By similarity). FT REGION 1561 1563 2-oxoglutarate binding (By similarity). FT REGION 1567 1569 Substrate binding (By similarity). FT METAL 701 701 Zinc 1 (By similarity). FT METAL 703 703 Zinc 1 (By similarity). FT METAL 761 761 Zinc 2 (By similarity). FT METAL 787 787 Zinc 1; via pros nitrogen (By FT similarity). FT METAL 789 789 Zinc 1 (By similarity). FT METAL 839 839 Zinc 2 (By similarity). FT METAL 841 841 Zinc 2 (By similarity). FT METAL 857 857 Zinc 3 (By similarity). FT METAL 866 866 Zinc 3 (By similarity). FT METAL 926 926 Zinc 3 (By similarity). FT METAL 948 948 Zinc 2; via tele nitrogen (By FT similarity). FT METAL 950 950 Iron; catalytic (By similarity). FT METAL 952 952 Iron; catalytic (By similarity). FT METAL 1546 1546 Iron; catalytic (By similarity). FT METAL 1577 1577 Zinc 3; via pros nitrogen (By FT similarity). FT BINDING 829 829 2-oxoglutarate (By similarity). FT BINDING 942 942 2-oxoglutarate (By similarity). FT BINDING 955 955 Substrate (By similarity). FT BINDING 984 984 2-oxoglutarate (By similarity). FT VAR_SEQ 705 719 EQIVEKDEGPYYTHL -> GRWEWSRAFFLSVEH (in FT isoform 2). FT /FTId=VSP_034193. FT VAR_SEQ 720 1668 Missing (in isoform 2). FT /FTId=VSP_034194. FT MUTAGEN 950 950 H->Y: Loss of enzyme activity; when FT associated with A-952. FT MUTAGEN 952 952 D->A: Loss of enzyme activity; when FT associated with Y-950. FT CONFLICT 962 962 V -> A (in Ref. 3; AAH96437). SQ SEQUENCE 1668 AA; 180378 MW; 73DD97090F917199 CRC64; MDSGPVYHGD SRQLSTSGAP VNGAREPAGP GLLGAAGPWR VDQKPDWEAA SGPTHAARLE DAHDLVAFSA VAEAVSSYGA LSTRLYETFN REMSREAGSN GRGPRPESCS EGSEDLDTLQ TALALARHGM KPPNCTCDGP ECPDFLEWLE GKIKSMAMEG GQGRPRLPGA LPPSEAGLPA PSTRPPLLSS EVPQVPPLEG LPLSQSALSI AKEKNISLQT AIAIEALTQL SSALPQPSHS TSQASCPLPE ALSPSAPFRS PQSYLRAPSW PVVPPEEHPS FAPDSPAFPP ATPRPEFSEA WGTDTPPATP RNSWPVPRPS PDPMAELEQL LGSASDYIQS VFKRPEALPT KPKVKVEAPS SSPAPVPSPI SQREAPLLSS EPDTHQKAQT ALQQHLHHKR NLFLEQAQDA SFPTSTEPQA PGWWAPPGSP APRPPDKPPK EKKKKPPTPA GGPVGAEKTT PGIKTSVRKP IQIKKSRSRD MQPLFLPVRQ IVLEGLKPQA SEGQAPLPAQ LSVPPPASQG AASQSCATPL TPEPSLALFA PSPSGDSLLP PTQEMRSPSP MVALQSGSTG GPLPPADDKL EELIRQFEAE FGDSFGLPGP PSVPIQEPEN QSTCLPAPES PFATRSPKKI KIESSGAVTV LSTTCFHSEE GGQEATPTKA ENPLTPTLSG FLESPLKYLD TPTKSLLDTP AKKAQSEFPT CDCVEQIVEK DEGPYYTHLG SGPTVASIRE LMEDRYGEKG KAIRIEKVIY TGKEGKSSRG CPIAKWVIRR HTLEEKLLCL VRHRAGHHCQ NAVIVILILA WEGIPRSLGD TLYQELTDTL RKYGNPTSRR CGLNDDRTCA CQGKDPNTCG ASFSFGCSWS MYFNGCKYAR SKTPRKFRLT GDNPKEEEVL RNSFQDLATE VAPLYKRLAP QAYQNQVTNE DVAIDCRLGL KEGRPFSGVT ACMDFCAHAH KDQHNLYNGC TVVCTLTKED NRCVGQIPED EQLHVLPLYK MASTDEFGSE ENQNAKVSSG AIQVLTAFPR EVRRLPEPAK SCRQRQLEAR KAAAEKKKLQ KEKLSTPEKI KQEALELAGV TTDPGLSLKG GLSQQSLKPS LKVEPQNHFS SFKYSGNAVV ESYSVLGSCR PSDPYSMSSV YSYHSRYAQP GLASVNGFHS KYTLPSFGYY GFPSSNPVFP SQFLGPSAWG HGGSGGSFEK KPDLHALHNS LNPAYGGAEF AELPGQAVAT DNHHPIPHHQ QPAYPGPKEY LLPKVPQLHP ASRDPSPFAQ SSSCYNRSIK QEPIDPLTQA ESIPRDSAKM SRTPLPEASQ NGGPSHLWGQ YSGGPSMSPK RTNSVGGNWG VFPPGESPTI VPDKLNSFGA SCLTPSHFPE SQWGLFTGEG QQSAPHAGAR LRGKPWSPCK FGNGTSALTG PSLTEKPWGM GTGDFNPALK GGPGFQDKLW NPVKVEEGRI PTPGANPLDK AWQAFGMPLS SNEKLFGALK SEEKLWDPFS LEEGTAEEPP SKGVVKEEKS GPTVEEDEEE LWSDSEHNFL DENIGGVAVA PAHCSILIEC ARRELHATTP LKKPNRCHPT RISLVFYQHK NLNQPNHGLA LWEAKMKQLA ERARQRQEEA ARLGLGQQEA KLYGKKRKWG GAMVAEPQHK EKKGAIPTRQ ALAMPTDSAV TVSSYAYTKV TGPYSRWI // ID TMLH_MOUSE Reviewed; 421 AA. AC Q91ZE0; Q3TSX6; Q3UMX1; Q91XH1; DT 20-JUN-2002, integrated into UniProtKB/Swiss-Prot. DT 20-JUN-2002, sequence version 2. DT 19-MAR-2014, entry version 102. DE RecName: Full=Trimethyllysine dioxygenase, mitochondrial; DE EC=1.14.11.8; DE AltName: Full=Epsilon-trimethyllysine 2-oxoglutarate dioxygenase; DE AltName: Full=TML hydroxylase; DE AltName: Full=TML-alpha-ketoglutarate dioxygenase; DE Short=TML dioxygenase; DE Short=TMLD; DE Flags: Precursor; GN Name=Tmlhe; Synonyms=Tmlh; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Lung, and Thymus; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Liver; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 13-421. RC STRAIN=FVB/N; RX PubMed=11431483; DOI=10.1074/jbc.M105929200; RA Vaz F.M., Ofman R., Westinga K., Back J.W., Wanders R.J.A.; RT "Molecular and biochemical characterization of rat epsilon-N- RT trimethyllysine hydroxylase, the first enzyme of carnitine RT biosynthesis."; RL J. Biol. Chem. 276:33512-33517(2001). RN [6] RP DEVELOPMENTAL STAGE. RX PubMed=17408883; DOI=10.1016/j.gene.2007.02.012; RA Monfregola J., Napolitano G., Conte I., Cevenini A., Migliaccio C., RA D'Urso M., Ursini M.V.; RT "Functional characterization of the TMLH gene: promoter analysis, in RT situ hybridization, identification and mapping of alternative splicing RT variants."; RL Gene 395:86-97(2007). RN [7] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-179, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23576753; DOI=10.1073/pnas.1302961110; RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., RA Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.; RT "Label-free quantitative proteomics of the lysine acetylome in RT mitochondria identifies substrates of SIRT3 in metabolic pathways."; RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013). CC -!- FUNCTION: Converts trimethyllysine (TML) into CC hydroxytrimethyllysine (HTML). CC -!- CATALYTIC ACTIVITY: N(6),N(6),N(6)-trimethyl-L-lysine + 2- CC oxoglutarate + O(2) = 3-hydroxy-N(6),N(6),N(6)-trimethyl-L-lysine CC + succinate + CO(2). CC -!- COFACTOR: Binds 1 Fe(2+) ion per subunit (By similarity). CC -!- COFACTOR: Ascorbate. CC -!- PATHWAY: Amine and polyamine biosynthesis; carnitine biosynthesis. CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix (By similarity). CC -!- DEVELOPMENTAL STAGE: Present already at 9.0 dpc. At 10.5 dpc, CC expressed throughout the embryo. At 12.5 dpc, higher levels in the CC developing lung, liver and brain compared to other tissues. In the CC postnatal day 7 brain, high levels in the Purkinje cell layer of CC the cerebellum and in the hyppocampal areas of the dentate gyrus CC and CA1, CA2 and CA3 pyramidal cells. CC -!- SIMILARITY: Belongs to the gamma-BBH/TMLD family. CC -!- SEQUENCE CAUTION: CC Sequence=AAK54387.1; Type=Erroneous initiation; Note=Translation N-terminally extended; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK144627; BAE25977.1; -; mRNA. DR EMBL; AK161724; BAE36549.1; -; mRNA. DR EMBL; CAAA01137825; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CAAA01183048; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CAAA01120074; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CAAA01019119; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH466822; EDL07804.1; -; Genomic_DNA. DR EMBL; BC010495; AAH10495.1; -; mRNA. DR EMBL; BC115365; AAI15366.1; -; mRNA. DR EMBL; AY033513; AAK54387.1; ALT_INIT; mRNA. DR RefSeq; NP_620097.1; NM_138758.1. DR UniGene; Mm.394228; -. DR ProteinModelPortal; Q91ZE0; -. DR SMR; Q91ZE0; 53-417. DR IntAct; Q91ZE0; 1. DR MINT; MINT-4138064; -. DR PhosphoSite; Q91ZE0; -. DR PaxDb; Q91ZE0; -. DR PRIDE; Q91ZE0; -. DR Ensembl; ENSMUST00000115964; ENSMUSP00000111624; ENSMUSG00000079834. DR GeneID; 192289; -. DR KEGG; mmu:192289; -. DR UCSC; uc009uyo.1; mouse. DR CTD; 55217; -. DR MGI; MGI:2180203; Tmlhe. DR eggNOG; COG2175; -. DR GeneTree; ENSGT00530000063582; -. DR HOGENOM; HOG000210004; -. DR HOVERGEN; HBG035650; -. DR InParanoid; Q91ZE0; -. DR KO; K00474; -. DR OMA; HPRILWN; -. DR OrthoDB; EOG7XPZ5P; -. DR TreeFam; TF313805; -. DR BRENDA; 1.14.11.8; 3474. DR UniPathway; UPA00118; -. DR NextBio; 371290; -. DR PRO; PR:Q91ZE0; -. DR Bgee; Q91ZE0; -. DR CleanEx; MM_TMLHE; -. DR Genevestigator; Q91ZE0; -. DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0031418; F:L-ascorbic acid binding; IEA:InterPro. DR GO; GO:0016702; F:oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen; IDA:MGI. DR GO; GO:0050353; F:trimethyllysine dioxygenase activity; IEA:UniProtKB-EC. DR GO; GO:0045329; P:carnitine biosynthetic process; IDA:MGI. DR GO; GO:0051354; P:negative regulation of oxidoreductase activity; IEA:Ensembl. DR InterPro; IPR010376; DUF971. DR InterPro; IPR003819; Taurine_dOase. DR InterPro; IPR012776; Trimethyllysine_dOase. DR PANTHER; PTHR10696:SF2; PTHR10696:SF2; 1. DR Pfam; PF06155; DUF971; 1. DR Pfam; PF02668; TauD; 1. DR TIGRFAMs; TIGR02410; carnitine_TMLD; 1. PE 1: Evidence at protein level; KW Acetylation; Carnitine biosynthesis; Complete proteome; Dioxygenase; KW Iron; Metal-binding; Mitochondrion; Oxidoreductase; KW Reference proteome; Transit peptide. FT TRANSIT 1 15 Mitochondrion (By similarity). FT CHAIN 16 421 Trimethyllysine dioxygenase, FT mitochondrial. FT /FTId=PRO_0000002796. FT METAL 242 242 Iron; catalytic (By similarity). FT METAL 244 244 Iron; catalytic (By similarity). FT METAL 389 389 Iron; catalytic (By similarity). FT MOD_RES 179 179 N6-acetyllysine. FT MOD_RES 236 236 N6-acetyllysine (By similarity). FT CONFLICT 8 8 H -> Q (in Ref. 1; BAE36549). FT CONFLICT 188 188 G -> K (in Ref. 1; BAE36549). SQ SEQUENCE 421 AA; 49610 MW; 1474AD5742E88F43 CRC64; MWYHKLLHQQ SRLRNLMKRG NIAQGLHLSN FKSLFSSSIH WCHTTSKSVN CTWHQHEDHL ELQYAGTVMR FDYVWLRDHC RSASCYNSKT HQRSLDTASV DLCIKPKTVH LDETMLFFTW PDGHVTRYDL DWLVKNSYEG QKQKVIQPRI LWNSKLYQQA QVPSVDFQCF LETNEGLKKF LQNFLLYGIA FVENVPPTEE HTEKLAERIS LIRETIYGRM WYFTSDFSRG DTAYTKLALD RHTDTTYFQE PCGIQVFHCL KHEGTGGRTL LVDGFYAAQQ VLQKAPEEFE LLSKVPLKHE YIENVGQCHN HMIGVGPILN IYPWNKELYL IRYNNYDRAV INTVPYDVVH RWYTAHRTLT TELRRPENEL WVKLKPGKVL FIDNWRVLHG RESFTGYRQL CGCYLTRDDV LNTARLLGLH A // ID TPH1_MOUSE Reviewed; 447 AA. AC P17532; DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1990, sequence version 1. DT 19-MAR-2014, entry version 129. DE RecName: Full=Tryptophan 5-hydroxylase 1; DE EC=1.14.16.4; DE AltName: Full=Tryptophan 5-monooxygenase 1; GN Name=Tph1; Synonyms=Tph; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=2110547; DOI=10.1016/0888-7543(90)90522-V; RA Stoll J., Kozak C.A., Goldman D.; RT "Characterization and chromosomal mapping of a cDNA encoding RT tryptophan hydroxylase from a mouse mastocytoma cell line."; RL Genomics 7:88-96(1990). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6; TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- CATALYTIC ACTIVITY: L-tryptophan + tetrahydrobiopterin + O(2) = 5- CC hydroxy-L-tryptophan + 4a-hydroxytetrahydrobiopterin. CC -!- COFACTOR: Fe(2+) ion. CC -!- PATHWAY: Aromatic compound metabolism; serotonin biosynthesis; CC serotonin from L-tryptophan: step 1/2. CC -!- SUBUNIT: Homotetramer. CC -!- SIMILARITY: Belongs to the biopterin-dependent aromatic amino acid CC hydroxylase family. CC -!- SIMILARITY: Contains 1 ACT domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; J04758; AAA63401.1; -; mRNA. DR EMBL; BC072582; AAH72582.1; -; mRNA. DR PIR; A34582; A34582. DR RefSeq; NP_001129556.1; NM_001136084.2. DR RefSeq; NP_033440.1; NM_009414.3. DR RefSeq; XP_006540850.1; XM_006540787.1. DR UniGene; Mm.248684; -. DR UniGene; Mm.398047; -. DR ProteinModelPortal; P17532; -. DR SMR; P17532; 6-441. DR PhosphoSite; P17532; -. DR PaxDb; P17532; -. DR PRIDE; P17532; -. DR Ensembl; ENSMUST00000049298; ENSMUSP00000037752; ENSMUSG00000040046. DR Ensembl; ENSMUST00000107669; ENSMUSP00000103296; ENSMUSG00000040046. DR GeneID; 21990; -. DR KEGG; mmu:21990; -. DR UCSC; uc009gyq.2; mouse. DR CTD; 7166; -. DR MGI; MGI:98796; Tph1. DR eggNOG; COG3186; -. DR HOGENOM; HOG000233373; -. DR HOVERGEN; HBG006841; -. DR InParanoid; P17532; -. DR KO; K00502; -. DR OMA; TWGTVFQ; -. DR OrthoDB; EOG7KM5T1; -. DR TreeFam; TF313327; -. DR UniPathway; UPA00846; UER00799. DR NextBio; 301724; -. DR PRO; PR:P17532; -. DR ArrayExpress; P17532; -. DR Bgee; P17532; -. DR CleanEx; MM_TPH1; -. DR Genevestigator; P17532; -. DR GO; GO:0043005; C:neuron projection; IEA:Ensembl. DR GO; GO:0016597; F:amino acid binding; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0004510; F:tryptophan 5-monooxygenase activity; IDA:MGI. DR GO; GO:0009072; P:aromatic amino acid family metabolic process; IEA:InterPro. DR GO; GO:0046849; P:bone remodeling; IGI:MGI. DR GO; GO:0007623; P:circadian rhythm; IEA:Ensembl. DR GO; GO:0060749; P:mammary gland alveolus development; IMP:MGI. DR GO; GO:0030279; P:negative regulation of ossification; IEA:Ensembl. DR GO; GO:0035902; P:response to immobilization stress; IEA:Ensembl. DR GO; GO:0042427; P:serotonin biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 1.10.800.10; -; 1. DR InterPro; IPR002912; ACT_dom. DR InterPro; IPR001273; ArAA_hydroxylase. DR InterPro; IPR018301; ArAA_hydroxylase_Fe/CU_BS. DR InterPro; IPR019774; Aromatic-AA_hydroxylase_C. DR InterPro; IPR005963; Trp_5_mOase. DR InterPro; IPR019773; Tyrosine_3-monooxygenase-like. DR PANTHER; PTHR11473; PTHR11473; 1. DR Pfam; PF01842; ACT; 1. DR Pfam; PF00351; Biopterin_H; 1. DR PIRSF; PIRSF000336; TH; 1. DR PRINTS; PR00372; FYWHYDRXLASE. DR SUPFAM; SSF56534; SSF56534; 1. DR TIGRFAMs; TIGR01270; Trp_5_monoox; 1. DR PROSITE; PS51671; ACT; 1. DR PROSITE; PS00367; BH4_AAA_HYDROXYL_1; 1. DR PROSITE; PS51410; BH4_AAA_HYDROXYL_2; 1. PE 2: Evidence at transcript level; KW Complete proteome; Iron; Metal-binding; Monooxygenase; Oxidoreductase; KW Phosphoprotein; Reference proteome; Serotonin biosynthesis. FT CHAIN 1 447 Tryptophan 5-hydroxylase 1. FT /FTId=PRO_0000205569. FT DOMAIN 22 97 ACT. FT METAL 275 275 Iron (By similarity). FT METAL 280 280 Iron (By similarity). FT METAL 320 320 Iron (By similarity). FT BINDING 238 238 Tryptophan (By similarity). FT BINDING 260 260 Tryptophan (By similarity). FT BINDING 268 268 Tryptophan (By similarity). FT BINDING 339 339 Tryptophan (By similarity). FT BINDING 369 369 Tryptophan; via carbonyl oxygen (By FT similarity). FT MOD_RES 61 61 Phosphoserine; by PKA (Potential). SQ SEQUENCE 447 AA; 51343 MW; 16C839F22A138BCA CRC64; MIEDNKENKE NKDHSSERGR VTLIFSLENE VGGLIKVLKI FQENHVSLLH IESRKSKQRN SEFEIFVDCD ISREQLNDIF PLLKSHATVL SVDSPDQLTA KEDVMETVPW FPKKISDLDF CANRVLLYGS ELDADHPGFK DNVYRRRRKY FAELAMNYKH GDPIPKIEFT EEEIKTWGTI FRELNKLYPT HACREYLRNL PLLSKYCGYR EDNIPQLEDV SNFLKERTGF SIRPVAGYLS PRDFLSGLAF RVFHCTQYVR HSSDPLYTPE PDTCHELLGH VPLLAEPSFA QFSQEIGLAS LGASEETVQK LATCYFFTVE FGLCKQDGQL RVFGAGLLSS ISELKHALSG HAKVKPFDPK IACKQECLIT SFQDVYFVSE SFEDAKEKMR EFAKTVKRPF GLKYNPYTQS VQVLRDTKSI TSAMNELRYD LDVISDALAR VTRWPSV // ID TPH2_MOUSE Reviewed; 488 AA. AC Q8CGV2; Q0VBT4; DT 09-MAY-2003, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 2. DT 19-FEB-2014, entry version 91. DE RecName: Full=Tryptophan 5-hydroxylase 2; DE EC=1.14.16.4; DE AltName: Full=Neuronal tryptophan hydroxylase; DE AltName: Full=Tryptophan 5-monooxygenase 2; GN Name=Tph2; Synonyms=Ntph; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=12511643; DOI=10.1126/science.1078197; RA Walther D.J., Peter J.-U., Bashammakh S., Hortnagl H., Voits M., RA Fink H., Bader M.; RT "Synthesis of serotonin by a second tryptophan hydroxylase isoform."; RL Science 299:76-76(2003). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- CATALYTIC ACTIVITY: L-tryptophan + tetrahydrobiopterin + O(2) = 5- CC hydroxy-L-tryptophan + 4a-hydroxytetrahydrobiopterin. CC -!- COFACTOR: Fe(2+) ion (By similarity). CC -!- PATHWAY: Aromatic compound metabolism; serotonin biosynthesis; CC serotonin from L-tryptophan: step 1/2. CC -!- TISSUE SPECIFICITY: Brain specific. CC -!- SIMILARITY: Belongs to the biopterin-dependent aromatic amino acid CC hydroxylase family. CC -!- SIMILARITY: Contains 1 ACT domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AY090565; AAM08923.1; -; mRNA. DR EMBL; BC120514; AAI20515.1; -; mRNA. DR EMBL; BC125430; AAI25431.1; -; mRNA. DR RefSeq; NP_775567.2; NM_173391.3. DR UniGene; Mm.31597; -. DR ProteinModelPortal; Q8CGV2; -. DR SMR; Q8CGV2; 55-482. DR STRING; 10090.ENSMUSP00000006949; -. DR PhosphoSite; Q8CGV2; -. DR PaxDb; Q8CGV2; -. DR PRIDE; Q8CGV2; -. DR Ensembl; ENSMUST00000006949; ENSMUSP00000006949; ENSMUSG00000006764. DR GeneID; 216343; -. DR KEGG; mmu:216343; -. DR UCSC; uc007haw.2; mouse. DR CTD; 121278; -. DR MGI; MGI:2651811; Tph2. DR eggNOG; COG3186; -. DR GeneTree; ENSGT00390000010268; -. DR HOGENOM; HOG000233373; -. DR HOVERGEN; HBG006841; -. DR InParanoid; Q0VBT4; -. DR KO; K00502; -. DR OMA; EDVSMFL; -. DR OrthoDB; EOG7KM5T1; -. DR TreeFam; TF313327; -. DR BRENDA; 1.14.16.4; 3474. DR UniPathway; UPA00846; UER00799. DR NextBio; 375107; -. DR PRO; PR:Q8CGV2; -. DR Bgee; Q8CGV2; -. DR CleanEx; MM_TPH2; -. DR Genevestigator; Q8CGV2; -. DR GO; GO:0043005; C:neuron projection; IDA:MGI. DR GO; GO:0016597; F:amino acid binding; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0004510; F:tryptophan 5-monooxygenase activity; IDA:MGI. DR GO; GO:0071285; P:cellular response to lithium ion; IEA:Ensembl. DR GO; GO:0007623; P:circadian rhythm; IEA:Ensembl. DR GO; GO:0014823; P:response to activity; IEA:Ensembl. DR GO; GO:0051592; P:response to calcium ion; IEA:Ensembl. DR GO; GO:0043627; P:response to estrogen; IEA:Ensembl. DR GO; GO:0051384; P:response to glucocorticoid; IEA:Ensembl. DR GO; GO:0031667; P:response to nutrient levels; IEA:Ensembl. DR GO; GO:0006587; P:serotonin biosynthetic process from tryptophan; IC:MGI. DR Gene3D; 1.10.800.10; -; 1. DR InterPro; IPR002912; ACT_dom. DR InterPro; IPR001273; ArAA_hydroxylase. DR InterPro; IPR018301; ArAA_hydroxylase_Fe/CU_BS. DR InterPro; IPR019774; Aromatic-AA_hydroxylase_C. DR InterPro; IPR005963; Trp_5_mOase. DR InterPro; IPR019773; Tyrosine_3-monooxygenase-like. DR PANTHER; PTHR11473; PTHR11473; 1. DR Pfam; PF01842; ACT; 1. DR Pfam; PF00351; Biopterin_H; 1. DR PIRSF; PIRSF000336; TH; 1. DR PRINTS; PR00372; FYWHYDRXLASE. DR SUPFAM; SSF56534; SSF56534; 1. DR TIGRFAMs; TIGR01270; Trp_5_monoox; 1. DR PROSITE; PS51671; ACT; 1. DR PROSITE; PS00367; BH4_AAA_HYDROXYL_1; 1. DR PROSITE; PS51410; BH4_AAA_HYDROXYL_2; 1. PE 2: Evidence at transcript level; KW Complete proteome; Iron; Metal-binding; Monooxygenase; Oxidoreductase; KW Reference proteome; Serotonin biosynthesis. FT CHAIN 1 488 Tryptophan 5-hydroxylase 2. FT /FTId=PRO_0000205575. FT DOMAIN 63 138 ACT. FT METAL 316 316 Iron (By similarity). FT METAL 321 321 Iron (By similarity). FT METAL 361 361 Iron (By similarity). FT CONFLICT 447 447 P -> R (in Ref. 1; AAM08923). SQ SEQUENCE 488 AA; 55859 MW; 876B59C784E80E4A CRC64; MQPAMMMFSS KYWARRGLSL DSAVPEDHQL LGSLTQNKAI KSEDKKSGKE PGKGDTTESS KTAVVFSLKN EVGGLVKALR LFQEKHVNML HIESRRSRRR SSEVEIFVDC ECGKTEFNEL IQLLKFQTTI VTLNPPESIW TEEEDLEDVP WFPRKISELD RCSHRVLMYG TELDADHPGF KDNVYRQRRK YFVDVAMGYK YGQPIPRVEY TEEETKTWGV VFRELSKLYP THACREYLKN LPLLTKYCGY REDNVPQLED VSMFLKERSG FTVRPVAGYL SPRDFLAGLA YRVFHCTQYV RHGSDPLYTP EPDTCHELLG HVPLLADPKF AQFSQEIGLA SLGASDEDVQ KLATCYFFTI EFGLCKQEGQ LRAYGAGLLS SIGELKHALS DKACVKSFDP KTTCLQECLI TTFQDAYFVS DSFEEAKEKM RDFAKSITRP FSVYFNPYTQ SIEILKDTRS IENVVQDLRS DLNTVCDALN KMNQYLGI // ID TRXR1_MOUSE Reviewed; 613 AA. AC Q9JMH6; Q3UEB7; Q3UK84; Q8CI31; Q99P49; Q9CSV5; DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot. DT 26-FEB-2008, sequence version 3. DT 19-MAR-2014, entry version 127. DE RecName: Full=Thioredoxin reductase 1, cytoplasmic; DE Short=TR; DE EC=1.8.1.9; DE AltName: Full=Thioredoxin reductase TR1; GN Name=Txnrd1; Synonyms=Trxr1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND SUBCELLULAR LOCATION. RC TISSUE=Thymus; RX PubMed=10721726; DOI=10.1016/S0378-1119(99)00498-9; RA Kawai H., Ota T., Suzuki F., Tatsuka M.; RT "Molecular cloning of mouse thioredoxin reductases."; RL Gene 242:321-330(2000). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND IDENTIFICATION BY MASS RP SPECTROMETRY. RX PubMed=11060283; DOI=10.1074/jbc.M004750200; RA Sun Q.-A., Zappacosta F., Factor V.M., Wirth P.J., Hatfield D.L., RA Gladyshev V.N.; RT "Heterogeneity within animal thioredoxin reductases: evidence for RT alternative first exon splicing."; RL J. Biol. Chem. 276:3106-3114(2001). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC STRAIN=C57BL/6J, and DBA/2; TISSUE=Embryo; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC STRAIN=FVB/N-3; TISSUE=Mammary tumor; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP ALTERNATIVE SPLICING (ISOFORMS 1 AND 2). RX PubMed=11737861; RA Osborne S.A., Tonissen K.F.; RT "Genomic organisation and alternative splicing of mouse and human RT thioredoxin reductase 1 genes."; RL BMC Genomics 2:10-10(2001). RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-245, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=15592455; DOI=10.1038/nbt1046; RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., RA Zha X.-M., Polakiewicz R.D., Comb M.J.; RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer RT cells."; RL Nat. Biotechnol. 23:94-101(2005). RN [7] RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-182, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic fibroblast; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., RA Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). CC -!- CATALYTIC ACTIVITY: Thioredoxin + NADP(+) = thioredoxin disulfide CC + NADPH. CC -!- COFACTOR: Binds 1 FAD per subunit (By similarity). CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9JMH6-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9JMH6-2; Sequence=VSP_031566; CC -!- MISCELLANEOUS: The active site is a redox-active disulfide bond. CC The selenocysteine residue is also essential for catalytic CC activity (By similarity). CC -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide CC oxidoreductase family. CC -!- SEQUENCE CAUTION: CC Sequence=AAH37643.1; Type=Erroneous termination; Positions=612; Note=Translated as Sec; CC Sequence=BAE26918.1; Type=Erroneous termination; Positions=612; Note=Translated as Sec; CC Sequence=BAE40292.1; Type=Erroneous termination; Positions=612; Note=Translated as Sec; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AB027565; BAA86985.2; -; mRNA. DR EMBL; AF333036; AAK01140.1; -; mRNA. DR EMBL; AK011902; BAB27905.1; -; mRNA. DR EMBL; AK146125; BAE26918.1; ALT_SEQ; mRNA. DR EMBL; AK149625; BAE28994.1; -; mRNA. DR EMBL; AK168356; BAE40292.1; ALT_SEQ; mRNA. DR EMBL; BC037643; AAH37643.1; ALT_SEQ; mRNA. DR RefSeq; NP_001035978.1; NM_001042513.1. DR RefSeq; NP_001035979.1; NM_001042514.1. DR RefSeq; NP_001035988.1; NM_001042523.1. DR RefSeq; NP_056577.2; NM_015762.2. DR UniGene; Mm.210155; -. DR UniGene; Mm.471159; -. DR ProteinModelPortal; Q9JMH6; -. DR SMR; Q9JMH6; 40-611. DR IntAct; Q9JMH6; 3. DR MINT; MINT-1869051; -. DR PhosphoSite; Q9JMH6; -. DR REPRODUCTION-2DPAGE; Q9JMH6; -. DR PaxDb; Q9JMH6; -. DR PRIDE; Q9JMH6; -. DR Ensembl; ENSMUST00000020484; ENSMUSP00000020484; ENSMUSG00000020250. [Q9JMH6-2] DR GeneID; 50493; -. DR KEGG; mmu:50493; -. DR UCSC; uc007gjy.1; mouse. [Q9JMH6-1] DR CTD; 7296; -. DR MGI; MGI:1354175; Txnrd1. DR eggNOG; COG1249; -. DR GeneTree; ENSGT00390000007578; -. DR HOGENOM; HOG000276712; -. DR HOVERGEN; HBG004959; -. DR InParanoid; Q9JMH6; -. DR KO; K00384; -. DR OMA; HPVCAEI; -. DR OrthoDB; EOG779NXG; -. DR TreeFam; TF314782; -. DR BRENDA; 1.8.1.9; 3474. DR ChiTaRS; TXNRD1; mouse. DR NextBio; 307476; -. DR PRO; PR:Q9JMH6; -. DR ArrayExpress; Q9JMH6; -. DR Bgee; Q9JMH6; -. DR CleanEx; MM_TXNRD1; -. DR Genevestigator; Q9JMH6; -. DR GO; GO:0005829; C:cytosol; IDA:MGI. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR GO; GO:0005730; C:nucleolus; IEA:Ensembl. DR GO; GO:0005634; C:nucleus; IDA:MGI. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. DR GO; GO:0050661; F:NADP binding; IEA:InterPro. DR GO; GO:0004791; F:thioredoxin-disulfide reductase activity; IDA:MGI. DR GO; GO:0008283; P:cell proliferation; IMP:MGI. DR GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro. DR GO; GO:0001707; P:mesoderm formation; IMP:MGI. DR Gene3D; 3.30.390.30; -; 1. DR InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer. DR InterPro; IPR013027; FAD_pyr_nucl-diS_OxRdtase. DR InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer. DR InterPro; IPR023753; Pyr_nucl-diS_OxRdtase_FAD/NAD. DR InterPro; IPR012999; Pyr_OxRdtase_I_AS. DR InterPro; IPR001327; Pyr_OxRdtase_NAD-bd_dom. DR InterPro; IPR006338; Thioredoxin/glutathione_Rdtase. DR PANTHER; PTHR22912:SF23; PTHR22912:SF23; 1. DR Pfam; PF00070; Pyr_redox; 1. DR Pfam; PF07992; Pyr_redox_2; 1. DR Pfam; PF02852; Pyr_redox_dim; 1. DR PRINTS; PR00368; FADPNR. DR SUPFAM; SSF55424; SSF55424; 1. DR TIGRFAMs; TIGR01438; TGR; 1. DR PROSITE; PS00076; PYRIDINE_REDOX_1; 1. PE 1: Evidence at protein level; KW Alternative splicing; Complete proteome; Cytoplasm; Disulfide bond; KW FAD; Flavoprotein; NADP; Oxidoreductase; Phosphoprotein; KW Redox-active center; Reference proteome; Selenocysteine. FT CHAIN 1 613 Thioredoxin reductase 1, cytoplasmic. FT /FTId=PRO_0000067982. FT NP_BIND 156 173 FAD (By similarity). FT COMPBIAS 26 90 Pro-rich. FT ACT_SITE 586 586 Proton acceptor (By similarity). FT NON_STD 612 612 Selenocysteine (By similarity). FT MOD_RES 182 182 N6-succinyllysine. FT MOD_RES 245 245 Phosphotyrosine. FT DISULFID 173 178 Redox-active (By similarity). FT CROSSLNK 611 612 Cysteinyl-selenocysteine (Cys-Sec) (By FT similarity). FT VAR_SEQ 1 114 Missing (in isoform 2). FT /FTId=VSP_031566. FT CONFLICT 238 238 K -> E (in Ref. 3; BAE28994). FT CONFLICT 372 372 Q -> R (in Ref. 3; BAE26918). FT CONFLICT 607 607 L -> V (in Ref. 3; BAE26918). SQ SEQUENCE 613 AA; 67084 MW; C9FD2E2E8C55118C CRC64; MPVDDCWLYF PASRGRTFVQ TVWVAPTCPN CCWFPGFLPP VPRPPHVPRV LLRGPRGAVL PASRPSKTLP SSSQTPCPTD PCICPPPSTP DSRQEKNTQS ELPNKKGQLQ KLPTMNGSKD PPGSYDFDLI IIGGGSGGLA AAKEAAKFDK KVLVLDFVTP TPLGTRWGLG GTCVNVGCIP KKLMHQAALL GQALKDSRNY GWKVEDTVKH DWEKMTESVQ SHIGSLNWGY RVALREKKVV YENAYGRFIG PHRIVATNNK GKEKIYSAER FLIATGERPR YLGIPGDKEY CISSDDLFSL PYCPGKTLVV GASYVALECA GFLAGIGLDV TVMVRSILLR GFDQDMANKI GEHMEEHGIK FIRQFVPTKI EQIEAGTPGR LRVTAQSTNS EETIEGEFNT VLLAVGRDSC TRTIGLETVG VKINEKTGKI PVTDEEQTNV PYIYAIGDIL EGKLELTPVA IQAGRLLAQR LYGGSNVKCD YDNVPTTVFT PLEYGCCGLS EEKAVEKFGE ENIEVYHSFF WPLEWTVPSR DNNKCYAKII CNLKDDERVV GFHVLGPNAG EVTQGFAAAL KCGLTKQQLD STIGIHPVCA EIFTTLSVTK RSGGDILQSG CUG // ID TRXR2_MOUSE Reviewed; 524 AA. AC Q9JLT4; Q6KG49; Q80VZ4; Q91YX4; Q9JHA7; Q9JMH5; DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot. DT 26-FEB-2008, sequence version 4. DT 19-MAR-2014, entry version 118. DE RecName: Full=Thioredoxin reductase 2, mitochondrial; DE EC=1.8.1.9; DE AltName: Full=Thioredoxin reductase TR3; DE Flags: Precursor; GN Name=Txnrd2; Synonyms=Trxr2; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY. RC TISSUE=Liver; RX PubMed=10500251; DOI=10.1016/S0167-4781(99)00129-3; RA Miranda-Vizuete A., Damdimopoulos A.E., Spyrou G.; RT "cDNA cloning, expression and chromosomal localization of the mouse RT mitochondrial thioredoxin reductase gene."; RL Biochim. Biophys. Acta 1447:113-118(1999). RN [2] RP NUCLEOTIDE SEQUENCE (ISOFORM 1), TISSUE SPECIFICITY, AND SUBCELLULAR RP LOCATION. RC TISSUE=Thymocyte; RX PubMed=10721726; DOI=10.1016/S0378-1119(99)00498-9; RA Kawai H., Ota T., Suzuki F., Tatsuka M.; RT "Molecular cloning of mouse thioredoxin reductases."; RL Gene 242:321-330(2000). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 35-44; RP 65-76; 255-277 AND 341-373, AND TISSUE SPECIFICITY. RC TISSUE=Liver; RX PubMed=10455115; DOI=10.1074/jbc.274.35.24522; RA Sun Q.-A., Wu Y., Zappacosta F., Jeang K.-T., Lee B.J., Hatfield D.L., RA Gladyshev V.N.; RT "Redox regulation of cell signaling by selenocysteine in mammalian RT thioredoxin reductases."; RL J. Biol. Chem. 274:24522-24530(1999). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 4), AND RP ALTERNATIVE SPLICING. RC STRAIN=BALB/c; RX PubMed=12132591; RA Miranda-Vizuete A., Spyrou G.; RT "Genomic organization and identification of a novel alternative RT splicing variant of mouse mitochondrial thioredoxin reductase (TrxR2) RT gene."; RL Mol. Cells 13:488-492(2002). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3). RC STRAIN=FVB/N; TISSUE=Limb, and Mammary tumor; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP ALTERNATIVE SPLICING. RX PubMed=11060283; DOI=10.1074/jbc.M004750200; RA Sun Q.-A., Zappacosta F., Factor V.M., Wirth P.J., Hatfield D.L., RA Gladyshev V.N.; RT "Heterogeneity within animal thioredoxin reductases: evidence for RT alternative first exon splicing."; RL J. Biol. Chem. 276:3106-3114(2001). RN [7] RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-79; LYS-175 AND LYS-329, RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., RA Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). CC -!- FUNCTION: Maintains thioredoxin in a reduced state. Implicated in CC the defenses against oxidative stress. May play a role in redox- CC regulated cell signaling. CC -!- CATALYTIC ACTIVITY: Thioredoxin + NADP(+) = thioredoxin disulfide CC + NADPH. CC -!- COFACTOR: FAD (By similarity). CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SUBCELLULAR LOCATION: Mitochondrion. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; CC IsoId=Q9JLT4-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9JLT4-2; Sequence=VSP_008293; CC Name=3; CC IsoId=Q9JLT4-3; Sequence=VSP_008294, VSP_008295; CC Note=No experimental confirmation available; CC Name=4; CC IsoId=Q9JLT4-4; Sequence=VSP_008296; CC -!- TISSUE SPECIFICITY: Expressed in liver, heart, testis and kidney. CC -!- MISCELLANEOUS: The active site is a redox-active disulfide bond. CC The selenocysteine residue is also essential for catalytic CC activity (By similarity). CC -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide CC oxidoreductase family. CC -!- SEQUENCE CAUTION: CC Sequence=AAF03359.1; Type=Erroneous initiation; CC Sequence=AAH52157.3; Type=Erroneous initiation; CC Sequence=AAL90457.1; Type=Erroneous initiation; CC Sequence=AAQ03230.1; Type=Erroneous initiation; CC Sequence=BAA86986.2; Type=Erroneous initiation; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF136399; AAF03359.1; ALT_INIT; mRNA. DR EMBL; AF171053; AAD51323.1; -; mRNA. DR EMBL; AB027566; BAA86986.2; ALT_INIT; mRNA. DR EMBL; AF414359; AAL90457.1; ALT_INIT; Genomic_DNA. DR EMBL; AF414356; AAL90457.1; JOINED; Genomic_DNA. DR EMBL; AF414357; AAL90457.1; JOINED; Genomic_DNA. DR EMBL; AF414358; AAL90457.1; JOINED; Genomic_DNA. DR EMBL; AF412308; AAQ03230.1; ALT_INIT; mRNA. DR EMBL; BC013688; AAH13688.1; -; mRNA. DR EMBL; BC052157; AAH52157.3; ALT_INIT; mRNA. DR RefSeq; NP_038739.2; NM_013711.3. DR UniGene; Mm.390906; -. DR PDB; 1ZDL; X-ray; 3.00 A; A=31-524. DR PDB; 1ZKQ; X-ray; 2.60 A; A=31-524. DR PDB; 3DGZ; X-ray; 2.25 A; A=34-521. DR PDBsum; 1ZDL; -. DR PDBsum; 1ZKQ; -. DR PDBsum; 3DGZ; -. DR ProteinModelPortal; Q9JLT4; -. DR SMR; Q9JLT4; 37-518. DR IntAct; Q9JLT4; 3. DR MINT; MINT-1862055; -. DR PhosphoSite; Q9JLT4; -. DR PaxDb; Q9JLT4; -. DR PRIDE; Q9JLT4; -. DR Ensembl; ENSMUST00000115604; ENSMUSP00000111267; ENSMUSG00000075704. [Q9JLT4-3] DR Ensembl; ENSMUST00000115606; ENSMUSP00000111269; ENSMUSG00000075704. [Q9JLT4-1] DR GeneID; 26462; -. DR KEGG; mmu:26462; -. DR UCSC; uc007ynx.1; mouse. [Q9JLT4-3] DR UCSC; uc007yny.1; mouse. [Q9JLT4-1] DR CTD; 10587; -. DR MGI; MGI:1347023; Txnrd2. DR eggNOG; COG1249; -. DR GeneTree; ENSGT00390000007578; -. DR HOGENOM; HOG000276712; -. DR HOVERGEN; HBG004959; -. DR KO; K00384; -. DR OMA; DAQEATS; -. DR OrthoDB; EOG779NXG; -. DR TreeFam; TF314782; -. DR EvolutionaryTrace; Q9JLT4; -. DR NextBio; 304577; -. DR PRO; PR:Q9JLT4; -. DR ArrayExpress; Q9JLT4; -. DR Bgee; Q9JLT4; -. DR CleanEx; MM_TXNRD2; -. DR Genevestigator; Q9JLT4; -. DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. DR GO; GO:0050661; F:NADP binding; IEA:InterPro. DR GO; GO:0004791; F:thioredoxin-disulfide reductase activity; ISS:UniProtKB. DR GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro. DR GO; GO:0007507; P:heart development; IMP:MGI. DR GO; GO:0030097; P:hemopoiesis; IMP:MGI. DR GO; GO:0000305; P:response to oxygen radical; TAS:UniProtKB. DR Gene3D; 3.30.390.30; -; 1. DR InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer. DR InterPro; IPR013027; FAD_pyr_nucl-diS_OxRdtase. DR InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer. DR InterPro; IPR023753; Pyr_nucl-diS_OxRdtase_FAD/NAD. DR InterPro; IPR012999; Pyr_OxRdtase_I_AS. DR InterPro; IPR001327; Pyr_OxRdtase_NAD-bd_dom. DR InterPro; IPR006338; Thioredoxin/glutathione_Rdtase. DR PANTHER; PTHR22912:SF23; PTHR22912:SF23; 1. DR Pfam; PF00070; Pyr_redox; 1. DR Pfam; PF07992; Pyr_redox_2; 1. DR Pfam; PF02852; Pyr_redox_dim; 1. DR PRINTS; PR00368; FADPNR. DR SUPFAM; SSF55424; SSF55424; 1. DR TIGRFAMs; TIGR01438; TGR; 1. DR PROSITE; PS00076; PYRIDINE_REDOX_1; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Complete proteome; KW Direct protein sequencing; Disulfide bond; FAD; Flavoprotein; KW Mitochondrion; NADP; Oxidoreductase; Redox-active center; KW Reference proteome; Selenocysteine; Transit peptide. FT TRANSIT 1 34 Mitochondrion. FT CHAIN 35 524 Thioredoxin reductase 2, mitochondrial. FT /FTId=PRO_0000030289. FT NP_BIND 41 70 FAD (By similarity). FT ACT_SITE 497 497 Proton acceptor (By similarity). FT NON_STD 523 523 Selenocysteine (By similarity). FT MOD_RES 79 79 N6-succinyllysine. FT MOD_RES 175 175 N6-succinyllysine. FT MOD_RES 329 329 N6-succinyllysine. FT DISULFID 86 91 Redox-active (By similarity). FT CROSSLNK 522 523 Cysteinyl-selenocysteine (Cys-Sec) (By FT similarity). FT VAR_SEQ 1 36 MVAAMVAALRGPSRRFRPRTRALTRGTRGAASAAGG -> M FT EG (in isoform 2). FT /FTId=VSP_008293. FT VAR_SEQ 318 356 RVPETRTLNLEKAGISTNPKNQKIIVDAQEATSVPHIYA FT -> KDAASHTDTVSSSRKPYFLGRRVFAFLPITSWILHSAG FT S (in isoform 3). FT /FTId=VSP_008294. FT VAR_SEQ 357 524 Missing (in isoform 3). FT /FTId=VSP_008295. FT VAR_SEQ 395 425 Missing (in isoform 4). FT /FTId=VSP_008296. FT CONFLICT 4 6 AMV -> GRMW (in Ref. 1; AAF03359). FT STRAND 39 45 FT HELIX 49 60 FT STRAND 65 68 FT HELIX 85 89 FT HELIX 91 112 FT HELIX 125 149 FT STRAND 153 155 FT STRAND 158 170 FT STRAND 176 186 FT STRAND 190 192 FT HELIX 201 204 FT HELIX 208 211 FT STRAND 220 224 FT HELIX 228 239 FT STRAND 244 250 FT TURN 252 255 FT HELIX 258 270 FT STRAND 274 277 FT STRAND 279 286 FT STRAND 292 298 FT TURN 299 301 FT STRAND 304 314 FT STRAND 318 321 FT HELIX 323 325 FT HELIX 327 330 FT STRAND 336 338 FT STRAND 345 348 FT STRAND 354 356 FT HELIX 358 360 FT STRAND 361 364 FT HELIX 368 383 FT STRAND 397 399 FT STRAND 401 409 FT HELIX 412 419 FT HELIX 421 423 FT STRAND 424 430 FT HELIX 434 438 FT STRAND 447 455 FT STRAND 459 467 FT HELIX 470 482 FT HELIX 487 491 FT HELIX 502 505 FT TURN 511 514 SQ SEQUENCE 524 AA; 56603 MW; 74D4713DC8EF6A80 CRC64; MVAAMVAALR GPSRRFRPRT RALTRGTRGA ASAAGGQQSF DLLVIGGGSG GLACAKEAAQ LGKKVAVADY VEPSPRGTKW GLGGTCVNVG CIPKKLMHQA ALLGGMIRDA HHYGWEVAQP VQHNWKTMAE AVQNHVKSLN WGHRVQLQDR KVKYFNIKAS FVDEHTVRGV DKGGKATLLS AEHIVIATGG RPRYPTQVKG ALEYGITSDD IFWLKESPGK TLVVGASYVA LECAGFLTGI GLDTTVMMRS IPLRGFDQQM SSLVTEHMES HGTQFLKGCV PSHIKKLPTN QLQVTWEDHA SGKEDTGTFD TVLWAIGRVP ETRTLNLEKA GISTNPKNQK IIVDAQEATS VPHIYAIGDV AEGRPELTPT AIKAGKLLAQ RLFGKSSTLM DYSNVPTTVF TPLEYGCVGL SEEEAVALHG QEHVEVYHAY YKPLEFTVAD RDASQCYIKM VCMREPPQLV LGLHFLGPNA GEVTQGFALG IKCGASYAQV MQTVGIHPTC SEEVVKLHIS KRSGLEPTVT GCUG // ID TRXR3_MOUSE Reviewed; 652 AA. AC Q99MD6; Q9CZE5; DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 29-MAY-2013, sequence version 3. DT 19-MAR-2014, entry version 92. DE RecName: Full=Thioredoxin reductase 3; DE EC=1.8.1.9; DE AltName: Full=Thioredoxin and glutathione reductase; DE AltName: Full=Thioredoxin reductase TR2; GN Name=Txnrd3; Synonyms=Tgr, Trxr3; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, RP SUBCELLULAR LOCATION, DOMAIN, 3D-STRUCTURE MODELING, AND RP SELENOCYSTEINE AT SEC-651. RX PubMed=11259642; DOI=10.1073/pnas.051454398; RA Sun Q.-A., Kirnarsky L., Sherman S., Gladyshev V.N.; RT "Selenoprotein oxidoreductase with specificity for thioredoxin and RT glutathione systems."; RL Proc. Natl. Acad. Sci. U.S.A. 98:3673-3678(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Embryo, and Thymus; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6; TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP PROTEIN SEQUENCE OF 191-202 AND 550-561, AND TISSUE SPECIFICITY. RX PubMed=10455115; DOI=10.1074/jbc.274.35.24522; RA Sun Q.-A., Wu Y., Zappacosta F., Jeang K.-T., Lee B.J., Hatfield D.L., RA Gladyshev V.N.; RT "Redox regulation of cell signaling by selenocysteine in mammalian RT thioredoxin reductases."; RL J. Biol. Chem. 274:24522-24530(1999). RN [5] RP DOMAIN, AND MUTAGENESIS OF SEC-651 AND 651-SEC-GLY-652. RX PubMed=16262253; DOI=10.1021/bi051321w; RA Sun Q.-A., Su D., Novoselov S.V., Carlson B.A., Hatfield D.L., RA Gladyshev V.N.; RT "Reaction mechanism and regulation of mammalian RT thioredoxin/glutathione reductase."; RL Biochemistry 44:14528-14537(2005). RN [6] RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL RP STAGE. RX PubMed=15901730; DOI=10.1074/jbc.M503638200; RA Su D., Novoselov S.V., Sun Q.-A., Moustafa M.E., Zhou Y., Oko R., RA Hatfield D.L., Gladyshev V.N.; RT "Mammalian selenoprotein thioredoxin-glutathione reductase. Roles in RT disulfide bond formation and sperm maturation."; RL J. Biol. Chem. 280:26491-26498(2005). RN [7] RP NON-AUG INITIATOR START CODON, AND TISSUE SPECIFICITY. RX PubMed=20018845; DOI=10.1074/jbc.M109.070532; RA Gerashchenko M.V., Su D., Gladyshev V.N.; RT "CUG start codon generates thioredoxin/glutathione reductase isoforms RT in mouse testes."; RL J. Biol. Chem. 285:4595-4602(2010). RN [8] RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-388, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., RA Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). CC -!- FUNCTION: Displays thioredoxin reductase, glutaredoxin and CC glutathione reductase activities. Catalyzes disulfide bond CC isomerization. Promotes disulfide bond formation between GPX4 and CC various sperm proteins and may play a role in sperm maturation by CC promoting formation of sperm structural components. CC -!- CATALYTIC ACTIVITY: Thioredoxin + NADP(+) = thioredoxin disulfide CC + NADPH. CC -!- COFACTOR: Binds 1 FAD per subunit (By similarity). CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=14.7 uM for 5,5'-dithiobis(2-nitrobenzoic acid); CC KM=10.7 uM for NADPH; CC KM=3.0 uM for thioredoxin; CC KM=8.84 uM for oxidized glutathione; CC KM=45.2 uM for beta-hydroxyethyl disulfide; CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Microsome. Endoplasmic CC reticulum. Note=Detected in cytoplasm and nucleus in late CC spermatids. CC -!- TISSUE SPECIFICITY: Expressed preferentially in testis where it is CC found in spermatids and spermatocytes but not in sperm. In CC elongating spermatids, expressed at the site of mitochondrial CC sheath formation. Low levels in other tissues including heart, CC lung, liver, kidney, brain, muscle and prostate. CC -!- DEVELOPMENTAL STAGE: Accumulates in the testis after puberty. Not CC detected in 20-day-old mice but highly expressed in testes of 7- CC month-old mice. CC -!- DOMAIN: The N-terminal glutaredoxin domain does not contain the C- CC X-X-C redox-active motif normally found in glutaredoxins but CC activity may be mediated through a single cysteine. The C-terminal CC Cys-Sec motif of one subunit of the homodimer may transfer CC electrons from the thiol-disulfide center to the glutaredoxin CC domain of the other subunit. CC -!- MISCELLANEOUS: The thioredoxin reductase active site is a redox- CC active disulfide bond. The selenocysteine residue is also CC essential for catalytic activity (By similarity). CC -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide CC oxidoreductase family. CC -!- SIMILARITY: Contains 1 glutaredoxin domain. CC -!- CAUTION: This sequence initiates at a CTG codon (PubMed:20018845). CC -!- SEQUENCE CAUTION: CC Sequence=AAH76605.1; Type=Erroneous termination; Positions=651; Note=Translated as Sec; CC Sequence=AAH76605.1; Type=Miscellaneous discrepancy; Note=Unusual initiator. The initiator methionine is coded by a non-canonical CTG leucine codon; CC Sequence=AAK31172.1; Type=Erroneous initiation; CC Sequence=BAB28419.1; Type=Erroneous termination; Positions=651; Note=Translated as Sec; CC Sequence=BAB28419.1; Type=Frameshift; Positions=29, 38; CC Sequence=BAB28419.1; Type=Miscellaneous discrepancy; Note=Unusual initiator. The initiator methionine is coded by a non-canonical CTG leucine codon; CC Sequence=BAC37890.1; Type=Erroneous termination; Positions=651; Note=Translated as Sec; CC Sequence=BAC37890.1; Type=Miscellaneous discrepancy; Note=Unusual initiator. The initiator methionine is coded by a non-canonical CTG leucine codon; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF349659; AAK31172.1; ALT_INIT; mRNA. DR EMBL; AK012699; BAB28419.1; ALT_SEQ; mRNA. DR EMBL; AK080362; BAC37890.1; ALT_SEQ; mRNA. DR EMBL; BC076605; AAH76605.1; ALT_SEQ; mRNA. DR RefSeq; NP_001171529.1; NM_001178058.1. DR RefSeq; NP_694802.2; NM_153162.3. DR UniGene; Mm.229332; -. DR PDB; 2LV3; NMR; -; A=60-161. DR PDBsum; 2LV3; -. DR ProteinModelPortal; Q99MD6; -. DR STRING; 10090.ENSMUSP00000000828; -. DR PhosphoSite; Q99MD6; -. DR PaxDb; Q99MD6; -. DR PRIDE; Q99MD6; -. DR GeneID; 232223; -. DR KEGG; mmu:232223; -. DR UCSC; uc009cwj.1; mouse. DR CTD; 114112; -. DR MGI; MGI:2386711; Txnrd3. DR eggNOG; COG1249; -. DR HOGENOM; HOG000276712; -. DR HOVERGEN; HBG004959; -. DR InParanoid; Q99MD6; -. DR KO; K00384; -. DR NextBio; 380996; -. DR CleanEx; MM_TXNRD3; -. DR Genevestigator; Q99MD6; -. DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. DR GO; GO:0050661; F:NADP binding; IEA:InterPro. DR GO; GO:0015035; F:protein disulfide oxidoreductase activity; IEA:InterPro. DR GO; GO:0004791; F:thioredoxin-disulfide reductase activity; IDA:MGI. DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW. DR GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro. DR GO; GO:0006749; P:glutathione metabolic process; IDA:MGI. DR GO; GO:0007275; P:multicellular organismal development; IEA:UniProtKB-KW. DR GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW. DR Gene3D; 3.30.390.30; -; 1. DR Gene3D; 3.40.30.10; -; 1. DR InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer. DR InterPro; IPR013027; FAD_pyr_nucl-diS_OxRdtase. DR InterPro; IPR002109; Glutaredoxin. DR InterPro; IPR011899; Glutaredoxin_euk/vir. DR InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer. DR InterPro; IPR023753; Pyr_nucl-diS_OxRdtase_FAD/NAD. DR InterPro; IPR012999; Pyr_OxRdtase_I_AS. DR InterPro; IPR001327; Pyr_OxRdtase_NAD-bd_dom. DR InterPro; IPR012336; Thioredoxin-like_fold. DR InterPro; IPR006338; Thioredoxin/glutathione_Rdtase. DR PANTHER; PTHR22912:SF23; PTHR22912:SF23; 1. DR Pfam; PF00462; Glutaredoxin; 1. DR Pfam; PF00070; Pyr_redox; 1. DR Pfam; PF07992; Pyr_redox_2; 1. DR Pfam; PF02852; Pyr_redox_dim; 1. DR PRINTS; PR00368; FADPNR. DR SUPFAM; SSF52833; SSF52833; 1. DR SUPFAM; SSF55424; SSF55424; 1. DR TIGRFAMs; TIGR02180; GRX_euk; 1. DR TIGRFAMs; TIGR01438; TGR; 1. DR PROSITE; PS51354; GLUTAREDOXIN_2; 1. DR PROSITE; PS00076; PYRIDINE_REDOX_1; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Cytoplasm; Developmental protein; KW Differentiation; Direct protein sequencing; Disulfide bond; KW Electron transport; Endoplasmic reticulum; FAD; Flavoprotein; KW Microsome; NADP; Nucleus; Oxidoreductase; Phosphoprotein; KW Redox-active center; Reference proteome; Selenocysteine; KW Spermatogenesis; Transport. FT CHAIN 1 652 Thioredoxin reductase 3. FT /FTId=PRO_0000320696. FT DOMAIN 65 165 Glutaredoxin. FT NP_BIND 167 196 FAD (By similarity). FT ACT_SITE 625 625 Proton acceptor (By similarity). FT NON_STD 651 651 Selenocysteine. FT MOD_RES 50 50 Phosphoserine (By similarity). FT MOD_RES 388 388 N6-succinyllysine. FT DISULFID 212 217 Redox-active (By similarity). FT CROSSLNK 650 651 Cysteinyl-selenocysteine (Cys-Sec) (By FT similarity). FT MUTAGEN 651 652 Missing: Abolishes thioredoxin reductase, FT glutaredoxin and gluthioine reductase FT activities. FT MUTAGEN 651 651 U->C: Thioredoxin reductase activity FT reduced to 21%. Glutaredoxin activity FT reduced to 14%. Glutathione reductase FT activity reduced to 18%. FT MUTAGEN 651 651 U->S: Abolishes thioredoxin reductase, FT glutaredoxin and gluthioine reductase FT activities. FT CONFLICT 8 8 P -> R (in Ref. 2; BAB28419). FT CONFLICT 16 16 S -> W (in Ref. 2; BAB28419). FT HELIX 61 74 FT STRAND 75 81 FT TURN 86 89 FT HELIX 90 97 FT STRAND 103 106 FT TURN 107 109 FT HELIX 113 124 FT STRAND 126 128 FT STRAND 133 136 FT HELIX 144 151 FT HELIX 155 159 SQ SEQUENCE 652 AA; 71319 MW; AC6342C64DDEC1BC CRC64; MEKPPSPPPP PRAQTSPGLG KVGVLPNRRL GAVRGGLMSS PPGRRARLAS PGTSRPSSEA REELRRRLRD LIEGNRVMIF SKSYCPHSTR VKELFSSLGV VYNILELDQV DDGASVQEVL TEISNQKTVP NIFVNKVHVG GCDRTFQAHQ NGLLQKLLQD DSAHDYDLII IGGGSGGLSC AKEAANLGKK VMVLDFVVPS PQGTTWGLGG TCVNVGCIPK KLMHQAALLG HALQDAKKYG WEYNQQVKHN WEAMTEAIQS HIGSLNWGYR VTLREKGVTY VNSFGEFVDL HKIKATNKKG QETFYTASKF VIATGERPRY LGIQGDKEYC ITSDDLFSLP YCPGCTLVVG ASYVGLECAG FLAGLGLDVT VMVRSVLLRG FDQEMAEKVG SYLEQQGVKF QRKFTPILVQ QLEKGLPGKL KVVAKSTEGP ETVEGIYNTV LLAIGRDSCT RKIGLEKIGV KINEKNGKIP VNDVEQTNVP HVYAIGDILD GKPELTPVAI QAGKLLARRL FGVSLEKCDY INIPTTVFTP LEYGCCGLSE EKAIEMYKKE NLEVYHTLFW PLEWTVAGRD NNTCYAKIIC NKFDNERVVG FHLLGPNAGE ITQGFAAAMK CGLTKQLLDD TIGIHPTCGE VFTTLEITKS SGLDITQKGC UG // ID TXD12_MOUSE Reviewed; 170 AA. AC Q9CQU0; Q53YN1; DT 11-APR-2003, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 19-FEB-2014, entry version 98. DE RecName: Full=Thioredoxin domain-containing protein 12; DE EC=1.8.4.2; DE AltName: Full=Endoplasmic reticulum resident protein 19; DE Short=ER protein 19; DE Short=ERp19; DE AltName: Full=Thioredoxin-like protein p19; DE Flags: Precursor; GN Name=Txndc12; Synonyms=Tlp19; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION. RC TISSUE=Embryo; RX PubMed=12930873; DOI=10.1074/mcp.M300053-MCP200; RA Knoblach B., Keller B.O., Groenendyk J., Aldred S., Zheng J., RA Lemire B.D., Li L., Michalak M.; RT "ERp19 and ERp46, new members of the thioredoxin family of endoplasmic RT reticulum proteins."; RL Mol. Cell. Proteomics 2:1104-1119(2003). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Embryo, and Kidney; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Mammary gland; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: Possesses significant protein thiol-disulfide oxidase CC activity (By similarity). CC -!- CATALYTIC ACTIVITY: 2 glutathione + protein-disulfide = CC glutathione disulfide + protein-dithiol. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen. CC -!- SIMILARITY: Contains 1 thioredoxin domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AY548113; AAS55653.1; -; mRNA. DR EMBL; AK003481; BAB22811.1; -; mRNA. DR EMBL; AK002862; BAB22413.1; -; mRNA. DR EMBL; BC006857; AAH06857.1; -; mRNA. DR RefSeq; NP_079610.1; NM_025334.3. DR UniGene; Mm.159965; -. DR ProteinModelPortal; Q9CQU0; -. DR SMR; Q9CQU0; 28-161. DR IntAct; Q9CQU0; 6. DR MINT; MINT-4137999; -. DR STRING; 10090.ENSMUSP00000030296; -. DR PhosphoSite; Q9CQU0; -. DR REPRODUCTION-2DPAGE; Q9CQU0; -. DR PaxDb; Q9CQU0; -. DR PRIDE; Q9CQU0; -. DR Ensembl; ENSMUST00000030296; ENSMUSP00000030296; ENSMUSG00000028567. DR GeneID; 66073; -. DR KEGG; mmu:66073; -. DR UCSC; uc008ubs.1; mouse. DR CTD; 51060; -. DR MGI; MGI:1913323; Txndc12. DR eggNOG; NOG77442; -. DR GeneTree; ENSGT00530000063273; -. DR HOGENOM; HOG000231100; -. DR HOVERGEN; HBG107174; -. DR InParanoid; Q9CQU0; -. DR KO; K05360; -. DR OMA; SYKYFYT; -. DR OrthoDB; EOG7DNNX2; -. DR TreeFam; TF321449; -. DR ChiTaRS; TXNDC12; mouse. DR NextBio; 320548; -. DR PRO; PR:Q9CQU0; -. DR Bgee; Q9CQU0; -. DR Genevestigator; Q9CQU0; -. DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell. DR GO; GO:0019153; F:protein-disulfide reductase (glutathione) activity; IEA:UniProtKB-EC. DR GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro. DR Gene3D; 3.40.30.10; -; 1. DR InterPro; IPR012336; Thioredoxin-like_fold. DR InterPro; IPR017937; Thioredoxin_CS. DR SUPFAM; SSF52833; SSF52833; 1. DR PROSITE; PS00014; ER_TARGET; 1. DR PROSITE; PS00194; THIOREDOXIN_1; 1. DR PROSITE; PS51352; THIOREDOXIN_2; 1. PE 2: Evidence at transcript level; KW Complete proteome; Disulfide bond; Endoplasmic reticulum; KW Glycoprotein; Oxidoreductase; Redox-active center; Reference proteome; KW Signal. FT SIGNAL 1 24 By similarity. FT CHAIN 25 170 Thioredoxin domain-containing protein 12. FT /FTId=PRO_0000034190. FT MOTIF 167 170 Prevents secretion from ER (Potential). FT CARBOHYD 128 128 N-linked (GlcNAc...) (Potential). FT DISULFID 64 67 Redox-active (Potential). SQ SEQUENCE 170 AA; 19049 MW; 5B91FC9BE12C5E44 CRC64; MSLRFGATCL LSFSFLLLIT SSDGRTGLGK GFGDHIHWRT LEDGKKEAAA SGLPLMVIIH KSWCGACKAL KPKFAESTEI SELSHNFVMV NLEDEEEPRD EDFSPDGGYI PRILFLDPSG KVRPEIINES GNPSYKYFYV SAEQVVQGMK EAQERLTGDA FREKHFQDEL // ID TY3H_MOUSE Reviewed; 498 AA. AC P24529; DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 19-FEB-2014, entry version 119. DE RecName: Full=Tyrosine 3-monooxygenase; DE EC=1.14.16.2; DE AltName: Full=Tyrosine 3-hydroxylase; DE Short=TH; GN Name=Th; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=1674869; DOI=10.1016/0006-291X(91)90472-J; RA Ichikawa S., Sasaoka T., Nagatsu T.; RT "Primary structure of mouse tyrosine hydroxylase deduced from its RT cDNA."; RL Biochem. Biophys. Res. Commun. 176:1610-1616(1991). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1-30. RC STRAIN=BALB/c; RA Morgan W.W., Bermudez J., Sharp Z.D.; RL Submitted (APR-1992) to the EMBL/GenBank/DDBJ databases. RN [3] RP PROTEIN SEQUENCE OF 78-90. RC TISSUE=Brain; RA Lubec G., Yang J.W., Zigmond M.; RL Submitted (JUL-2007) to UniProtKB. CC -!- FUNCTION: Plays an important role in the physiology of adrenergic CC neurons. CC -!- CATALYTIC ACTIVITY: L-tyrosine + tetrahydrobiopterin + O(2) = L- CC dopa + 4a-hydroxytetrahydrobiopterin. CC -!- COFACTOR: Fe(2+) ion. CC -!- ENZYME REGULATION: Phosphorylation leads to an increase in the CC catalytic activity. CC -!- PATHWAY: Catecholamine biosynthesis; dopamine biosynthesis; CC dopamine from L-tyrosine: step 1/2. CC -!- SIMILARITY: Belongs to the biopterin-dependent aromatic amino acid CC hydroxylase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M69200; AAA40434.1; -; mRNA. DR EMBL; X53503; CAA37580.1; -; Genomic_DNA. DR PIR; JN0068; JN0068. DR RefSeq; NP_033403.1; NM_009377.1. DR UniGene; Mm.1292; -. DR ProteinModelPortal; P24529; -. DR SMR; P24529; 80-498. DR IntAct; P24529; 1. DR MINT; MINT-4138908; -. DR STRING; 10090.ENSMUSP00000000219; -. DR PhosphoSite; P24529; -. DR PaxDb; P24529; -. DR PRIDE; P24529; -. DR DNASU; 21823; -. DR Ensembl; ENSMUST00000000219; ENSMUSP00000000219; ENSMUSG00000000214. DR GeneID; 21823; -. DR KEGG; mmu:21823; -. DR UCSC; uc009koi.1; mouse. DR CTD; 7054; -. DR MGI; MGI:98735; Th. DR eggNOG; COG3186; -. DR GeneTree; ENSGT00390000010268; -. DR HOGENOM; HOG000233373; -. DR HOVERGEN; HBG006841; -. DR InParanoid; P24529; -. DR KO; K00501; -. DR OMA; ELDKCHH; -. DR OrthoDB; EOG7KM5T1; -. DR TreeFam; TF313327; -. DR UniPathway; UPA00747; UER00733. DR NextBio; 301244; -. DR PRO; PR:P24529; -. DR ArrayExpress; P24529; -. DR Bgee; P24529; -. DR CleanEx; MM_TH; -. DR Genevestigator; P24529; -. DR GO; GO:0030424; C:axon; IDA:MGI. DR GO; GO:0005737; C:cytoplasm; IDA:MGI. DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; IEA:Ensembl. DR GO; GO:0005829; C:cytosol; IEA:Ensembl. DR GO; GO:0030425; C:dendrite; IEA:Ensembl. DR GO; GO:0033162; C:melanosome membrane; IEA:Ensembl. DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl. DR GO; GO:0005634; C:nucleus; IDA:MGI. DR GO; GO:0043204; C:perikaryon; IDA:MGI. DR GO; GO:0005790; C:smooth endoplasmic reticulum; IEA:Ensembl. DR GO; GO:0008021; C:synaptic vesicle; IEA:Ensembl. DR GO; GO:0043195; C:terminal bouton; IEA:Ensembl. DR GO; GO:0016597; F:amino acid binding; IEA:Ensembl. DR GO; GO:0035240; F:dopamine binding; IEA:Ensembl. DR GO; GO:0008199; F:ferric iron binding; IEA:Ensembl. DR GO; GO:0008198; F:ferrous iron binding; IEA:Ensembl. DR GO; GO:0019825; F:oxygen binding; IEA:Ensembl. DR GO; GO:0034617; F:tetrahydrobiopterin binding; IEA:Ensembl. DR GO; GO:0004511; F:tyrosine 3-monooxygenase activity; TAS:MGI. DR GO; GO:0035690; P:cellular response to drug; IEA:Ensembl. DR GO; GO:0071333; P:cellular response to glucose stimulus; IEA:Ensembl. DR GO; GO:0071363; P:cellular response to growth factor stimulus; IEA:Ensembl. DR GO; GO:0071287; P:cellular response to manganese ion; IEA:Ensembl. DR GO; GO:0071316; P:cellular response to nicotine; IEA:Ensembl. DR GO; GO:0021987; P:cerebral cortex development; IEA:Ensembl. DR GO; GO:0042745; P:circadian sleep/wake cycle; IEA:Ensembl. DR GO; GO:0006585; P:dopamine biosynthetic process from tyrosine; IDA:MGI. DR GO; GO:0042755; P:eating behavior; IMP:MGI. DR GO; GO:0048596; P:embryonic camera-type eye morphogenesis; IMP:BHF-UCL. DR GO; GO:0042418; P:epinephrine biosynthetic process; IEA:Ensembl. DR GO; GO:0042462; P:eye photoreceptor cell development; IMP:BHF-UCL. DR GO; GO:0006631; P:fatty acid metabolic process; IEA:Ensembl. DR GO; GO:0016137; P:glycoside metabolic process; IEA:Ensembl. DR GO; GO:0007507; P:heart development; IMP:MGI. DR GO; GO:0033076; P:isoquinoline alkaloid metabolic process; IEA:Ensembl. DR GO; GO:0007612; P:learning; IMP:MGI. DR GO; GO:0007626; P:locomotory behavior; IMP:MGI. DR GO; GO:0007617; P:mating behavior; IMP:MGI. DR GO; GO:0007613; P:memory; IMP:MGI. DR GO; GO:0010259; P:multicellular organismal aging; IEA:Ensembl. DR GO; GO:0042136; P:neurotransmitter biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0042421; P:norepinephrine biosynthetic process; IEA:Ensembl. DR GO; GO:0018963; P:phthalate metabolic process; IEA:Ensembl. DR GO; GO:0052314; P:phytoalexin metabolic process; IEA:Ensembl. DR GO; GO:0008016; P:regulation of heart contraction; IMP:MGI. DR GO; GO:0014823; P:response to activity; IEA:Ensembl. DR GO; GO:0001975; P:response to amphetamine; IEA:Ensembl. DR GO; GO:0051412; P:response to corticosterone; IEA:Ensembl. DR GO; GO:0051602; P:response to electrical stimulus; IEA:Ensembl. DR GO; GO:0032355; P:response to estradiol; IEA:Ensembl. DR GO; GO:0045471; P:response to ethanol; IEA:Ensembl. DR GO; GO:0045472; P:response to ether; IEA:Ensembl. DR GO; GO:0009635; P:response to herbicide; IEA:Ensembl. DR GO; GO:0001666; P:response to hypoxia; IEA:Ensembl. DR GO; GO:0009416; P:response to light stimulus; IEA:Ensembl. DR GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl. DR GO; GO:0031667; P:response to nutrient levels; IEA:Ensembl. DR GO; GO:0043434; P:response to peptide hormone; IEA:Ensembl. DR GO; GO:0046684; P:response to pyrethroid; IEA:Ensembl. DR GO; GO:0009651; P:response to salt stress; IEA:Ensembl. DR GO; GO:0009414; P:response to water deprivation; IEA:Ensembl. DR GO; GO:0010043; P:response to zinc ion; IEA:Ensembl. DR GO; GO:0007605; P:sensory perception of sound; IEA:Ensembl. DR GO; GO:0035176; P:social behavior; IEA:Ensembl. DR GO; GO:0006665; P:sphingolipid metabolic process; IEA:Ensembl. DR GO; GO:0001963; P:synaptic transmission, dopaminergic; IMP:MGI. DR GO; GO:0015842; P:synaptic vesicle amine transport; IEA:Ensembl. DR GO; GO:0042214; P:terpene metabolic process; IEA:Ensembl. DR GO; GO:0007601; P:visual perception; IMP:BHF-UCL. DR Gene3D; 1.10.800.10; -; 1. DR InterPro; IPR001273; ArAA_hydroxylase. DR InterPro; IPR018301; ArAA_hydroxylase_Fe/CU_BS. DR InterPro; IPR019774; Aromatic-AA_hydroxylase_C. DR InterPro; IPR005962; Tyr_3_mOase. DR InterPro; IPR019773; Tyrosine_3-monooxygenase-like. DR InterPro; IPR021164; Tyrosine_hydroxylase_CS. DR PANTHER; PTHR11473; PTHR11473; 1. DR Pfam; PF00351; Biopterin_H; 1. DR Pfam; PF12549; TOH_N; 2. DR PIRSF; PIRSF000336; TH; 1. DR PRINTS; PR00372; FYWHYDRXLASE. DR SUPFAM; SSF56534; SSF56534; 1. DR TIGRFAMs; TIGR01269; Tyr_3_monoox; 1. DR PROSITE; PS00367; BH4_AAA_HYDROXYL_1; 1. DR PROSITE; PS51410; BH4_AAA_HYDROXYL_2; 1. PE 1: Evidence at protein level; KW Catecholamine biosynthesis; Complete proteome; KW Direct protein sequencing; Iron; Metal-binding; Monooxygenase; KW Neurotransmitter biosynthesis; Oxidoreductase; Phosphoprotein; KW Reference proteome. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 498 Tyrosine 3-monooxygenase. FT /FTId=PRO_0000205562. FT COMPBIAS 51 59 Poly-Ala. FT METAL 331 331 Iron (By similarity). FT METAL 336 336 Iron (By similarity). FT METAL 376 376 Iron (By similarity). FT MOD_RES 19 19 Phosphoserine; by CaMK2 (By similarity). FT MOD_RES 31 31 Phosphoserine (By similarity). FT MOD_RES 40 40 Phosphoserine; by CaMK2 and PKA (By FT similarity). SQ SEQUENCE 498 AA; 55993 MW; 62790179664F6DC6 CRC64; MPTPSASSPQ PKGFRRAVSE QDTKQAEAVT SPRFIGRRQS LIEDARKERE AAAAAAAAAV ASAEPGNPLE AVVFEERDGN AVLNLLFSLR GTKPSSLSRA LKVFETFEAK IHHLETRPAQ RPLAGSPHLE YFVRFEVPSG DLAALLSSVR RVSDDVRSAR EDKVPWFPRK VSELDKCHHL VTKFDPDLDL DHPGFSDQAY RQRRKLIAEI AFQYKQGEPI PHVEYTKEEI ATWKEVYATL KGLYATHACR EHLEAFQLLE RYCGYREDSI PQLEDVSHFL KERTGFQLRP VAGLLSARDF LASLAFRVFQ CTQYIRHASS PMHSPEPDCC HELLGHVPML ADRTFAQFSQ DIGLASLGAS DEEIEKLSTV YWFTVEFGLC KQNGELKAYG AGLLSSYGEL LHSLSEEPEV RAFDPDTAAV QPYQDQTYQP VYFVSESFSD AKDKLRNYAS RIQRPFSVKF DPYTLAIDVL DSPHTIRRSL EGVQDELHTL TQALSAIS // ID TYRO_MOUSE Reviewed; 533 AA. AC P11344; DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot. DT 29-MAY-2007, sequence version 3. DT 19-MAR-2014, entry version 145. DE RecName: Full=Tyrosinase; DE EC=1.14.18.1; DE AltName: Full=Albino locus protein; DE AltName: Full=Monophenol monooxygenase; DE Flags: Precursor; GN Name=Tyr; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=C57BL/6J; RA Yamamoto H., Takeuchi S., Kudo T., Makino K., Nakata A., Shinoda T., RA Takeuchi T.; RT "Cloning and sequencing of mouse tyrosinase cDNA."; RL Jpn. J. Genet. 62:271-274(1987). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT SER-103. RC STRAIN=DBA/2J; RX PubMed=3134020; DOI=10.1016/S0006-291X(88)81370-6; RA Kwon B.S., Wakulchik M., Haq A.K., Halaban R., Kestler D.; RT "Sequence analysis of mouse tyrosinase cDNA and the effect of RT melanotropin on its gene expression."; RL Biochem. Biophys. Res. Commun. 153:1301-1309(1988). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=3141148; RA Mueller G., Ruppert S., Schmid E., Schuetz G.; RT "Functional analysis of alternatively spliced tyrosinase gene RT transcripts."; RL EMBO J. 7:2723-2730(1988). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ARG-420. RC STRAIN=Himalayan; RX PubMed=2567165; DOI=10.1016/0006-291X(89)91588-X; RA Kwon B.S., Halaban R., Chintamaneni C.; RT "Molecular basis of mouse Himalayan mutation."; RL Biochem. Biophys. Res. Commun. 161:252-260(1989). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=2494997; DOI=10.1016/0006-291X(89)90072-7; RA Terao M., Tabe L., Garattini E., Sartori D., Studer M., Mintz B.; RT "Isolation and characterization of variant cDNAs encoding mouse RT tyrosinase."; RL Biochem. Biophys. Res. Commun. 159:848-853(1989). RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-273. RX PubMed=2517217; DOI=10.1266/jjg.64.121; RA Yamamoto H., Takeuchi S., Kudo T., Sato C., Takeuchi T.; RT "Melanin production in cultured albino melanocytes transfected with RT mouse tyrosinase cDNA."; RL Jpn. J. Genet. 64:121-135(1989). RN [7] RP NUCLEOTIDE SEQUENCE OF 1-273, AND VARIANT ALBINO SER-103. RC STRAIN=BALB/c; RX PubMed=2507645; DOI=10.1111/1523-1747.ep12319693; RA Kwon B.S., Haq A.K., Wakulchik M., Kestler D., Barton D.E., RA Francke U., Lamoreux M.L., Whitney J.B. III, Halaban R.; RT "Isolation, chromosomal mapping, and expression of the mouse RT tyrosinase gene."; RL J. Invest. Dermatol. 93:589-594(1989). RN [8] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-13, AND VARIANT ALBINO SER-103. RC STRAIN=BALB/c; RX PubMed=2110899; DOI=10.1111/j.1432-1033.1990.tb15510.x; RA Shibahara S., Okinaga S., Tomita Y., Takeda A., Yamamoto H., Sato M., RA Takeuchi T.; RT "A point mutation in the tyrosinase gene of BALB/c albino mouse RT causing the cysteine-->serine substitution at position 85."; RL Eur. J. Biochem. 189:455-461(1990). RN [9] RP VARIANT CHINCHILLA MICE THR-482. RX PubMed=2118105; RA Beermann F., Ruppert S., Hummler E., Bosch F.X., Mueller G., RA Ruether U., Schuetz G.; RT "Rescue of the albino phenotype by introduction of a functional RT tyrosinase gene into mice."; RL EMBO J. 9:2819-2826(1990). CC -!- FUNCTION: This is a copper-containing oxidase that functions in CC the formation of pigments such as melanins and other polyphenolic CC compounds. Catalyzes the rate-limiting conversions of tyrosine to CC DOPA, DOPA to DOPA-quinone and possibly 5,6-dihydroxyindole to CC indole-5,6 quinone. CC -!- CATALYTIC ACTIVITY: 2 L-dopa + O(2) = 2 dopaquinone + 2 H(2)O. CC -!- CATALYTIC ACTIVITY: L-tyrosine + O(2) = dopaquinone + H(2)O. CC -!- COFACTOR: Binds 2 copper ions per subunit. CC -!- INTERACTION: CC P07147:Tyrp1; NbExp=2; IntAct=EBI-821603, EBI-821614; CC -!- SUBCELLULAR LOCATION: Melanosome membrane; Single-pass type I CC membrane protein. CC -!- DISEASE: Note=Defects in Tyr result in various forms of albinism. CC Himalayan strain tyrosinase is temperature-sensitive. CC -!- SIMILARITY: Belongs to the tyrosinase family. CC -!- SEQUENCE CAUTION: CC Sequence=BAA00079.1; Type=Miscellaneous discrepancy; CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=Snowy stardom - Issue CC 49 of August 2004; CC URL="http://web.expasy.org/spotlight/back_issues/049"; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; D00440; BAA00341.1; -; mRNA. DR EMBL; D00131; BAA00079.1; ALT_SEQ; mRNA. DR EMBL; M20234; AAA40516.1; -; mRNA. DR EMBL; X12782; CAA31273.1; -; mRNA. DR EMBL; M26729; AAA37806.1; -; mRNA. DR EMBL; M24560; AAA40517.1; -; mRNA. DR EMBL; D00439; BAA00340.1; -; Genomic_DNA. DR EMBL; X51743; CAA36033.1; -; Genomic_DNA. DR PIR; A27711; YRMSCS. DR RefSeq; NP_035791.1; NM_011661.4. DR UniGene; Mm.238127; -. DR ProteinModelPortal; P11344; -. DR SMR; P11344; 116-450. DR BioGrid; 204394; 7. DR IntAct; P11344; 1. DR BindingDB; P11344; -. DR ChEMBL; CHEMBL5346; -. DR PhosphoSite; P11344; -. DR PRIDE; P11344; -. DR Ensembl; ENSMUST00000004770; ENSMUSP00000004770; ENSMUSG00000004651. DR GeneID; 22173; -. DR KEGG; mmu:22173; -. DR UCSC; uc009ifo.1; mouse. DR CTD; 7299; -. DR MGI; MGI:98880; Tyr. DR eggNOG; NOG08919; -. DR HOGENOM; HOG000118376; -. DR HOVERGEN; HBG003553; -. DR InParanoid; P11344; -. DR KO; K00505; -. DR OMA; CLSLTQY; -. DR OrthoDB; EOG7TJ3HG; -. DR TreeFam; TF315865; -. DR NextBio; 302123; -. DR PRO; PR:P11344; -. DR ArrayExpress; P11344; -. DR Bgee; P11344; -. DR CleanEx; MM_TYR; -. DR Genevestigator; P11344; -. DR GO; GO:0016021; C:integral component of membrane; TAS:UniProtKB. DR GO; GO:0042470; C:melanosome; IDA:UniProtKB. DR GO; GO:0033162; C:melanosome membrane; IEA:UniProtKB-SubCell. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl. DR GO; GO:0005507; F:copper ion binding; IEA:Ensembl. DR GO; GO:0004503; F:monophenol monooxygenase activity; TAS:UniProtKB. DR GO; GO:0046982; F:protein heterodimerization activity; IDA:UniProtKB. DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB. DR GO; GO:0008283; P:cell proliferation; IMP:MGI. DR GO; GO:0042438; P:melanin biosynthetic process; IMP:MGI. DR GO; GO:0043473; P:pigmentation; IMP:MGI. DR GO; GO:0048538; P:thymus development; IMP:MGI. DR Gene3D; 1.10.1280.10; -; 1. DR InterPro; IPR002227; Tyrosinase. DR InterPro; IPR008922; Unchr_di-copper_centre. DR Pfam; PF00264; Tyrosinase; 1. DR PRINTS; PR00092; TYROSINASE. DR SUPFAM; SSF48056; SSF48056; 2. DR PROSITE; PS00497; TYROSINASE_1; 1. DR PROSITE; PS00498; TYROSINASE_2; 1. PE 1: Evidence at protein level; KW Albinism; Complete proteome; Copper; Disease mutation; Glycoprotein; KW Melanin biosynthesis; Membrane; Metal-binding; Monooxygenase; KW Oxidoreductase; Reference proteome; Signal; Transmembrane; KW Transmembrane helix. FT SIGNAL 1 18 Potential. FT CHAIN 19 533 Tyrosinase. FT /FTId=PRO_0000035880. FT TOPO_DOM 19 476 Lumenal, melanosome (Potential). FT TRANSMEM 477 497 Helical; (Potential). FT TOPO_DOM 498 533 Cytoplasmic (Potential). FT COMPBIAS 503 508 Poly-Lys. FT METAL 180 180 Copper A (By similarity). FT METAL 202 202 Copper A (By similarity). FT METAL 211 211 Copper A (By similarity). FT METAL 363 363 Copper B (By similarity). FT METAL 367 367 Copper B (By similarity). FT METAL 390 390 Copper B (By similarity). FT CARBOHYD 86 86 N-linked (GlcNAc...) (Potential). FT CARBOHYD 111 111 N-linked (GlcNAc...) (Potential). FT CARBOHYD 161 161 N-linked (GlcNAc...) (Potential). FT CARBOHYD 230 230 N-linked (GlcNAc...) (Potential). FT CARBOHYD 337 337 N-linked (GlcNAc...) (Potential). FT CARBOHYD 371 371 N-linked (GlcNAc...) (Potential). FT VARIANT 103 103 C -> S (in albino mice). FT VARIANT 420 420 H -> R (in strain: Himalayan). FT VARIANT 482 482 A -> T (in chinchilla mice). FT CONFLICT 40 40 M -> I (in Ref. 4; AAA37806). FT CONFLICT 197 197 D -> Q (in Ref. 4; AAA37806). FT CONFLICT 264 264 S -> I (in Ref. 3; CAA31273). FT CONFLICT 346 346 G -> V (in Ref. 2; AAA40516). SQ SEQUENCE 533 AA; 60606 MW; A4C109A97CBD5D6A CRC64; MFLAVLYCLL WSFQISDGHF PRACASSKNL LAKECCPPWM GDGSPCGQLS GRGSCQDILL SSAPSGPQFP FKGVDDRESW PSVFYNRTCQ CSGNFMGFNC GNCKFGFGGP NCTEKRVLIR RNIFDLSVSE KNKFFSYLTL AKHTISSVYV IPTGTYGQMN NGSTPMFNDI NIYDLFVWMH YYVSRDTLLG GSEIWRDIDF AHEAPGFLPW HRLFLLLWEQ EIRELTGDEN FTVPYWDWRD AENCDICTDE YLGGRHPENP NLLSPASFFS SWQIICSRSE EYNSHQVLCD GTPEGPLLRN PGNHDKAKTP RLPSSADVEF CLSLTQYESG SMDRTANFSF RNTLEGFASP LTGIADPSQS SMHNALHIFM NGTMSQVQGS ANDPIFLLHH AFVDSIFEQW LRRHRPLLEV YPEANAPIGH NRDSYMVPFI PLYRNGDFFI TSKDLGYDYS YLQESDPGFY RNYIEPYLEQ ASRIWPWLLG AALVGAVIAA ALSGLSSRLC LQKKKKKKQP QEERQPLLMD KDDYHSLLYQ SHL // ID TYRP1_MOUSE Reviewed; 537 AA. AC P07147; DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1988, sequence version 1. DT 19-FEB-2014, entry version 133. DE RecName: Full=5,6-dihydroxyindole-2-carboxylic acid oxidase; DE Short=DHICA oxidase; DE EC=1.14.18.-; DE AltName: Full=Brown locus protein; DE AltName: Full=Catalase B; DE AltName: Full=Tyrosinase-related protein 1; DE Short=TRP; DE Short=TRP-1; DE Short=TRP1; DE Flags: Precursor; GN Name=Tyrp1; Synonyms=Tyrp-1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Melanoma; RX PubMed=3008090; DOI=10.1093/nar/14.6.2413; RA Shibahara S., Tomita Y., Sakakura T., Nager C., Chaudhuri B., RA Mueller R.; RT "Cloning and expression of cDNA encoding mouse tyrosinase."; RL Nucleic Acids Res. 14:2413-2427(1986). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6; TISSUE=Eye; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP IDENTIFICATION OF PROTEIN. RX PubMed=3132713; DOI=10.1073/pnas.85.12.4392; RA Jackson I.J.; RT "A cDNA encoding tyrosinase-related protein maps to the brown locus in RT mouse."; RL Proc. Natl. Acad. Sci. U.S.A. 85:4392-4396(1988). RN [4] RP POSSIBLE FUNCTION. RX PubMed=1693779; DOI=10.1073/pnas.87.12.4809; RA Halaban R., Moellmann G.; RT "Murine and human b locus pigmentation genes encode a glycoprotein RT (gp75) with catalase activity."; RL Proc. Natl. Acad. Sci. U.S.A. 87:4809-4813(1990). RN [5] RP POSSIBLE FUNCTION. RX PubMed=8270621; RA Winder A.J., Wittbjer A., Rosengren E., Rorsman H.; RT "The mouse brown (b) locus protein has dopachrome tautomerase activity RT and is located in lysosomes in transfected fibroblasts."; RL J. Cell Sci. 106:153-166(1993). RN [6] RP FUNCTION. RX PubMed=7813420; RA Kobayashi T., Urabe K., Winder A., Jimenez-Cervantes C., Imokawa G., RA Brewington T., Solano F., Garcia-Borron J.C., Hearing V.J.; RT "Tyrosinase related protein 1 (TRP1) functions as a DHICA oxidase in RT melanin biosynthesis."; RL EMBO J. 13:5818-5825(1994). RN [7] RP SUBCELLULAR LOCATION. RX PubMed=17182842; DOI=10.1091/mbc.E06-12-1066; RA Setty S.R., Tenza D., Truschel S.T., Chou E., Sviderskaya E.V., RA Theos A.C., Lamoreux M.L., Di Pietro S.M., Starcevic M., Bennett D.C., RA Dell'Angelica E.C., Raposo G., Marks M.S.; RT "BLOC-1 is required for cargo-specific sorting from vacuolar early RT endosomes toward lysosome-related organelles."; RL Mol. Biol. Cell 18:768-780(2007). RN [8] RP VARIANTS BROWN TYR-110 AND HIS-326. RX PubMed=2245916; RA Zdarsky E., Favor J., Jackson I.J.; RT "The molecular basis of brown, an old mouse mutation, and of an RT induced revertant to wild type."; RL Genetics 126:443-449(1990). CC -!- FUNCTION: Oxidation of 5,6-dihydroxyindole-2-carboxylic acid CC (DHICA) into indole-5,6-quinone-2-carboxylic acid. May regulate or CC influence the type of melanin synthesized. CC -!- COFACTOR: Binds 2 copper ions per subunit (By similarity). CC -!- PATHWAY: Pigment biosynthesis; melanin biosynthesis. CC -!- INTERACTION: CC P11344:Tyr; NbExp=2; IntAct=EBI-821614, EBI-821603; CC -!- SUBCELLULAR LOCATION: Melanosome membrane; Single-pass type I CC membrane protein. Note=Located to mature stage III and IV CC melanosomes and apposed endosomal tubular membranes. Transported CC to pigmented melanosomes by the BLOC-1 complex. CC -!- TISSUE SPECIFICITY: Pigment cells. CC -!- DISEASE: Note=Defects in Tyrp1 are the cause of the brown (b) CC phenotype. Brown mice have a brown or hypopigmented coat. CC -!- SIMILARITY: Belongs to the tyrosinase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X03687; CAA27323.1; -; mRNA. DR EMBL; BC076598; AAH76598.1; -; mRNA. DR PIR; A24933; YRMSB6. DR RefSeq; NP_001268943.1; NM_001282014.1. DR RefSeq; NP_001268944.1; NM_001282015.1. DR RefSeq; NP_112479.1; NM_031202.3. DR UniGene; Mm.30438; -. DR ProteinModelPortal; P07147; -. DR SMR; P07147; 128-466. DR IntAct; P07147; 1. DR PhosphoSite; P07147; -. DR PRIDE; P07147; -. DR Ensembl; ENSMUST00000006151; ENSMUSP00000006151; ENSMUSG00000005994. DR Ensembl; ENSMUST00000102831; ENSMUSP00000099895; ENSMUSG00000005994. DR GeneID; 22178; -. DR KEGG; mmu:22178; -. DR UCSC; uc008tjq.2; mouse. DR CTD; 7306; -. DR MGI; MGI:98881; Tyrp1. DR eggNOG; NOG86242; -. DR HOGENOM; HOG000118376; -. DR HOVERGEN; HBG003553; -. DR InParanoid; P07147; -. DR KO; K00506; -. DR OMA; VKKTFLG; -. DR TreeFam; TF315865; -. DR BioCyc; MetaCyc:MONOMER-15620; -. DR UniPathway; UPA00785; -. DR ChiTaRS; TYRP1; mouse. DR NextBio; 302135; -. DR PRO; PR:P07147; -. DR ArrayExpress; P07147; -. DR Bgee; P07147; -. DR CleanEx; MM_TYRP1; -. DR Genevestigator; P07147; -. DR GO; GO:0030669; C:clathrin-coated endocytic vesicle membrane; IEA:Ensembl. DR GO; GO:0010008; C:endosome membrane; IEA:Ensembl. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0033162; C:melanosome membrane; IDA:UniProtKB. DR GO; GO:0005507; F:copper ion binding; IEA:InterPro. DR GO; GO:0016716; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, another compound as one donor, and incorporation of one atom of oxygen; IEA:InterPro. DR GO; GO:0046982; F:protein heterodimerization activity; IDA:UniProtKB. DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB. DR GO; GO:0043438; P:acetoacetic acid metabolic process; IMP:MGI. DR GO; GO:0006583; P:melanin biosynthetic process from tyrosine; TAS:UniProtKB. DR GO; GO:0030318; P:melanocyte differentiation; IMP:MGI. DR GO; GO:0032438; P:melanosome organization; IMP:MGI. DR Gene3D; 1.10.1280.10; -; 1. DR InterPro; IPR015559; DiOHindole_carboxylic_A_Oxase. DR InterPro; IPR002227; Tyrosinase. DR InterPro; IPR008922; Unchr_di-copper_centre. DR PANTHER; PTHR11474:SF3; PTHR11474:SF3; 1. DR Pfam; PF00264; Tyrosinase; 1. DR PRINTS; PR00092; TYROSINASE. DR SUPFAM; SSF48056; SSF48056; 2. DR PROSITE; PS00497; TYROSINASE_1; 1. DR PROSITE; PS00498; TYROSINASE_2; 1. PE 1: Evidence at protein level; KW Albinism; Complete proteome; Copper; Disease mutation; Glycoprotein; KW Melanin biosynthesis; Membrane; Metal-binding; Monooxygenase; KW Oxidoreductase; Reference proteome; Signal; Transmembrane; KW Transmembrane helix. FT SIGNAL 1 24 FT CHAIN 25 537 5,6-dihydroxyindole-2-carboxylic acid FT oxidase. FT /FTId=PRO_0000035890. FT TOPO_DOM 25 477 Lumenal, melanosome (Potential). FT TRANSMEM 478 501 Helical; (Potential). FT TOPO_DOM 502 537 Cytoplasmic (Potential). FT METAL 192 192 Copper A (By similarity). FT METAL 215 215 Copper A (By similarity). FT METAL 224 224 Copper A (By similarity). FT METAL 377 377 Copper B (By similarity). FT METAL 381 381 Copper B (By similarity). FT METAL 404 404 Copper B (By similarity). FT CARBOHYD 96 96 N-linked (GlcNAc...) (Potential). FT CARBOHYD 104 104 N-linked (GlcNAc...) (Potential). FT CARBOHYD 181 181 N-linked (GlcNAc...) (Potential). FT CARBOHYD 304 304 N-linked (GlcNAc...) (Potential). FT CARBOHYD 350 350 N-linked (GlcNAc...) (Potential). FT CARBOHYD 385 385 N-linked (GlcNAc...) (Potential). FT VARIANT 110 110 C -> Y (in brown). FT VARIANT 326 326 R -> H (in brown). SQ SEQUENCE 537 AA; 60761 MW; 86570998AA9EB0BC CRC64; MKSYNVLPLA YISLFLMLFY QVWAQFPREC ANIEALRRGV CCPDLLPSSG PGTDPCGSSS GRGRCVAVIA DSRPHSRHYP HDGKDDREAW PLRFFNRTCQ CNDNFSGHNC GTCRPGWRGA ACNQKILTVR RNLLDLSPEE KSHFVRALDM AKRTTHPQFV IATRRLEDIL GPDGNTPQFE NISVYNYFVW THYYSVKKTF LGTGQESFGD VDFSHEGPAF LTWHRYHLLQ LERDMQEMLQ EPSFSLPYWN FATGKNVCDV CTDDLMGSRS NFDSTLISPN SVFSQWRVVC ESLEEYDTLG TLCNSTEGGP IRRNPAGNVG RPAVQRLPEP QDVTQCLEVR VFDTPPFYSN STDSFRNTVE GYSAPTGKYD PAVRSLHNLA HLFLNGTGGQ THLSPNDPIF VLLHTFTDAV FDEWLRRYNA DISTFPLENA PIGHNRQYNM VPFWPPVTNT EMFVTAPDNL GYAYEVQWPG QEFTVSEIIT IAVVAALLLV AAIFGVASCL IRSRSTKNEA NQPLLTDHYQ RYAEDYEELP NPNHSMV // ID TYW5_MOUSE Reviewed; 315 AA. AC A2RSX7; Q3UT82; Q4KL17; DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot. DT 13-NOV-2007, sequence version 2. DT 19-MAR-2014, entry version 52. DE RecName: Full=tRNA wybutosine-synthesizing protein 5; DE EC=1.14.11.42; DE AltName: Full=tRNA(Phe) (7-(3-amino-3-carboxypropyl)wyosine(37)-C(2))-hydroxylase; GN Name=Tyw5; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC STRAIN=C57BL/6J; TISSUE=Egg; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE RP SEQUENCE [LARGE SCALE MRNA] OF 10-315 (ISOFORM 2). RC TISSUE=Brain, and Thyroid; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: tRNA hydroxylase that acts as a component of the CC wybutosine biosynthesis pathway. Wybutosine is a hyper modified CC guanosine with a tricyclic base found at the 3'-position adjacent CC to the anticodon of eukaryotic phenylalanine tRNA. Catalyzes the CC hydroxylation of 7-(a-amino-a-carboxypropyl)wyosine (yW-72) into CC undermodified hydroxywybutosine (OHyW*). OHyW* being further CC transformed into hydroxywybutosine (OHyW) by LCMT2/TYW4. OHyW is a CC derivative of wybutosine found in higher eukaryotes (By CC similarity). CC -!- CATALYTIC ACTIVITY: 7-(3-amino-3-carboxypropyl)wyosine(37) in CC tRNA(Phe) + 2-oxoglutarate + O(2) = 7-(2-hydroxy-3-amino-3- CC carboxypropyl)wyosine(37) in tRNA(Phe) + succinate + CO(2). CC -!- COFACTOR: Binds 1 Fe(2+) ion per subunit (By similarity). CC -!- PATHWAY: tRNA modification; wybutosine-tRNA(Phe) biosynthesis. CC -!- SUBUNIT: Homodimer (By similarity). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=A2RSX7-1; Sequence=Displayed; CC Name=2; CC IsoId=A2RSX7-2; Sequence=VSP_029107, VSP_029108; CC -!- SIMILARITY: Belongs to the TYW5 family. CC -!- SIMILARITY: Contains 1 JmjC domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK139666; BAE24098.1; -; mRNA. DR EMBL; BC099495; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; BC132289; AAI32290.1; -; mRNA. DR RefSeq; NP_001032831.2; NM_001037742.2. DR RefSeq; NP_001107574.1; NM_001114102.1. DR UniGene; Mm.288490; -. DR ProteinModelPortal; A2RSX7; -. DR SMR; A2RSX7; 1-311. DR PhosphoSite; A2RSX7; -. DR PaxDb; A2RSX7; -. DR PRIDE; A2RSX7; -. DR Ensembl; ENSMUST00000079998; ENSMUSP00000078912; ENSMUSG00000048495. [A2RSX7-2] DR Ensembl; ENSMUST00000161780; ENSMUSP00000125487; ENSMUSG00000048495. [A2RSX7-2] DR Ensembl; ENSMUST00000162686; ENSMUSP00000125427; ENSMUSG00000048495. [A2RSX7-1] DR GeneID; 68736; -. DR KEGG; mmu:68736; -. DR UCSC; uc007baz.2; mouse. [A2RSX7-1] DR UCSC; uc007bbb.2; mouse. [A2RSX7-2] DR CTD; 129450; -. DR MGI; MGI:1915986; Tyw5. DR eggNOG; NOG276154; -. DR GeneTree; ENSGT00530000062914; -. DR HOVERGEN; HBG096249; -. DR InParanoid; A2RSX7; -. DR OMA; NVFWRHL; -. DR OrthoDB; EOG7X3QRF; -. DR TreeFam; TF332364; -. DR UniPathway; UPA00375; -. DR NextBio; 327810; -. DR PRO; PR:A2RSX7; -. DR ArrayExpress; A2RSX7; -. DR Bgee; A2RSX7; -. DR CleanEx; MM_1110034B05RIK; -. DR Genevestigator; A2RSX7; -. DR GO; GO:0005506; F:iron ion binding; ISS:UniProtKB. DR GO; GO:0016706; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors; ISS:UniProtKB. DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB. DR GO; GO:0000049; F:tRNA binding; ISS:UniProtKB. DR GO; GO:0031591; P:wybutosine biosynthetic process; ISS:UniProtKB. DR InterPro; IPR003347; JmjC_dom. DR SMART; SM00558; JmjC; 1. DR PROSITE; PS51184; JMJC; 1. PE 2: Evidence at transcript level; KW Alternative splicing; Complete proteome; Dioxygenase; Iron; KW Metal-binding; Oxidoreductase; Reference proteome; tRNA processing. FT CHAIN 1 315 tRNA wybutosine-synthesizing protein 5. FT /FTId=PRO_0000309275. FT DOMAIN 102 267 JmjC. FT METAL 160 160 Iron; catalytic (By similarity). FT METAL 162 162 Iron; catalytic (By similarity). FT METAL 235 235 Iron; catalytic (By similarity). FT BINDING 106 106 2-oxoglutarate (By similarity). FT BINDING 166 166 2-oxoglutarate (By similarity). FT BINDING 175 175 2-oxoglutarate (By similarity). FT VAR_SEQ 72 121 SKNFVYRTLPFNKLVQRAAEETHKEFFISEDEKYYLRSLGE FT DPRKDVADI -> KLYLLTSWSREQPKKHIKNSSFQRMRNT FT TYGHLEKTQGRMLQTSDSSSHH (in isoform 2). FT /FTId=VSP_029107. FT VAR_SEQ 122 315 Missing (in isoform 2). FT /FTId=VSP_029108. FT CONFLICT 5 5 R -> H (in Ref. 2; AAI32290). SQ SEQUENCE 315 AA; 36633 MW; 26B51EF4662C55A3 CRC64; MAEQRLPVPR LRGVSREQFM EHLYPQRKPL VLEGLDLGSC TSKWTVDYLS QVGGTKEVKI HVAAVPQMDF ISKNFVYRTL PFNKLVQRAA EETHKEFFIS EDEKYYLRSL GEDPRKDVAD IRQQFPSLGG DITFPMFFRE EQFFSSVFRI SSPGLQLWTH YDVMDNFLIQ VTGKKRITLF NPRDAQYLYL SGSKSEVLNI DSPDLDKYPL FPKARRYECS LEAGDVLFIP ALWFHNVVSE EFGVGVNIFW KHLPSECYDT TDTYGNKDPV AASRAVQILD RALKTLAELP EEYRDFYARQ MVLRIQDKAY SKNFE // ID UCRI_MOUSE Reviewed; 274 AA. AC Q9CR68; Q5SVV1; DT 13-SEP-2004, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 19-MAR-2014, entry version 102. DE RecName: Full=Cytochrome b-c1 complex subunit Rieske, mitochondrial; DE EC=1.10.2.2; DE AltName: Full=Complex III subunit 5; DE AltName: Full=Cytochrome b-c1 complex subunit 5; DE AltName: Full=Rieske iron-sulfur protein; DE Short=RISP; DE AltName: Full=Ubiquinol-cytochrome c reductase iron-sulfur subunit; DE Contains: DE RecName: Full=Cytochrome b-c1 complex subunit 11; DE AltName: Full=Complex III subunit IX; DE AltName: Full=Ubiquinol-cytochrome c reductase 8 kDa protein; DE Flags: Precursor; GN Name=Uqcrfs1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Bone marrow, and Liver; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Mammary tumor; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP PROTEIN SEQUENCE OF 8-46; 85-92; 94-101; 131-151; 156-163; 171-177 AND RP 183-204, AND MASS SPECTROMETRY. RC STRAIN=C57BL/6; TISSUE=Brain; RA Lubec G., Kang S.U.; RL Submitted (APR-2007) to UniProtKB. CC -!- FUNCTION: Component of the ubiquinol-cytochrome c reductase CC complex (complex III or cytochrome b-c1 complex), which is a CC respiratory chain that generates an electrochemical potential CC coupled to ATP synthesis. CC -!- FUNCTION: The transit peptide of the Rieske protein seems to form CC part of the bc1 complex and is considered to be the subunit 11/IX CC of that complex (By similarity). CC -!- CATALYTIC ACTIVITY: Quinol + 2 ferricytochrome c = quinone + 2 CC ferrocytochrome c + 2 H(+). CC -!- COFACTOR: Binds 1 2Fe-2S cluster per subunit (By similarity). CC -!- SUBUNIT: The bc1 complex contains 11 subunits: 3 respiratory CC subunits (cytochrome b, cytochrome c1 and Rieske/UQCRFS1), 2 core CC proteins (UQCRC1/QCR1 and UQCRC2/QCR2) and 6 low-molecular weight CC proteins (UQCRH/QCR6, UQCRB/QCR7, UQCRQ/QCR8, UQCR10/QCR9, CC UQCR11/QCR10 and a cleavage product of Rieske/UQCRFS1) (By CC similarity). CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Single-pass CC membrane protein. CC -!- MISCELLANEOUS: The Rieske protein is a high potential 2Fe-2S CC protein. CC -!- SIMILARITY: Contains 1 Rieske domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK003966; BAB23097.1; -; mRNA. DR EMBL; AK012180; BAB28081.1; -; mRNA. DR EMBL; AK014470; BAB29374.1; -; mRNA. DR EMBL; AK153139; BAE31751.1; -; mRNA. DR EMBL; AK152391; BAE31179.1; -; mRNA. DR EMBL; AL611944; CAI24872.1; -; Genomic_DNA. DR EMBL; BC019934; AAH19934.1; -; mRNA. DR RefSeq; NP_079986.1; NM_025710.2. DR UniGene; Mm.181933; -. DR ProteinModelPortal; Q9CR68; -. DR SMR; Q9CR68; 1-57, 79-274. DR BioGrid; 211651; 1. DR IntAct; Q9CR68; 4. DR MINT; MINT-1842979; -. DR PhosphoSite; Q9CR68; -. DR PaxDb; Q9CR68; -. DR PRIDE; Q9CR68; -. DR Ensembl; ENSMUST00000042834; ENSMUSP00000045284; ENSMUSG00000038462. DR GeneID; 66694; -. DR KEGG; mmu:66694; -. DR UCSC; uc007pyv.2; mouse. DR CTD; 7386; -. DR MGI; MGI:1913944; Uqcrfs1. DR eggNOG; COG0723; -. DR GeneTree; ENSGT00390000001014; -. DR HOGENOM; HOG000255193; -. DR HOVERGEN; HBG001040; -. DR InParanoid; Q9CR68; -. DR KO; K00411; -. DR OMA; DYRRAEV; -. DR OrthoDB; EOG7GBFXQ; -. DR TreeFam; TF105037; -. DR NextBio; 322393; -. DR PRO; PR:Q9CR68; -. DR Bgee; Q9CR68; -. DR Genevestigator; Q9CR68; -. DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:MGI. DR GO; GO:0005750; C:mitochondrial respiratory chain complex III; IEA:Ensembl. DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008121; F:ubiquinol-cytochrome-c reductase activity; IEA:UniProtKB-EC. DR GO; GO:1902600; P:hydrogen ion transmembrane transport; IEA:GOC. DR GO; GO:0046677; P:response to antibiotic; IEA:Ensembl. DR GO; GO:0042493; P:response to drug; IEA:Ensembl. DR GO; GO:0009725; P:response to hormone; IEA:Ensembl. DR Gene3D; 1.20.5.270; -; 1. DR Gene3D; 2.102.10.10; -; 1. DR InterPro; IPR011070; Globular_prot_asu/bsu. DR InterPro; IPR017941; Rieske_2Fe-2S. DR InterPro; IPR014349; Rieske_Fe-S_prot. DR InterPro; IPR005805; Rieske_Fe-S_prot_C. DR InterPro; IPR015248; Ubiqinol_cyt_c_Rdtase_N. DR InterPro; IPR006317; Ubiquinol_cyt_c_Rdtase_Fe-S-su. DR InterPro; IPR004192; Ubiquinol_cyt_Rdtase_TM. DR PANTHER; PTHR10134; PTHR10134; 1. DR Pfam; PF00355; Rieske; 1. DR Pfam; PF09165; Ubiq-Cytc-red_N; 1. DR Pfam; PF02921; UCR_TM; 1. DR PRINTS; PR00162; RIESKE. DR SUPFAM; SSF50022; SSF50022; 1. DR SUPFAM; SSF56568; SSF56568; 1. DR TIGRFAMs; TIGR01416; Rieske_proteo; 1. DR PROSITE; PS51296; RIESKE; 1. PE 1: Evidence at protein level; KW 2Fe-2S; Complete proteome; Direct protein sequencing; Disulfide bond; KW Electron transport; Iron; Iron-sulfur; Membrane; Metal-binding; KW Mitochondrion; Mitochondrion inner membrane; Oxidoreductase; KW Reference proteome; Respiratory chain; Transit peptide; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1 78 Cytochrome b-c1 complex subunit 11 (By FT similarity). FT /FTId=PRO_0000307244. FT TRANSIT 1 78 Mitochondrion (By similarity). FT CHAIN 79 274 Cytochrome b-c1 complex subunit Rieske, FT mitochondrial. FT /FTId=PRO_0000030667. FT TRANSMEM 103 140 Helical; (By similarity). FT DOMAIN 187 272 Rieske. FT METAL 217 217 Iron-sulfur (2Fe-2S) (By similarity). FT METAL 219 219 Iron-sulfur (2Fe-2S); via pros nitrogen FT (By similarity). FT METAL 236 236 Iron-sulfur (2Fe-2S) (By similarity). FT METAL 239 239 Iron-sulfur (2Fe-2S); via pros nitrogen FT (By similarity). FT DISULFID 222 238 By similarity. SQ SEQUENCE 274 AA; 29368 MW; 17E55DE0BBD09961 CRC64; MLSVAARSGP FAPVLSATSR GVAGALRPLL QGAVPAASEP PVLDVKRPFL CRESLSGQAA ARPLVATVGL NVPASVRFSH TDVKVPDFSD YRRAEVLDST KSSKESSEAR KGFSYLVTAT TTVGVAYAAK NVVSQFVSSM SASADVLAMS KIEIKLSDIP EGKNMAFKWR GKPLFVRHRT KKEIDQEAAV EVSQLRDPQH DLDRVKKPEW VILIGVCTHL GCVPIANAGD FGGYYCPCHG SHYDASGRIR KGPAPLNLEV PAYEFTSDDV VVVG // ID UGDH_MOUSE Reviewed; 493 AA. AC O70475; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1998, sequence version 1. DT 19-MAR-2014, entry version 113. DE RecName: Full=UDP-glucose 6-dehydrogenase; DE Short=UDP-Glc dehydrogenase; DE Short=UDP-GlcDH; DE Short=UDPGDH; DE EC=1.1.1.22; GN Name=Ugdh; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, AND FUNCTION. RX PubMed=9737970; DOI=10.1074/jbc.273.39.25117; RA Spicer A.P., Kaback L.A., Smith T.J., Seldin M.F.; RT "Molecular cloning and characterization of the human and mouse UDP- RT glucose dehydrogenase genes."; RL J. Biol. Chem. 273:25117-25124(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Mammary gland; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-474, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=17242355; DOI=10.1073/pnas.0609836104; RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; RT "Large-scale phosphorylation analysis of mouse liver."; RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). RN [4] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=18630941; DOI=10.1021/pr800223m; RA Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.; RT "Specific phosphopeptide enrichment with immobilized titanium ion RT affinity chromatography adsorbent for phosphoproteome analysis."; RL J. Proteome Res. 7:3957-3967(2008). RN [5] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-474, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic fibroblast; RX PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200; RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.; RT "Large scale localization of protein phosphorylation by use of RT electron capture dissociation mass spectrometry."; RL Mol. Cell. Proteomics 8:904-912(2009). RN [6] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-107, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic fibroblast; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., RA Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). CC -!- FUNCTION: Involved in the biosynthesis of glycosaminoglycans; CC hyaluronan, chondroitin sulfate, and heparan sulfate. CC -!- CATALYTIC ACTIVITY: UDP-glucose + 2 NAD(+) + H(2)O = UDP- CC glucuronate + 2 NADH. CC -!- ENZYME REGULATION: UDP-alpha-D-xylose (UDX) acts as a feedback CC inhibitor by activating an allosteric switch (By similarity). CC -!- PATHWAY: Nucleotide-sugar biosynthesis; UDP-alpha-D-glucuronate CC biosynthesis; UDP-alpha-D-glucuronate from UDP-alpha-D-glucose: CC step 1/1. CC -!- SUBUNIT: Homohexamer (By similarity). CC -!- SIMILARITY: Belongs to the UDP-glucose/GDP-mannose dehydrogenase CC family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF061017; AAC36096.1; -; mRNA. DR EMBL; BC006749; AAH06749.1; -; mRNA. DR RefSeq; NP_033492.1; NM_009466.2. DR RefSeq; XP_006503925.1; XM_006503862.1. DR UniGene; Mm.344831; -. DR ProteinModelPortal; O70475; -. DR SMR; O70475; 1-466. DR IntAct; O70475; 3. DR MINT; MINT-1854432; -. DR PhosphoSite; O70475; -. DR PaxDb; O70475; -. DR PRIDE; O70475; -. DR Ensembl; ENSMUST00000031103; ENSMUSP00000031103; ENSMUSG00000029201. DR GeneID; 22235; -. DR KEGG; mmu:22235; -. DR UCSC; uc008xns.1; mouse. DR CTD; 7358; -. DR MGI; MGI:1306785; Ugdh. DR eggNOG; COG1004; -. DR HOGENOM; HOG000153773; -. DR HOVERGEN; HBG003512; -. DR InParanoid; O70475; -. DR KO; K00012; -. DR OMA; NEVGNIC; -. DR TreeFam; TF105671; -. DR UniPathway; UPA00038; UER00491. DR NextBio; 302285; -. DR PRO; PR:O70475; -. DR ArrayExpress; O70475; -. DR Bgee; O70475; -. DR CleanEx; MM_UGDH; -. DR Genevestigator; O70475; -. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR GO; GO:0003979; F:UDP-glucose 6-dehydrogenase activity; IEA:UniProtKB-EC. DR GO; GO:0001702; P:gastrulation with mouth forming second; IMP:MGI. DR GO; GO:0006065; P:UDP-glucuronate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.720; -; 2. DR InterPro; IPR008927; 6-PGluconate_DH_C-like. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR017476; UDP-Glc/GDP-Man. DR InterPro; IPR014027; UDP-Glc/GDP-Man_DH_C. DR InterPro; IPR014026; UDP-Glc/GDP-Man_DH_dimer. DR InterPro; IPR001732; UDP-Glc/GDP-Man_DH_N. DR InterPro; IPR028356; UDPglc_DH_euk. DR PANTHER; PTHR11374; PTHR11374; 1. DR PANTHER; PTHR11374:SF3; PTHR11374:SF3; 1. DR Pfam; PF00984; UDPG_MGDP_dh; 1. DR Pfam; PF03720; UDPG_MGDP_dh_C; 1. DR Pfam; PF03721; UDPG_MGDP_dh_N; 1. DR PIRSF; PIRSF500133; UDPglc_DH_euk; 1. DR PIRSF; PIRSF000124; UDPglc_GDPman_dh; 1. DR SMART; SM00984; UDPG_MGDP_dh_C; 1. DR SUPFAM; SSF48179; SSF48179; 1. DR SUPFAM; SSF52413; SSF52413; 1. DR TIGRFAMs; TIGR03026; NDP-sugDHase; 1. PE 1: Evidence at protein level; KW Acetylation; Allosteric enzyme; Complete proteome; NAD; KW Oxidoreductase; Phosphoprotein; Reference proteome. FT CHAIN 1 493 UDP-glucose 6-dehydrogenase. FT /FTId=PRO_0000074061. FT NP_BIND 11 16 NAD (By similarity). FT NP_BIND 89 93 NAD (By similarity). FT NP_BIND 130 131 NAD (By similarity). FT NP_BIND 276 279 NAD (By similarity). FT REGION 161 165 Substrate binding (By similarity). FT REGION 220 227 Substrate binding (By similarity). FT REGION 260 273 Substrate binding (By similarity). FT REGION 338 339 Substrate binding (By similarity). FT ACT_SITE 276 276 Nucleophile (By similarity). FT BINDING 36 36 NAD (By similarity). FT BINDING 41 41 NAD (By similarity). FT BINDING 165 165 NAD (By similarity). FT BINDING 346 346 NAD (By similarity). FT BINDING 442 442 Substrate (By similarity). FT MOD_RES 107 107 N6-acetyllysine. FT MOD_RES 474 474 Phosphothreonine. SQ SEQUENCE 493 AA; 54832 MW; C6234F3C1D7480C7 CRC64; MVEIKKICCI GAGYVGGPTC SVIAHMCPEI RVTVVDVNEA RINAWNSPTL PIYEPGLKEV VESCRGKNLF FSTNIDDAIR EADLVFISVN TPTKTYGMGK GRAADLKYIE ACARRIVQNS NGYKIVTEKS TVPVRAAESI RRIFDANTKP NLNLQVLSNP EFLAEGTAIK DLKNPDRVLI GGDETPEGQK AVRALCAVYE HWVPKEKILT TNTWSSELSK LAANAFLAQR ISSINSISAL CEATGADVEE VATAIGMDQR IGNKFLKASV GFGGSCFQKD VLNLVYLCEA LNLPEVARYW QQVIDMNDYQ RRRFASRIID SLFNTVTDKK IAILGFAFKK DTGDTRESSS IYISKYLMDE GAHLHIYDPK VPREQIVVDL SHPGVSADDQ VSRLVTISKD PYEACDGAHA LVICTEWDMF KELDYERIHK KMLKPAFIFD GRRVLDGLHS ELQTIGFQIE TIGKKVSSKR IPYTPGEIPK FSLQDPPNKK PKV // ID URIC_MOUSE Reviewed; 303 AA. AC P25688; DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 19-MAR-2014, entry version 117. DE RecName: Full=Uricase; DE EC=1.7.3.3; DE AltName: Full=Urate oxidase; GN Name=Uox; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=2594778; DOI=10.1073/pnas.86.23.9412; RA Wu X., Lee C.C., Muzny D.M., Caskey C.T.; RT "Urate oxidase: primary structure and evolutionary implications."; RL Proc. Natl. Acad. Sci. U.S.A. 86:9412-9416(1989). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Liver; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP PROTEIN SEQUENCE OF 2-18; 42-52; 56-80; 86-107; 148-158; 165-185; RP 188-196; 203-214 AND 221-236, CLEAVAGE OF INITIATOR METHIONINE, RP ACETYLATION AT ALA-2, AND MASS SPECTROMETRY. RC STRAIN=C57BL/6; TISSUE=Liver; RA Kanor S., Bienvenut W.V.; RL Submitted (OCT-2005) to UniProtKB. RN [4] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=17242355; DOI=10.1073/pnas.0609836104; RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; RT "Large-scale phosphorylation analysis of mouse liver."; RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). RN [5] RP SUBCELLULAR LOCATION. RX PubMed=23085393; DOI=10.1016/j.febslet.2012.10.009; RA Nakamura Y., Ogura M., Ogura K., Tanaka D., Inagaki N.; RT "SIRT5 deacetylates and activates urate oxidase in liver mitochondria RT of mice."; RL FEBS Lett. 586:4076-4081(2012). RN [6] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, SUCCINYLATION [LARGE RP SCALE ANALYSIS] AT LYS-10; LYS-23; LYS-220 AND LYS-227, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., RA Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). RN [7] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-10; LYS-23; LYS-27; LYS-36; RP LYS-118; LYS-122; LYS-164; LYS-175; LYS-185; LYS-220; LYS-227 AND RP LYS-277, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Liver; RX PubMed=23576753; DOI=10.1073/pnas.1302961110; RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., RA Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.; RT "Label-free quantitative proteomics of the lysine acetylome in RT mitochondria identifies substrates of SIRT3 in metabolic pathways."; RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013). CC -!- FUNCTION: Catalyzes the oxidation of uric acid to 5- CC hydroxyisourate, which is further processed to form (S)-allantoin. CC -!- CATALYTIC ACTIVITY: Urate + O(2) + H(2)O = 5-hydroxyisourate + CC H(2)O(2). CC -!- PATHWAY: Purine metabolism; urate degradation; (S)-allantoin from CC urate: step 1/3. CC -!- SUBCELLULAR LOCATION: Peroxisome. Mitochondrion. CC -!- PTM: Acetylation of Lys-118, Lys-164 and Lys-290 is observed in CC liver mitochondria from fasted mice but not from fed mice. May be CC deacetylated by Sirt5; however it is unclear whether Sirt5 CC mediates deacetylation or desuccinylation of Uox; additional CC evidence is required to validate these results (PubMed:23085393). CC -!- SIMILARITY: Belongs to the uricase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M27695; AAA40538.1; -; mRNA. DR EMBL; BC019771; AAH19771.1; -; mRNA. DR PIR; B36227; B36227. DR RefSeq; NP_033500.1; NM_009474.5. DR UniGene; Mm.10865; -. DR ProteinModelPortal; P25688; -. DR SMR; P25688; 21-297. DR IntAct; P25688; 6. DR MINT; MINT-4139643; -. DR PhosphoSite; P25688; -. DR SWISS-2DPAGE; P25688; -. DR PaxDb; P25688; -. DR PRIDE; P25688; -. DR Ensembl; ENSMUST00000029837; ENSMUSP00000029837; ENSMUSG00000028186. DR GeneID; 22262; -. DR KEGG; mmu:22262; -. DR UCSC; uc008rrp.1; mouse. DR CTD; 391051; -. DR MGI; MGI:98907; Uox. DR eggNOG; COG3648; -. DR HOGENOM; HOG000250659; -. DR HOVERGEN; HBG018060; -. DR InParanoid; P25688; -. DR KO; K00365; -. DR OMA; SDIIPTD; -. DR OrthoDB; EOG79KPFH; -. DR TreeFam; TF323438; -. DR UniPathway; UPA00394; UER00650. DR NextBio; 302359; -. DR PRO; PR:P25688; -. DR ArrayExpress; P25688; -. DR Bgee; P25688; -. DR CleanEx; MM_UOX; -. DR Genevestigator; P25688; -. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR GO; GO:0005777; C:peroxisome; TAS:MGI. DR GO; GO:0004846; F:urate oxidase activity; TAS:MGI. DR GO; GO:0006144; P:purine nucleobase metabolic process; TAS:MGI. DR GO; GO:0019628; P:urate catabolic process; IEA:UniProtKB-UniPathway. DR InterPro; IPR002042; Uricase. DR InterPro; IPR019842; Uricase_CS. DR PANTHER; PTHR10395:SF1; PTHR10395:SF1; 1. DR Pfam; PF01014; Uricase; 2. DR PIRSF; PIRSF000241; Urate_oxidase; 1. DR PRINTS; PR00093; URICASE. DR TIGRFAMs; TIGR03383; urate_oxi; 1. DR PROSITE; PS00366; URICASE; 1. PE 1: Evidence at protein level; KW Acetylation; Complete proteome; Direct protein sequencing; KW Mitochondrion; Oxidoreductase; Peroxisome; Phosphoprotein; KW Purine metabolism; Reference proteome. FT INIT_MET 1 1 Removed. FT CHAIN 2 303 Uricase. FT /FTId=PRO_0000165986. FT REGION 68 69 Substrate binding (By similarity). FT REGION 234 235 Substrate binding (By similarity). FT MOTIF 301 303 Microbody targeting signal (Potential). FT ACT_SITE 187 187 Charge relay system (By similarity). FT ACT_SITE 235 235 Charge relay system (By similarity). FT BINDING 187 187 Substrate (By similarity). FT MOD_RES 2 2 N-acetylalanine. FT MOD_RES 10 10 N6-acetyllysine; alternate. FT MOD_RES 10 10 N6-succinyllysine; alternate. FT MOD_RES 23 23 N6-acetyllysine; alternate. FT MOD_RES 23 23 N6-succinyllysine; alternate. FT MOD_RES 27 27 N6-acetyllysine. FT MOD_RES 36 36 N6-acetyllysine. FT MOD_RES 63 63 Phosphoserine. FT MOD_RES 118 118 N6-acetyllysine. FT MOD_RES 122 122 N6-acetyllysine. FT MOD_RES 164 164 N6-acetyllysine. FT MOD_RES 175 175 N6-acetyllysine. FT MOD_RES 185 185 N6-acetyllysine. FT MOD_RES 220 220 N6-acetyllysine; alternate. FT MOD_RES 220 220 N6-succinyllysine; alternate. FT MOD_RES 227 227 N6-acetyllysine; alternate. FT MOD_RES 227 227 N6-succinyllysine; alternate. FT MOD_RES 277 277 N6-acetyllysine. SQ SEQUENCE 303 AA; 35039 MW; F521383D05370FA2 CRC64; MAHYHDNYGK NDEVEFVRTG YGKDMVKVLH IQRDGKYHSI KEVATSVQLT LRSKKDYLHG DNSDIIPTDT IKNTVHVLAK LRGIRNIETF AMNICEHFLS SFNHVTRAHV YVEEVPWKRF EKNGIKHVHA FIHTPTGTHF CEVEQMRNGP PVIHSGIKDL KVLKTTQSGF EGFLKDQFTT LPEVKDRCFA TQVYCKWRYQ RRDVDFEAIW GAVRDIVLQK FAGPYDKGEY SPSVQKTLYD IQVLSLSQLP EIEDMEISLP NIHYFNIDMS KMGLINKEEV LLPLDNPYGK ITGTVKRKLP SRL // ID UTY_MOUSE Reviewed; 1212 AA. AC P79457; O97979; DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1999, sequence version 2. DT 19-FEB-2014, entry version 110. DE RecName: Full=Histone demethylase UTY; DE EC=1.14.11.-; DE AltName: Full=Male-specific histocompatibility antigen H-YDB; DE AltName: Full=Ubiquitously transcribed TPR protein on the Y chromosome; DE AltName: Full=Ubiquitously transcribed Y chromosome tetratricopeptide repeat protein; GN Name=Uty; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=RIII; TISSUE=Testis; RX PubMed=9736773; DOI=10.1093/hmg/7.11.1713; RA Mazeyrat S., Saut N., Sargent C.A., Grimmond S., Longepied G., RA Ehrmann I.E., Ellis P.S., Greenfield A., Affara N.A., Mitchell M.J.; RT "The mouse Y chromosome interval necessary for spermatogonial RT proliferation is gene dense with syntenic homology to the human AZFa RT region."; RL Hum. Mol. Genet. 7:1713-1724(1998). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=Swiss; RX PubMed=8944031; DOI=10.1038/ng1296-474; RA Greenfield A., Scott D., Pennisi D., Ehrmann I., Ellis P.S., RA Cooper L., Simpson E., Koopman P.; RT "An H-YDb epitope is encoded by a novel mouse Y chromosome gene."; RL Nat. Genet. 14:474-478(1996). RN [3] RP INTERACTION WITH TLE1 AND TLE2. RX PubMed=9854018; DOI=10.1042/0264-6021:3370013; RA Grbavec D., Lo R., Liu Y., Greenfield A., Stifani S.; RT "Groucho/transducin-like enhancer of split (TLE) family members RT interact with the yeast transcriptional co-repressor SSN6 and RT mammalian SSN6-related proteins: implications for evolutionary RT conservation of transcription repression mechanisms."; RL Biochem. J. 337:13-17(1999). CC -!- FUNCTION: Histone demethylase (By similarity). CC -!- COFACTOR: Ascorbate (By similarity). CC -!- COFACTOR: Fe(2+) (By similarity). CC -!- SUBUNIT: Binds TLE1 and TLE2. CC -!- SUBCELLULAR LOCATION: Nucleus (Potential). CC -!- SIMILARITY: Belongs to the UTX family. CC -!- SIMILARITY: Contains 1 JmjC domain. CC -!- SIMILARITY: Contains 8 TPR repeats. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF057367; AAC67385.1; -; mRNA. DR EMBL; Y09222; CAA70422.1; -; mRNA. DR PIR; T42387; T42387. DR PIR; T42729; T42729. DR UniGene; Mm.20477; -. DR ProteinModelPortal; P79457; -. DR SMR; P79457; 698-1209. DR PhosphoSite; P79457; -. DR PRIDE; P79457; -. DR MGI; MGI:894810; Uty. DR eggNOG; COG0457; -. DR HOGENOM; HOG000220834; -. DR HOVERGEN; HBG018063; -. DR InParanoid; P79457; -. DR PRO; PR:P79457; -. DR Genevestigator; P79457; -. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0051864; F:histone demethylase activity (H3-K36 specific); IMP:MGI. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0000978; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding; IDA:MGI. DR GO; GO:0060070; P:canonical Wnt signaling pathway; IDA:MGI. DR GO; GO:0086003; P:cardiac muscle cell contraction; IMP:MGI. DR GO; GO:0045184; P:establishment of protein localization; IDA:MGI. DR GO; GO:0007507; P:heart development; IMP:MGI. DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI. DR GO; GO:0031935; P:regulation of chromatin silencing; IMP:MGI. DR Gene3D; 1.25.40.10; -; 1. DR InterPro; IPR003347; JmjC_dom. DR InterPro; IPR013026; TPR-contain_dom. DR InterPro; IPR011990; TPR-like_helical. DR InterPro; IPR001440; TPR_1. DR InterPro; IPR019734; TPR_repeat. DR Pfam; PF02373; JmjC; 1. DR Pfam; PF00515; TPR_1; 3. DR Pfam; PF13181; TPR_8; 1. DR SMART; SM00558; JmjC; 1. DR SMART; SM00028; TPR; 6. DR PROSITE; PS51184; JMJC; 1. DR PROSITE; PS50005; TPR; 7. DR PROSITE; PS50293; TPR_REGION; 1. PE 1: Evidence at protein level; KW Chromatin regulator; Complete proteome; Dioxygenase; Iron; KW Metal-binding; Nucleus; Oxidoreductase; Reference proteome; Repeat; KW TPR repeat. FT CHAIN 1 1212 Histone demethylase UTY. FT /FTId=PRO_0000106413. FT REPEAT 88 121 TPR 1. FT REPEAT 125 158 TPR 2. FT REPEAT 165 193 TPR 3. FT REPEAT 200 233 TPR 4. FT REPEAT 245 278 TPR 5. FT REPEAT 279 312 TPR 6. FT REPEAT 313 346 TPR 7. FT REPEAT 347 380 TPR 8. FT DOMAIN 907 1070 JmjC. FT METAL 958 958 Iron (By similarity). FT METAL 960 960 Iron (By similarity). FT CONFLICT 1069 1069 E -> Q (in Ref. 2; CAA70422). FT CONFLICT 1149 1212 EVFNLLFVTNESNSQKTYIVHCQNCARKTSGNLENFVVLEQ FT YKMEDLIQVYDQFTLAPSLSSAS -> STRDLLPQLHLRQC FT HLQGPTDKAAILEFHLTEGSGDMH (in Ref. 2; FT CAA70422). SQ SEQUENCE 1212 AA; 136737 MW; 2AE1A816F3D6ACB5 CRC64; MKSYGLSLTT AALGNEEKKM AAEKARGEGE EGSFSLTVEE KKALCGLDSS FFGFLTRCKD GAKMKTLLNK AIHFYESLIV KAEGKVESDF FCQLGHFNLL LEDYSKALSS YQRYYSLQTD YWKNAAFLYG LGLVYFYYNA FQWAIRAFQE VLYVDPNFCR AKEIHLRLGF MFKMNTDYES SLKHFQLALI DCNVCTLSSV EIQFHIAHLY ETQRKYHSAK AAYEQLLQIE SLPSQVKATV LQQLGWMHHN MDLIGDNTTK ERYAIQYLQK SLEEDPNSGQ SWYFLGRCYS CIGKVQDAFV SYRQSIDKSE ASADTWCSIG VLYQQQNQPM DALQAYICAV QLDHGHAAAW MDLGILYESC NQPQDAIKCY LNAARSKSCN NTSALTSRIK FLQAQLCNLP QSSLQNKTKL LPSIEEAWSL PIPAELTSRQ GAMNTAQQSV SDTWNSVQTA SHHSVQQKVY TQCFTAQKLQ SFGKDQQPPF QTGSTRYLQA ASTNDQNQNG NHTLPQNSKG DAQNHFLRIP TSEEQKIINF TKESKDSRSK SLTSKTSRKD RDTSNICVNA KKHSNHIYQI SSVPISSLNN KESVSPDLII VDNPQLSVLV GETIDNVDHD IGTCNKVNNV HLAIHKKPDN LSASSPSSAI STETLSLKLT EQTHIVTSFI SPHSGLHTIN GEGHENLESS ASVNVGLRPR SQIIPSMSVS IYSSSTEVLK ACRSLGKNGL SNGHILLDIC PPPRPPTSPY PPLPKEKLNP PTPSIYLENK RDAFFPPLHQ FCINPKNPVT VIRGLAGALK LDLGLFSTKT LVEANNEHIV EVRTQLLQPA DENWDPSGTK KIWRYENKSS HTTIAKYAQY QACSFQESLR EENERRTQVK DYSDNESTCS DNSGRRQKAP FKTIKCGINI DLSDNKKWKL QLHELTKLPA FVRVVSAGNL LSHVGYTILG MNSVQLCMKV PGSRIPGHQE NNNFCSVNIN IGPGDCEWFV VPEDYWGVLN DFCEKNNLNF LMSSWWPNLE DLYEANVPVY RFIQRPGDLV WINAGTVHWV QAIGWCNNIT WNVGPLTAFQ YKLAVERYEW NKLQSVKSVV PMVHLSWNMA RNIKVSDPKL FEMIKYCLLK ILKHCQTLRE ALVAAGKEVL WHGRINDEPA PYCSICEVEV FNLLFVTNES NSQKTYIVHC QNCARKTSGN LENFVVLEQY KMEDLIQVYD QFTLAPSLSS AS // ID VAT1L_MOUSE Reviewed; 417 AA. AC Q80TB8; Q6PGM9; DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot. DT 27-SEP-2004, sequence version 2. DT 19-FEB-2014, entry version 85. DE RecName: Full=Synaptic vesicle membrane protein VAT-1 homolog-like; DE EC=1.-.-.-; GN Name=Vat1l; Synonyms=Kiaa1576; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; RX PubMed=12693553; DOI=10.1093/dnares/10.1.35; RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S., RA Nakajima D., Nagase T., Ohara O., Koga H.; RT "Prediction of the coding sequences of mouse homologues of KIAA gene: RT II. The complete nucleotide sequences of 400 mouse KIAA-homologous RT cDNAs identified by screening of terminal sequences of cDNA clones RT randomly sampled from size-fractionated libraries."; RL DNA Res. 10:35-48(2003). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6; TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase CC family. Quinone oxidoreductase subfamily. CC -!- SEQUENCE CAUTION: CC Sequence=BAC65809.1; Type=Erroneous initiation; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK122527; BAC65809.1; ALT_INIT; mRNA. DR EMBL; BC056927; AAH56927.1; -; mRNA. DR RefSeq; NP_766604.2; NM_173016.3. DR UniGene; Mm.334825; -. DR ProteinModelPortal; Q80TB8; -. DR SMR; Q80TB8; 37-382. DR BioGrid; 234760; 1. DR IntAct; Q80TB8; 1. DR STRING; 10090.ENSMUSP00000053431; -. DR PhosphoSite; Q80TB8; -. DR PaxDb; Q80TB8; -. DR PRIDE; Q80TB8; -. DR Ensembl; ENSMUST00000049509; ENSMUSP00000053431; ENSMUSG00000046844. DR GeneID; 270097; -. DR KEGG; mmu:270097; -. DR UCSC; uc009noa.1; mouse. DR CTD; 57687; -. DR MGI; MGI:2142534; Vat1l. DR eggNOG; COG0604; -. DR GeneTree; ENSGT00550000074483; -. DR HOGENOM; HOG000294681; -. DR HOVERGEN; HBG002466; -. DR InParanoid; Q80TB8; -. DR OMA; DSENKER; -. DR OrthoDB; EOG7VQJD4; -. DR TreeFam; TF314255; -. DR ChiTaRS; VAT1L; mouse. DR NextBio; 393208; -. DR PRO; PR:Q80TB8; -. DR ArrayExpress; Q80TB8; -. DR Bgee; Q80TB8; -. DR Genevestigator; Q80TB8; -. DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR Gene3D; 3.40.50.720; -; 1. DR Gene3D; 3.90.180.10; -; 1. DR InterPro; IPR013154; ADH_GroES-like. DR InterPro; IPR002085; ADH_SF_Zn-type. DR InterPro; IPR011032; GroES-like. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR002364; Quin_OxRdtase/zeta-crystal_CS. DR PANTHER; PTHR11695; PTHR11695; 1. DR Pfam; PF08240; ADH_N; 1. DR SUPFAM; SSF50129; SSF50129; 1. DR PROSITE; PS01162; QOR_ZETA_CRYSTAL; 1. PE 2: Evidence at transcript level; KW Complete proteome; Oxidoreductase; Reference proteome. FT CHAIN 1 417 Synaptic vesicle membrane protein VAT-1 FT homolog-like. FT /FTId=PRO_0000160923. SQ SEQUENCE 417 AA; 45817 MW; 604E25BDFC698CB2 CRC64; MAKEGVEKAE ETEQMIEKET SKEPAEGGDG SHRLGDAQEM RAVVLAGFGG LNKLRLSRKA MPEPQDGELK IRVKACGLNF IDLMVRQGNI DNPPKTPLVP GFECSGIVEA LGDSVKGYEI GDRVMAFVNY NAWAEVVCTP VEFVYKIPDD MSFSEAAAFP MNFVTAYTML FEIANLREGM SVLVHSAGGG VGQAVAQLCS TVPNVTVFGT ASTFKHEAIK DSVTHLFDRN ADYVQEVKRI SAEGVDIVLD CLCGDNTGKG LSLLKPLGTY ILYGSSNMVT GETKSFFSFA KSWWQVEKVN PIKLYEENKV IAGFSLLNLL FKQGRSGLIR GVVEKLIGLY NQKKIKPVVD SLWALEEVKE AMQRIHDRGN IGKLILDVEK TPTPLMANDS TETSEAGEEE EDHEGDSENK ERMPFIQ // ID VAT1_MOUSE Reviewed; 406 AA. AC Q62465; Q8R3G0; Q8R3T8; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 27-SEP-2004, sequence version 3. DT 19-FEB-2014, entry version 98. DE RecName: Full=Synaptic vesicle membrane protein VAT-1 homolog; DE EC=1.-.-.-; GN Name=Vat1; Synonyms=Vat-1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Czech II, and FVB/N; TISSUE=Mammary tumor; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] OF 105-209, PROTEIN SEQUENCE OF 239-258; RP 264-308; 369-378; 386-390 AND 396-404, AND FUNCTION. RX PubMed=9581869; RX DOI=10.1002/(SICI)1097-4644(19980601)69:3<304::AID-JCB8>3.3.CO;2-U; RA Hayess K., Kraft R., Sachsinger J., Janke J., Beckmann G., Rohde K., RA Jandrig B., Benndorf R.; RT "Mammalian protein homologous to VAT-1 of Torpedo californica: RT isolation from Ehrlich ascites tumor cells, biochemical RT characterization, and organization of its gene."; RL J. Cell. Biochem. 69:304-315(1998). CC -!- FUNCTION: Plays a part in calcium-regulated keratinocyte CC activation in epidermal repair mechanisms. Has no effect on cell CC proliferation (By similarity). Possesses ATPase activity. CC Negatively regulates mitochondrial fusion in cooperation with CC mitofusin proteins (MFN1-2) (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm. Mitochondrion outer membrane; CC Peripheral membrane protein. Note=The majority is localized in the CC cytoplasm a small amount is associated with mitochondria (By CC similarity). CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase CC family. Quinone oxidoreductase subfamily. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK034795; BAC28833.1; -; mRNA. DR EMBL; BC024586; AAH24586.1; -; mRNA. DR EMBL; BC025496; AAH25496.1; -; mRNA. DR EMBL; X95562; CAA64807.1; -; mRNA. DR RefSeq; NP_036167.1; NM_012037.2. DR UniGene; Mm.29210; -. DR ProteinModelPortal; Q62465; -. DR SMR; Q62465; 61-398. DR BioGrid; 205084; 3. DR IntAct; Q62465; 5. DR MINT; MINT-4997313; -. DR PhosphoSite; Q62465; -. DR PaxDb; Q62465; -. DR PRIDE; Q62465; -. DR Ensembl; ENSMUST00000040430; ENSMUSP00000048350; ENSMUSG00000034993. DR GeneID; 26949; -. DR KEGG; mmu:26949; -. DR UCSC; uc007loy.1; mouse. DR CTD; 10493; -. DR MGI; MGI:1349450; Vat1. DR eggNOG; COG0604; -. DR GeneTree; ENSGT00550000074483; -. DR HOGENOM; HOG000294681; -. DR HOVERGEN; HBG002466; -. DR InParanoid; Q62465; -. DR KO; K00540; -. DR OMA; VAIMMAK; -. DR OrthoDB; EOG7VQJD4; -. DR TreeFam; TF314255; -. DR ChiTaRS; VAT1; mouse. DR NextBio; 304887; -. DR PRO; PR:Q62465; -. DR ArrayExpress; Q62465; -. DR Bgee; Q62465; -. DR Genevestigator; Q62465; -. DR GO; GO:0005741; C:mitochondrial outer membrane; ISS:UniProtKB. DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0010637; P:negative regulation of mitochondrial fusion; ISS:UniProtKB. DR Gene3D; 3.40.50.720; -; 1. DR Gene3D; 3.90.180.10; -; 1. DR InterPro; IPR013149; ADH_C. DR InterPro; IPR013154; ADH_GroES-like. DR InterPro; IPR002085; ADH_SF_Zn-type. DR InterPro; IPR011032; GroES-like. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR002364; Quin_OxRdtase/zeta-crystal_CS. DR PANTHER; PTHR11695; PTHR11695; 1. DR Pfam; PF08240; ADH_N; 1. DR Pfam; PF00107; ADH_zinc_N; 1. DR SUPFAM; SSF50129; SSF50129; 1. DR PROSITE; PS01162; QOR_ZETA_CRYSTAL; 1. PE 1: Evidence at protein level; KW Acetylation; Complete proteome; Cytoplasm; Direct protein sequencing; KW Membrane; Mitochondrion; Mitochondrion outer membrane; Oxidoreductase; KW Phosphoprotein; Reference proteome. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 406 Synaptic vesicle membrane protein VAT-1 FT homolog. FT /FTId=PRO_0000160919. FT MOD_RES 2 2 N-acetylserine (By similarity). FT MOD_RES 33 33 Phosphoserine (By similarity). SQ SEQUENCE 406 AA; 43097 MW; 3F704C3667C21E37 CRC64; MSAEREAAEA ATVAAATEAG AETGTGAGEG APSQPPTVEV ASDPQPPPAP EASASASAPP LRCLVLTGFG GYDKVKLQSR PAVPPAPGPG QLTLRVRACG LNFADLMGRQ GLYDRLPPLP VTPGMEGAGV VVAVGEGVGD RKAGDRVMVL NRSGMWQEEV TVPSAQTFLM PEAMTFEEAA ALLVNYITAY MVLFDFGNLR PGHSVLVHMA AGGVGMAALQ LCRTVENVTV FGTASASKHE VLKENGVTHP IDYHTTDYVD EIKKISPKGV DIVMDPLGGS DTAKGYHLLK PMGKVVTYGM ANLLTGPKRN LMAMARTWWN QFSVTALQLL QANRAVCGFH LGYLDGEVEL VNSVVTRLVA LYNQGHIKPR IDSVWPFEKV ADAMKQMQEK KNIGKVLLVP GPEKET // ID VKOR1_MOUSE Reviewed; 161 AA. AC Q9CRC0; DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 19-FEB-2014, entry version 82. DE RecName: Full=Vitamin K epoxide reductase complex subunit 1; DE EC=1.1.4.1; DE AltName: Full=Vitamin K1 2,3-epoxide reductase subunit 1; GN Name=Vkorc1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Head, Kidney, and Small intestine; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Czech II; TISSUE=Mammary gland; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: Involved in vitamin K metabolism. Catalytic subunit of CC the vitamin K epoxide reductase (VKOR) complex which reduces CC inactive vitamin K 2,3-epoxide to active vitamin K (By CC similarity). CC -!- CATALYTIC ACTIVITY: 2-methyl-3-phytyl-1,4-naphthoquinone + CC oxidized dithiothreitol = 2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl- CC 1,4-naphthoquinone + 1,4-dithiothreitol. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass CC membrane protein (By similarity). CC -!- MISCELLANEOUS: The location of two cysteine active-site residues CC within a proposed transmembrane is consistent both with the known CC hydrophobic environment of the thiol redox site of the enzyme and CC with the lipophilicity of vitamin K and warfarin. CC -!- SIMILARITY: Belongs to the VKOR family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK013996; BAB29106.1; -; mRNA. DR EMBL; AK002742; BAB22320.1; -; mRNA. DR EMBL; AK003237; BAB22661.1; -; mRNA. DR EMBL; AK008509; BAB25708.1; -; mRNA. DR EMBL; AK008578; BAB25757.1; -; mRNA. DR EMBL; BC031732; AAH31732.1; -; mRNA. DR RefSeq; NP_848715.1; NM_178600.2. DR UniGene; Mm.29703; -. DR ProteinModelPortal; Q9CRC0; -. DR SMR; Q9CRC0; 6-153. DR STRING; 10090.ENSMUSP00000033074; -. DR PhosphoSite; Q9CRC0; -. DR PaxDb; Q9CRC0; -. DR PRIDE; Q9CRC0; -. DR Ensembl; ENSMUST00000033074; ENSMUSP00000033074; ENSMUSG00000096145. DR GeneID; 27973; -. DR KEGG; mmu:27973; -. DR UCSC; uc009jxe.1; mouse. DR CTD; 79001; -. DR MGI; MGI:106442; Vkorc1. DR eggNOG; NOG46570; -. DR GeneTree; ENSGT00390000002103; -. DR HOGENOM; HOG000230752; -. DR HOVERGEN; HBG076672; -. DR InParanoid; Q9CRC0; -. DR KO; K05357; -. DR OMA; RARWASI; -. DR OrthoDB; EOG7TQV2D; -. DR TreeFam; TF328467; -. DR ChiTaRS; VKORC1; mouse. DR NextBio; 306466; -. DR PRO; PR:Q9CRC0; -. DR ArrayExpress; Q9CRC0; -. DR Bgee; Q9CRC0; -. DR CleanEx; MM_VKORC1; -. DR Genevestigator; Q9CRC0; -. DR GO; GO:0005783; C:endoplasmic reticulum; ISA:MGI. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0047057; F:vitamin-K-epoxide reductase (warfarin-sensitive) activity; IDA:MGI. DR GO; GO:0050820; P:positive regulation of coagulation; IMP:MGI. DR GO; GO:0042371; P:vitamin K biosynthetic process; ISA:MGI. DR InterPro; IPR012932; VKOR. DR Pfam; PF07884; VKOR; 1. DR SMART; SM00756; VKc; 1. PE 2: Evidence at transcript level; KW Complete proteome; Disulfide bond; Endoplasmic reticulum; Membrane; KW Oxidoreductase; Redox-active center; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 161 Vitamin K epoxide reductase complex FT subunit 1. FT /FTId=PRO_0000191669. FT TOPO_DOM 1 8 Lumenal (Potential). FT TRANSMEM 9 29 Helical; (Potential). FT TOPO_DOM 30 100 Cytoplasmic (Potential). FT TRANSMEM 101 123 Helical; (Potential). FT TOPO_DOM 124 126 Lumenal (Potential). FT TRANSMEM 127 149 Helical; (Potential). FT TOPO_DOM 150 161 Cytoplasmic (Potential). FT DISULFID 132 135 Redox-active (Potential). SQ SEQUENCE 161 AA; 17768 MW; 044BEED047A57FD9 CRC64; MGTTWRSPGL VRLALCLAGL ALSLYALHVK AARARDENYR ALCDVGTAIS CSRVFSSRWG RGFGLVEHML GADSVLNQSN SIFGCLFYTL QLLLGCLRGR WASILLVLSS LVSVAGSVYL AWILFFVLYD FCIVCITTYA INVGLMLLSF QKVPEHKTKK H // ID WWOX_MOUSE Reviewed; 414 AA. AC Q91WL8; Q8C8J6; Q920Y2; Q9D2B3; Q9D339; Q9JLF5; DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 19-MAR-2014, entry version 112. DE RecName: Full=WW domain-containing oxidoreductase; DE EC=1.1.1.-; GN Name=Wwox; Synonyms=Wox1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INDUCTION, RP SUBCELLULAR LOCATION, MUTAGENESIS OF 51-LYS--ARG-54, DOMAIN, AND RP INTERACTION WITH TP53. RC TISSUE=Fibroblast; RX PubMed=11058590; DOI=10.1074/jbc.M007140200; RA Chang N.-S., Pratt N., Heath J., Schultz L., Sleve D., Carey G.B., RA Zevotek N.; RT "Hyaluronidase induction of a WW domain-containing oxidoreductase that RT enhances tumor necrosis factor cytotoxicity."; RL J. Biol. Chem. 276:3361-3370(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3 AND 4). RC STRAIN=C57BL/6J; TISSUE=Cerebellum, Colon, Embryo, and Pituitary; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC STRAIN=FVB/N; TISSUE=Kidney; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 173-414. RX PubMed=11979549; DOI=10.1002/gcc.10047; RA Krummel K.A., Denison S.R., Calhoun E., Phillips L.A., Smith D.I.; RT "The common fragile site FRA16D and its associated gene WWOX are RT highly conserved in the mouse at Fra8E1."; RL Genes Chromosomes Cancer 34:154-167(2002). RN [5] RP INTERACTION WITH MAPK8 AND TP53. RX PubMed=12514174; DOI=10.1074/jbc.M208373200; RA Chang N.-S., Doherty J., Ensign A.; RT "JNK1 physically interacts with WW domain-containing oxidoreductase RT (WOX1) and inhibits WOX1-mediated apoptosis."; RL J. Biol. Chem. 278:9195-9202(2003). RN [6] RP INTERACTION WITH MAPT. RX PubMed=15126504; DOI=10.1074/jbc.M401399200; RA Sze C.-I., Su M., Pugazhenthi S., Jambal P., Hsu L.-J., Heath J., RA Schultz L., Chang N.-S.; RT "Down-regulation of WW domain-containing oxidoreductase induces Tau RT phosphorylation in vitro. A potential role in Alzheimer's disease."; RL J. Biol. Chem. 279:30498-30506(2004). RN [7] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic brain; RX PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200; RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.; RT "Phosphoproteomic analysis of the developing mouse brain."; RL Mol. Cell. Proteomics 3:1093-1101(2004). RN [8] RP DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY. RX PubMed=15026124; DOI=10.1016/j.neuroscience.2003.12.036; RA Chen S.-T., Chuang J.-I., Wang J.P., Tsai M.S., Li H., Chang N.-S.; RT "Expression of WW domain-containing oxidoreductase WOX1 in the RT developing murine nervous system."; RL Neuroscience 124:831-839(2004). RN [9] RP INTERACTION WITH TP53, AND DOMAIN. RX PubMed=16219768; DOI=10.1074/jbc.M505590200; RA Chang N.-S., Doherty J., Ensign A., Schultz L., Hsu L.-J., Hong Q.; RT "WOX1 is essential for tumor necrosis factor-, UV light-, RT staurosporine-, and p53-mediated cell death, and its tyrosine 33- RT phosphorylated form binds and stabilizes serine 46-phosphorylated RT p53."; RL J. Biol. Chem. 280:43100-43108(2005). RN [10] RP INDUCTION. RX PubMed=15664696; DOI=10.1016/j.neuroscience.2004.07.054; RA Chen S.-T., Chuang J.-I., Cheng C.-L., Hsu L.-J., Chang N.-S.; RT "Light-induced retinal damage involves tyrosine 33 phosphorylation, RT mitochondrial and nuclear translocation of WW domain-containing RT oxidoreductase in vivo."; RL Neuroscience 130:397-407(2005). RN [11] RP DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY. RX PubMed=17360458; DOI=10.1073/pnas.0609783104; RA Aqeilan R.I., Trapasso F., Hussain S., Costinean S., Marshall D., RA Pekarsky Y., Hagan J.P., Zanesi N., Kaou M., Stein G.S., Lian J.B., RA Croce C.M.; RT "Targeted deletion of Wwox reveals a tumor suppressor function."; RL Proc. Natl. Acad. Sci. U.S.A. 104:3949-3954(2007). RN [12] RP DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY. RX PubMed=18487609; DOI=10.1074/jbc.M800855200; RA Aqeilan R.I., Hassan M.Q., de Bruin A., Hagan J.P., Volinia S., RA Palumbo T., Hussain S., Lee S.-H., Gaur T., Stein G.S., Lian J.B., RA Croce C.M.; RT "The WWOX tumor suppressor is essential for postnatal survival and RT normal bone metabolism."; RL J. Biol. Chem. 283:21629-21639(2008). RN [13] RP FUNCTION, PHOSPHORYLATION AT TYR-33, SUBCELLULAR LOCATION, AND RP INTERACTION WITH HYAL2. RX PubMed=19366691; DOI=10.1074/jbc.M806688200; RA Hsu L.-J., Schultz L., Hong Q., Van Moer K., Heath J., Li M.-Y., RA Lai F.-J., Lin S.-R., Lee M.-H., Lo C.-P., Lin Y.-S., Chen S.-T., RA Chang N.-S.; RT "Transforming growth factor beta1 signaling via interaction with cell RT surface Hyal-2 and recruitment of WWOX/WOX1."; RL J. Biol. Chem. 284:16049-16059(2009). CC -!- FUNCTION: Putative oxidoreductase. Acts as a tumor suppressor and CC plays a role in apoptosis. May function synergistically with CC p53/TP53 to control genotoxic stress-induced cell death. Plays a CC role in TGFB1 signaling and TGFB1-mediated cell death. Inhibits CC Wnt signaling, probably by sequestering DVL2 in the cytoplasm (By CC similarity). May also play a role in tumor necrosis factor (TNF)- CC mediated cell death. Required for normal bone development. CC -!- SUBUNIT: Interacts with TP53, TP73/p73 and MAPK8. Interacts with CC MAPT/TAU. Forms a ternary complex with TP53 and MDM2 and interacts CC with ERBB4, LITAF and WBP1. May interact with FAM189B and SCOTIN CC (By similarity). Interacts with HYAL2 and RUNX2. Interacts with CC TNK2 (By similarity). Interacts with TMEM207 (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Mitochondrion (By CC similarity). Note=Partially localizes to the mitochondria (By CC similarity). Translocates to the nucleus in response to TGFB1 (By CC similarity). Translocates to the nucleus upon genotoxic stress or CC TNF stimulation. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; Synonyms=Wox1; CC IsoId=Q91WL8-1; Sequence=Displayed; CC Name=2; CC IsoId=Q91WL8-2; Sequence=VSP_016370, VSP_016371; CC Note=No experimental confirmation available; CC Name=3; CC IsoId=Q91WL8-3; Sequence=VSP_016373, VSP_016374; CC Note=No experimental confirmation available; CC Name=4; CC IsoId=Q91WL8-4; Sequence=VSP_016372, VSP_016375; CC Note=No experimental confirmation available; CC -!- TISSUE SPECIFICITY: Ubiquitous. In the brain, expressed in cortex, CC striatum, hippocampus and cerebellum (at protein level). Detected CC in embryonic skeleton, in cranofacial bones, vertebrae and limb CC bones. Detected in chondrocytes and osteoblasts. CC -!- DEVELOPMENTAL STAGE: Expression starts at E8 in the developing CC heart. Higher expression in the brain is detected between E12 and CC E16. High levels of expression in dorsal root ganglia and spinal CC nerves were observed throughout all developmental stages. In later CC developmental stages expression is more prominent in skeletal CC systems (at protein level). CC -!- INDUCTION: By hyaluronidase. Up-regulated in outer and inner CC nuclear layers during retinal degeneration. CC -!- DOMAIN: The WW 1 domain mediates interaction with TP73, TFAP2C, CC LITAF, WBP1 and probably TP53. CC -!- PTM: Phosphorylated upon genotoxic stress. Phosphorylation of Tyr- CC 33 regulates interaction with TP53, TP73 and MAPK8. May also CC regulate proapoptotic activity. Phosphorylation by TNK2 is CC associated with polyubiquitination and degradation (By CC similarity). CC -!- PTM: Ubiquitinated when phosphorylated by TNK2, leading to its CC degradation (By similarity). CC -!- DISRUPTION PHENOTYPE: Indistinguishable from wild-type at birth, CC but die after three weeks due to metabolic syndrome characterized CC by serum hypoproteinemia, hypoalbuminemia, hypoglycemia, CC hypocalcemia, hypotriglyceridemia and hypocholesterolemia, growth CC retardation, decreased bone formation and increased bone CC resorption. In addition, spontaneous tumor development was CC observed. CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases CC (SDR) family. CC -!- SIMILARITY: Contains 2 WW domains. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF187014; AAF31693.1; -; mRNA. DR EMBL; AK018507; BAB31244.1; -; mRNA. DR EMBL; AK019911; BAB31911.1; -; mRNA. DR EMBL; AK046903; BAC32916.1; -; mRNA. DR EMBL; AK078528; BAC37325.1; -; mRNA. DR EMBL; BC014716; AAH14716.1; -; mRNA. DR EMBL; AH011063; AAL03972.1; -; Genomic_DNA. DR RefSeq; NP_062519.2; NM_019573.3. DR RefSeq; XP_006531577.1; XM_006531514.1. DR UniGene; Mm.440420; -. DR ProteinModelPortal; Q91WL8; -. DR SMR; Q91WL8; 13-101, 120-407. DR BioGrid; 219796; 4. DR PhosphoSite; Q91WL8; -. DR PaxDb; Q91WL8; -. DR PRIDE; Q91WL8; -. DR DNASU; 80707; -. DR Ensembl; ENSMUST00000004756; ENSMUSP00000004756; ENSMUSG00000004637. [Q91WL8-1] DR Ensembl; ENSMUST00000109107; ENSMUSP00000104735; ENSMUSG00000004637. [Q91WL8-2] DR Ensembl; ENSMUST00000109108; ENSMUSP00000104736; ENSMUSG00000004637. [Q91WL8-4] DR Ensembl; ENSMUST00000160862; ENSMUSP00000125626; ENSMUSG00000004637. [Q91WL8-3] DR GeneID; 80707; -. DR KEGG; mmu:80707; -. DR UCSC; uc009noc.2; mouse. [Q91WL8-2] DR UCSC; uc009nod.2; mouse. [Q91WL8-1] DR CTD; 51741; -. DR MGI; MGI:1931237; Wwox. DR eggNOG; COG1028; -. DR GeneTree; ENSGT00570000078948; -. DR HOGENOM; HOG000169779; -. DR HOVERGEN; HBG078800; -. DR InParanoid; Q91WL8; -. DR OMA; YSNIHRS; -. DR OrthoDB; EOG73Z2TK; -. DR TreeFam; TF105428; -. DR ChiTaRS; WWOX; mouse. DR NextBio; 350059; -. DR PRO; PR:Q91WL8; -. DR Bgee; Q91WL8; -. DR CleanEx; MM_WWOX; -. DR Genevestigator; Q91WL8; -. DR GO; GO:0005829; C:cytosol; IEA:Ensembl. DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl. DR GO; GO:0005902; C:microvillus; IEA:Ensembl. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR GO; GO:0005634; C:nucleus; IDA:BHF-UCL. DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl. DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW. DR GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IDA:BHF-UCL. DR GO; GO:0097191; P:extrinsic apoptotic signaling pathway; IDA:MGI. DR GO; GO:0072332; P:intrinsic apoptotic signaling pathway by p53 class mediator; IGI:MGI. DR GO; GO:0030178; P:negative regulation of Wnt signaling pathway; ISS:UniProtKB. DR GO; GO:0001649; P:osteoblast differentiation; IMP:MGI. DR GO; GO:2001241; P:positive regulation of extrinsic apoptotic signaling pathway in absence of ligand; IDA:MGI. DR GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:BHF-UCL. DR GO; GO:0048705; P:skeletal system morphogenesis; IMP:MGI. DR GO; GO:0006366; P:transcription from RNA polymerase II promoter; NAS:GOC. DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR002198; DH_sc/Rdtase_SDR. DR InterPro; IPR002347; Glc/ribitol_DH. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR001202; WW_dom. DR Pfam; PF00106; adh_short; 1. DR Pfam; PF00397; WW; 2. DR PRINTS; PR00081; GDHRDH. DR SMART; SM00456; WW; 2. DR SUPFAM; SSF51045; SSF51045; 2. DR PROSITE; PS01159; WW_DOMAIN_1; 2. DR PROSITE; PS50020; WW_DOMAIN_2; 2. PE 1: Evidence at protein level; KW Alternative splicing; Apoptosis; Complete proteome; Cytoplasm; KW Mitochondrion; NADP; Nucleus; Oxidoreductase; Phosphoprotein; KW Reference proteome; Repeat; Tumor suppressor; Ubl conjugation; KW Wnt signaling pathway. FT CHAIN 1 414 WW domain-containing oxidoreductase. FT /FTId=PRO_0000054816. FT DOMAIN 16 49 WW 1. FT DOMAIN 57 90 WW 2. FT NP_BIND 131 137 NADP (By similarity). FT REGION 125 414 Interaction with MAPT. FT REGION 209 273 Mediates targeting to the mitochondria. FT MOTIF 50 55 Nuclear localization signal. FT ACT_SITE 293 293 Proton acceptor (By similarity). FT BINDING 260 260 Substrate (By similarity). FT MOD_RES 12 12 Phosphothreonine (By similarity). FT MOD_RES 14 14 Phosphoserine (By similarity). FT MOD_RES 33 33 Phosphotyrosine. FT MOD_RES 287 287 Phosphotyrosine; by TNK2 (By similarity). FT VAR_SEQ 137 158 GFETAKSFALHGAHVILACRNL -> ALSPLLGERCIRRRQ FT VLCSVFG (in isoform 2). FT /FTId=VSP_016370. FT VAR_SEQ 159 414 Missing (in isoform 2). FT /FTId=VSP_016371. FT VAR_SEQ 353 367 QQGAATTVYCAVAPE -> KPCMIGHTCDPNPRN (in FT isoform 4). FT /FTId=VSP_016372. FT VAR_SEQ 353 354 QQ -> IL (in isoform 3). FT /FTId=VSP_016373. FT VAR_SEQ 355 414 Missing (in isoform 3). FT /FTId=VSP_016374. FT VAR_SEQ 368 414 Missing (in isoform 4). FT /FTId=VSP_016375. FT MUTAGEN 51 54 KRKR->QGTG: Abolishes the TNF-induced FT nuclear translocation. FT CONFLICT 135 135 G -> V (in Ref. 2; BAB31244). FT CONFLICT 231 231 V -> A (in Ref. 1; AAF31693 and 4; FT AAL03972). SQ SEQUENCE 414 AA; 46512 MW; 3C83AE3085B6A931 CRC64; MAALRYAGLD DTDSEDELPP GWEERTTKDG WVYYANHTEE KTQWEHPKTG KRKRVAGDLP YGWEQETDEN GQVFFVDHIN KRTTYLDPRL AFTVDDNPTK PTTRQRYDGS TTAMEILQGR DFTGKVVLVT GANSGIGFET AKSFALHGAH VILACRNLSR ASEAVSRILE EWHKAKVEAM TLDLAVLRSV QHFAEAFKAK NVSLHVLVCN AGTFALPWGL TKDGLETTFQ VNHLGHFYLV QLLQDVLCRS SPARVIVVSS ESHRFTDIND SSGKLDLSRL SPPRSDYWAM LAYNRSKLCN ILFSNELHRR LSPRGVTSNA VHPGNMMYSA IHRNSWVYKL LFTLARPFTK SMQQGAATTV YCAVAPELEG LGGMYFNNCC RCLPSEEAQS EETARALWEL SERLIQDRLG SPSS // ID XDH_MOUSE Reviewed; 1335 AA. AC Q00519; E9QLM9; DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 5. DT 19-MAR-2014, entry version 130. DE RecName: Full=Xanthine dehydrogenase/oxidase; DE Includes: DE RecName: Full=Xanthine dehydrogenase; DE Short=XD; DE EC=1.17.1.4; DE Includes: DE RecName: Full=Xanthine oxidase; DE Short=XO; DE EC=1.17.3.2; DE AltName: Full=Xanthine oxidoreductase; DE Short=XOR; GN Name=Xdh; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=129/Sv; TISSUE=Spleen; RX PubMed=7835888; DOI=10.1006/geno.1994.1515; RA Cazzaniga G., Terao M., Lo Schiavo P., Galbiati F., Segalla F., RA Seldin M.F., Garattini E.; RT "Chromosomal mapping, isolation, and characterization of the mouse RT xanthine dehydrogenase gene."; RL Genomics 23:390-402(1994). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=C57BL/6; TISSUE=Liver; RX PubMed=1590774; RA Terao M., Cazzaniga G., Ghezzi P., Bianchi M., Falciani F., Perani P., RA Garattini E.; RT "Molecular cloning of a cDNA coding for mouse liver xanthine RT dehydrogenase. Regulation of its transcript by interferons in vivo."; RL Biochem. J. 283:863-870(1992). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [4] RP PROTEIN SEQUENCE OF 2-9, AND INTERACTION WITH BTN1A1. RX PubMed=8541302; DOI=10.1016/0304-4165(95)00102-6; RA Ishii T., Aoki N., Noda A., Adachi T., Nakamura R., Matsuda T.; RT "Carboxy-terminal cytoplasmic domain of mouse butyrophilin RT specifically associates with a 150-kDa protein of mammary epithelial RT cells and milk fat globule membrane."; RL Biochim. Biophys. Acta 1245:285-292(1995). CC -!- FUNCTION: Key enzyme in purine degradation. Catalyzes the CC oxidation of hypoxanthine to xanthine. Catalyzes the oxidation of CC xanthine to uric acid. Contributes to the generation of reactive CC oxygen species (By similarity). CC -!- CATALYTIC ACTIVITY: Xanthine + NAD(+) + H(2)O = urate + NADH. CC -!- CATALYTIC ACTIVITY: Hypoxanthine + NAD(+) + H(2)O = xanthine + CC NADH. CC -!- CATALYTIC ACTIVITY: Xanthine + H(2)O + O(2) = urate + H(2)O(2). CC -!- COFACTOR: Binds 2 2Fe-2S clusters (By similarity). CC -!- COFACTOR: FAD (By similarity). CC -!- COFACTOR: Binds 1 molybdenum-molybdopterin (Mo-MPT) cofactor per CC subunit (By similarity). CC -!- ENZYME REGULATION: Can be converted from the dehydrogenase form CC (D) to the oxidase form (O) irreversibly by proteolysis or CC reversibly through the oxidation of sulfhydryl groups (By CC similarity). CC -!- SUBUNIT: Homodimer. Interacts with BTN1A1. CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Peroxisome (By CC similarity). Secreted (By similarity). CC -!- INDUCTION: By interferon. CC -!- PTM: Subject to partial proteolysis; this alters the enzyme from CC the dehydrogenase form (D) to the oxidase form (O) (By CC similarity). CC -!- PTM: Contains sulfhydryl groups that are easily oxidized (in CC vitro); this alters the enzyme from the dehydrogenase form (D) to CC the oxidase form (O) (By similarity). CC -!- SIMILARITY: Belongs to the xanthine dehydrogenase family. CC -!- SIMILARITY: Contains 1 2Fe-2S ferredoxin-type domain. CC -!- SIMILARITY: Contains 1 FAD-binding PCMH-type domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X75129; CAA52997.1; -; Genomic_DNA. DR EMBL; X75128; CAA52997.1; JOINED; Genomic_DNA. DR EMBL; X75127; CAA52997.1; JOINED; Genomic_DNA. DR EMBL; X75126; CAA52997.1; JOINED; Genomic_DNA. DR EMBL; X75125; CAA52997.1; JOINED; Genomic_DNA. DR EMBL; X75124; CAA52997.1; JOINED; Genomic_DNA. DR EMBL; X75123; CAA52997.1; JOINED; Genomic_DNA. DR EMBL; X75122; CAA52997.1; JOINED; Genomic_DNA. DR EMBL; X75121; CAA52997.1; JOINED; Genomic_DNA. DR EMBL; X75120; CAA52997.1; JOINED; Genomic_DNA. DR EMBL; X75119; CAA52997.1; JOINED; Genomic_DNA. DR EMBL; X75130; CAA52997.1; JOINED; Genomic_DNA. DR EMBL; X75131; CAA52997.1; JOINED; Genomic_DNA. DR EMBL; X75132; CAA52997.1; JOINED; Genomic_DNA. DR EMBL; X75133; CAA52997.1; JOINED; Genomic_DNA. DR EMBL; X75134; CAA52997.1; JOINED; Genomic_DNA. DR EMBL; X75135; CAA52997.1; JOINED; Genomic_DNA. DR EMBL; X75136; CAA52997.1; JOINED; Genomic_DNA. DR EMBL; X75137; CAA52997.1; JOINED; Genomic_DNA. DR EMBL; X75138; CAA52997.1; JOINED; Genomic_DNA. DR EMBL; X75139; CAA52997.1; JOINED; Genomic_DNA. DR EMBL; X75140; CAA52997.1; JOINED; Genomic_DNA. DR EMBL; X75141; CAA52997.1; JOINED; Genomic_DNA. DR EMBL; X75142; CAA52997.1; JOINED; Genomic_DNA. DR EMBL; X75143; CAA52997.1; JOINED; Genomic_DNA. DR EMBL; X75151; CAA52997.1; JOINED; Genomic_DNA. DR EMBL; X75152; CAA52997.1; JOINED; Genomic_DNA. DR EMBL; X75153; CAA52997.1; JOINED; Genomic_DNA. DR EMBL; X75154; CAA52997.1; JOINED; Genomic_DNA. DR EMBL; X75144; CAA52997.1; JOINED; Genomic_DNA. DR EMBL; X75145; CAA52997.1; JOINED; Genomic_DNA. DR EMBL; X75146; CAA52997.1; JOINED; Genomic_DNA. DR EMBL; X75147; CAA52997.1; JOINED; Genomic_DNA. DR EMBL; X75148; CAA52997.1; JOINED; Genomic_DNA. DR EMBL; X75149; CAA52997.1; JOINED; Genomic_DNA. DR EMBL; X75150; CAA52997.1; JOINED; Genomic_DNA. DR EMBL; X62932; CAA44705.1; -; mRNA. DR EMBL; AC159187; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CT025731; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR PIR; I48374; XOMSDH. DR RefSeq; NP_035853.2; NM_011723.3. DR UniGene; Mm.11223; -. DR ProteinModelPortal; Q00519; -. DR SMR; Q00519; 7-166, 197-530, 574-1318. DR IntAct; Q00519; 2. DR MINT; MINT-1866314; -. DR STRING; 10090.ENSMUSP00000024866; -. DR PhosphoSite; Q00519; -. DR PaxDb; Q00519; -. DR PRIDE; Q00519; -. DR Ensembl; ENSMUST00000024866; ENSMUSP00000024866; ENSMUSG00000024066. DR GeneID; 22436; -. DR KEGG; mmu:22436; -. DR UCSC; uc008dno.1; mouse. DR CTD; 7498; -. DR MGI; MGI:98973; Xdh. DR eggNOG; COG4630; -. DR GeneTree; ENSGT00390000003772; -. DR HOGENOM; HOG000191197; -. DR HOVERGEN; HBG004182; -. DR InParanoid; Q00519; -. DR KO; K00106; -. DR OMA; CDETFFA; -. DR OrthoDB; EOG7QRQSZ; -. DR TreeFam; TF353036; -. DR BioCyc; MetaCyc:MONOMER-14019; -. DR ChiTaRS; XDH; mouse. DR NextBio; 302885; -. DR PRO; PR:Q00519; -. DR ArrayExpress; Q00519; -. DR Bgee; Q00519; -. DR CleanEx; MM_XDH; -. DR Genevestigator; Q00519; -. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell. DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; ISS:UniProtKB. DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; ISS:UniProtKB. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0030151; F:molybdenum ion binding; IEA:InterPro. DR GO; GO:0043546; F:molybdopterin cofactor binding; ISS:UniProtKB. DR GO; GO:0008762; F:UDP-N-acetylmuramate dehydrogenase activity; IEA:InterPro. DR GO; GO:0004854; F:xanthine dehydrogenase activity; ISS:UniProtKB. DR GO; GO:0004855; F:xanthine oxidase activity; ISS:UniProtKB. DR GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IEA:Ensembl. DR GO; GO:0007595; P:lactation; IMP:MGI. DR GO; GO:0045602; P:negative regulation of endothelial cell differentiation; IEA:Ensembl. DR GO; GO:0001937; P:negative regulation of endothelial cell proliferation; IEA:Ensembl. DR GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl. DR GO; GO:0051898; P:negative regulation of protein kinase B signaling; IEA:Ensembl. DR GO; GO:0001933; P:negative regulation of protein phosphorylation; IEA:Ensembl. DR GO; GO:1900747; P:negative regulation of vascular endothelial growth factor signaling pathway; IEA:Ensembl. DR GO; GO:2001213; P:negative regulation of vasculogenesis; IEA:Ensembl. DR GO; GO:1900745; P:positive regulation of p38MAPK cascade; IEA:Ensembl. DR GO; GO:2000379; P:positive regulation of reactive oxygen species metabolic process; IEA:Ensembl. DR GO; GO:0030856; P:regulation of epithelial cell differentiation; IMP:MGI. DR GO; GO:0009115; P:xanthine catabolic process; ISS:UniProtKB. DR Gene3D; 1.10.150.120; -; 1. DR Gene3D; 3.10.20.30; -; 1. DR Gene3D; 3.30.365.10; -; 6. DR Gene3D; 3.30.43.10; -; 1. DR Gene3D; 3.30.465.10; -; 1. DR Gene3D; 3.90.1170.50; -; 1. DR InterPro; IPR002888; 2Fe-2S-bd. DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type. DR InterPro; IPR006058; 2Fe2S_fd_BS. DR InterPro; IPR000674; Ald_Oxase/Xan_DH_a/b. DR InterPro; IPR016208; Ald_Oxase/xanthine_DH. DR InterPro; IPR008274; AldOxase/xan_DH_Mopterin-bd. DR InterPro; IPR012675; Beta-grasp_dom. DR InterPro; IPR005107; CO_DH_flav_C. DR InterPro; IPR016169; CO_DH_flavot_FAD-bd_sub2. DR InterPro; IPR016166; FAD-bd_2. DR InterPro; IPR016167; FAD-bd_2_sub1. DR InterPro; IPR002346; Mopterin_DH_FAD-bd. DR InterPro; IPR022407; OxRdtase_Mopterin_BS. DR InterPro; IPR014309; Xanthine_DH_Mopterin-bd_su. DR InterPro; IPR014307; Xanthine_DH_ssu. DR Pfam; PF01315; Ald_Xan_dh_C; 1. DR Pfam; PF02738; Ald_Xan_dh_C2; 1. DR Pfam; PF03450; CO_deh_flav_C; 1. DR Pfam; PF00941; FAD_binding_5; 1. DR Pfam; PF00111; Fer2; 1. DR Pfam; PF01799; Fer2_2; 1. DR PIRSF; PIRSF000127; Xanthine_DH; 1. DR SMART; SM01008; Ald_Xan_dh_C; 1. DR SMART; SM01092; CO_deh_flav_C; 1. DR SUPFAM; SSF47741; SSF47741; 1. DR SUPFAM; SSF54292; SSF54292; 1. DR SUPFAM; SSF54665; SSF54665; 1. DR SUPFAM; SSF55447; SSF55447; 1. DR SUPFAM; SSF56003; SSF56003; 1. DR SUPFAM; SSF56176; SSF56176; 1. DR TIGRFAMs; TIGR02963; xanthine_xdhA; 1. DR TIGRFAMs; TIGR02965; xanthine_xdhB; 1. DR PROSITE; PS00197; 2FE2S_FER_1; 1. DR PROSITE; PS51085; 2FE2S_FER_2; 1. DR PROSITE; PS51387; FAD_PCMH; 1. DR PROSITE; PS00559; MOLYBDOPTERIN_EUK; 1. PE 1: Evidence at protein level; KW 2Fe-2S; Complete proteome; Cytoplasm; Direct protein sequencing; KW Disulfide bond; FAD; Flavoprotein; Glycoprotein; Iron; Iron-sulfur; KW Metal-binding; Molybdenum; NAD; Oxidoreductase; Peroxisome; KW Reference proteome; Secreted. FT INIT_MET 1 1 Removed. FT CHAIN 2 1335 Xanthine dehydrogenase/oxidase. FT /FTId=PRO_0000166085. FT DOMAIN 7 94 2Fe-2S ferredoxin-type. FT DOMAIN 231 416 FAD-binding PCMH-type. FT NP_BIND 259 266 FAD (By similarity). FT NP_BIND 349 353 FAD (By similarity). FT ACT_SITE 1264 1264 Proton acceptor (By similarity). FT METAL 46 46 Iron-sulfur 1 (By similarity). FT METAL 51 51 Iron-sulfur 1 (By similarity). FT METAL 54 54 Iron-sulfur 1 (By similarity). FT METAL 76 76 Iron-sulfur 1 (By similarity). FT METAL 115 115 Iron-sulfur 2 (By similarity). FT METAL 118 118 Iron-sulfur 2 (By similarity). FT METAL 150 150 Iron-sulfur 2 (By similarity). FT METAL 152 152 Iron-sulfur 2 (By similarity). FT METAL 770 770 Molybdenum (By similarity). FT METAL 801 801 Molybdenum; via carbonyl oxygen (By FT similarity). FT METAL 915 915 Molybdenum; via amide nitrogen (By FT similarity). FT METAL 1082 1082 Molybdenum; via amide nitrogen (By FT similarity). FT BINDING 339 339 FAD (By similarity). FT BINDING 362 362 FAD (By similarity). FT BINDING 406 406 FAD; via amide nitrogen and carbonyl FT oxygen (By similarity). FT BINDING 424 424 FAD (By similarity). FT BINDING 805 805 Substrate (By similarity). FT BINDING 883 883 Substrate (By similarity). FT BINDING 917 917 Substrate (By similarity). FT BINDING 1013 1013 Substrate; via amide nitrogen (By FT similarity). FT CARBOHYD 1076 1076 N-linked (GlcNAc...) (Potential). FT DISULFID 538 995 In oxidase form (By similarity). FT CONFLICT 241 241 V -> I (in Ref. 2; CAA44705). FT CONFLICT 621 621 M -> T (in Ref. 1; CAA52997). FT CONFLICT 1247 1247 L -> V (in Ref. 1; CAA52997 and 2; FT CAA44705). SQ SEQUENCE 1335 AA; 146562 MW; 56AD3E0C75E00F98 CRC64; MTRTTVDELV FFVNGKKVVE KNADPETTLL VYLRRKLGLC GTKLGCGEGG CGACTVMISK YDRLQNKIVH FSVNACLTPI CSLHHVAVTT VEGIGNTKKL HPVQERIAKS HGSQCGFCTP GIVMSMYTLL RNKPEPTVEE IENAFQGNLC RCTGYRPILQ GFRTFAKDGG CCGGSGNNPN CCMSQTKDQT IAPSSSLFNP EDFKPLDPTQ EPIFPPELLR LKDTPRKTLR FEGERVTWIQ VSTMEELLDL KAQHPDAKLV VGNTEIGIEM KFKNMLFPLI ICPAWILELT SVAHGPEGIS FGAACPLSLV ESVLADAIAT LPEQRTEVFR GVMEQLRWFA GKQVKSVASI GGNIITASPI SDLNPVLMAS RAKLTLASRG TKRTVWMDHT FFPGYRRTLL SPEEILVSIV IPYSRKGEFF SAFKQASRRE DDIAKVTSGM RVLFKPGTTE VQELSLCFGG MADRTVSALK TTPKQLSKSW NEELLQDVCA GLAEELHLAP DAPGGMVEFR RTLTLSFFFK FYLTVLQKLG RADLEGMCGK LDPTFASATL LFQKDPPANV QLFQEVPKGQ SEEDMVGRPM PHLAADMQAS GEAVYCDDIP RYENELSLRL VTSTRAHAKI MSIDTSEAKK VPGFVCFLTS EDVPGSNITG IFNDETVFAK DEVTCVGHII GAVVADTPEH AHRAARGVKI TYEDLPAIIT IQDAIKNNSF YGPEVKIEKG DLKKGFSEAD NVVSGELYIG GQEHFYLETH CTIAVPKGEA GEMELFVSTQ NTMKTQSFIA KMLGVPDNRI VVRVKRMGGG FGGKETRSTL ISTAVALAAY KTGRPVRCML DRDEDMLITG GRHPFLAKYK VGFMKTGTIV ALEVAHFSNG GNSEDLSRSI MERAVFHMDN AYKIPNIRGT GRICKTNLPS NTAFRGFGGP QGMLIAEYWM SEVAVTCGLP AEEVRRKNMY KEGDLTHFNQ KLEGFTLPRC WDECIASSQY QARKMEVEKF NRENCWKKRG LCIIPTKFGI SFTLSFLNQG GALVHVYTDG SVLLTHGGTE MGQGLHTKMV QVASRALKIP TSKIHITETS TNTVPNTSPT AASASADLNG QAIYEACQTI LKRLEPFKKK NPSGSWESWV MDAYTSAVSL SATGFYKTPN LGYSFETNSG NPFHYFSYGV ACSEVEIDCL TGDHKNLRTD IVMDVGSSLN PAIDIGQVEG AFVQGLGLFT MEELHYSPEG SLHTRGPSTY KIPAFGSIPI EFRVSLLRDC PNKRAIYASK AVGEPPLFLA SSIFFAIKDA IRAARAQHGD SNAKQLFQLD SPATPEKIRN ACVDQFTTLC ATGTPENCKS WSVRI // ID ZADH2_MOUSE Reviewed; 377 AA. AC Q8BGC4; DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 19-MAR-2014, entry version 86. DE RecName: Full=Zinc-binding alcohol dehydrogenase domain-containing protein 2; DE EC=1.-.-.-; GN Name=Zadh2; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Cerebellum, Head, and Spinal cord; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP SUBCELLULAR LOCATION, AND INDUCTION. RX PubMed=19091015; DOI=10.1186/1471-2105-9-S12-S16; RA Mizuno Y., Kurochkin I.V., Herberth M., Okazaki Y., Schoenbach C.; RT "Predicted mouse peroxisome-targeted proteins and their actual RT subcellular locations."; RL BMC Bioinformatics 9:S16-S16(2008). RN [3] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-35, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23576753; DOI=10.1073/pnas.1302961110; RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., RA Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.; RT "Label-free quantitative proteomics of the lysine acetylome in RT mitochondria identifies substrates of SIRT3 in metabolic pathways."; RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013). CC -!- SUBCELLULAR LOCATION: Peroxisome. CC -!- INDUCTION: Up-regulated by high fat diet. CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase CC family. Quinone oxidoreductase subfamily. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK047559; BAC33086.1; -; mRNA. DR EMBL; AK081988; BAC38389.1; -; mRNA. DR EMBL; AK083082; BAC38754.1; -; mRNA. DR RefSeq; NP_666202.2; NM_146090.5. DR UniGene; Mm.147052; -. DR UniGene; Mm.440718; -. DR ProteinModelPortal; Q8BGC4; -. DR SMR; Q8BGC4; 33-371. DR PhosphoSite; Q8BGC4; -. DR PaxDb; Q8BGC4; -. DR PRIDE; Q8BGC4; -. DR Ensembl; ENSMUST00000060223; ENSMUSP00000052544; ENSMUSG00000049090. DR GeneID; 225791; -. DR KEGG; mmu:225791; -. DR UCSC; uc008fun.1; mouse. DR CTD; 284273; -. DR MGI; MGI:2444835; Zadh2. DR eggNOG; COG2130; -. DR GeneTree; ENSGT00550000074483; -. DR HOGENOM; HOG000294682; -. DR HOVERGEN; HBG056525; -. DR InParanoid; Q8BGC4; -. DR KO; K07119; -. DR OMA; DINYSAG; -. DR OrthoDB; EOG7FNC7F; -. DR TreeFam; TF328691; -. DR NextBio; 377795; -. DR PRO; PR:Q8BGC4; -. DR ArrayExpress; Q8BGC4; -. DR Bgee; Q8BGC4; -. DR Genevestigator; Q8BGC4; -. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR GO; GO:0005777; C:peroxisome; IDA:UniProtKB. DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR Gene3D; 3.40.50.720; -; 1. DR Gene3D; 3.90.180.10; -; 1. DR InterPro; IPR013149; ADH_C. DR InterPro; IPR013154; ADH_GroES-like. DR InterPro; IPR002085; ADH_SF_Zn-type. DR InterPro; IPR011032; GroES-like. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR002364; Quin_OxRdtase/zeta-crystal_CS. DR PANTHER; PTHR11695; PTHR11695; 1. DR Pfam; PF08240; ADH_N; 1. DR Pfam; PF00107; ADH_zinc_N; 1. DR SUPFAM; SSF50129; SSF50129; 2. DR PROSITE; PS01162; QOR_ZETA_CRYSTAL; 1. PE 1: Evidence at protein level; KW Acetylation; Complete proteome; NADP; Oxidoreductase; Peroxisome; KW Reference proteome. FT CHAIN 1 377 Zinc-binding alcohol dehydrogenase FT domain-containing protein 2. FT /FTId=PRO_0000223466. FT NP_BIND 303 305 NADP (By similarity). FT BINDING 185 185 NADP; via amide nitrogen (By similarity). FT BINDING 205 205 NADP (By similarity). FT BINDING 209 209 NADP (By similarity). FT BINDING 224 224 NADP (By similarity). FT BINDING 247 247 NADP (By similarity). FT BINDING 269 269 NADP; via carbonyl oxygen (By FT similarity). FT BINDING 275 275 NADP (By similarity). FT BINDING 361 361 NADP (By similarity). FT MOD_RES 35 35 N6-acetyllysine. SQ SEQUENCE 377 AA; 40529 MW; AA23871FCC081CEE CRC64; MLRLAAAGAR AIVDMSYARH FLDFQGSAIP RTMQKLVVTR LSPNFHEAVT LRRDCPVPLP GDGDLLVRNR FVGINASDIN YSAGRYDPSL KPPFDIGFEG IGEVVALGLS ASARYTVGQA VAYMAPGSFA EYTVVPASIA IPMPSVKPEY LTMLVSGTTA YLSLEELGEL SEGKKVLVTA AAGGTGQFAV QLSKIAKCHV IGTCSSDEKA AFLKSIGCDR PINYRTEPVE TVLKQEYPEG VDVVYESVGG AMFDLAVDAL ATKGRLIVIG FISGYQSPTG LSPIKAGVLP TKLLKKSASL RGFFLNHYFS KYQAAMERLL ELYARGDLVC EVDLGHLAPD GRFIGLESVF QAVDYMYTGK NTGKLVVELP HPVSSKL //